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Multivesicular body subunit 12A (CIN85/CD2AP family-binding protein) (ESCRT-I complex subunit MVB12A) (Protein FAM125A)

 MB12A_HUMAN             Reviewed;         273 AA.
Q96EY5; Q96I18;
05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
27-SEP-2017, entry version 127.
RecName: Full=Multivesicular body subunit 12A;
AltName: Full=CIN85/CD2AP family-binding protein;
AltName: Full=ESCRT-I complex subunit MVB12A;
AltName: Full=Protein FAM125A;
Name=MVB12A; Synonyms=CFBP, FAM125A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Pancreas, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[2]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, ALTERNATIVE SPLICING
(ISOFORMS 1; 2 AND 3), SUBCELLULAR LOCATION, PHOSPHORYLATION AT
TYR-204, TISSUE SPECIFICITY, INTERACTION WITH CD2AP AND SH3KBP1, AND
MUTAGENESIS OF TYR-204.
PubMed=16895919; DOI=10.1074/jbc.M605693200;
Konishi H., Tashiro K., Murata Y., Nabeshi H., Yamauchi E.,
Taniguchi H.;
"CFBP is a novel tyrosine-phosphorylated protein that might function
as a regulator of CIN85/CD2AP.";
J. Biol. Chem. 281:28919-28931(2006).
[3]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[4]
INTERACTION WITH TSG101; VPS28; VPS37B; VPS37C AND VPS37D,
IDENTIFICATION IN THE ESCRT-I COMPLEX, RECONSTITUTION OF THE ESCRT-I
COMPLEX, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-130; SER-163;
SER-170; SER-207 AND SER-232, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18005716; DOI=10.1016/j.chom.2007.06.003;
Morita E., Sandrin V., Alam S.L., Eckert D.M., Gygi S.P.,
Sundquist W.I.;
"Identification of human MVB12 proteins as ESCRT-I subunits that
function in HIV budding.";
Cell Host Microbe 2:41-53(2007).
[5]
INTERACTION WITH CEP55.
PubMed=17853893; DOI=10.1038/sj.emboj.7601850;
Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P.,
Rodesch C.K., Sundquist W.I.;
"Human ESCRT and ALIX proteins interact with proteins of the midbody
and function in cytokinesis.";
EMBO J. 26:4215-4227(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170 AND SER-202, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170; SER-195 AND
SER-202, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Component of the ESCRT-I complex, a regulator of
vesicular trafficking process. Required for the sorting of
endocytic ubiquitinated cargos into multivesicular bodies. May be
involved in the ligand-mediated internalization and down-
regulation of EGF receptor. {ECO:0000269|PubMed:16895919}.
-!- SUBUNIT: Component of the ESCRT-I complex (endosomal sorting
complex required for transport I) which consists of TSG101, VPS28,
a VPS37 protein (VPS37A to -D) and MVB12A or MVB12B in a 1:1:1:1
stoichiometry. Interacts with CD2AP and CIN85/SH3KBP1. Interacts
with CD2AP (via one of the SH3 domains). Interacts with TSG101;
the association appears to be mediated by the TSG101-VPS37 binary
subcomplex. Interacts with VPS28. Interacts with VPS37B; the
association appears to be mediated by the TSG101-VPS37 binary
subcomplex. Interacts with VPS37C; the association appears to be
mediated by the TSG101-VPS37 binary subcomplex. Interacts with
VPS37D; the association appears to be mediated by the TSG101-VPS37
binary subcomplex. Interacts with CEP55.
{ECO:0000269|PubMed:16895919, ECO:0000269|PubMed:17853893,
ECO:0000269|PubMed:18005716}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Endosome. Cytoplasm,
cytoskeleton, microtubule organizing center, centrosome. Late
endosome membrane {ECO:0000305}; Peripheral membrane protein
{ECO:0000305}. Note=Colocalizes with F-actin. Some fraction may be
nuclear.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q96EY5-1; Sequence=Displayed;
Name=2; Synonyms=Delta 5;
IsoId=Q96EY5-2; Sequence=VSP_020629;
Note=Does not interact with CD2AP.;
Name=3; Synonyms=Delta 8;
IsoId=Q96EY5-3; Sequence=VSP_020630;
-!- TISSUE SPECIFICITY: Ubiquitously expressed except in skeletal
muscle. {ECO:0000269|PubMed:16895919}.
-!- PTM: Phosphorylated on Tyr-204 upon EGF stimulation.
Phosphorylation is required for interaction with CD2AP and
CIN85/SH3KBP1. {ECO:0000269|PubMed:16895919,
ECO:0000269|PubMed:18005716}.
-!- SIMILARITY: Belongs to the MVB12 family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; BC007883; AAH07883.2; -; mRNA.
EMBL; BC011840; AAH11840.1; -; mRNA.
CCDS; CCDS12359.1; -. [Q96EY5-1]
RefSeq; NP_612410.1; NM_138401.3. [Q96EY5-1]
UniGene; Hs.515243; -.
ProteinModelPortal; Q96EY5; -.
SMR; Q96EY5; -.
BioGrid; 125018; 30.
IntAct; Q96EY5; 11.
STRING; 9606.ENSP00000324810; -.
iPTMnet; Q96EY5; -.
PhosphoSitePlus; Q96EY5; -.
BioMuta; MVB12A; -.
DMDM; 74731632; -.
EPD; Q96EY5; -.
MaxQB; Q96EY5; -.
PaxDb; Q96EY5; -.
PeptideAtlas; Q96EY5; -.
PRIDE; Q96EY5; -.
DNASU; 93343; -.
