MMTA2_HUMAN
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-AUG-2022, entry version 160.
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;
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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; 303.
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 PRIDE; 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 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; 1325819at2759; -.
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 993 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; PTHR14580; 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
