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ZN133_HUMAN
ID   ZN133_HUMAN             Reviewed;         654 AA.
AC   P52736; A8K5S4; B4DHU7; B4DIB8; B7ZAS1; F5H289; J3KQ11; J3KQJ0; Q53XU1;
AC   Q5JXV8; Q9BUV2; Q9H443;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 202.
DE   RecName: Full=Zinc finger protein 133;
DE   AltName: Full=Zinc finger protein 150;
GN   Name=ZNF133; Synonyms=ZNF150;
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), AND VARIANT THR-193.
RC   TISSUE=Insulinoma;
RX   PubMed=7649249; DOI=10.1016/0014-5793(95)00728-r;
RA   Vissing H., Meyer W.-K., Aagaard L., Tommerup N., Thiesen H.-J.;
RT   "Repression of transcriptional activity by heterologous KRAB domains
RT   present in zinc finger proteins.";
RL   FEBS Lett. 369:153-157(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT THR-193.
RC   TISSUE=Insulinoma;
RX   PubMed=7557990; DOI=10.1006/geno.1995.1040;
RA   Tommerup N., Vissing H.;
RT   "Isolation and fine mapping of 16 novel human zinc finger-encoding cDNAs
RT   identify putative candidate genes for developmental and malignant
RT   disorders.";
RL   Genomics 27:259-264(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-193.
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), AND
RP   VARIANT THR-193.
RC   TISSUE=Brain, Caudate nucleus, Hippocampus, and Testis;
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   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-193.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-193.
RC   TISSUE=Lung;
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   [8]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-310; LYS-338; LYS-506; LYS-576;
RP   LYS-604 AND LYS-618, 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 be involved in transcriptional regulation as a repressor.
CC   -!- INTERACTION:
CC       P52736; P01100: FOS; NbExp=4; IntAct=EBI-2687350, EBI-852851;
CC       P52736; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-2687350, EBI-10172290;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=P52736-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P52736-2; Sequence=VSP_039148;
CC       Name=3;
CC         IsoId=P52736-3; Sequence=VSP_055021;
CC       Name=4;
CC         IsoId=P52736-4; Sequence=VSP_055022;
CC       Name=5;
CC         IsoId=P52736-5; Sequence=VSP_055023;
CC   -!- TISSUE SPECIFICITY: Seems ubiquitous. Seen in the heart, brain,
CC       placenta, lung, liver, skeletal muscle, kidney and pancreas.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; U09366; AAC50260.1; -; mRNA.
DR   EMBL; BT007310; AAP35974.1; -; mRNA.
DR   EMBL; AK291389; BAF84078.1; -; mRNA.
DR   EMBL; AK295273; BAG58259.1; -; mRNA.
DR   EMBL; AK295513; BAG58430.1; -; mRNA.
DR   EMBL; AK316386; BAH14757.1; -; mRNA.
DR   EMBL; AL049646; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471133; EAX10250.1; -; Genomic_DNA.
DR   EMBL; CH471133; EAX10251.1; -; Genomic_DNA.
DR   EMBL; CH471133; EAX10252.1; -; Genomic_DNA.
DR   EMBL; CH471133; EAX10253.1; -; Genomic_DNA.
DR   EMBL; BC001887; AAH01887.1; -; mRNA.
DR   CCDS; CCDS13134.1; -. [P52736-2]
DR   CCDS; CCDS63233.1; -. [P52736-5]
DR   CCDS; CCDS63234.1; -. [P52736-1]
DR   CCDS; CCDS63235.1; -. [P52736-4]
DR   CCDS; CCDS74703.1; -. [P52736-3]
DR   CCDS; CCDS74704.1; -. [P52736-3]
DR   PIR; A57785; A57785.
DR   RefSeq; NP_001076799.1; NM_001083330.2. [P52736-2]
DR   RefSeq; NP_001269924.1; NM_001282995.1. [P52736-2]
DR   RefSeq; NP_001269926.1; NM_001282997.1. [P52736-1]
DR   RefSeq; NP_001269927.1; NM_001282998.1. [P52736-1]
DR   RefSeq; NP_001269928.1; NM_001282999.1. [P52736-1]
DR   RefSeq; NP_001269929.1; NM_001283000.1. [P52736-1]
DR   RefSeq; NP_001269930.1; NM_001283001.1. [P52736-1]
DR   RefSeq; NP_001269937.1; NM_001283008.1. [P52736-3]
DR   RefSeq; NP_003425.2; NM_003434.5. [P52736-2]
DR   RefSeq; XP_005260876.1; XM_005260819.1.
DR   RefSeq; XP_005260877.1; XM_005260820.4.
DR   RefSeq; XP_011527638.1; XM_011529336.1.
DR   RefSeq; XP_011527639.1; XM_011529337.1. [P52736-1]
DR   RefSeq; XP_011527640.1; XM_011529338.2.
DR   RefSeq; XP_011527641.1; XM_011529339.1. [P52736-1]
DR   RefSeq; XP_016883530.1; XM_017028041.1. [P52736-5]
DR   RefSeq; XP_016883531.1; XM_017028042.1. [P52736-5]
DR   RefSeq; XP_016883533.1; XM_017028044.1.
DR   RefSeq; XP_016883534.1; XM_017028045.1.
DR   RefSeq; XP_016883535.1; XM_017028046.1.
DR   RefSeq; XP_016883536.1; XM_017028047.1. [P52736-1]
DR   RefSeq; XP_016883537.1; XM_017028048.1. [P52736-1]
DR   RefSeq; XP_016883538.1; XM_017028049.1.
DR   RefSeq; XP_016883539.1; XM_017028050.1.
DR   RefSeq; XP_016883540.1; XM_017028051.1.
DR   RefSeq; XP_016883541.1; XM_017028052.1.
DR   RefSeq; XP_016883542.1; XM_017028053.1.
DR   RefSeq; XP_016883543.1; XM_017028054.1.
DR   RefSeq; XP_016883544.1; XM_017028055.1.
DR   RefSeq; XP_016883545.1; XM_017028056.1.
DR   RefSeq; XP_016883546.1; XM_017028057.1.
DR   AlphaFoldDB; P52736; -.
DR   SMR; P52736; -.
DR   BioGRID; 113487; 27.
DR   IntAct; P52736; 22.
DR   MINT; P52736; -.
DR   STRING; 9606.ENSP00000439427; -.
DR   iPTMnet; P52736; -.
DR   PhosphoSitePlus; P52736; -.
DR   BioMuta; ZNF133; -.
DR   DMDM; 116242855; -.
DR   MassIVE; P52736; -.
DR   MaxQB; P52736; -.
DR   PaxDb; P52736; -.
DR   PeptideAtlas; P52736; -.
DR   PRIDE; P52736; -.
DR   ProteomicsDB; 25897; -.
DR   ProteomicsDB; 56508; -. [P52736-1]
DR   ProteomicsDB; 56509; -. [P52736-2]
DR   Antibodypedia; 814; 183 antibodies from 19 providers.
DR   DNASU; 7692; -.
DR   Ensembl; ENST00000316358.8; ENSP00000346090.3; ENSG00000125846.16. [P52736-1]
DR   Ensembl; ENST00000377671.7; ENSP00000366899.3; ENSG00000125846.16. [P52736-2]
DR   Ensembl; ENST00000396026.7; ENSP00000400897.3; ENSG00000125846.16. [P52736-2]
DR   Ensembl; ENST00000401790.5; ENSP00000383945.1; ENSG00000125846.16. [P52736-1]
DR   Ensembl; ENST00000402618.6; ENSP00000385279.2; ENSG00000125846.16. [P52736-4]
DR   Ensembl; ENST00000425686.3; ENSP00000406638.2; ENSG00000125846.16. [P52736-1]
DR   Ensembl; ENST00000622607.4; ENSP00000481326.1; ENSG00000125846.16. [P52736-1]
DR   Ensembl; ENST00000628216.2; ENSP00000487315.1; ENSG00000125846.16. [P52736-5]
DR   Ensembl; ENST00000630056.1; ENSP00000485741.1; ENSG00000125846.16. [P52736-3]
DR   GeneID; 7692; -.
DR   KEGG; hsa:7692; -.
DR   MANE-Select; ENST00000425686.3; ENSP00000406638.2; NM_001352452.2; NP_001339381.2.
DR   UCSC; uc002wql.6; human. [P52736-1]
DR   CTD; 7692; -.
DR   DisGeNET; 7692; -.
DR   GeneCards; ZNF133; -.
DR   HGNC; HGNC:12917; ZNF133.
DR   HPA; ENSG00000125846; Low tissue specificity.
DR   MIM; 604075; gene.
DR   neXtProt; NX_P52736; -.
DR   OpenTargets; ENSG00000125846; -.
DR   PharmGKB; PA134900961; -.
DR   VEuPathDB; HostDB:ENSG00000125846; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000162260; -.
DR   HOGENOM; CLU_002678_44_5_1; -.
DR   InParanoid; P52736; -.
DR   OMA; CKECGWC; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; P52736; -.
DR   TreeFam; TF338096; -.
DR   PathwayCommons; P52736; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   SignaLink; P52736; -.
DR   BioGRID-ORCS; 7692; 64 hits in 1108 CRISPR screens.
DR   ChiTaRS; ZNF133; human.
DR   GeneWiki; ZNF133; -.
DR   GenomeRNAi; 7692; -.
DR   Pharos; P52736; Tbio.
DR   PRO; PR:P52736; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; P52736; protein.
DR   Bgee; ENSG00000125846; Expressed in cerebellar hemisphere and 184 other tissues.
DR   ExpressionAtlas; P52736; baseline and differential.
DR   Genevisible; P52736; HS.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; 13.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 15.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 8.
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   Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..654
FT                   /note="Zinc finger protein 133"
FT                   /id="PRO_0000047417"
FT   DOMAIN          1..72
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         214..236
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         242..264
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         270..292
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         298..320
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         326..348
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         354..376
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         382..404
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         410..432
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         438..460
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         466..488
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         494..516
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         522..544
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         550..572
FT                   /note="C2H2-type 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         578..600
FT                   /note="C2H2-type 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         606..631
FT                   /note="C2H2-type 15; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          119..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          622..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        310
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        338
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        506
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        576
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        604
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        618
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         1..95
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055021"
FT   VAR_SEQ         1..72
FT                   /note="MAFRDVAVDFTQDEWRLLSPAQRTLYREVMLENYSNLVSLGISFSKPELITQ
FT                   LEQGKETWREEKKCSPATCP -> MCNGRKTVL (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055022"
FT   VAR_SEQ         1
FT                   /note="M -> MAHM (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055023"
FT   VAR_SEQ         73
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT                   /id="VSP_039148"
FT   VARIANT         193
FT                   /note="S -> T (in dbSNP:rs1033545)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7557990,
FT                   ECO:0000269|PubMed:7649249, ECO:0000269|Ref.3,
FT                   ECO:0000269|Ref.6"
FT                   /id="VAR_028228"
FT   VARIANT         194
FT                   /note="G -> E (in dbSNP:rs2228273)"
FT                   /id="VAR_028229"
FT   CONFLICT        228
FT                   /note="N -> S (in Ref. 4; BAG58259)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        363
FT                   /note="F -> Y (in Ref. 4; BAG58430)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   654 AA;  73388 MW;  CF1D47B223A6DD84 CRC64;
     MAFRDVAVDF TQDEWRLLSP AQRTLYREVM LENYSNLVSL GISFSKPELI TQLEQGKETW
     REEKKCSPAT CPADPEPELY LDPFCPPGFS SQKFPMQHVL CNHPPWIFTC LCAEGNIQPG
     DPGPGDQEKQ QQASEGRPWS DQAEGPEGEG AMPLFGRTKK RTLGAFSRPP QRQPVSSRNG
     LRGVELEASP AQSGNPEETD KLLKRIEVLG FGTVNCGECG LSFSKMTNLL SHQRIHSGEK
     PYVCGVCEKG FSLKKSLARH QKAHSGEKPI VCRECGRGFN RKSTLIIHER THSGEKPYMC
     SECGRGFSQK SNLIIHQRTH SGEKPYVCRE CGKGFSQKSA VVRHQRTHLE EKTIVCSDCG
     LGFSDRSNLI SHQRTHSGEK PYACKECGRC FRQRTTLVNH QRTHSKEKPY VCGVCGHSFS
     QNSTLISHRR THTGEKPYVC GVCGRGFSLK SHLNRHQNIH SGEKPIVCKD CGRGFSQQSN
     LIRHQRTHSG EKPMVCGECG RGFSQKSNLV AHQRTHSGER PYVCRECGRG FSHQAGLIRH
     KRKHSREKPY MCRQCGLGFG NKSALITHKR AHSEEKPCVC RECGQGFLQK SHLTLHQMTH
     TGEKPYVCKT CGRGFSLKSH LSRHRKTTSV HHRLPVQPDP EPCAGQPSDS LYSL
 
 
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