Ensembl; ENST00000317040; ENSP00000324810; ENSG00000141971. [Q96EY5-1]
Ensembl; ENST00000543795; ENSP00000444653; ENSG00000141971. [Q96EY5-1]
GeneID; 93343; -.
KEGG; hsa:93343; -.
UCSC; uc002ngo.2; human. [Q96EY5-1]
CTD; 93343; -.
EuPathDB; HostDB:ENSG00000141971.12; -.
GeneCards; MVB12A; -.
HGNC; HGNC:25153; MVB12A.
HPA; HPA041885; -.
HPA; HPA042231; -.
neXtProt; NX_Q96EY5; -.
OpenTargets; ENSG00000141971; -.
PharmGKB; PA162385826; -.
eggNOG; KOG4000; Eukaryota.
eggNOG; ENOG4110KHY; LUCA.
GeneTree; ENSGT00530000063575; -.
HOGENOM; HOG000231822; -.
HOVERGEN; HBG055538; -.
InParanoid; Q96EY5; -.
KO; K12186; -.
OMA; FEGKSCG; -.
OrthoDB; EOG091G0ELJ; -.
PhylomeDB; Q96EY5; -.
TreeFam; TF314477; -.
Reactome; R-HSA-162588; Budding and maturation of HIV virion.
Reactome; R-HSA-174490; Membrane binding and targetting of GAG proteins.
Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
GenomeRNAi; 93343; -.
PMAP-CutDB; Q96EY5; -.
PRO; PR:Q96EY5; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000141971; -.
CleanEx; HS_FAM125A; -.
ExpressionAtlas; Q96EY5; baseline and differential.
Genevisible; Q96EY5; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0000813; C:ESCRT I complex; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0043657; C:host cell; IEA:GOC.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0031982; C:vesicle; IDA:UniProtKB.
GO; GO:0008289; F:lipid binding; IMP:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0043130; F:ubiquitin binding; IMP:UniProtKB.
GO; GO:0016197; P:endosomal transport; TAS:Reactome.
GO; GO:0075733; P:intracellular transport of virus; TAS:Reactome.
GO; GO:0016236; P:macroautophagy; TAS:ParkinsonsUK-UCL.
GO; GO:0036258; P:multivesicular body assembly; TAS:ParkinsonsUK-UCL.
GO; GO:0048524; P:positive regulation of viral process; IMP:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0042058; P:regulation of epidermal growth factor receptor signaling pathway; IMP:UniProtKB.
GO; GO:1903772; P:regulation of viral budding via host ESCRT complex; IMP:UniProtKB.
GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IC:UniProtKB.
GO; GO:0039702; P:viral budding via host ESCRT complex; TAS:ParkinsonsUK-UCL.
GO; GO:0019058; P:viral life cycle; TAS:Reactome.
GO; GO:0019075; P:virus maturation; IMP:UniProtKB.
InterPro; IPR023341; MABP.
InterPro; IPR018798; MVB12A/B.
InterPro; IPR023340; UMA.
Pfam; PF10240; DUF2464; 1.
PROSITE; PS51498; MABP; 1.
PROSITE; PS51497; UMA; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton;
Endosome; Membrane; Nucleus; Phosphoprotein; Polymorphism;
Protein transport; Reference proteome; SH3-binding; Transport.
CHAIN 1 273 Multivesicular body subunit 12A.
/FTId=PRO_0000249069.
DOMAIN 9 151 MABP. {ECO:0000255|PROSITE-
ProRule:PRU00831}.
DOMAIN 215 265 UMA. {ECO:0000255|PROSITE-
ProRule:PRU00830}.
REGION 192 273 Interaction with TSG101, VPS37B and
VPS28. {ECO:0000269|PubMed:18005716}.
MOTIF 155 160 SH3-binding.
MOD_RES 130 130 Phosphothreonine.
{ECO:0000269|PubMed:18005716}.
MOD_RES 163 163 Phosphoserine.
{ECO:0000269|PubMed:18005716}.
MOD_RES 170 170 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:18005716}.
MOD_RES 195 195 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 202 202 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 204 204 Phosphotyrosine.
{ECO:0000269|PubMed:16895919}.
MOD_RES 207 207 Phosphoserine.
{ECO:0000269|PubMed:18005716}.
MOD_RES 232 232 Phosphoserine.
{ECO:0000269|PubMed:18005716}.
VAR_SEQ 139 178 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_020629.
VAR_SEQ 238 253 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_020630.
VARIANT 106 106 C -> Y (in dbSNP:rs34949802).
/FTId=VAR_049018.
MUTAGEN 204 204 Y->D: Mimics constitutively
phosphorylated form and has the ability
to interact with CD2AP and CIN85/SH3KBP1
without EGF treatment.
{ECO:0000269|PubMed:16895919}.
MUTAGEN 204 204 Y->F: Abolishes interaction with CD2AP
and CIN85/SH3KBP1.
{ECO:0000269|PubMed:16895919}.
SEQUENCE 273 AA; 28783 MW; 7C765A0E96DC0F45 CRC64;
MDPVPGTDSA PLAGLAWSSA SAPPPRGFSA ISCTVEGAPA SFGKSFAQKS GYFLCLSSLG
SLENPQENVV ADIQIVVDKS PLPLGFSPVC DPMDSKASVS KKKRMCVKLL PLGATDTAVF
DVRLSGKTKT VPGYLRIGDM GGFAIWCKKA KAPRPVPKPR GLSRDMQGLS LDAASQPSKG
GLLERTASRL GSRASTLRRN DSIYEASSLY GISAMDGVPF TLHPRFEGKS CSPLAFSAFG
DLTIKSLADI EEEYNYGFVV EKTAAARLPP SVS


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