ZN711_HUMAN
ID ZN711_HUMAN Reviewed; 761 AA.
AC Q9Y462; B4DSV4; Q6NX42; Q9Y4J6;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Zinc finger protein 711;
DE AltName: Full=Zinc finger protein 6;
GN Name=ZNF711; Synonyms=CMPX1, ZNF6;
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 GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 185-761 (ISOFORM 3).
RC TISSUE=Brain;
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 PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=1923752; DOI=10.1093/nar/19.18.4835;
RA Lloyd S.L., Sargent C.A., Chalmers J., Lim E., Habeebu S.S., Affara N.A.;
RT "An X linked zinc finger gene mapping to Xq21.1-q21.3 closely related to
RT ZFX and ZFY. Possible origins from a common ancestral gene.";
RL Nucleic Acids Res. 19:4835-4841(1991).
RN [5]
RP INVOLVEMENT IN XLID97, AND VARIANTS [LARGE SCALE ANALYSIS] XLID97 GLU-139;
RP ALA-221; ARG-274; THR-524; SER-601 AND ASP-622.
RX PubMed=19377476; DOI=10.1038/ng.367;
RA Tarpey P.S., Smith R., Pleasance E., Whibley A., Edkins S., Hardy C.,
RA O'Meara S., Latimer C., Dicks E., Menzies A., Stephens P., Blow M.,
RA Greenman C., Xue Y., Tyler-Smith C., Thompson D., Gray K., Andrews J.,
RA Barthorpe S., Buck G., Cole J., Dunmore R., Jones D., Maddison M.,
RA Mironenko T., Turner R., Turrell K., Varian J., West S., Widaa S., Wray P.,
RA Teague J., Butler A., Jenkinson A., Jia M., Richardson D., Shepherd R.,
RA Wooster R., Tejada M.I., Martinez F., Carvill G., Goliath R.,
RA de Brouwer A.P., van Bokhoven H., Van Esch H., Chelly J., Raynaud M.,
RA Ropers H.H., Abidi F.E., Srivastava A.K., Cox J., Luo Y., Mallya U.,
RA Moon J., Parnau J., Mohammed S., Tolmie J.L., Shoubridge C., Corbett M.,
RA Gardner A., Haan E., Rujirabanjerd S., Shaw M., Vandeleur L., Fullston T.,
RA Easton D.F., Boyle J., Partington M., Hackett A., Field M., Skinner C.,
RA Stevenson R.E., Bobrow M., Turner G., Schwartz C.E., Gecz J., Raymond F.L.,
RA Futreal P.A., Stratton M.R.;
RT "A systematic, large-scale resequencing screen of X-chromosome coding exons
RT in mental retardation.";
RL Nat. Genet. 41:535-543(2009).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP PHF8.
RX PubMed=20346720; DOI=10.1016/j.molcel.2010.03.002;
RA Kleine-Kohlbrecher D., Christensen J., Vandamme J., Abarrategui I., Bak M.,
RA Tommerup N., Shi X., Gozani O., Rappsilber J., Salcini A.E., Helin K.;
RT "A functional link between the histone demethylase PHF8 and the
RT transcription factor ZNF711 in X-linked mental retardation.";
RL Mol. Cell 38:165-178(2010).
RN [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-224; LYS-235 AND LYS-296, 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).
RN [8]
RP VARIANT XLID97 THR-244.
RX PubMed=27993705; DOI=10.1016/j.gene.2016.12.013;
RA van der Werf I.M., Van Dijck A., Reyniers E., Helsmoortel C., Kumar A.A.,
RA Kalscheuer V.M., de Brouwer A.P., Kleefstra T., van Bokhoven H.,
RA Mortier G., Janssens S., Vandeweyer G., Kooy R.F.;
RT "Mutations in two large pedigrees highlight the role of ZNF711 in X-linked
RT intellectual disability.";
RL Gene 605:92-98(2017).
CC -!- FUNCTION: Transcription regulator required for brain development.
CC Probably acts as a transcription factor that binds to the promoter of
CC target genes and recruits PHF8 histone demethylase, leading to activate
CC expression of genes involved in neuron development, such as KDM5C.
CC {ECO:0000269|PubMed:20346720}.
CC -!- SUBUNIT: Interacts with PHF8. {ECO:0000269|PubMed:20346720}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:20346720}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y462-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y462-2; Sequence=VSP_016912;
CC Name=3;
CC IsoId=Q9Y462-3; Sequence=VSP_039887;
CC -!- TISSUE SPECIFICITY: Expressed in neural tissues.
CC {ECO:0000269|PubMed:20346720}.
CC -!- DISEASE: Intellectual developmental disorder, X-linked 97 (XLID97)
CC [MIM:300803]: A disorder characterized by significantly below average
CC general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period.
CC {ECO:0000269|PubMed:19377476, ECO:0000269|PubMed:27993705}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG61766.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA39837.2; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA39837.2; Type=Miscellaneous discrepancy; Note=Chimera.; Evidence={ECO:0000305};
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DR EMBL; Z82216; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC067294; AAH67294.1; -; mRNA.
