TRIM28 (Kr.19q13.43), TIF1B, KAP1, RNF96 (CVI, PHD, BROMO)
- Tällä geenillä on useita nimiä. Sen koodaama proteiini TRIM28 välittää transkriptionaalista kontrollia tekemällä KRAB-ZFP interaktion (Krüppel-associated box domain - Zinc finger protein) Eli trimin RBBCC-domaani sitoo tämän KRAB- boxin jossa on kolme Zn2+ kantava jatke, joka asettuu DNA- kohde sekvenssille.
- Sen takia TRIM29 on sanut nimen KAP1, Krab Associated protein 1.Myös KRAB interacting protein 1 KRIP-1. KRAB rekrytoi TRIM28.
- Se on myös TIF1B Transcription intermediating factor B. Sinkkisormiproteiineissa sen numero on RNF96. Proteiini lokalisoituu tumaan ja assosioituu siellä spesifiseen kromatiinialueeseen. Kaiken kaikkiaan siinä on sinkkiä sitovia domaaneja RING, Box1 ja Box2. Sillä on helikaalinen Coiled coil domeeni. Rakenteelliaesti C-terminaalin perusteella se on ryhmää VI. Siinä erotetaan PHD-domaani ja BROMO, jotka tekevät proteiini-proteiini interaktioita. Geeniä ilmenee 27 eri kudoksessa, eniten ovariossa ja testiksessä.
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- Also known as KAP1; TF1B; RNF96; TIF1B; PPP1R157
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- Summary The protein encoded by this gene mediates transcriptional control by interaction with the Kruppel-associated box repression domain found in many transcription factors. The protein localizes to the nucleus and is thought to associate with specific chromatin regions. The protein is a member of the tripartite motif family. This tripartite motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. [provided by RefSeq, Jul 2008] Expression Ubiquitous expression in ovary (RPKM 89.1), testis (RPKM 80.5) and 25 other tissues See more
Nimet ovat monet:
- Preferred Names
- transcription intermediary factor 1-beta
- Names
- E3 SUMO-protein ligase TRIM28
- KAP-1
- KRAB [Kruppel-associated box domain]-associated protein 1
- KRAB-interacting protein 1
- KRIP-1
- RING finger protein 96
- RING-type E3 ubiquitin transferase TIF1-beta
- TIF1-beta
- nuclear corepressor KAP-1
- protein phosphatase 1, regulatory subunit 157 , PPP1R157
- transcriptional intermediary factor 1-beta
Konservoidut domeenit:Conserved Domains (7) summary
- cd05502
Location:696 → 802 - Bromo_tif1_like; Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of the tripartite motif (TRIM) protein family, which is characterized by a particular domain architecture. It functions by recruiting coactivators and/or ...
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smart00502
Location:252 → 378 - BBC; B-Box C-terminal domain
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smart00336
Location:148 → 184 - BBOX; B-Box-type zinc finger
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cd00021
Location:207 → 245 - BBOX; B-Box-type zinc finger; zinc binding domain (CHC3H2); often present in combination with other motifs, like RING zinc finger, NHL motif, coiled-coil or RFP domain in functionally unrelated proteins, most likely mediating protein-protein interaction.
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cd15623
Location:627 → 669 - PHD_TIF1beta; PHD finger found in transcription intermediary factor 1-beta (TIF1-beta)
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cd16765
Location:62 → 124 - RING-HC_TIF1beta; RING finger, HC subclass, found in transcription inknown asiary factor 1-beta (TIF1-beta)
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cl25756
Location:525 → 620 - BASP1; Brain acid soluble protein 1 (BASP1 protein)
transcription
intermediary factor 1-beta [Homo sapiens]
TRIM28 PEPTIDIRAKENNE, 835 aminohappoa.
