| Tag | Content |
|---|
| CPLM ID | CPLM-013668 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Melanoma inhibitory activity protein 3 |
Protein Synonyms/Alias | C219-reactive peptide; D320; Transport and Golgi organization protein 1 |
Gene Name | MIA3 |
Gene Synonyms/Alias | KIAA0268; TANGO; TANGO1; UNQ6077/PRO20088 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 1477 | DLKLLQLKLRASVST | ubiquitination | [1, 2] |
|
Reference | [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles. Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C. Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [ PMID: 21890473] [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties. Chen Z, Zhou Y, Song J, Zhang Z. Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [ PMID: 23603789] |
Functional Description | Required for collagen VII (COL7A1) secretion by loading COL7A1 into transport carriers. May participate in cargo loading of COL7A1 at endoplasmic reticulum exit sites by binding to COPII coat subunits Sec23/24 and guiding SH3-bound COL7A1 into a growing carrier. Does not play a role in global protein secretion and is apparently specific to COL7A1 cargo loading. However, it may participate in secretion of other proteins in cells that do not secrete COL7A1. |
Sequence Annotation | DOMAIN 45 107 SH3.
MOD_RES 382 382 Phosphothreonine (By similarity).
MOD_RES 1727 1727 Phosphoserine (By similarity).
MOD_RES 1739 1739 Phosphoserine (By similarity).
MOD_RES 1740 1740 Phosphoserine (By similarity).
MOD_RES 1745 1745 Phosphoserine.
MOD_RES 1892 1892 Phosphoserine (By similarity).
MOD_RES 1906 1906 Phosphoserine.
CARBOHYD 246 246 N-linked (GlcNAc...) (Potential).
CARBOHYD 589 589 N-linked (GlcNAc...). |
Keyword | Alternative splicing; Coiled coil; Complete proteome; Endoplasmic reticulum; ER-Golgi transport; Exocytosis; Glycoprotein; Membrane; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; SH3 domain; Signal; Transmembrane; Transmembrane helix; Transport. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1907 AA |
Protein Sequence | MAAAPGLLVW LLVLRLPWRV PGQLDPSTGR RFSEHKLCAD DECSMLMYRG EALEDFTGPD 60
CRFVNFKKGD PVYVYYKLAR GWPEVWAGSV GRTFGYFPKD LIQVVHEYTK EELQVPTDET 120
DFVCFDGGRD DFHNYNVEEL LGFLELYNSA ATDSEKAVEK TLQDMEKNPE LSKEREPEPE 180
PVEANSEESD SVFSENTEDL QEQFTTQKHH SHANSQANHA QGEQASFESF EEMLQDKLKV 240
PESENNKTSN SSQVSNEQDK IDAYKLLKKE MTLDLKTKFG STADALVSDD ETTRLVTSLE 300
DDFDEELDTE YYAVGKEDEE NQEDFDELPL LTFTDGEDMK TPAKSGVEKY PTDKEQNSNE 360
EDKVQLTVPP GIKNDDKNIL TTWGDTIFSI VTGGEETRDT MDLESSSSEE EKEDDDDALV 420
PDSKQGKPQS ATDYSDPDNV DDGLFIVDIP KTNNDKEVNA EHHIKGKGRG VQESKRGLVQ 480
DKTELEDENQ EGMTVHSSVH SNNLNSMPAA EKGKDTLKSA YDDTENDLKG AAIHISKGML 540
HEEKPGEQIL EGGSESESAQ KAAGNQMNDR KIQQESLGSA PLMGDDHPNA SRDSVEGDAL 600
VNGAKLHTLS VEHQREELKE ELVLKTQNQP RFSSPDEIDL PRELEDEVPI LGRNLPWQQE 660
RDVAATASKQ MSEKIRLSEG EAKEDSLDEE FFHHKAMQGT EVGQTDQTDS TGGPAFLSKV 720
EEDDYPSEEL LEDENAINAK RSKEKNPGNQ GRQFDVNLQV PDRAVLGTIH PDPEIEESKQ 780
ETSMILDSEK TSETAAKGVN TGGREPNTMV EKERPLADKK AQRPFERSDF SDSIKIQTPE 840
LGEVFQNKDS DYLKNDNPEE HLKTSGLAGE PEGELSKEDH ENTEKYMGTE SQGSAAAEPE 900
DDSFHWTPHT SVEPGHSDKR EDLLIISSFF KEQQSLQRFQ KYFNVHELEA LLQEMSSKLK 960
SAQQESLPYN MEKVLDKVFR ASESQILSIA EKMLDTRVAE NRDLGMNENN IFEEAAVLDD 1020
IQDLIYFVRY KHSTAEETAT LVMAPPLEEG LGGAMEEMQP LHEDNFSREK TAELNVQVPE 1080
EPTHLDQRVI GDTHASEVSQ KPNTEKDLDP GPVTTEDTPM DAIDANKQPE TAAEEPASVT 1140
PLENAILLIY SFMFYLTKSL VATLPDDVQP GPDFYGLPWK PVFITAFLGI ASFAIFLWRT 1200
VLVVKDRVYQ VTEQQISEKL KTIMKENTEL VQKLSNYEQK IKESKKHVQE TRKQNMILSD 1260
EAIKYKDKIK TLEKNQEILD DTAKNLRVML ESEREQNVKN QDLISENKKS IEKLKDVISM 1320
NASEFSEVQI ALNEAKLSEE KVKSECHRVQ EENARLKKKK EQLQQEIEDW SKLHAELSEQ 1380
IKSFEKSQKD LEVALTHKDD NINALTNCIT QLNLLECESE SEGQNKGGND SDELANGEVG 1440
GDRNEKMKNQ IKQMMDVSRT QTAISVVEED LKLLQLKLRA SVSTKCNLED QVKKLEDDRN 1500
SLQAAKAGLE DECKTLRQKV EILNELYQQK EMALQKKLSQ EEYERQEREH RLSAADEKAV 1560
SAAEEVKTYK RRIEEMEDEL QKTERSFKNQ IATHEKKAHE NWLKARAAER AIAEEKREAA 1620
NLRHKLLELT QKMAMLQEEP VIVKPMPGKP NTQNPPRRGP LSQNGSFGPS PVSGGECSPP 1680
LTVEPPVRPL SATLNRRDMP RSEFGSVDGP LPHPRWSAEA SGKPSPSDPG SGTATMMNSS 1740
SRGSSPTRVL DEGKVNMAPK GPPPFPGVPL MSTPMGGPVP PPIRYGPPPQ LCGPFGPRPL 1800
PPPFGPGMRP PLGLREFAPG VPPGRRDLPL HPRGFLPGHA PFRPLGSLGP REYFIPGTRL 1860
PPPTHGPQEY PPPPAVRDLL PSGSRDEPPP ASQSTSQDCS QALKQSP 1907 |
Gene Ontology | GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. GO:0016021; C:integral to membrane; IDA:UniProtKB. GO:0006887; P:exocytosis; IMP:UniProtKB. GO:0007162; P:negative regulation of cell adhesion; IDA:BHF-UCL. GO:0030336; P:negative regulation of cell migration; IDA:BHF-UCL. GO:0002687; P:positive regulation of leukocyte migration; IDA:BHF-UCL. GO:0015031; P:protein transport; IMP:UniProtKB. GO:0042060; P:wound healing; IDA:BHF-UCL. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |