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Q96EY5

- MB12A_HUMAN

UniProt

Q96EY5 - MB12A_HUMAN

Protein

Multivesicular body subunit 12A

Gene

MVB12A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    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.1 Publication

    GO - Molecular functioni

    1. lipid binding Source: UniProt
    2. protein binding Source: UniProt
    3. ubiquitin binding Source: UniProt

    GO - Biological processi

    1. protein transport Source: UniProtKB-KW
    2. regulation of epidermal growth factor receptor signaling pathway Source: UniProt
    3. ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Source: UniProt

    Keywords - Biological processi

    Protein transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Multivesicular body subunit 12A
    Alternative name(s):
    CIN85/CD2AP family-binding protein
    ESCRT-I complex subunit MVB12A
    Protein FAM125A
    Gene namesi
    Name:MVB12A
    Synonyms:CFBP, FAM125A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:25153. MVB12A.

    Subcellular locationi

    Cytoplasm. Nucleus. Endosome. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Late endosome membrane Curated; Peripheral membrane protein Curated
    Note: Colocalizes with F-actin. Some fraction may be nuclear.

    GO - Cellular componenti

    1. aggresome Source: HPA
    2. cytoplasm Source: HPA
    3. cytosol Source: UniProt
    4. ESCRT I complex Source: UniProt
    5. extracellular vesicular exosome Source: UniProt
    6. intracellular membrane-bounded organelle Source: HPA
    7. late endosome membrane Source: UniProtKB-SubCell
    8. microtubule organizing center Source: UniProtKB-SubCell
    9. nucleus Source: HPA
    10. vesicle Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Endosome, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi204 – 2041Y → D: Mimics constitutively phosphorylated form and has the ability to interact with CD2AP and CIN85/SH3KBP1 without EGF treatment. 1 Publication
    Mutagenesisi204 – 2041Y → F: Abolishes interaction with CD2AP and CIN85/SH3KBP1. 1 Publication

    Organism-specific databases

    PharmGKBiPA162385826.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 273273Multivesicular body subunit 12APRO_0000249069Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei130 – 1301Phosphothreonine1 Publication
    Modified residuei163 – 1631Phosphoserine1 Publication
    Modified residuei170 – 1701Phosphoserine4 Publications
    Modified residuei202 – 2021Phosphoserine1 Publication
    Modified residuei204 – 2041Phosphotyrosine1 Publication
    Modified residuei207 – 2071Phosphoserine1 Publication
    Modified residuei232 – 2321Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated on Tyr-204 upon EGF stimulation. Phosphorylation is required for interaction with CD2AP and CIN85/SH3KBP1.5 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ96EY5.
    PaxDbiQ96EY5.
    PRIDEiQ96EY5.

    PTM databases

    PhosphoSiteiQ96EY5.

    Miscellaneous databases

    PMAP-CutDBQ96EY5.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed except in skeletal muscle.1 Publication

    Gene expression databases

    ArrayExpressiQ96EY5.
    BgeeiQ96EY5.
    CleanExiHS_FAM125A.
    GenevestigatoriQ96EY5.

    Organism-specific databases

    HPAiHPA041885.
    HPA042231.

    Interactioni

    Subunit structurei

    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 stoechiometry. 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 CEP55.3 Publications

    Protein-protein interaction databases

    BioGridi125018. 10 interactions.
    IntActiQ96EY5. 1 interaction.
    STRINGi9606.ENSP00000324810.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96EY5.
    SMRiQ96EY5. Positions 11-146.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini9 – 151143MABPPROSITE-ProRule annotationAdd
    BLAST
    Domaini215 – 26551UMAPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni192 – 27382Interaction with TSG101, VPS37B and VPS28Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi155 – 1606SH3-binding

    Sequence similaritiesi

    Belongs to the MVB12 family.Curated
    Contains 1 MABP domain.PROSITE-ProRule annotation
    Contains 1 UMA domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH3-binding

    Phylogenomic databases

    eggNOGiNOG301965.
    HOGENOMiHOG000231822.
    HOVERGENiHBG055538.
    InParanoidiQ96EY5.
    KOiK12186.
    OMAiIENEYNY.
    OrthoDBiEOG7K3TMB.
    PhylomeDBiQ96EY5.
    TreeFamiTF314477.

    Family and domain databases

    InterProiIPR018798. FAM125.
    IPR023341. MABP.
    IPR023340. UMA.
    [Graphical view]
    PfamiPF10240. DUF2464. 1 hit.
    [Graphical view]
    PROSITEiPS51498. MABP. 1 hit.
    PS51497. UMA. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96EY5-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDPVPGTDSA PLAGLAWSSA SAPPPRGFSA ISCTVEGAPA SFGKSFAQKS    50
    GYFLCLSSLG SLENPQENVV ADIQIVVDKS PLPLGFSPVC DPMDSKASVS 100
    KKKRMCVKLL PLGATDTAVF DVRLSGKTKT VPGYLRIGDM GGFAIWCKKA 150
    KAPRPVPKPR GLSRDMQGLS LDAASQPSKG GLLERTASRL GSRASTLRRN 200
    DSIYEASSLY GISAMDGVPF TLHPRFEGKS CSPLAFSAFG DLTIKSLADI 250
    EEEYNYGFVV EKTAAARLPP SVS 273
    Length:273
    Mass (Da):28,783
    Last modified:December 1, 2001 - v1
    Checksum:i7C765A0E96DC0F45
    GO
    Isoform 2 (identifier: Q96EY5-2) [UniParc]FASTAAdd to Basket

    Also known as: Delta 5

    The sequence of this isoform differs from the canonical sequence as follows:
         139-178: Missing.