LOCUS NP_005753 835 aa linear PRI 08-APR-2018 DEFINITION transcription intermediary factor 1-beta [Homo sapiens]. ACCESSION NP_005753 VERSION NP_005753.1 DBSOURCE REFSEQ: accession NM_005762.2 KEYWORDS RefSeq. SOURCE Homo sapiens (human) ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 835) AUTHORS Shen LT, Chou HE and Kato M. TITLE TIF1beta is phosphorylated at serine 473 in colorectal tumor cells through p38 mitogen-activated protein kinase as an oxidative defense mechanism JOURNAL Biochem. Biophys. Res. Commun. 492 (3), 310-315 (2017) PUBMED 28864417 REMARK GeneRIF: it is primarily peroxide-induced p38 MAPK that mediates Ser473 phosphorylation and activation of TIF1beta to enable more efficient DNA repair to assist in tumor cell survival against exogenous ROS REFERENCE 2 (residues 1 to 835) AUTHORS Liu L, Xiao L, Liang X, Chen L, Cheng L, Zhang L, Wu X, Xu Q and Ma C. TITLE TRIM28 knockdown increases sensitivity to etoposide by upregulating E2F1 in non-small cell lung cancer JOURNAL Oncol. Rep. 37 (6), 3597-3605 (2017) PUBMED 28498400 REMARK GeneRIF: Cell proliferation and apoptosis were almost completely abolished in the PAa cells cotreated with TRIM28 siRNA and etoposide following knockdown of E2F1. The results of our study demonstrated that the combination of TRIM28 siRNA and etoposide may be effective against nonsmall cell lung cancer (NSCLC)and has the potential of being a new therapeutic tool for future treatment. REFERENCE 3 (residues 1 to 835) AUTHORS Wang Y, Li J, Huang Y, Dai X, Liu Y, Liu Z, Wang Y, Wang N and Zhang P. TITLE Tripartite motif-containing 28 bridges endothelial inflammation and angiogenic activity by retaining expression of TNFR-1 and -2 and VEGFR2 in endothelial cells JOURNAL FASEB J. 31 (5), 2026-2036 (2017) PUBMED 28159803 REMARK GeneRIF: TRIM28 acts as a central factor in controlling endothelial inflammatory responses and angiogenic activities by retaining expression of TNFR-1 and -2 and VEGF receptor 2 in endothelial cells REFERENCE 4 (residues 1 to 835) AUTHORS Damineni S, Balaji SA, Shettar A, Nayanala S, Kumar N, Kruthika BS, Subramanian K, Vijayakumar M, Mukherjee G, Gupta V and Kondaiah P. TITLE Expression of tripartite motif-containing protein 28 in primary breast carcinoma predicts metastasis and is involved in the stemness, chemoresistance, and tumor growth JOURNAL Tumour Biol. 39 (4), 1010428317695919 (2017) PUBMED 28381187 REMARK GeneRIF: a role for TRIM28 on EMT, drug resistance, and stemness in addition to the already reported protumorigenic actions in breast and other cancers. REFERENCE 5 (residues 1 to 835) AUTHORS Li X, Burton EM and Bhaduri-McIntosh S. TITLE Chloroquine triggers Epstein-Barr virus replication through phosphorylation of KAP1/TRIM28 in Burkitt lymphoma cells JOURNAL PLoS Pathog. 13 (3), e1006249 (2017) PUBMED 28249048 REMARK GeneRIF: These findings provide a unique context in which ataxia telangiectasia mutated proteins modify KAP1 to regulate persistence of a herpesvirus in humans Publication Status: Online-Only REFERENCE 6 (residues 1 to 835) AUTHORS Eng FC, Barsalou A, Akutsu N, Mercier I, Zechel C, Mader S and White JH. TITLE Different classes of coactivators recognize distinct but overlapping binding sites on the estrogen receptor ligand binding domain JOURNAL J. Biol. Chem. 273 (43), 28371-28377 (1998) PUBMED 9774463 REFERENCE 7 (residues 1 to 835) AUTHORS Chang CJ, Chen YL and Lee SC. TITLE Coactivator TIF1beta interacts with transcription factor C/EBPbeta and glucocorticoid receptor to induce alpha1-acid glycoprotein gene expression JOURNAL Mol. Cell. Biol. 18 (10), 5880-5887 (1998) PUBMED 9742105 REFERENCE 8 (residues 1 to 835) AUTHORS Kim SS, Chen YM, O'Leary E, Witzgall R, Vidal M and Bonventre JV. TITLE A novel member of the RING finger family, KRIP-1, associates with the KRAB-A transcriptional repressor domain of zinc finger proteins JOURNAL Proc. Natl. Acad. Sci. U.S.A. 93 (26), 15299-15304 (1996) PUBMED 8986806 REFERENCE 9 (residues 1 to 835) AUTHORS Moosmann P, Georgiev O, Le Douarin B, Bourquin JP and Schaffner W. TITLE Transcriptional repression by RING finger protein TIF1 beta that interacts with the KRAB repressor domain of KOX1 JOURNAL Nucleic Acids Res. 24 (24), 4859-4867 (1996) PUBMED 9016654 REFERENCE 10 (residues 1 to 835) AUTHORS Friedman JR, Fredericks WJ, Jensen DE, Speicher DW, Huang XP, Neilson EG and Rauscher FJ 3rd. TITLE KAP-1, a novel corepressor for the highly conserved KRAB repression domain JOURNAL Genes Dev. 10 (16), 2067-2078 (1996) PUBMED 8769649 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from BC004978.1. This sequence is a reference standard in the RefSeqGene project. Summary: The protein encoded by this gene mediates transcriptional control by interaction with the Kruppel-associated box repression domain found in many transcription factors. The protein localizes to the nucleus and is thought to associate with specific chromatin regions. The protein is a member of the tripartite motif family. This tripartite motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC004978.1, SRR1163658.177162.