TSH2_HUMAN
ID TSH2_HUMAN Reviewed; 1034 AA.
AC Q9NRE2; B7Z7W1; J3KNQ0; Q4VXM4; Q6N003; Q8N260;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Teashirt homolog 2;
DE AltName: Full=Ovarian cancer-related protein 10-2;
DE Short=OVC10-2;
DE AltName: Full=Zinc finger protein 218;
GN Name=TSHZ2; Synonyms=C20orf17, TSH2, ZNF218;
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] (ISOFORMS 1 AND 2), AND VARIANT
RP SER-113.
RC TISSUE=Testis, and Tongue;
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 1), AND VARIANT SER-113.
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovarian carcinoma;
RA Yue W., Li C., Sun L.;
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUMOYLATION.
RX PubMed=15561718; DOI=10.1074/jbc.m411718200;
RA Gocke C.B., Yu H., Kang J.;
RT "Systematic identification and analysis of mammalian small ubiquitin-like
RT modifier substrates.";
RL J. Biol. Chem. 280:5004-5012(2005).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=19343227; DOI=10.1371/journal.pone.0005071;
RA Kajiwara Y., Akram A., Katsel P., Haroutunian V., Schmeidler J.,
RA Beecham G., Haines J.L., Pericak-Vance M.A., Buxbaum J.D.;
RT "FE65 binds Teashirt, inhibiting expression of the primate-specific
RT caspase-4.";
RL PLoS ONE 4:E5071-E5071(2009).
RN [7]
RP DEVELOPMENTAL STAGE.
RX PubMed=19745106; DOI=10.1093/ndt/gfp453;
RA Jenkins D., Caubit X., Dimovski A., Matevska N., Lye C.M., Cabuk F.,
RA Gucev Z., Tasic V., Fasano L., Woolf A.S.;
RT "Analysis of TSHZ2 and TSHZ3 genes in congenital pelvi-ureteric junction
RT obstruction.";
RL Nephrol. Dial. Transplant. 25:54-60(2010).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-480, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-188; LYS-306; LYS-315; LYS-417;
RP LYS-461; LYS-480; LYS-497; LYS-601; LYS-652; LYS-800; LYS-820 AND LYS-966,
RP AND 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 -!- FUNCTION: Probable transcriptional regulator involved in developmental
CC processes. May act as a transcriptional repressor (Potential).
CC {ECO:0000305}.
CC -!- SUBUNIT: Interacts (via homeobox domain) with APBB1 (via PID domain 1).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9NRE2; Q9BYV9: BACH2; NbExp=3; IntAct=EBI-10687282, EBI-1642333;
CC Q9NRE2; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-10687282, EBI-10961624;
CC Q9NRE2; A6NC98: CCDC88B; NbExp=3; IntAct=EBI-10687282, EBI-347573;
CC Q9NRE2; Q8N137: CNTROB; NbExp=3; IntAct=EBI-10687282, EBI-947360;
CC Q9NRE2; Q96JB2-2: COG3; NbExp=3; IntAct=EBI-10687282, EBI-9091495;
CC Q9NRE2; Q8N4Y2-3: CRACR2B; NbExp=3; IntAct=EBI-10687282, EBI-11982645;
CC Q9NRE2; O75420: GIGYF1; NbExp=3; IntAct=EBI-10687282, EBI-947774;
CC Q9NRE2; Q08379: GOLGA2; NbExp=3; IntAct=EBI-10687282, EBI-618309;
CC Q9NRE2; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-10687282, EBI-717919;
CC Q9NRE2; P23508: MCC; NbExp=3; IntAct=EBI-10687282, EBI-307531;
CC Q9NRE2; Q9BSU1: PHAF1; NbExp=3; IntAct=EBI-10687282, EBI-946080;
CC Q9NRE2; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-10687282, EBI-14066006;
CC Q9NRE2; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-10687282, EBI-302345;
CC Q9NRE2; Q15276: RABEP1; NbExp=3; IntAct=EBI-10687282, EBI-447043;
CC Q9NRE2; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-10687282, EBI-726876;
CC Q9NRE2; P02549: SPTA1; NbExp=3; IntAct=EBI-10687282, EBI-375617;
CC Q9NRE2; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-10687282, EBI-1105213;
CC Q9NRE2; Q13077: TRAF1; NbExp=3; IntAct=EBI-10687282, EBI-359224;
CC Q9NRE2; Q12933: TRAF2; NbExp=3; IntAct=EBI-10687282, EBI-355744;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NRE2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NRE2-2; Sequence=VSP_046071;
CC -!- TISSUE SPECIFICITY: Expressed in brain; strongly reduced in post-mortem
CC elderly subjects with Alzheimer disease. {ECO:0000269|PubMed:19343227}.
CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:15561718}.
CC -!- SIMILARITY: Belongs to the teashirt C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF76850.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown due translation of a 3'-UTR region.; Evidence={ECO:0000305};
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DR EMBL; AK091206; BAC03610.1; -; mRNA.
DR EMBL; AK302570; BAH13747.1; -; mRNA.
DR EMBL; BX640770; CAE45871.1; -; mRNA.
DR EMBL; AL121902; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX276189; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL050316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL109930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354772; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354993; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF230201; AAF76850.1; ALT_SEQ; mRNA.
DR CCDS; CCDS33490.1; -. [Q9NRE2-1]
DR CCDS; CCDS54474.1; -. [Q9NRE2-2]
DR RefSeq; NP_001180350.1; NM_001193421.1. [Q9NRE2-2]
DR RefSeq; NP_775756.3; NM_173485.5. [Q9NRE2-1]
DR RefSeq; XP_016883129.1; XM_017027640.1. [Q9NRE2-1]
DR AlphaFoldDB; Q9NRE2; -.
DR BioGRID; 126131; 34.
DR IntAct; Q9NRE2; 21.
DR STRING; 9606.ENSP00000360552; -.
DR iPTMnet; Q9NRE2; -.
DR PhosphoSitePlus; Q9NRE2; -.
DR BioMuta; TSHZ2; -.
DR DMDM; 108935911; -.
DR jPOST; Q9NRE2; -.
DR MassIVE; Q9NRE2; -.
DR MaxQB; Q9NRE2; -.
DR PaxDb; Q9NRE2; -.
DR PeptideAtlas; Q9NRE2; -.
DR PRIDE; Q9NRE2; -.
DR ProteomicsDB; 82344; -. [Q9NRE2-1]
DR Antibodypedia; 52541; 121 antibodies from 27 providers.
DR DNASU; 128553; -.
DR Ensembl; ENST00000329613.7; ENSP00000333114.5; ENSG00000182463.16. [Q9NRE2-2]
DR Ensembl; ENST00000371497.10; ENSP00000360552.3; ENSG00000182463.16. [Q9NRE2-1]
DR Ensembl; ENST00000603338.2; ENSP00000475114.1; ENSG00000182463.16. [Q9NRE2-2]
DR GeneID; 128553; -.
DR KEGG; hsa:128553; -.
DR MANE-Select; ENST00000371497.10; ENSP00000360552.3; NM_173485.6; NP_775756.3.
DR UCSC; uc002xwo.3; human. [Q9NRE2-1]
DR CTD; 128553; -.
DR DisGeNET; 128553; -.
DR GeneCards; TSHZ2; -.
DR HGNC; HGNC:13010; TSHZ2.
DR HPA; ENSG00000182463; Low tissue specificity.
DR MIM; 614118; gene.
DR neXtProt; NX_Q9NRE2; -.
DR OpenTargets; ENSG00000182463; -.
DR PharmGKB; PA37589; -.
DR VEuPathDB; HostDB:ENSG00000182463; -.
DR eggNOG; ENOG502QV71; Eukaryota.
DR GeneTree; ENSGT00950000183051; -.
DR HOGENOM; CLU_010469_0_0_1; -.
DR InParanoid; Q9NRE2; -.
DR OMA; TGHYQDN; -.
DR OrthoDB; 106971at2759; -.
DR PhylomeDB; Q9NRE2; -.
DR TreeFam; TF328447; -.
DR PathwayCommons; Q9NRE2; -.
DR SignaLink; Q9NRE2; -.
DR BioGRID-ORCS; 128553; 13 hits in 1077 CRISPR screens.
DR ChiTaRS; TSHZ2; human.
DR GenomeRNAi; 128553; -.
DR Pharos; Q9NRE2; Tbio.
DR PRO; PR:Q9NRE2; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9NRE2; protein.
DR Bgee; ENSG00000182463; Expressed in buccal mucosa cell and 165 other tissues.