    Note: Does not interact with CD2AP.

    Show »
    Length:233
    Mass (Da):24,532
    Checksum:iE5E04F5CFBC399C4
    GO
    Isoform 3 (identifier: Q96EY5-3) [UniParc]FASTAAdd to Basket

    Also known as: Delta 8

    The sequence of this isoform differs from the canonical sequence as follows:
         238-253: Missing.

    Show »
    Length:257
    Mass (Da):27,050
    Checksum:iCE551F6F2AA734C9
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti106 – 1061C → Y.
    Corresponds to variant rs34949802 [ dbSNP | Ensembl ].
    VAR_049018

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei139 – 17840Missing in isoform 2. CuratedVSP_020629Add
    BLAST
    Alternative sequencei238 – 25316Missing in isoform 3. CuratedVSP_020630Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC007883 mRNA. Translation: AAH07883.2.
    BC011840 mRNA. Translation: AAH11840.1.
    CCDSiCCDS12359.1. [Q96EY5-1]
    RefSeqiNP_612410.1. NM_138401.2. [Q96EY5-1]
    UniGeneiHs.515243.

    Genome annotation databases

    EnsembliENST00000317040; ENSP00000324810; ENSG00000141971. [Q96EY5-1]
    ENST00000543795; ENSP00000444653; ENSG00000141971. [Q96EY5-1]
    GeneIDi93343.
    KEGGihsa:93343.
    UCSCiuc002ngo.1. human. [Q96EY5-1]

    Polymorphism databases

    DMDMi74731632.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC007883 mRNA. Translation: AAH07883.2 .
    BC011840 mRNA. Translation: AAH11840.1 .
    CCDSi CCDS12359.1. [Q96EY5-1 ]
    RefSeqi NP_612410.1. NM_138401.2. [Q96EY5-1 ]
    UniGenei Hs.515243.

    3D structure databases

    ProteinModelPortali Q96EY5.
    SMRi Q96EY5. Positions 11-146.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125018. 10 interactions.
    IntActi Q96EY5. 1 interaction.
    STRINGi 9606.ENSP00000324810.

    PTM databases

    PhosphoSitei Q96EY5.

    Polymorphism databases

    DMDMi 74731632.

    Proteomic databases

    MaxQBi Q96EY5.
    PaxDbi Q96EY5.
    PRIDEi Q96EY5.

    Protocols and materials databases

    DNASUi 93343.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000317040 ; ENSP00000324810 ; ENSG00000141971 . [Q96EY5-1 ]
    ENST00000543795 ; ENSP00000444653 ; ENSG00000141971 . [Q96EY5-1 ]
    GeneIDi 93343.
    KEGGi hsa:93343.
    UCSCi uc002ngo.1. human. [Q96EY5-1 ]

    Organism-specific databases

    CTDi 93343.
    GeneCardsi GC19P017605.
    HGNCi HGNC:25153. MVB12A.
    HPAi HPA041885.
    HPA042231.
    neXtProti NX_Q96EY5.
    PharmGKBi PA162385826.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG301965.
    HOGENOMi HOG000231822.
    HOVERGENi HBG055538.
    InParanoidi Q96EY5.
    KOi K12186.
    OMAi IENEYNY.
    OrthoDBi EOG7K3TMB.
    PhylomeDBi Q96EY5.
    TreeFami TF314477.

    Miscellaneous databases

    ChiTaRSi FAM125A. human.
    GenomeRNAii 93343.
    NextBioi 78049.
    PMAP-CutDB Q96EY5.
    PROi Q96EY5.

    Gene expression databases

    ArrayExpressi Q96EY5.
    Bgeei Q96EY5.
    CleanExi HS_FAM125A.
    Genevestigatori Q96EY5.

    Family and domain databases

    InterProi IPR018798. FAM125.
    IPR023341. MABP.
    IPR023340. UMA.
    [Graphical view ]
    Pfami PF10240. DUF2464. 1 hit.
    [Graphical view ]
    PROSITEi PS51498. MABP. 1 hit.
    PS51497. UMA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Pancreas and Uterus.
    2. "CFBP is a novel tyrosine-phosphorylated protein that might function as a regulator of CIN85/CD2AP."
      Konishi H., Tashiro K., Murata Y., Nabeshi H., Yamauchi E., Taniguchi H.
      J. Biol. Chem. 281:28919-28931(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: 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, MUTAGENESIS OF TYR-204.
    3. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    4. "Identification of human MVB12 proteins as ESCRT-I subunits that function in HIV budding."
      Morita E., Sandrin V., Alam S.L., Eckert D.M., Gygi S.P., Sundquist W.I.
      Cell Host Microbe 2:41-53(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY.
    5. "Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis."
      Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P., Rodesch C.K., Sundquist W.I.
      EMBO J. 26:4215-4227(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CEP55.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      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.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170 AND SER-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMB12A_HUMAN
    AccessioniPrimary (citable) accession number: Q96EY5
    Secondary accession number(s): Q96I18
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2006
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 96 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3