MB12B_HUMAN
ID MB12B_HUMAN Reviewed; 319 AA.
AC Q9H7P6; Q8N6S7;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Multivesicular body subunit 12B;
DE AltName: Full=ESCRT-I complex subunit MVB12B;
DE AltName: Full=Protein FAM125B;
GN Name=MVB12B; Synonyms=C9orf28, FAM125B;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 INTERACTION WITH TSG101; VPS28; VPS37B AND VPS37C, IDENTIFICATION IN THE
RP ESCRT-I COMPLEX, PHOSPHORYLATION AT SER-46; SER-101; THR-122; THR-204;
RP THR-205 AND SER-309, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18005716; DOI=10.1016/j.chom.2007.06.003;
RA Morita E., Sandrin V., Alam S.L., Eckert D.M., Gygi S.P., Sundquist W.I.;
RT "Identification of human MVB12 proteins as ESCRT-I subunits that function
RT in HIV budding.";
RL Cell Host Microbe 2:41-53(2007).
CC -!- FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular
CC trafficking process. Required for the sorting of endocytic
CC ubiquitinated cargos into multivesicular bodies.
CC -!- SUBUNIT: Component of the ESCRT-I complex (endosomal sorting complex
CC required for transport I) which consists of TSG101, VPS28, a VPS37
CC protein (VPS37A to -D) and MVB12A or MVB12B in a 1:1:1:1 stoichiometry.
CC Interacts with TSG101; the association appears to be mediated by the
CC TSG101-VPS37 binary subcomplex. Interacts with VPS28. Interacts with
CC VPS37B; the association appears to be mediated by the TSG101-VPS37
CC binary subcomplex. Interacts with VPS37C; the association appears to be
CC mediated by the TSG101-VPS37 binary subcomplex.
CC {ECO:0000269|PubMed:18005716}.
CC -!- INTERACTION:
CC Q9H7P6; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-6149062, EBI-739832;
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000305}. Late endosome membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H7P6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H7P6-2; Sequence=VSP_020364;
CC -!- SIMILARITY: Belongs to the MVB12 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15722.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK024432; BAB15722.1; ALT_INIT; mRNA.
DR EMBL; BC028675; AAH28675.1; -; mRNA.
DR CCDS; CCDS35142.1; -. [Q9H7P6-1]
DR CCDS; CCDS48022.1; -. [Q9H7P6-2]
DR RefSeq; NP_001011703.1; NM_001011703.2. [Q9H7P6-2]
DR RefSeq; NP_258257.1; NM_033446.2. [Q9H7P6-1]
DR PDB; 3TOW; X-ray; 1.34 A; A=47-192.
DR PDBsum; 3TOW; -.
DR AlphaFoldDB; Q9H7P6; -.
DR SMR; Q9H7P6; -.
DR BioGRID; 124621; 17.
DR ComplexPortal; CPX-7146; ESCRT-I complex, VPS37A-MVB12B variant. [Q9H7P6-1]
DR ComplexPortal; CPX-7164; ESCRT-I complex, VPS37B-MVB12B variant. [Q9H7P6-1]
DR ComplexPortal; CPX-7166; ESCRT-I complex, VPS37C-MVB12B variant. [Q9H7P6-1]
DR ComplexPortal; CPX-7167; ESCRT-I complex, VPS37D-MVB12B variant. [Q9H7P6-1]
DR IntAct; Q9H7P6; 9.
DR STRING; 9606.ENSP00000354772; -.
DR iPTMnet; Q9H7P6; -.
DR MetOSite; Q9H7P6; -.
DR PhosphoSitePlus; Q9H7P6; -.
DR BioMuta; MVB12B; -.
DR DMDM; 114149296; -.
DR EPD; Q9H7P6; -.
DR jPOST; Q9H7P6; -.
DR MassIVE; Q9H7P6; -.
DR MaxQB; Q9H7P6; -.
DR PaxDb; Q9H7P6; -.
DR PeptideAtlas; Q9H7P6; -.
DR PRIDE; Q9H7P6; -.
DR ProteomicsDB; 81133; -. [Q9H7P6-1]
DR ProteomicsDB; 81134; -. [Q9H7P6-2]
DR Antibodypedia; 56615; 23 antibodies from 11 providers.