DR ExpressionAtlas; Q9NRE2; baseline and differential.
DR Genevisible; Q9NRE2; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR027008; Teashirt_fam.
DR InterPro; IPR027010; Tshz2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR12487; PTHR12487; 1.
DR PANTHER; PTHR12487:SF3; PTHR12487:SF3; 1.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Developmental protein; DNA-binding;
KW Homeobox; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1034
FT /note="Teashirt homolog 2"
FT /id="PRO_0000047064"
FT ZN_FING 215..239
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 275..299
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 380..404
FT /note="C2H2-type 3; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 841..911
FT /note="Homeobox; atypical"
FT ZN_FING 926..948
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 994..1017
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 13..38
FT /evidence="ECO:0000255"
FT COMPBIAS 23..37
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1034
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 980
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FE9"
FT CROSSLNK 188
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 306
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 315
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 417
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 461
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 480
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 497
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 601
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 652
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 800
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 820
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 966
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..13
FT /note="MPRRKQQAPKRAA -> MMAAALLHYT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046071"
FT VARIANT 113
FT /note="R -> S (in dbSNP:rs739869)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_026679"
FT VARIANT 681
FT /note="A -> T (in dbSNP:rs6097319)"
FT /id="VAR_026680"
FT CONFLICT 198
FT /note="Y -> C (in Ref. 2; CAE45871)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="A -> T (in Ref. 2; CAE45871)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="Q -> R (in Ref. 1; BAC03610)"
FT /evidence="ECO:0000305"
FT CONFLICT 916
FT /note="L -> P (in Ref. 2; CAE45871)"
FT /evidence="ECO:0000305"
FT CONFLICT 983
FT /note="T -> A (in Ref. 1; BAH13747)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1034 AA; 115005 MW; 4FC14F93D4CD48F6 CRC64;
MPRRKQQAPK RAAGYAQEEQ LKEEEEIKEE EEEEDSGSVA QLQGGNDTGT DEELETGPEQ
KGCFSYQNSP GSHLSNQDAE NESLLSDASD QVSDIKSVCG RDASDKKAHT HVRLPNEAHN
CMDKMTAVYA NILSDSYWSG LGLGFKLSNS ERRNCDTRNG SNKSDFDWHQ DALSKSLQQN
LPSRSVSKPS LFSSVQLYRQ SSKMCGTVFT GASRFRCRQC SAAYDTLVEL TVHMNETGHY
QDDNRKKDKL RPTSYSKPRK RAFQDMDKED AQKVLKCMFC GDSFDSLQDL SVHMIKTKHY
QKVPLKEPVP TISSKMVTPA KKRVFDVNRP CSPDSTTGSF ADSFSSQKNA NLQLSSNNRY
GYQNGASYTW QFEACKSQIL KCMECGSSHD TLQQLTTHMM VTGHFLKVTS SASKKGKQLV
LDPLAVEKMQ SLSEAPNSDS LAPKPSSNSA SDCTASTTEL KKESKKERPE ETSKDEKVVK
SEDYEDPLQK PLDPTIKYQY LREEDLEDGS KGGGDILKSL ENTVTTAINK AQNGAPSWSA
YPSIHAAYQL SEGTKPPLPM GSQVLQIRPN LTNKLRPIAP KWKVMPLVSM PTHLAPYTQV
KKESEDKDEA VKECGKESPH EEASSFSHSE GDSFRKSETP PEAKKTELGP LKEEEKLMKE
GSEKEKPQPL EPTSALSNGC ALANHAPALP CINPLSALQS VLNNHLGKAT EPLRSPSCSS
PSSSTISMFH KSNLNVMDKP VLSPASTRSA SVSRRYLFEN SDQPIDLTKS KSKKAESSQA
QSCMSPPQKH ALSDIADMVK VLPKATTPKP ASSSRVPPMK LEMDVRRFED VSSEVSTLHK
RKGRQSNWNP QHLLILQAQF ASSLFQTSEG KYLLSDLGPQ ERMQISKFTG LSMTTISHWL
ANVKYQLRKT GGTKFLKNMD KGHPIFYCSD CASQFRTPST YISHLESHLG FQMKDMTRLS
VDQQSKVEQE ISRVSSAQRS PETIAAEEDT DSKFKCKLCC RTFVSKHAVK LHLSKTHSKS
PEHHSQFVTD VDEE
