ID   VP26B_HUMAN             Reviewed;         336 AA.
AC   Q4G0F5; Q96A55;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 2.
DT   27-MAR-2024, entry version 148.
DE   RecName: Full=Vacuolar protein sorting-associated protein 26B;
DE   AltName: Full=Vesicle protein sorting 26B;
GN   Name=VPS26B;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Kim N.-S., Shon H.-Y., Oh J.-H., Lee J.-Y., Kim J.-M., Hahn Y., Park H.-S.,
RA   Kim S., Kim Y.S.;
RL   Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye, Lung, and Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-319, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302 AND SER-304, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Acts as a component of the retromer cargo-selective complex
CC       (CSC). The CSC is believed to be the core functional component of
CC       retromer or respective retromer complex variants acting to prevent
CC       missorting of selected transmembrane cargo proteins into the lysosomal
CC       degradation pathway. The recruitment of the CSC to the endosomal
CC       membrane involves RAB7A and SNX3. The SNX-BAR retromer mediates
CC       retrograde transport of cargo proteins from endosomes to the trans-
CC       Golgi network (TGN) and is involved in endosome-to-plasma membrane
CC       transport for cargo protein recycling. The SNX3-retromer mediates the
CC       retrograde transport of WLS distinct from the SNX-BAR retromer pathway.
CC       The SNX27-retromer is believed to be involved in endosome-to-plasma
CC       membrane trafficking and recycling of a broad spectrum of cargo
CC       proteins. The CSC seems to act as recruitment hub for other proteins,
CC       such as the WASH complex and TBC1D5. May be involved in retrograde
CC       transport of SORT1 but not of IGF2R. Acts redundantly with VSP26A in
CC       SNX-27 mediated endocytic recycling of SLC2A1/GLUT1 (By similarity).
CC       {ECO:0000250|UniProtKB:O75436, ECO:0000250|UniProtKB:Q8C0E2}.
CC   -!- SUBUNIT: Component of the heterotrimeric retromer cargo-selective
CC       complex (CSC), also described as vacuolar protein sorting VPS
CC       subcomplex (VPS,) formed by VPS26 (VPS26A or VPS26B), VPS29 and VPS35.
CC       The CSC has a highly elongated structure with VPS26 and VPS29 binding
CC       independently at opposite distal ends of VPS35 as central platform. The
CC       CSC is believed to associate with variable sorting nexins to form
CC       functionally distinct retromer complex variants. The originally
CC       described retromer complex (also called SNX-BAR retromer) is a pentamer
CC       containing the CSC and a heterodimeric membrane-deforming subcomplex
CC       formed between SNX1 or SNX2 and SNX5 or SNX6 (also called SNX-BAR
CC       subcomplex); the respective CSC and SNX-BAR subcomplexes associate with
CC       low affinity. The CSC associates with SNX3 to form a SNX3-retromer
CC       complex. The CSC associates with SNX27, the WASH complex and the SNX-
CC       BAR subcomplex to form the SNX27-retromer complex. Interacts with
CC       VPS29, VPS35, TBC1D5, GOLPH3, SNX27 (By similarity).
CC       {ECO:0000250|UniProtKB:O75436, ECO:0000250|UniProtKB:Q8C0E2}.
CC   -!- INTERACTION:
CC       Q4G0F5; Q8TAT6: NPLOC4; NbExp=3; IntAct=EBI-6151831, EBI-1994109;
CC       Q4G0F5; Q96QK1: VPS35; NbExp=9; IntAct=EBI-6151831, EBI-1054634;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8C0E2}.
CC       Membrane; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8C0E2}.
CC       Early endosome {ECO:0000250|UniProtKB:Q8C0E2}. Late endosome
CC       {ECO:0000250|UniProtKB:Q8C0E2}. Note=Localizes to early and late
CC       endosomal structures (By similarity). {ECO:0000250|UniProtKB:Q8C0E2}.
CC   -!- SIMILARITY: Belongs to the VPS26 family. {ECO:0000305}.
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DR   EMBL; AF452718; AAP13353.1; -; mRNA.
DR   EMBL; BC009747; AAH09747.1; -; mRNA.
DR   EMBL; BC014128; AAH14128.1; -; mRNA.
DR   EMBL; BC098386; AAH98386.1; -; mRNA.
DR   CCDS; CCDS8495.1; -.
DR   RefSeq; NP_443107.1; NM_052875.4.
DR   AlphaFoldDB; Q4G0F5; -.
DR   SMR; Q4G0F5; -.
DR   BioGRID; 125215; 78.
DR   ComplexPortal; CPX-7843; Retromer complex, VPS26B variant.
DR   CORUM; Q4G0F5; -.
DR   IntAct; Q4G0F5; 46.
DR   MINT; Q4G0F5; -.
DR   STRING; 9606.ENSP00000281187; -.
DR   TCDB; 9.A.3.1.1; the sorting nexin27 (snx27)-retromer assembly apparatus (retromeraa) family.
DR   GlyGen; Q4G0F5; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q4G0F5; -.
