ID MMTA2_HUMAN Reviewed; 263 AA. AC Q9BU76; Q6P5Y0; Q6ZTZ6; Q6ZWA6; Q8IZH3; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 03-MAY-2023, entry version 164. DE RecName: Full=Multiple myeloma tumor-associated protein 2; DE Short=hMMTAG2; GN Name=MMTAG2; Synonyms=C1orf35; 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 [MRNA] (ISOFORM 1). RC TISSUE=Myeloma; RX PubMed=12545221; RA Tian J.Y., Hu W.X., Tian E.M., Shi Y.W., Shen Q.X., Tang L.J., Jiang Y.S.; RT "Cloning and sequence analysis of tumor-associated gene hMMTAG2 from human RT multiple myeloma cell line ARH-77."; RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 35:143-148(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4). RC TISSUE=Caudate nucleus; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Blood, and Lymph; 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 [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; 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., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-164, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; 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 [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-219, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; 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., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [9] 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., Buerckstuemmer T., RA 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-215 AND SER-220, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123; SER-127; SER-216; RP SER-217 AND SER-220, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; 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 [12] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-104, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [13] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-22; LYS-104 AND LYS-113, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). CC -!- INTERACTION: CC Q9BU76; Q96CW1: AP2M1; NbExp=3; IntAct=EBI-742459, EBI-297683; CC Q9BU76; A0A0C4DG62: ARL6IP4; NbExp=3; IntAct=EBI-742459, EBI-12248874; CC Q9BU76; Q96LM5: C4orf45; NbExp=3; IntAct=EBI-742459, EBI-12020542; CC Q9BU76; Q9UK58: CCNL1; NbExp=3; IntAct=EBI-742459, EBI-2836773; CC Q9BU76; Q8NHQ1: CEP70; NbExp=5; IntAct=EBI-742459, EBI-739624; CC Q9BU76; P68400: CSNK2A1; NbExp=4; IntAct=EBI-742459, EBI-347804; CC Q9BU76; Q5HYN5: CT45A1; NbExp=3; IntAct=EBI-742459, EBI-12051833; CC Q9BU76; Q9UI36-2: DACH1; NbExp=3; IntAct=EBI-742459, EBI-10186082; CC Q9BU76; Q92997: DVL3; NbExp=3; IntAct=EBI-742459, EBI-739789; CC Q9BU76; Q8N9E0: FAM133A; NbExp=3; IntAct=EBI-742459, EBI-10268158; CC Q9BU76; P51114-2: FXR1; NbExp=5; IntAct=EBI-742459, EBI-11022345; CC Q9BU76; P51116: FXR2; NbExp=6; IntAct=EBI-742459, EBI-740459; CC Q9BU76; O95995: GAS8; NbExp=3; IntAct=EBI-742459, EBI-1052570; CC Q9BU76; Q5VSY0: GKAP1; NbExp=3; IntAct=EBI-742459, EBI-743722; CC Q9BU76; Q08379: GOLGA2; NbExp=4; IntAct=EBI-742459, EBI-618309; CC Q9BU76; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-742459, EBI-5916454; CC Q9BU76; O75031: HSF2BP; NbExp=3; IntAct=EBI-742459, EBI-7116203; CC Q9BU76; Q0VD86: INCA1; NbExp=3; IntAct=EBI-742459, EBI-6509505; CC Q9BU76; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-742459, EBI-10172526; CC Q9BU76; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-742459, EBI-2548751; CC Q9BU76; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-742459, EBI-11522433; CC Q9BU76; Q6ZUT1: NKAPD1; NbExp=3; IntAct=EBI-742459, EBI-3920396; CC Q9BU76; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-742459, EBI-79165; CC Q9BU76; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-742459, EBI-742388; CC Q9BU76; Q9Y388: RBMX2; NbExp=3; IntAct=EBI-742459, EBI-7704044; CC Q9BU76; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-742459, EBI-726876; CC Q9BU76; Q2KHN1: RNF151; NbExp=3; IntAct=EBI-742459, EBI-12002474; CC Q9BU76; Q8TA86: RP9; NbExp=3; IntAct=EBI-742459, EBI-630339; CC Q9BU76; O00560: SDCBP; NbExp=3; IntAct=EBI-742459, EBI-727004; CC Q9BU76; Q9H190: SDCBP2; NbExp=4; IntAct=EBI-742459, EBI-742426; CC Q9BU76; P78362: SRPK2; NbExp=3; IntAct=EBI-742459, EBI-593303; CC Q9BU76; A7MD48: SRRM4; NbExp=3; IntAct=EBI-742459, EBI-3867173; CC Q9BU76; Q96MF2: STAC3; NbExp=5; IntAct=EBI-742459, EBI-745680; CC Q9BU76; P54274: TERF1; NbExp=2; IntAct=EBI-742459, EBI-710997; CC Q9BU76; Q9NVV9: THAP1; NbExp=9; IntAct=EBI-742459, EBI-741515; CC Q9BU76; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-742459, EBI-2130429; CC Q9BU76; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-742459, EBI-527853; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q9BU76-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BU76-2; Sequence=VSP_015129, VSP_015130; CC Name=3; CC IsoId=Q9BU76-3; Sequence=VSP_015131, VSP_015132; CC Name=4; CC IsoId=Q9BU76-4; Sequence=VSP_015133, VSP_015134; 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; AY137773; AAN15215.1; -; mRNA. DR