DR EMBL; AK299933; BAG61766.1; ALT_INIT; mRNA.
DR EMBL; X56465; CAA39837.2; ALT_SEQ; mRNA.
DR CCDS; CCDS35344.1; -. [Q9Y462-1]
DR CCDS; CCDS83481.1; -. [Q9Y462-3]
DR PIR; S25409; S25409.
DR RefSeq; NP_001317503.1; NM_001330574.1. [Q9Y462-3]
DR RefSeq; NP_068838.3; NM_021998.4. [Q9Y462-1]
DR RefSeq; XP_005262243.1; XM_005262186.2.
DR RefSeq; XP_005262244.1; XM_005262187.1. [Q9Y462-3]
DR RefSeq; XP_005262245.1; XM_005262188.1. [Q9Y462-3]
DR RefSeq; XP_005262246.1; XM_005262189.2.
DR RefSeq; XP_011529326.1; XM_011531024.1.
DR RefSeq; XP_011529328.1; XM_011531026.1.
DR RefSeq; XP_016885294.1; XM_017029805.1.
DR RefSeq; XP_016885295.1; XM_017029806.1.
DR RefSeq; XP_016885296.1; XM_017029807.1.
DR RefSeq; XP_016885297.1; XM_017029808.1.
DR RefSeq; XP_016885298.1; XM_017029809.1. [Q9Y462-1]
DR AlphaFoldDB; Q9Y462; -.
DR SMR; Q9Y462; -.
DR BioGRID; 113384; 27.
DR IntAct; Q9Y462; 7.
DR MINT; Q9Y462; -.
DR STRING; 9606.ENSP00000362260; -.
DR iPTMnet; Q9Y462; -.
DR PhosphoSitePlus; Q9Y462; -.
DR BioMuta; ZNF711; -.
DR DMDM; 308153535; -.
DR jPOST; Q9Y462; -.
DR MassIVE; Q9Y462; -.
DR MaxQB; Q9Y462; -.
DR PaxDb; Q9Y462; -.
DR PeptideAtlas; Q9Y462; -.
DR PRIDE; Q9Y462; -.
DR ProteomicsDB; 86107; -. [Q9Y462-1]
DR ProteomicsDB; 86108; -. [Q9Y462-2]
DR ProteomicsDB; 86109; -. [Q9Y462-3]
DR Antibodypedia; 44077; 57 antibodies from 20 providers.
DR DNASU; 7552; -.
DR Ensembl; ENST00000276123.7; ENSP00000276123.3; ENSG00000147180.17. [Q9Y462-1]
DR Ensembl; ENST00000360700.4; ENSP00000353922.4; ENSG00000147180.17. [Q9Y462-3]
DR Ensembl; ENST00000373165.7; ENSP00000362260.3; ENSG00000147180.17. [Q9Y462-1]
DR Ensembl; ENST00000674551.1; ENSP00000502839.1; ENSG00000147180.17. [Q9Y462-3]
DR GeneID; 7552; -.
DR KEGG; hsa:7552; -.
DR MANE-Select; ENST00000674551.1; ENSP00000502839.1; NM_001330574.2; NP_001317503.1. [Q9Y462-3]
DR UCSC; uc004eeo.4; human. [Q9Y462-1]
DR CTD; 7552; -.
DR DisGeNET; 7552; -.
DR GeneCards; ZNF711; -.
DR HGNC; HGNC:13128; ZNF711.
DR HPA; ENSG00000147180; Tissue enhanced (testis).
DR MalaCards; ZNF711; -.
DR MIM; 300803; phenotype.
DR MIM; 314990; gene.
DR neXtProt; NX_Q9Y462; -.
DR OpenTargets; ENSG00000147180; -.
DR Orphanet; 777; X-linked non-syndromic intellectual disability.
DR PharmGKB; PA37702; -.
DR VEuPathDB; HostDB:ENSG00000147180; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000159611; -.
DR HOGENOM; CLU_021097_0_0_1; -.
DR InParanoid; Q9Y462; -.
DR OMA; GTDLPYK; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9Y462; -.
DR TreeFam; TF335557; -.
DR PathwayCommons; Q9Y462; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q9Y462; -.
DR BioGRID-ORCS; 7552; 14 hits in 729 CRISPR screens.
DR ChiTaRS; ZNF711; human.
DR GenomeRNAi; 7552; -.
DR Pharos; Q9Y462; Tbio.
DR PRO; PR:Q9Y462; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9Y462; protein.
DR Bgee; ENSG00000147180; Expressed in endothelial cell and 165 other tissues.
DR Genevisible; Q9Y462; HS.
DR GO; GO:0000785; C:chromatin; ISS:ARUK-UCL.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:ARUK-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:ARUK-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:ARUK-UCL.
DR InterPro; IPR006794; Transcrp_activ_Zfx/Zfy-dom.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 6.
