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tisdag 22 maj 2018

VPS15 (Kr3q22.1) , PI3KR4

PI3P synteesi , VPS 15 ja VPS34 , mitä ne tekevät vakuolaaristen proteiinien lajitelujärjstlmään assosioituneina?

Vacuolar Protein Sorting Associated protein 15

VPS15 (Kr. 3q22.3), PIK3R4, Phosphoinositide-3-kinase regulatory subunit 4.
Also known as p150; VPS15
Expression Ubiquitous expression in thyroid (RPKM 9.2), testis (RPKM 8.7) and 25 other tissues See moreOrthologs mouse all

Preferred Names

phosphoinositide 3-kinase regulatory subunit 4
Names
PI3-kinase p150 subunit
PI3-kinase regulatory subunit 4
phosphatidylinositol 3-kinase-associated p150
phosphoinositide 3-kinase adaptor protein
phosphoinositide-3-kinase, regulatory subunit 4, p150
NP_055417.1

Peptidirakenne:

smart00320
Location:1327 → 1358
WD40; WD40 repeats
smart00220
Location:26 → 309
S_TKc; Serine/Threonine protein kinases, catalytic domain
COG2319
Location:991 → 1358
WD40; WD40 repeat [General function prediction only]
cd13980
Location:25 → 320
STKc_Vps15; Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein 15
pfam07539
Location:352 → 448
DRIM; Down-regulated in metastasis
sd00044
Location:539 → 566
HEAT; HEAT repeat [structural motif]
sd00039
Location:997 → 1040
7WD40; WD40 repeat [structural motif]
cl02567
Location:985 → 1269
WD40;... WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.

Related articles in PubMed

  1. Autophagy dysregulation in Danon disease. Nascimbeni AC, et al. Cell Death Dis, 2017 Jan 19. PMID 28102838, Free PMC Article
  2. Signal transduction pathways mediated by the interaction of CpG DNA with Toll-like receptor 9. Takeshita F, et al. Semin Immunol, 2004 Feb. PMID 14751759
See all (37) citations in PubMed
See citations in PubMed for homologs of this gene provided by HomoloGene

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

  1. hVps15, but not Ca2+/CaM, is required for the activity and regulation of hVps34 in mammalian cells

Rakenne ja historia

phosphoinositide 3-kinase regulatory subunit 4 [Homo sapiens]
(Kts.mys  Fytiiniblogista  rakenne)
NCBI Reference Sequence: NP_055417.1
Identical Proteins FASTA Graphics


LOCUS       NP_055417               1358 aa            linear   PRI 01-APR-2018
DEFINITION  phosphoinositide 3-kinase regulatory subunit 4 [Homo sapiens].
AC
ORIGIN      
        1 mgnqlagiap sqilsvesyf sdihdfeydk slgstrffkv arakhreglv vvkvfaiqdp
       61 tlpltsykqe leelkirlns aqnclpfqka sekasekaam lfrqyvrdnl ydristrpfl
      121 nniekrwiaf qiltavdqah ksgvrhgdik tenvmvtswn wvlltdfasf kptylpednp
      181 adfnyffdts rrrtcyiape rfvdggmfat eleymrdpst plvdlnsnqr trgelkramd
      241 ifsagcviae lftegvplfd lsqllayrng hffpeqvlnk iedhsirelv tqmihrepdk
      301 rleaedylkq qrgnafpeif ytflqpymaq faketflsad erilvirkdl gniihnlcgh
      361 dlpekaegep kenglvilvs vitsclqtlk ycdsklaale lilhlaprls veilldritp
      421 yllhfsndsv prvraealrt ltkvlalvke vprndiniyp eyilpgiahl aqddativrl
      481 ayaenialla etalrflelv qlknlnmend pnneeidevt hpngnydtel qalhemvqqk
      541 vvtllsdpen ivkqtlmeng itrlcvffgr qkandvllsh mitflndknd whlrgaffds
      601 ivgvaayvgw qsssilkpll qqglsdaeef vivkalyalt cmcqlgllqk phvyefasdi
      661 apflchpnlw irygavgfit vvarqistad vycklmpyld pyitqpiiqi erklvllsvl
      721 kepvsrsifd yalrskdits lfrhlhmrqk krngslpdcp ppedpaiaql lkkllsqgmt
      781 eeeedkllal kdfmmksnka kanivdqshl hdssqkgvid laalgitgrq vdlvktkqep
      841 ddkrarkhvk qdsnvneewk smfgsldppn mpqalpkgsd qeviqtgkpp rsessagicv
      901 plstssqvpe vttvqnkkpv ipvlsstilp styqirittc ktelqqliqq kreqcnaeri
      961 akqmmenaew eskppppgwr pkgllvahlh ehksavnrir vsdehslfat csndgtvkiw
     1021 nsqkmegktt ttrsiltysr iggrvktltf cqgshylaia sdngavqllg ieasklpksp
     1081 kihplqsril dqkedgcvvd mhhfnsgaqs vlayatvngs lvgwdlrsss nawtlkhdlk
     1141 sglitsfavd ihqcwlcigt ssgtmacwdm rfqlpisshc hpsrarirrl smhplyqswv
     1201 iaavqgnnev smwdmetgdr rftlwassap plselqpsph svhgiycspa dgnpilltag
     1261 sdmkirfwdl aypersyvva gstsspsvsy yrkiiegtev vqeiqnkqkv gpsddtprrg
     1321 peslpvghhd iitdvatfqt tqgfivtasr dgivkvwk
//

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