RBAK_HUMAN
ID RBAK_HUMAN Reviewed; 714 AA.
AC Q9NYW8; A6NDF2; A8KAK4; B2RN44; B9EGS1; F8W6M7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=RB-associated KRAB zinc finger protein;
DE AltName: Full=RB-associated KRAB repressor;
DE Short=hRBaK;
DE AltName: Full=Zinc finger protein 769;
GN Name=RBAK; Synonyms=ZNF769;
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), FUNCTION, INTERACTION WITH RB1,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10702291; DOI=10.1074/jbc.275.10.7212;
RA Skapek S.X., Jansen D., Wei T.-F., McDermott T., Huang W., Olson E.N.,
RA Lee E.Y.-H.P.;
RT "Cloning and characterization of a novel Kruppel-associated box family
RT transcriptional repressor that interacts with the retinoblastoma gene
RT product, RB.";
RL J. Biol. Chem. 275:7212-7223(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=8889548; DOI=10.1101/gr.6.9.791;
RA Bonaldo M.F., Lennon G., Soares M.B.;
RT "Normalization and subtraction: two approaches to facilitate gene
RT discovery.";
RL Genome Res. 6:791-806(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Testis;
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 [7]
RP FUNCTION, AND INTERACTION WITH AR.
RX PubMed=14664718; DOI=10.1677/jme.0.0310583;
RA Hofman K., Swinnen J.V., Claessens F., Verhoeven G., Heyns W.;
RT "The retinoblastoma protein-associated transcription repressor RBaK
RT interacts with the androgen receptor and enhances its transcriptional
RT activity.";
RL J. Mol. Endocrinol. 31:583-596(2003).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-534, 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-534, 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 [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-97; LYS-259; LYS-315; LYS-357;
RP LYS-534 AND LYS-537, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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: May repress E2F-dependent transcription. May promote AR-
CC dependent transcription. {ECO:0000269|PubMed:10702291,
CC ECO:0000269|PubMed:14664718}.
CC -!- SUBUNIT: Interacts with AR and RB1. May also interact with other
CC nuclear hormone receptors such as NR3C1/GR.
CC {ECO:0000269|PubMed:10702291, ECO:0000269|PubMed:14664718}.
CC -!- INTERACTION:
CC Q9NYW8; P29972: AQP1; NbExp=3; IntAct=EBI-1210429, EBI-745213;
CC Q9NYW8; Q13895: BYSL; NbExp=3; IntAct=EBI-1210429, EBI-358049;
CC Q9NYW8; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-1210429, EBI-11530605;
CC Q9NYW8; Q96Q77: CIB3; NbExp=3; IntAct=EBI-1210429, EBI-10292696;
CC Q9NYW8; Q9BSW2: CRACR2A; NbExp=3; IntAct=EBI-1210429, EBI-739773;
CC Q9NYW8; O95967: EFEMP2; NbExp=3; IntAct=EBI-1210429, EBI-743414;
CC Q9NYW8; Q8N9N8: EIF1AD; NbExp=3; IntAct=EBI-1210429, EBI-750700;
CC Q9NYW8; P61328-2: FGF12; NbExp=3; IntAct=EBI-1210429, EBI-10699759;
CC Q9NYW8; O95995: GAS8; NbExp=3; IntAct=EBI-1210429, EBI-1052570;
CC Q9NYW8; Q969R5: L3MBTL2; NbExp=3; IntAct=EBI-1210429, EBI-739909;
CC Q9NYW8; P61968: LMO4; NbExp=3; IntAct=EBI-1210429, EBI-2798728;
CC Q9NYW8; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-1210429, EBI-739832;
CC Q9NYW8; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-1210429, EBI-746778;
CC Q9NYW8; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-1210429, EBI-11750983;
CC Q9NYW8; Q13976-2: PRKG1; NbExp=3; IntAct=EBI-1210429, EBI-4280187;
CC Q9NYW8; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-1210429, EBI-1567797;
CC Q9NYW8; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-1210429, EBI-748391;
CC Q9NYW8; Q9UBX3-2: SLC25A10; NbExp=3; IntAct=EBI-1210429, EBI-12056597;
CC Q9NYW8; Q9Y4C2-2: TCAF1; NbExp=3; IntAct=EBI-1210429, EBI-11974855;
CC Q9NYW8; Q63HR2: TNS2; NbExp=3; IntAct=EBI-1210429, EBI-949753;
CC Q9NYW8; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-1210429, EBI-725997;
CC Q9NYW8; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-1210429, EBI-744794;
CC Q9NYW8; P42681: TXK; NbExp=3; IntAct=EBI-1210429, EBI-7877438;
CC Q9NYW8; P58317: ZNF121; NbExp=3; IntAct=EBI-1210429, EBI-1228269;
CC Q9NYW8; Q9Y3S2: ZNF330; NbExp=3; IntAct=EBI-1210429, EBI-373456;
CC Q9NYW8; Q5T619: ZNF648; NbExp=3; IntAct=EBI-1210429, EBI-11985915;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10702291}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NYW8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NYW8-2; Sequence=VSP_044805, VSP_044806;
CC -!- TISSUE SPECIFICITY: Expressed in bone, brain, heart, kidney, liver,
CC lung, pancreas and placenta. {ECO:0000269|PubMed:10702291}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AF226869; AAF43389.1; -; mRNA.
DR EMBL; BM929719; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK293069; BAF85758.1; -; mRNA.
DR EMBL; AC092032; AAQ93364.1; -; Genomic_DNA.
DR EMBL; AC008167; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471144; EAW87321.1; -; Genomic_DNA.
DR EMBL; BC136675; AAI36676.1; -; mRNA.
DR EMBL; BC136676; AAI36677.1; -; mRNA.
DR CCDS; CCDS5337.1; -. [Q9NYW8-1]
DR RefSeq; NP_001191385.1; NM_001204456.1. [Q9NYW8-1]
DR RefSeq; NP_066986.1; NM_021163.3. [Q9NYW8-1]
DR AlphaFoldDB; Q9NYW8; -.
DR SMR; Q9NYW8; -.
DR BioGRID; 121759; 52.
DR BioGRID; 1529617; 1.
DR DIP; DIP-39336N; -.
DR IntAct; Q9NYW8; 39.
DR MINT; Q9NYW8; -.
DR STRING; 9606.ENSP00000380120; -.
DR iPTMnet; Q9NYW8; -.
DR PhosphoSitePlus; Q9NYW8; -.
DR BioMuta; RBAK; -.
DR DMDM; 74761820; -.
DR EPD; Q9NYW8; -.
DR jPOST; Q9NYW8; -.
DR MassIVE; Q9NYW8; -.
DR MaxQB; Q9NYW8; -.
DR PaxDb; Q9NYW8; -.
DR PeptideAtlas; Q9NYW8; -.
DR PRIDE; Q9NYW8; -.
DR ProteomicsDB; 29813; -.
DR ProteomicsDB; 83294; -. [Q9NYW8-1]
DR Antibodypedia; 11262; 153 antibodies from 27 providers.
DR DNASU; 57786; -.
DR Ensembl; ENST00000353796.7; ENSP00000275423.4; ENSG00000146587.18. [Q9NYW8-1]
DR Ensembl; ENST00000396912.2; ENSP00000380120.1; ENSG00000146587.18. [Q9NYW8-1]
DR GeneID; 57786; -.
DR KEGG; hsa:57786; -.
DR MANE-Select; ENST00000396912.2; ENSP00000380120.1; NM_021163.4; NP_066986.1.
DR UCSC; uc003sns.1; human. [Q9NYW8-1]
DR CTD; 57786; -.
DR DisGeNET; 57786; -.
DR GeneCards; RBAK; -.
DR HGNC; HGNC:17680; RBAK.
DR HPA; ENSG00000146587; Low tissue specificity.
DR MIM; 608191; gene.
DR neXtProt; NX_Q9NYW8; -.
DR OpenTargets; ENSG00000146587; -.
DR PharmGKB; PA162400745; -.