DR Pfam; PF04704; Zfx_Zfy_act; 2.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Intellectual disability;
KW Isopeptide bond; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..761
FT /note="Zinc finger protein 711"
FT /id="PRO_0000047329"
FT ZN_FING 383..408
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 414..436
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 476..499
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 505..527
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 533..556
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 562..584
FT /note="C2H2-type 6; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 590..613
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 619..641
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 647..670
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 676..698
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 704..727
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 733..755
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 224
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 235
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 296
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 306..321
FT /note="RDERRVSRRYEDCQAS -> SCAEIADEVYMEVIVGEEEGTSLPEIQLEDSD
FT VNKTVVPVVWAAAY (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_016912"
FT VAR_SEQ 306
FT /note="R -> SCAEIADEVYMEVIVGEEEGTSLPEIQLEDSDVNKTVVPVVWAAAYG
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039887"
FT VARIANT 139
FT /note="G -> E (in XLID97; unknown pathological
FT significance; dbSNP:rs367654949)"
FT /evidence="ECO:0000269|PubMed:19377476"
FT /id="VAR_062990"
FT VARIANT 221
FT /note="T -> A (in dbSNP:rs148609081)"
FT /evidence="ECO:0000269|PubMed:19377476"
FT /id="VAR_062991"
FT VARIANT 244
FT /note="I -> T (in XLID97; dbSNP:rs1060505033)"
FT /evidence="ECO:0000269|PubMed:27993705"
FT /id="VAR_078572"
FT VARIANT 274
FT /note="H -> R (in XLID97; unknown pathological
FT significance; dbSNP:rs777239465)"
FT /evidence="ECO:0000269|PubMed:19377476"
FT /id="VAR_062992"
FT VARIANT 524
FT /note="M -> T (in dbSNP:rs368788919)"
FT /evidence="ECO:0000269|PubMed:19377476"
FT /id="VAR_062993"
FT VARIANT 601
FT /note="N -> S (in XLID97; unknown pathological
FT significance; dbSNP:rs760346140)"
FT /evidence="ECO:0000269|PubMed:19377476"
FT /id="VAR_062994"
FT VARIANT 622
FT /note="E -> D (in XLID97; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:19377476"
FT /id="VAR_062995"
FT CONFLICT 264..266
FT /note="IVT -> MSP (in Ref. 4; CAA39837)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="R -> K (in Ref. 4; CAA39837)"
FT /evidence="ECO:0000305"
FT CONFLICT 475..476
FT /note="MH -> TD (in Ref. 4; CAA39837)"
FT /evidence="ECO:0000305"
FT CONFLICT 577
FT /note="L -> P (in Ref. 3; BAG61766)"
FT /evidence="ECO:0000305"
FT CONFLICT 648
FT /note="Q -> T (in Ref. 4; CAA39837)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="I -> L (in Ref. 4; CAA39837)"
FT /evidence="ECO:0000305"
FT CONFLICT 680..682
FT /note="RCK -> GCT (in Ref. 4; CAA39837)"
FT /evidence="ECO:0000305"
FT CONFLICT 703
FT /note="I -> S (in Ref. 4; CAA39837)"
FT /evidence="ECO:0000305"
FT CONFLICT 739
FT /note="K -> N (in Ref. 4; CAA39837)"
FT /evidence="ECO:0000305"
FT CONFLICT 754
FT /note="R -> K (in Ref. 4; CAA39837)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 761 AA; 86245 MW; 8E95362C9F008B25 CRC64;
MDSGGGSLGL HTPDSRMAHT MIMQDFVAGM AGTAHIDGDH IVVSVPEAVL VSDVVTDDGI
TLDHGLAAEV VHGPDIITET DVVTEGVIVP EAVLEADVAI EEDLEEDDGD HILTSELITE
TVRVPEQVFV ADLVTGPNGH LEHVVQDCVS GVDSPTMVSE EVLVTNSDTE TVIQAAGGVP
GSTVTIKTED DDDDDVKSTS EDYLMISLDD VGEKLEHMGN TPLKIGSDGS QEDAKEDGFG
SEVIKVYIFK AEAEDDVEIG GTEIVTESEY TSGHSVAGVL DQSRMQREKM VYMAVKDSSQ
EEDDIRDERR VSRRYEDCQA SGNTLDSALE SRSSTAAQYL QICDGINTNK VLKQKAKKRR
RGETRQWQTA VIIGPDGQPL TVYPCHICTK KFKSRGFLKR HMKNHPDHLM RKKYQCTDCD
FTTNKKVSFH NHLESHKLIN KVDKTHEFTE YTRRYREASP LSSNKLILRD KEPKMHKCKY
CDYETAEQGL LNRHLLAVHS KNFPHVCVEC GKGFRHPSEL KKHMRTHTGE KPYQCQYCIF
RCADQSNLKT HIKSKHGNNL PYKCEHCPQA FGDERELQRH LDLFQGHKTH QCPHCDHKST
NSSDLKRHII SVHTKDFPHK CEVCDKGFHR PSELKKHSDI HKGRKIHQCR HCDFKTSDPF
ILSGHILSVH TKDQPLKCKR CKRGFRQQNE LKKHMKTHTG RKIYQCEYCE YSTTDASGFK
RHVISIHTKD YPHRCEFCKK GFRRPSEKNQ HIMRHHKEAL M
