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Protein

Multivesicular body subunit 12B

Gene

MVB12B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies.

GO - Molecular functioni

  • lipid binding Source: UniProtKB

GO - Biological processi

  • positive regulation of viral process Source: UniProtKB
  • protein transport Source: UniProtKB-KW
  • regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
  • ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Source: UniProtKB
  • virus maturation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Multivesicular body subunit 12B
Alternative name(s):
ESCRT-I complex subunit MVB12B
Protein FAM125B
Gene namesi
Name:MVB12B
Synonyms:C9orf28, FAM125B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:23368. MVB12B.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • early endosome Source: UniProtKB
  • ESCRT I complex Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • late endosome Source: UniProtKB
  • late endosome membrane Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162385827.

Polymorphism and mutation databases

BioMutaiMVB12B.
DMDMi114149296.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 319319Multivesicular body subunit 12BPRO_0000249074Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 461Phosphoserine1 Publication
Modified residuei101 – 1011Phosphoserine1 Publication
Modified residuei122 – 1221Phosphothreonine1 Publication
Modified residuei204 – 2041Phosphothreonine1 Publication
Modified residuei205 – 2051Phosphothreonine1 Publication
Modified residuei224 – 2241PhosphoserineBy similarity
Modified residuei309 – 3091Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9H7P6.
MaxQBiQ9H7P6.
PaxDbiQ9H7P6.
PRIDEiQ9H7P6.

PTM databases

iPTMnetiQ9H7P6.
PhosphoSiteiQ9H7P6.

Expressioni

Gene expression databases

BgeeiQ9H7P6.
CleanExiHS_FAM125B.
ExpressionAtlasiQ9H7P6. baseline and differential.
GenevisibleiQ9H7P6. HS.

Organism-specific databases

HPAiHPA043683.

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 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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
LNX1Q8TBB13EBI-6149062,EBI-739832

Protein-protein interaction databases

BioGridi124621. 11 interactions.
IntActiQ9H7P6. 2 interactions.
STRINGi9606.ENSP00000354772.

Structurei

Secondary structure

1
319
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi52 – 587Combined sources
Beta strandi93 – 975Combined sources
Helixi105 – 1073Combined sources
Beta strandi109 – 11810Combined sources
Turni134 – 1363Combined sources
Beta strandi142 – 15211Combined sources
Helixi153 – 1553Combined sources
Beta strandi159 – 1679Combined sources
Beta strandi176 – 1827Combined sources
Beta strandi185 – 1928Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TOWX-ray1.34A47-192[»]
ProteinModelPortaliQ9H7P6.
SMRiQ9H7P6. Positions 47-192.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 193147MABPPROSITE-ProRule annotationAdd
BLAST
Domaini254 – 30350UMAPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG4000. Eukaryota.
ENOG4110KHY. LUCA.
GeneTreeiENSGT00530000063575.
HOGENOMiHOG000231822.
HOVERGENiHBG105828.
InParanoidiQ9H7P6.
KOiK12186.
OMAiFACAPEG.
OrthoDBiEOG7K3TMB.
PhylomeDBiQ9H7P6.
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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H7P6-1) [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

        10         20         30         40         50
MRSCFCVRRS RDPPPPQPPP PPPQRGTDQS TMPEVKDLSE ALPETSMDPI
60 70 80 90 100
TGVGVVASRN RAPTGYDVVA QTADGVDADL WKDGLFKSKV TRYLCFTRSF
110 120 130 140 150
SKENSHLGNV LVDMKLIDIK DTLPVGFIPI QETVDTQEVA FRKKRLCIKF
160 170 180 190 200
IPRDSTEAAI CDIRIMGRTK QAPPQYTFIG ELNSMGIWYR MGRVPRNHDS
210 220 230 240 250
SQPTTPSQSS AASTPAPNLP RHISLTLPAT FRGRNSTRTD YEYQHSNLYA
260 270 280 290 300
ISAMDGVPFM ISEKFSCVPE SMQPFDLLGI TIKSLAEIEK EYEYSFRTEQ
310
SAAARLPPSP TRCQQIPQS
Length:319
Mass (Da):35,620
Last modified:September 5, 2006 - v2
Checksum:i246E851D0C85D871
GO
Isoform 2 (identifier: Q9H7P6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     222-319: Missing.

