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Multivesicular body subunit 12B (ESCRT-I complex subunit MVB12B) (Protein FAM125B)

 MB12B_HUMAN             Reviewed;         319 AA.
Q9H7P6; Q8N6S7;
05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
05-SEP-2006, sequence version 2.
27-SEP-2017, entry version 112.
RecName: Full=Multivesicular body subunit 12B;
AltName: Full=ESCRT-I complex subunit MVB12B;
AltName: Full=Protein FAM125B;
Name=MVB12B; Synonyms=C9orf28, FAM125B;
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=Spleen;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
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).
[3]
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, 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).
-!- FUNCTION: Component of the ESCRT-I complex, a regulator of
vesicular trafficking process. Required for the sorting of
endocytic ubiquitinated cargos into multivesicular bodies.
-!- 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 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. {ECO:0000269|PubMed:18005716}.
-!- INTERACTION:
Q8TBB1:LNX1; NbExp=3; IntAct=EBI-6149062, EBI-739832;
-!- SUBCELLULAR LOCATION: Endosome {ECO:0000305}. Late endosome
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9H7P6-1; Sequence=Displayed;
Name=2;
IsoId=Q9H7P6-2; Sequence=VSP_020364;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the MVB12 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB15722.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK024432; BAB15722.1; ALT_INIT; mRNA.
EMBL; BC028675; AAH28675.1; -; mRNA.
CCDS; CCDS35142.1; -. [Q9H7P6-1]
CCDS; CCDS48022.1; -. [Q9H7P6-2]
RefSeq; NP_001011703.1; NM_001011703.2. [Q9H7P6-2]
RefSeq; NP_258257.1; NM_033446.2. [Q9H7P6-1]
UniGene; Hs.162659; -.
PDB; 3TOW; X-ray; 1.34 A; A=47-192.
PDBsum; 3TOW; -.
ProteinModelPortal; Q9H7P6; -.
SMR; Q9H7P6; -.
BioGrid; 124621; 11.
IntAct; Q9H7P6; 2.
STRING; 9606.ENSP00000354772; -.
iPTMnet; Q9H7P6; -.
PhosphoSitePlus; Q9H7P6; -.
BioMuta; MVB12B; -.
DMDM; 114149296; -.
EPD; Q9H7P6; -.
MaxQB; Q9H7P6; -.
PaxDb; Q9H7P6; -.
PeptideAtlas; Q9H7P6; -.
PRIDE; Q9H7P6; -.
DNASU; 89853; -.
Ensembl; ENST00000361171; ENSP00000354772; ENSG00000196814. [Q9H7P6-1]
Ensembl; ENST00000489637; ENSP00000485994; ENSG00000196814. [Q9H7P6-2]
GeneID; 89853; -.
KEGG; hsa:89853; -.
UCSC; uc004bqh.3; human. [Q9H7P6-1]
CTD; 89853; -.
DisGeNET; 89853; -.
EuPathDB; HostDB:ENSG00000196814.14; -.
GeneCards; MVB12B; -.
HGNC; HGNC:23368; MVB12B.
HPA; HPA043683; -.
HPA; HPA049383; -.
neXtProt; NX_Q9H7P6; -.
OpenTargets; ENSG00000196814; -.
PharmGKB; PA162385827; -.
eggNOG; KOG4000; Eukaryota.
eggNOG; ENOG4110KHY; LUCA.
GeneTree; ENSGT00530000063575; -.
HOGENOM; HOG000231822; -.
HOVERGEN; HBG105828; -.
InParanoid; Q9H7P6; -.
KO; K12186; -.
OMA; KRRLCIK; -.
OrthoDB; EOG091G0ELJ; -.
PhylomeDB; Q9H7P6; -.
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; 89853; -.
PRO; PR:Q9H7P6; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000196814; -.
CleanEx; HS_FAM125B; -.
ExpressionAtlas; Q9H7P6; baseline and differential.
Genevisible; Q9H7P6; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005769; C:early endosome; 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:0043657; C:host cell; IEA:GOC.
GO; GO:0005770; C:late endosome; IDA:UniProtKB.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0031982; C:vesicle; IDA:UniProtKB.
GO; GO:0008289; F:lipid binding; IMP:UniProtKB.
GO; GO:0016197; P:endosomal transport; TAS:Reactome.
GO; GO:0075733; P:intracellular transport of virus; TAS:Reactome.
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:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IC:UniProtKB.
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;
3D-structure; Alternative splicing; Complete proteome; Endosome;
Membrane; Phosphoprotein; Protein transport; Reference proteome;
Transport.
CHAIN 1 319 Multivesicular body subunit 12B.
/FTId=PRO_0000249074.
DOMAIN 47 193 MABP. {ECO:0000255|PROSITE-
ProRule:PRU00831}.
DOMAIN 254 303 UMA. {ECO:0000255|PROSITE-
ProRule:PRU00830}.
MOD_RES 46 46 Phosphoserine.
{ECO:0000269|PubMed:18005716}.
MOD_RES 101 101 Phosphoserine.
{ECO:0000269|PubMed:18005716}.
MOD_RES 122 122 Phosphothreonine.
{ECO:0000269|PubMed:18005716}.
MOD_RES 204 204 Phosphothreonine.
{ECO:0000269|PubMed:18005716}.
MOD_RES 205 205 Phosphothreonine.
{ECO:0000269|PubMed:18005716}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000250|UniProtKB:Q6KAU4}.
MOD_RES 309 309 Phosphoserine.
{ECO:0000269|PubMed:18005716}.
VAR_SEQ 222 319 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_020364.
STRAND 52 58 {ECO:0000244|PDB:3TOW}.
STRAND 93 97 {ECO:0000244|PDB:3TOW}.
HELIX 105 107 {ECO:0000244|PDB:3TOW}.
STRAND 109 118 {ECO:0000244|PDB:3TOW}.
TURN 134 136 {ECO:0000244|PDB:3TOW}.
STRAND 142 152 {ECO:0000244|PDB:3TOW}.
HELIX 153 155 {ECO:0000244|PDB:3TOW}.
STRAND 159 167 {ECO:0000244|PDB:3TOW}.
STRAND 176 182 {ECO:0000244|PDB:3TOW}.
STRAND 185 192 {ECO:0000244|PDB:3TOW}.
SEQUENCE 319 AA; 35620 MW; 246E851D0C85D871 CRC64;
MRSCFCVRRS RDPPPPQPPP PPPQRGTDQS TMPEVKDLSE ALPETSMDPI TGVGVVASRN
RAPTGYDVVA QTADGVDADL WKDGLFKSKV TRYLCFTRSF SKENSHLGNV LVDMKLIDIK
DTLPVGFIPI QETVDTQEVA FRKKRLCIKF IPRDSTEAAI CDIRIMGRTK QAPPQYTFIG
ELNSMGIWYR MGRVPRNHDS SQPTTPSQSS AASTPAPNLP RHISLTLPAT FRGRNSTRTD
YEYQHSNLYA ISAMDGVPFM ISEKFSCVPE SMQPFDLLGI TIKSLAEIEK EYEYSFRTEQ
SAAARLPPSP TRCQQIPQS


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