DR VEuPathDB; HostDB:ENSG00000146587; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000154303; -.
DR HOGENOM; CLU_002678_0_12_1; -.
DR InParanoid; Q9NYW8; -.
DR OMA; YECNQNG; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9NYW8; -.
DR TreeFam; TF350803; -.
DR PathwayCommons; Q9NYW8; -.
DR SignaLink; Q9NYW8; -.
DR BioGRID-ORCS; 57786; 15 hits in 1088 CRISPR screens.
DR ChiTaRS; RBAK; human.
DR GenomeRNAi; 57786; -.
DR Pharos; Q9NYW8; Tbio.
DR PRO; PR:Q9NYW8; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9NYW8; protein.
DR Bgee; ENSG00000146587; Expressed in epithelial cell of pancreas and 188 other tissues.
DR Genevisible; Q9NYW8; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; TAS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:UniProtKB.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 14.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 16.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 10.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 14.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 15.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..714
FT /note="RB-associated KRAB zinc finger protein"
FT /id="PRO_0000316976"
FT DOMAIN 8..79
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 261..283
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 289..311
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 317..339
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 345..367
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 373..395
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 401..423
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 429..451
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 457..479
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 485..505
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 511..533
FT /note="C2H2-type 10; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 539..561
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 567..589
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 595..617
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 623..645
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 651..673
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 679..701
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 171..260
FT /note="Required for interaction with RB1"
FT /evidence="ECO:0000269|PubMed:10702291"
FT REGION 417..714
FT /note="Interaction with AR"
FT /evidence="ECO:0000269|PubMed:14664718"
FT CROSSLNK 97
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 259
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 357
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 534
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 537
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 80..113
FT /note="EAWRVDDLIERIQENEDKHSRQAACINSKTLTEE -> AALPAGHVAPAVAA
FT AAAAPGRPGPHRQSRSPPGC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8889548"
FT /id="VSP_044805"
FT VAR_SEQ 114..714
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8889548"
FT /id="VSP_044806"
FT VARIANT 229
FT /note="G -> E (in dbSNP:rs35352738)"
FT /id="VAR_038438"
FT CONFLICT 273
FT /note="K -> E (in Ref. 3; BAF85758)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 714 AA; 82995 MW; 36D90A6206118F8B CRC64;
MNTLQGPVSF KDVAVDFTQE EWQQLDPDEK ITYRDVMLEN YSHLVSVGYD TTKPNVIIKL
EQGEEPWIMG GEFPCQHSPE AWRVDDLIER IQENEDKHSR QAACINSKTL TEEKENTFSQ
IYMETSLVPS SIIAHNCVSC GKNLESISQL ISSDGSYART KPDECNECGK TYHGEKMCEF
NQNGDTYSHN EENILQKISI LEKPFEYNEC MEALDNEAVF IAHKRAYIGE KPYEWNDSGP
DFIQMSNFNA YQRSQMEMKP FECSECGKSF CKKSKFIIHQ RAHTGEKPYE CNVCGKSFSQ
KGTLTVHRRS HLEEKPYKCN ECGKTFCQKL HLTQHLRTHS GEKPYECSEC GKTFCQKTHL
TLHQRNHSGE RPYPCNECGK SFSRKSALSD HQRTHTGEKL YKCNECGKSY YRKSTLITHQ
RTHTGEKPYQ CSECGKFFSR VSYLTIHYRS HLEEKPYECN ECGKTFNLNS AFIRHRKVHT
EEKSHECSEC GKFSQLYLTD HHTAHLEEKP YECNECGKTF LVNSAFDGHQ PLPKGEKSYE
CNVCGKLFNE LSYYTEHYRS HSEEKPYGCS ECGKTFSHNS SLFRHQRVHT GEKPYECYEC
GKFFSQKSYL TIHHRIHSGE KPYECSKCGK VFSRMSNLTV HYRSHSGEKP YECNECGKVF
SQKSYLTVHY RTHSGEKPYE CNECGKKFHH RSAFNSHQRI HRRGNMNVLD VENL