DR   MetOSite; Q4G0F5; -.
DR   PhosphoSitePlus; Q4G0F5; -.
DR   SwissPalm; Q4G0F5; -.
DR   BioMuta; VPS26B; -.
DR   DMDM; 110816482; -.
DR   EPD; Q4G0F5; -.
DR   jPOST; Q4G0F5; -.
DR   MassIVE; Q4G0F5; -.
DR   MaxQB; Q4G0F5; -.
DR   PaxDb; 9606-ENSP00000281187; -.
DR   PeptideAtlas; Q4G0F5; -.
DR   ProteomicsDB; 62102; -.
DR   Pumba; Q4G0F5; -.
DR   Antibodypedia; 33166; 141 antibodies from 26 providers.
DR   DNASU; 112936; -.
DR   Ensembl; ENST00000281187.10; ENSP00000281187.5; ENSG00000151502.11.
DR   Ensembl; ENST00000525095.2; ENSP00000434162.2; ENSG00000151502.11.
DR   GeneID; 112936; -.
DR   KEGG; hsa:112936; -.
DR   MANE-Select; ENST00000281187.10; ENSP00000281187.5; NM_052875.5; NP_443107.1.
DR   UCSC; uc001qhe.4; human.
DR   AGR; HGNC:28119; -.
DR   CTD; 112936; -.
DR   DisGeNET; 112936; -.
DR   GeneCards; VPS26B; -.
DR   HGNC; HGNC:28119; VPS26B.
DR   HPA; ENSG00000151502; Low tissue specificity.
DR   MIM; 610027; gene.
DR   neXtProt; NX_Q4G0F5; -.
DR   OpenTargets; ENSG00000151502; -.
DR   PharmGKB; PA128394747; -.
DR   VEuPathDB; HostDB:ENSG00000151502; -.
DR   eggNOG; KOG3063; Eukaryota.
DR   GeneTree; ENSGT00950000183064; -.
DR   HOGENOM; CLU_031077_0_0_1; -.
DR   InParanoid; Q4G0F5; -.
DR   OMA; FKWKFSS; -.
DR   OrthoDB; 597400at2759; -.
DR   PhylomeDB; Q4G0F5; -.
DR   TreeFam; TF300907; -.
DR   PathwayCommons; Q4G0F5; -.
DR   SignaLink; Q4G0F5; -.
DR   BioGRID-ORCS; 112936; 11 hits in 1155 CRISPR screens.
DR   ChiTaRS; VPS26B; human.
DR   GeneWiki; VPS26B; -.
DR   GenomeRNAi; 112936; -.
DR   Pharos; Q4G0F5; Tdark.
DR   PRO; PR:Q4G0F5; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q4G0F5; Protein.
DR   Bgee; ENSG00000151502; Expressed in cortical plate and 177 other cell types or tissues.
DR   ExpressionAtlas; Q4G0F5; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR   GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
DR   GO; GO:0030904; C:retromer complex; ISS:UniProtKB.
DR   GO; GO:0030906; C:retromer, cargo-selective complex; NAS:ParkinsonsUK-UCL.
DR   GO; GO:0071346; P:cellular response to type II interferon; IEA:Ensembl.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0016241; P:regulation of macroautophagy; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR   Gene3D; 2.60.40.640; -; 2.
DR   InterPro; IPR014752; Arrestin-like_C.
DR   InterPro; IPR028934; Vps26-related.
DR   PANTHER; PTHR12233; VACUOLAR PROTEIN SORTING 26 RELATED; 1.
DR   PANTHER; PTHR12233:SF5; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 26B; 1.
DR   Pfam; PF03643; Vps26; 1.
DR   Genevisible; Q4G0F5; HS.
PE   1: Evidence at protein level;
KW   Cytoplasm; Endosome; Membrane; Phosphoprotein; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..336
FT                   /note="Vacuolar protein sorting-associated protein 26B"
FT                   /id="PRO_0000247089"
FT   MOD_RES         302
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         304
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         319
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   CONFLICT        55
FT                   /note="K -> R (in Ref. 2; AAH98386)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   336 AA;  39155 MW;  1C07D0ABA7797A12 CRC64;
     MSFFGFGQSV EVEILLNDAE SRKRAEHKTE DGKKEKYFLF YDGETVSGKV SLALKNPNKR
     LEHQGIKIEF IGQIELYYDR GNHHEFVSLV KDLARPGEIT QSQAFDFEFT HVEKPYESYT
     GQNVKLRYFL RATISRRLND VVKEMDIVVH TLSTYPELNS SIKMEVGIED CLHIEFEYNK
     SKYHLKDVIV GKIYFLLVRI KIKHMEIDII KRETTGTGPN VYHENDTIAK YEIMDGAPVR
     GESIPIRLFL AGYELTPTMR DINKKFSVRY YLNLVLIDEE ERRYFKQQEV VLWRKGDIVR
     KSMSHQAAIA SQRFEGTTSL GEVRTPSQLS DNNCRQ
//