Note: No experimental confirmation available.
Show »
Length:221
Mass (Da):24,516
Checksum:i1B27BE5FE0B26B3C
GO

Sequence cautioni

The sequence BAB15722.1 differs from that shown. Reason: Erroneous initiation. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei222 – 31998Missing in isoform 2. 1 PublicationVSP_020364Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK024432 mRNA. Translation: BAB15722.1. Different initiation.
BC028675 mRNA. Translation: AAH28675.1.
CCDSiCCDS35142.1. [Q9H7P6-1]
CCDS48022.1. [Q9H7P6-2]
RefSeqiNP_001011703.1. NM_001011703.2. [Q9H7P6-2]
NP_258257.1. NM_033446.2. [Q9H7P6-1]
UniGeneiHs.162659.

Genome annotation databases

EnsembliENST00000361171; ENSP00000354772; ENSG00000196814. [Q9H7P6-1]
ENST00000489637; ENSP00000485994; ENSG00000196814. [Q9H7P6-2]
GeneIDi89853.
KEGGihsa:89853.
UCSCiuc004bqh.3. human. [Q9H7P6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK024432 mRNA. Translation: BAB15722.1. Different initiation.
BC028675 mRNA. Translation: AAH28675.1.
CCDSiCCDS35142.1. [Q9H7P6-1]
CCDS48022.1. [Q9H7P6-2]
RefSeqiNP_001011703.1. NM_001011703.2. [Q9H7P6-2]
NP_258257.1. NM_033446.2. [Q9H7P6-1]
UniGeneiHs.162659.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TOWX-ray1.34A47-192[»]
ProteinModelPortaliQ9H7P6.
SMRiQ9H7P6. Positions 47-192.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124621. 11 interactions.
IntActiQ9H7P6. 2 interactions.
STRINGi9606.ENSP00000354772.

PTM databases

iPTMnetiQ9H7P6.
PhosphoSiteiQ9H7P6.

Polymorphism and mutation databases

BioMutaiMVB12B.
DMDMi114149296.

Proteomic databases

EPDiQ9H7P6.
MaxQBiQ9H7P6.
PaxDbiQ9H7P6.
PRIDEiQ9H7P6.

Protocols and materials databases

DNASUi89853.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361171; ENSP00000354772; ENSG00000196814. [Q9H7P6-1]
ENST00000489637; ENSP00000485994; ENSG00000196814. [Q9H7P6-2]
GeneIDi89853.
KEGGihsa:89853.
UCSCiuc004bqh.3. human. [Q9H7P6-1]

Organism-specific databases

CTDi89853.
GeneCardsiMVB12B.
HGNCiHGNC:23368. MVB12B.
HPAiHPA043683.
neXtProtiNX_Q9H7P6.
PharmGKBiPA162385827.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4000. Eukaryota.
ENOG4110KHY. LUCA.
GeneTreeiENSGT00530000063575.
HOGENOMiHOG000231822.
HOVERGENiHBG105828.
InParanoidiQ9H7P6.
KOiK12186.
OMAiFACAPEG.
OrthoDBiEOG7K3TMB.
PhylomeDBiQ9H7P6.
TreeFamiTF314477.

Miscellaneous databases

GenomeRNAii89853.
NextBioi76346.
PROiQ9H7P6.

Gene expression databases

BgeeiQ9H7P6.
CleanExiHS_FAM125B.
ExpressionAtlasiQ9H7P6. baseline and differential.
GenevisibleiQ9H7P6. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Spleen.
  2. "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 2).
    Tissue: Brain.
  3. "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 AND VPS37C, IDENTIFICATION IN THE ESCRT-I COMPLEX, PHOSPHORYLATION AT SER-46; SER-101; THR-122; THR-204; THR-205 AND SER-309, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiMB12B_HUMAN
AccessioniPrimary (citable) accession number: Q9H7P6
Secondary accession number(s): Q8N6S7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 5, 2006
Last modified: March 16, 2016
This is version 101 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.