EMBL; AK123377; BAC85598.1; -; mRNA. DR EMBL; AK126087; BAC86431.1; -; mRNA. DR EMBL; AL136379; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC002843; AAH02843.1; -; mRNA. DR EMBL; BC062585; AAH62585.1; -; mRNA. DR CCDS; CCDS1566.1; -. [Q9BU76-1] DR RefSeq; NP_077295.1; NM_024319.3. [Q9BU76-1] DR AlphaFoldDB; Q9BU76; -. DR SMR; Q9BU76; -. DR BioGRID; 122586; 321. DR IntAct; Q9BU76; 80. DR MINT; Q9BU76; -. DR STRING; 9606.ENSP00000272139; -. DR GlyGen; Q9BU76; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9BU76; -. DR PhosphoSitePlus; Q9BU76; -. DR BioMuta; C1orf35; -. DR DMDM; 73621220; -. DR EPD; Q9BU76; -. DR jPOST; Q9BU76; -. DR MassIVE; Q9BU76; -. DR MaxQB; Q9BU76; -. DR PaxDb; Q9BU76; -. DR PeptideAtlas; Q9BU76; -. DR ProteomicsDB; 79060; -. [Q9BU76-1] DR ProteomicsDB; 79061; -. [Q9BU76-2] DR ProteomicsDB; 79062; -. [Q9BU76-3] DR ProteomicsDB; 79063; -. [Q9BU76-4] DR Antibodypedia; 52229; 72 antibodies from 20 providers. DR DNASU; 79169; -. DR Ensembl; ENST00000272139.5; ENSP00000272139.4; ENSG00000143793.13. [Q9BU76-1] DR GeneID; 79169; -. DR KEGG; hsa:79169; -. DR MANE-Select; ENST00000272139.5; ENSP00000272139.4; NM_024319.4; NP_077295.1. DR UCSC; uc001hrx.4; human. [Q9BU76-1] DR AGR; HGNC:19032; -. DR CTD; 79169; -. DR GeneCards; C1orf35; -. DR HGNC; HGNC:19032; C1orf35. DR HPA; ENSG00000143793; Low tissue specificity. DR neXtProt; NX_Q9BU76; -. DR OpenTargets; ENSG00000143793; -. DR PharmGKB; PA38781; -. DR VEuPathDB; HostDB:ENSG00000143793; -. DR eggNOG; KOG4520; Eukaryota. DR GeneTree; ENSGT00390000005590; -. DR HOGENOM; CLU_061193_0_1_1; -. DR InParanoid; Q9BU76; -. DR OMA; FTHHKVE; -. DR OrthoDB; 51935at2759; -. DR PhylomeDB; Q9BU76; -. DR TreeFam; TF332234; -. DR PathwayCommons; Q9BU76; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR SignaLink; Q9BU76; -. DR BioGRID-ORCS; 79169; 10 hits in 1041 CRISPR screens. DR ChiTaRS; C1orf35; human. DR GenomeRNAi; 79169; -. DR Pharos; Q9BU76; Tdark. DR PRO; PR:Q9BU76; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9BU76; protein. DR Bgee; ENSG00000143793; Expressed in sural nerve and 179 other tissues. DR Genevisible; Q9BU76; HS. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome. DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR InterPro; IPR019315; MMTA2_N. DR InterPro; IPR039207; MMTAG2-like. DR PANTHER; PTHR14580:SF0; MULTIPLE MYELOMA TUMOR-ASSOCIATED PROTEIN 2; 1. DR PANTHER; PTHR14580; MULTIPLE MYELOMA TUMOR-ASSOCIATED PROTEIN 2 FAMILY MEMBER; 1. DR Pfam; PF10159; MMtag; 1. PE 1: Evidence at protein level; KW Alternative splicing; Isopeptide bond; Phosphoprotein; Reference proteome; KW Ubl conjugation. FT CHAIN 1..263 FT /note="Multiple myeloma tumor-associated protein 2" FT /id="PRO_0000096518" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 105..132 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 148..263 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 166..183 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 184..205 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 220..241 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 123 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 127 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 164 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 215 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 216 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 217 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 219 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 220 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT CROSSLNK 22 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 104 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 113 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 125..141 FT /note="SGSVGRVAMSREDKEAA -> RCGRVSRGGQHWARLLG (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_015129" FT VAR_SEQ 142..263 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_015130" FT VAR_SEQ 150..155 FT /note="HHRVES -> VIPRPA (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_015131" FT VAR_SEQ 156..263 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_015132" FT VAR_SEQ 178..189 FT /note="SCESHRKSKKEK -> RGVSRVTLEERS (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_015133" FT VAR_SEQ 190..263 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_015134" FT CONFLICT 29 FT /note="N -> I (in Ref. 1; AAN15215)" FT /evidence="ECO:0000305" FT CONFLICT 154 FT /note="E -> K (in Ref. 1; AAN15215)" FT /evidence="ECO:0000305" FT CONFLICT 262 FT /note="E -> K (in Ref. 1; AAN15215)" FT /evidence="ECO:0000305" SQ SEQUENCE 263 AA; 29412 MW; 51A7DEE260DBD787 CRC64; MFGSSRGGVR GGQDQFNWED VKTDKQRENY LGNSLMAPVG RWQKGRDLTW YAKGRAPCAG PSREEELAAV REAEREALLA ALGYKNVKKQ PTGLSKEDFA EVCKREGGDP EEKGVDRLLG LGSASGSVGR VAMSREDKEA AKLGLSVFTH HRVESGGPGT SAASARRKPR AEDQTESSCE SHRKSKKEKK KKKKRKHKKE KKKKDKEHRR PAEATSSPTS PERPRHHHHD SDSNSPCCKR RKRGHSGDRR SPSRRWHDRG SEA //