DR DNASU; 89853; -.
DR Ensembl; ENST00000361171.8; ENSP00000354772.3; ENSG00000196814.15. [Q9H7P6-1]
DR Ensembl; ENST00000489637.3; ENSP00000485994.1; ENSG00000196814.15. [Q9H7P6-2]
DR GeneID; 89853; -.
DR KEGG; hsa:89853; -.
DR MANE-Select; ENST00000361171.8; ENSP00000354772.3; NM_033446.3; NP_258257.1.
DR UCSC; uc004bqh.3; human. [Q9H7P6-1]
DR CTD; 89853; -.
DR DisGeNET; 89853; -.
DR GeneCards; MVB12B; -.
DR HGNC; HGNC:23368; MVB12B.
DR HPA; ENSG00000196814; Tissue enhanced (brain).
DR neXtProt; NX_Q9H7P6; -.
DR OpenTargets; ENSG00000196814; -.
DR PharmGKB; PA162385827; -.
DR VEuPathDB; HostDB:ENSG00000196814; -.
DR eggNOG; KOG4000; Eukaryota.
DR GeneTree; ENSGT00940000155945; -.
DR HOGENOM; CLU_064823_1_0_1; -.
DR InParanoid; Q9H7P6; -.
DR OMA; ICFSKTE; -.
DR OrthoDB; 1021387at2759; -.
DR PhylomeDB; Q9H7P6; -.
DR TreeFam; TF314477; -.
DR PathwayCommons; Q9H7P6; -.
DR Reactome; R-HSA-162588; Budding and maturation of HIV virion.
DR Reactome; R-HSA-174490; Membrane binding and targetting of GAG proteins.
DR Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Reactome; R-HSA-9615710; Late endosomal microautophagy.
DR SignaLink; Q9H7P6; -.
DR BioGRID-ORCS; 89853; 10 hits in 1061 CRISPR screens.
DR ChiTaRS; MVB12B; human.
DR GenomeRNAi; 89853; -.
DR Pharos; Q9H7P6; Tbio.
DR PRO; PR:Q9H7P6; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9H7P6; protein.
DR Bgee; ENSG00000196814; Expressed in C1 segment of cervical spinal cord and 145 other tissues.
DR ExpressionAtlas; Q9H7P6; baseline and differential.
DR Genevisible; Q9H7P6; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0000813; C:ESCRT I complex; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IMP:UniProtKB.
DR GO; GO:0090148; P:membrane fission; IC:ComplexPortal.
DR GO; GO:0036258; P:multivesicular body assembly; IC:ComplexPortal.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IC:ComplexPortal.
DR GO; GO:0042058; P:regulation of epidermal growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IC:UniProtKB.
DR GO; GO:0046755; P:viral budding; IMP:UniProtKB.
DR GO; GO:0019075; P:virus maturation; IMP:UniProtKB.
DR InterPro; IPR023341; MABP.
DR InterPro; IPR018798; MVB12A/B.
DR InterPro; IPR040297; MVB12B.
DR InterPro; IPR023340; UMA.
DR PANTHER; PTHR31547; PTHR31547; 1.
DR Pfam; PF10240; DUF2464; 1.
DR PROSITE; PS51498; MABP; 1.
DR PROSITE; PS51497; UMA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Endosome; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..319
FT /note="Multivesicular body subunit 12B"
FT /id="PRO_0000249074"
FT DOMAIN 47..193
FT /note="MABP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00831"
FT DOMAIN 254..303
FT /note="UMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00830"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..27
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18005716"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18005716"
FT MOD_RES 122
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18005716"
FT MOD_RES 204
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18005716"
FT MOD_RES 205
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18005716"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6KAU4"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18005716"
FT VAR_SEQ 222..319
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020364"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:3TOW"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:3TOW"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:3TOW"
FT STRAND 109..118
FT /evidence="ECO:0007829|PDB:3TOW"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:3TOW"
FT STRAND 142..152
FT /evidence="ECO:0007829|PDB:3TOW"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:3TOW"
FT STRAND 159..167
FT /evidence="ECO:0007829|PDB:3TOW"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:3TOW"
FT STRAND 185..192
FT /evidence="ECO:0007829|PDB:3TOW"
SQ 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
