ID G3V599_HUMAN Unreviewed; 1339 AA. AC G3V599; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 13-FEB-2019, entry version 53. DE SubName: Full=Melanoma inhibitory activity protein 2 {ECO:0000313|Ensembl:ENSP00000452252}; GN Name=MIA2 {ECO:0000313|Ensembl:ENSP00000452252}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000452252, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000452252, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., RA Quetier F., Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [2] {ECO:0000213|PubMed:17081983} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [3] {ECO:0000213|PubMed:18220336} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.D., Yates J.R.; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for RT efficient phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [4] {ECO:0000213|PubMed:18669648} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [5] {ECO:0000213|PubMed:19690332} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:ra46-RA46(2009). RN [6] {ECO:0000213|PubMed:20068231} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:ra3-RA3(2010). RN [7] {ECO:0000213|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Burckstummer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [8] {ECO:0000313|Ensembl:ENSP00000452252} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. RN [9] {ECO:0000213|PubMed:23186163} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=23186163; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [10] {ECO:0000213|PubMed:24275569} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [11] {ECO:0000213|PubMed:24129315} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=24129315; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., RA Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., RA Vemulapalli V., Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [12] {ECO:0000213|PubMed:25944712} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL132639; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL157791; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; G3V599; -. DR EPD; G3V599; -. DR jPOST; G3V599; -. DR MaxQB; G3V599; -. DR PaxDb; G3V599; -. DR PeptideAtlas; G3V599; -. DR PRIDE; G3V599; -. DR Ensembl; ENST00000553728; ENSP00000452252; ENSG00000150527. DR UCSC; uc059bar.1; human. DR EuPathDB; HostDB:ENSG00000258941.3; -. DR HGNC; HGNC:18432; MIA2. DR OpenTargets; ENSG00000150527; -. DR eggNOG; ENOG410IJV2; Eukaryota. DR eggNOG; ENOG410ZUJU; LUCA. DR GeneTree; ENSGT00940000153207; -. DR OMA; KMKDWSS; -. DR TreeFam; TF333137; -. DR ChiTaRS; MIA2; human. DR Proteomes; UP000005640; Chromosome 14. DR Bgee; ENSG00000258941; Expressed in 29 organ(s), highest expression level in intestine. DR ExpressionAtlas; G3V599; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042954; F:lipoprotein transporter activity; IBA:GO_Central. DR GO; GO:0009306; P:protein secretion; IBA:GO_Central. DR CDD; cd11892; SH3_MIA2; 1. DR InterPro; IPR035555; MIA2_SH3. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR Pfam; PF07653; SH3_2; 1. DR SUPFAM; SSF50044; SSF50044; 1. DR PROSITE; PS50002; SH3; 1. PE 1: Evidence at protein level; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Proteomics identification {ECO:0000213|EPD:G3V599, KW ECO:0000213|MaxQB:G3V599, ECO:0000213|PeptideAtlas:G3V599}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW SH3 domain {ECO:0000256|PROSITE-ProRule:PRU00192}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 1339 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003457372. FT TRANSMEM 574 595 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 39 101 SH3. {ECO:0000259|PROSITE:PS50002}. FT COILED 652 728 {ECO:0000256|SAM:Coils}. FT COILED 736 777 {ECO:0000256|SAM:Coils}. FT COILED 875 930 {ECO:0000256|SAM:Coils}. FT COILED 942 994 {ECO:0000256|SAM:Coils}. FT COILED 1002 1029 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 1339 AA; 151720 MW; 648CE083EA9B8A3E CRC64; MAKFGVHRIL LLAISLTKCL ESTKLLADLK KCGDLECEAL INRVSAMRDY RGPDCRYLNF TKGEEISVYV KLAGEREDLW AGSKGKEFGY FPRDAVQIEE VFISEEIQMS TKESDFLCLL GVSYTFDNED SELNGDYGEN IYPYEEDKDE KSSIYESDFQ IEPGFYATYE STLFEDQVPA LEAPEDIGST SESKDWEEVV VESMEQDRIP EVHVPPSSAV SGVKEWFGLG GEQAEEKAFE SVIEPVQESS FRSRKIAVED ENDLEELNNG EPQTEHQQES ESEIDSVPKT QSELASESEH IPKPQSTGWF GGGFTSYLGF GDEDTGLELI AEESNPPLQD FPNSISSDKE ATVPCTEILT EKKDTITNDS LSLKPSWFDF GFAILGFAYA KEDKIMLDDR KNEEDGGADE HEHPLTSELD PEKEQEIETI KIIETEDQID KKPVSEKTDE SDTIPYLKKF LYNFDNPWNF QNIPKETELP FPKQILDQNN VIENEETGEF SIDNYPTDNT KVMIFKSSYS LSEDASEFQI LKYLFQIDVY DFMNSAFSPI VILTERVVAA LPEGMRPDSN LYGFPWELVI CAAVVGFFAV LFFLWRSFRS VRSRLYVGRE KKLALMLSGL IEEKSKLLEK FSLVQKEYEG YEVESSLKDA SFEKEATEAQ SLEATCEKLN RSNSELEDEI LCLEKELKEE KSKHSEQDEL MADISKRIQS LEDESKSLKS QVAEAKMTFK IFQMNEERLK IAIKDALNEN SQLQESQKQL LQEAEVWKEQ VSELNKQKVT FEDSKVHAEQ VLNDKESHIK TLTERLLKMK DWAAMLGEDI TDDDNLELEM NSESENGAYL DNPPKGALKK LIHAAKLNAS LKTLEGERNQ IYIQLSEVDK TKEELTEHIK NLQTEQASLQ SENTHFENEN QKLQQKLKVM TELYQENEMK LHRKLTVEEN YRLEKEEKLS KVDEKISHAT EELETYRKRA KDLEEELERT IHSYQGQIIS HEKKAHDNWL AARNAERNLN DLRKENAHNR QKLTETELKF ELLEKDPYAL DVPNTAFGRE HSPYGPSPLG WPSSETRAFL SPPTLLEGPL RLSPLLPGGG GRGSRGPGNP LDHQITNERG ESSCDRLTDP HRAPSDTGSL SPPWDQDRRM MFPPPGQSYP DSALPPQRQD RFCSNSGRLS GPAELRSFNM PSLDKMDGSM PSEMESSRND TKDDLGNLNV PDSSLPAENE ATGPGFVPPP LAPIRGPLFP VDARGPFLRR GPPFPPPPPG AMFGASRDYF PPGDFPGPPP APFAMRNVYP PRGFPPYLPP RPGFFPPPPH SEGRSEFPSG LIPPSNEPAT EHPEPQQET //