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## FEATURES Location/Qualifiers source 1..835 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="19" /map="19q13.43" Protein 1..835 /product="transcription intermediary factor 1-beta" /EC_number="2.3.2.27" /note="transcriptional intermediary factor 1-beta; nuclear corepressor KAP-1; KRIP-1; TIF1-beta; protein phosphatase 1, regulatory subunit 157; KRAB [Kruppel-associated box domain]-associated protein 1; RING finger protein 96; KRAB-interacting protein 1; E3 SUMO-protein ligase TRIM28; RING-type E3 ubiquitin transferase TIF1-beta" /calculated_mol_wt=88419 Site 2 /site_type="acetylation" /experiment="experimental evidence, no additional details recorded" /note="N-acetylalanine. {ECO:0000244|PubMed:19413330, ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:22223895, ECO:0000244|PubMed:22814378, ECO:0000269|Ref.5, ECO:0000269|Ref.6}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site 19 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine. {ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site 26 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine. {ECO:0000244|PubMed:23186163}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site 50 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine. {ECO:0000244|PubMed:18669648}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Region 62..124 /region_name="RING-HC_TIF1beta" /note="RING finger, HC subclass, found in transcription inknown asiary factor 1-beta (TIF1-beta); cd16765" /db_xref="CDD:319679" Region 65..376 /region_name="RBCC domain" /experiment="experimental evidence, no additional details recorded" /note="propagated from UniProtKB/Swiss-Prot (Q13263.5)" Region 65..120 /region_name="RING-HC finger (C3HC4-type)" /note="RING-HC finger (C3HC4-type) [structural motif]" /db_xref="CDD:319679" Site order(65,68,83,85,88,91,117,120) /site_type="other" /note="Zn binding site [ion binding]" /db_xref="CDD:319679" Site 138 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine. {ECO:0000244|PubMed:23186163}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Region 148..184 /region_name="BBOX" /note="B-Box-type zinc finger; smart00336" /db_xref="CDD:197662" Region 207..245 /region_name="BBOX" /note="B-Box-type zinc finger; zinc binding domain (CHC3H2); often present in combination with other motifs, like RING zinc finger, NHL motif, coiled-coil or RFP domain in functionally unrelated proteins, most likely mediating protein-protein interaction; cd00021" /db_xref="CDD:237988" Site order(209,212,232,237) /site_type="other" /note="Zn2+ binding site [ion binding]" /db_xref="CDD:237988" Region 246..376 /region_name="Leucine zipper alpha helical coiled-coil region" /experiment="experimental evidence, no additional details recorded" /note="propagated from UniProtKB/Swiss-Prot (Q13263.5)" Region 247..376 /region_name="Interaction with MAGEC2" /experiment="experimental evidence, no additional details recorded" /note="propagated from UniProtKB/Swiss-Prot (Q13263.5)" Region 252..378 /region_name="BBC" /note="B-Box C-terminal domain; smart00502" /db_xref="CDD:128778" Site 266 /site_type="acetylation" /experiment="experimental evidence, no additional details recorded" /note="N6-acetyllysine. {ECO:0000250|UniProtKB:Q62318}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site 304 /site_type="acetylation" /experiment="experimental evidence, no additional details recorded" /note="N6-acetyllysine, alternate. {ECO:0000244|PubMed:19608861}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site 340 /site_type="acetylation" /experiment="experimental evidence, no additional details recorded" /note="N6-acetyllysine. {ECO:0000244|PubMed:19608861}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Region 366..370 /region_name="Involved in binding PPP1CA" /experiment="experimental evidence, no additional details recorded" /note="propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site 377 /site_type="acetylation" /experiment="experimental evidence, no additional details recorded" /note="N6-acetyllysine, alternate. {ECO:0000244|PubMed:19608861}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site 417 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine. {ECO:0000244|PubMed:23186163}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site 437 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine. {ECO:0000250|UniProtKB:Q62318}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site 439 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine. {ECO:0000244|PubMed:18669648}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site 453 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine. {ECO:0000244|PubMed:23186163}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site 470 /site_type="modified" /experiment="experimental evidence, no additional details recorded" /note="Citrulline. {ECO:0000250}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site 471 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine. {ECO:0000244|PubMed:18669648}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site 472 /site_type="modified" /experiment="experimental evidence, no additional details recorded" /note="Citrulline. {ECO:0000250}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site 473 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine. {ECO:0000244|PubMed:16964243, ECO:0000244|PubMed:17081983, ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:23186163}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Region 476..513 /region_name="HP1 box" /experiment="experimental evidence, no additional details recorded" /note="propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site 479 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine. {ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:23186163}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Region 481..494 /region_name="PxVxL motif" /experiment="experimental evidence, no additional details recorded" /note="propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site 489 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine. {ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site 498 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphothreonine. {ECO:0000244|PubMed:23186163}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site 501 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine. {ECO:0000244|PubMed:17525332, ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Region <525 ..620="" b="" region_name="<b>BASP1"> /note="Brain acid soluble protein 1 (BASP1 protein); cl25756" /db_xref="CDD:330577" Site 541 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphothreonine. {ECO:0000244|PubMed:16964243, ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site 594 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine. {ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:24275569}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Region 627..669 /region_name="PHD_TIF1beta" /note="PHD finger found in transcription intermediary factor 1-beta (TIF1-beta); cd15623" /db_xref="CDD:277093" Site order(627,632..633,636..641,648,661..662) /site_type="other" /note="histone H3 binding site [polypeptide binding]" /db_xref="CDD:277093" Site order(628,631,640,643,648,651,666,669) /site_type="other" /note="Zn binding site [ion binding]" /db_xref="CDD:277093" Site 683 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine. {ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:24275569}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site 689 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine. {ECO:0000244|PubMed:24275569}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Region 696..802 /region_name="Bromo_tif1_like" /note="Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of the tripartite motif (TRIM) protein family, which is characterized by a particular domain architecture. It functions by recruiting coactivators and/or...; cd05502" /db_xref="CDD:99934" Site 697 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine. {ECO:0000244|PubMed:20068231}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site order(724,727,730,772,776,782) /site_type="other" /note="putative acetyllysine binding site [chemical binding]" /db_xref="CDD:99934" Site 752 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine. {ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site 755 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphotyrosine. {ECO:0000250|UniProtKB:Q62318}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site 757 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine. {ECO:0000244|PubMed:16964243, ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site 770 /site_type="acetylation" /experiment="experimental evidence, no additional details recorded" /note="N6-acetyllysine, alternate. {ECO:0000244|PubMed:19608861}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site 774 /site_type="acetylation" /experiment="experimental evidence, no additional details recorded" /note="N6-acetyllysine, alternate. {ECO:0000244|PubMed:19608861}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site 779 /site_type="acetylation" /experiment="experimental evidence, no additional details recorded" /note="N6-acetyllysine, alternate. {ECO:0000250|UniProtKB:Q62318}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site 784 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine. {ECO:0000244|PubMed:23186163}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" Site 824 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine, by ATM and ATR and dsDNA kinase. {ECO:0000269|PubMed:16862143, ECO:0000269|PubMed:17178852, ECO:0000269|PubMed:17942393, ECO:0000269|PubMed:20424263}; propagated from UniProtKB/Swiss-Prot (Q13263.5)" CDS 1..835 /gene="TRIM28" /gene_synonym="KAP1; PPP1R157; RNF96; TF1B; TIF1B" /coded_by="NM_005762.2:290..2797" /db_xref="CCDS:CCDS12985.1" /db_xref="GeneID:10155" /db_xref="HGNC:HGNC:16384" /db_xref="MIM:601742" ORIGIN 1 maasaaaasa aaasaasgsp gpgegsagge krstapsaaa sasasaaass pagggaeale 61 llehcgvcre rlrpereprl lpclhsacsa clgpaapaaa nssgdggaag dgtvvdcpvc 121 kqqcfskdiv enyfmrdsgs kaatdaqdan qcctscedna patsycvecs eplcetcvea 181 hqrvkytkdh tvrstgpaks rdgertvycn vhkheplvlf cescdtltcr dcqlnahkdh 241 qyqfledavr nqrkllaslv krlgdkhatl qkstkevrss irqvsdvqkr vqvdvkmail 301 qimkelnkrg rvlvndaqkv tegqqerler qhwtmtkiqk hqehilrfas walesdnnta 361 lllskkliyf qlhralkmiv dpvephgemk fqwdlnawtk saeafgkiva erpgtnstgp 421 apmapprapg plskqgsgss qpmevqegyg fgsgddpyss aephvsgvkr srsgegevsg 481 lmrkvprvsl erldldltad sqppvfkvfp gsttedynli viergaaaaa tgqpgtapag 541 tpgapplagm aivkeeetea aigapptate gpetkpvlma laegpgaegp rlaspsgsts 601 sglevvapeg tsapgggpgt lddsaticrv cqkpgdlvmc nqcefcfhld chlpalqdvp 661 geewscslch vlpdlkeedg slsldgadst gvvaklspan qrkcervlla lfchepcrpl 721 hqlatdstfs ldqpggtldl tlirarlqek lsppysspqe faqdvgrmfk qfnkltedka 781 dvqsiiglqr ffetrmneaf gdtkfsavlv epppmslpga glssqelsgg pgdgp //
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