ZN337_HUMAN
ID ZN337_HUMAN Reviewed; 751 AA.
AC Q9Y3M9; B4DSM2; Q9Y3Y5;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Zinc finger protein 337;
GN Name=ZNF337;
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] (ISOFORM 2).
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 256-751 (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-458, 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 [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-458, AND IDENTIFICATION BY MASS
RP 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: May be involved in transcriptional regulation.
CC -!- INTERACTION:
CC Q9Y3M9; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-714987, EBI-739580;
CC Q9Y3M9; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-714987, EBI-11977221;
CC Q9Y3M9; Q14749: GNMT; NbExp=3; IntAct=EBI-714987, EBI-744239;
CC Q9Y3M9; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-714987, EBI-2549423;
CC Q9Y3M9; Q6A162: KRT40; NbExp=3; IntAct=EBI-714987, EBI-10171697;
CC Q9Y3M9; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-714987, EBI-10172290;
CC Q9Y3M9; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-714987, EBI-742948;
CC Q9Y3M9; Q96KN7: RPGRIP1; NbExp=3; IntAct=EBI-714987, EBI-1050213;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y3M9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y3M9-2; Sequence=VSP_055949;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AK299811; BAG61684.1; -; mRNA.
DR EMBL; AL031673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021298; AAH21298.1; -; mRNA.
DR EMBL; AL049942; CAB43216.1; -; mRNA.
DR CCDS; CCDS13174.1; -. [Q9Y3M9-1]
DR PIR; T08674; T08674.
DR RefSeq; NP_001277190.1; NM_001290261.1. [Q9Y3M9-1]
DR RefSeq; NP_056470.1; NM_015655.3. [Q9Y3M9-1]
DR RefSeq; XP_005260759.1; XM_005260702.3. [Q9Y3M9-2]
DR RefSeq; XP_006723621.1; XM_006723558.3. [Q9Y3M9-1]
DR RefSeq; XP_011527521.1; XM_011529219.2. [Q9Y3M9-1]
DR RefSeq; XP_016883291.1; XM_017027802.1.
DR RefSeq; XP_016883292.1; XM_017027803.1. [Q9Y3M9-2]
DR AlphaFoldDB; Q9Y3M9; -.
DR SMR; Q9Y3M9; -.
DR BioGRID; 117583; 14.
DR IntAct; Q9Y3M9; 12.
DR MINT; Q9Y3M9; -.
DR STRING; 9606.ENSP00000365619; -.
DR iPTMnet; Q9Y3M9; -.
DR PhosphoSitePlus; Q9Y3M9; -.
DR BioMuta; ZNF337; -.
DR DMDM; 20141069; -.
DR EPD; Q9Y3M9; -.
DR jPOST; Q9Y3M9; -.
DR MassIVE; Q9Y3M9; -.
DR MaxQB; Q9Y3M9; -.
DR PaxDb; Q9Y3M9; -.
DR PeptideAtlas; Q9Y3M9; -.
DR PRIDE; Q9Y3M9; -.
DR ProteomicsDB; 5036; -.
DR ProteomicsDB; 86050; -. [Q9Y3M9-1]
DR Antibodypedia; 10099; 142 antibodies from 23 providers.
DR DNASU; 26152; -.
DR Ensembl; ENST00000252979.6; ENSP00000252979.5; ENSG00000130684.14. [Q9Y3M9-1]
DR Ensembl; ENST00000376436.5; ENSP00000365619.1; ENSG00000130684.14. [Q9Y3M9-1]
DR GeneID; 26152; -.
DR KEGG; hsa:26152; -.
DR MANE-Select; ENST00000252979.6; ENSP00000252979.5; NM_015655.4; NP_056470.1.
DR UCSC; uc002wva.4; human. [Q9Y3M9-1]
DR CTD; 26152; -.
DR DisGeNET; 26152; -.
DR GeneCards; ZNF337; -.
DR HGNC; HGNC:15809; ZNF337.
DR HPA; ENSG00000130684; Low tissue specificity.
DR neXtProt; NX_Q9Y3M9; -.
DR OpenTargets; ENSG00000130684; -.
DR PharmGKB; PA38043; -.
DR VEuPathDB; HostDB:ENSG00000130684; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000164820; -.
DR HOGENOM; CLU_002678_44_5_1; -.
DR InParanoid; Q9Y3M9; -.
DR OMA; KTVMGPQ; -.
DR OrthoDB; 908238at2759; -.
DR PhylomeDB; Q9Y3M9; -.
DR TreeFam; TF343410; -.
DR PathwayCommons; Q9Y3M9; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q9Y3M9; -.
DR BioGRID-ORCS; 26152; 7 hits in 1099 CRISPR screens.
DR ChiTaRS; ZNF337; human.
DR GenomeRNAi; 26152; -.
DR Pharos; Q9Y3M9; Tdark.
DR PRO; PR:Q9Y3M9; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9Y3M9; protein.
DR Bgee; ENSG00000130684; Expressed in cerebellar hemisphere and 203 other tissues.
DR Genevisible; Q9Y3M9; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
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; 15.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 20.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 12.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 19.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 20.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..751
FT /note="Zinc finger protein 337"
FT /id="PRO_0000047540"
FT DOMAIN 12..83
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 180..202
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 208..230
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 236..258
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 264..286
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 292..314
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 320..342
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 348..370
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 376..398
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 404..426
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 432..454
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 460..482
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 488..510
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 516..538
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 544..566
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 572..594
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 600..622
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 628..650
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 656..679
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 685..707
FT /note="C2H2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 713..735
FT /note="C2H2-type 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 101..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 458
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 VAR_SEQ 52..83
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055949"
FT VARIANT 17
FT /note="V -> I (in dbSNP:rs926487)"
FT /id="VAR_024213"
FT VARIANT 467
FT /note="R -> G (in dbSNP:rs16987972)"
FT /id="VAR_052814"
FT CONFLICT 476
FT /note="T -> A (in Ref. 4; CAB43216)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="E -> V (in Ref. 4; CAB43216)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 751 AA; 86875 MW; 482D9F9A57EC980E CRC64;
MGPQGARRQA FLAFGDVTVD FTQKEWRLLS PAQRALYREV TLENYSHLVS LGILHSKPEL
IRRLEQGEVP WGEERRRRPG PCAGIYAEHV LRPKNLGLAH QRQQQLQFSD QSFQSDTAEG
QEKEKSTKPM AFSSPPLRHA VSSRRRNSVV EIESSQGQRE NPTEIDKVLK GIENSRWGAF
KCAERGQDFS RKMMVIIHKK AHSRQKLFTC RECHQGFRDE SALLLHQNTH TGEKSYVCSV
CGRGFSLKAN LLRHQRTHSG EKPFLCKVCG RGYTSKSYLT VHERTHTGEK PYECQECGRR
FNDKSSYNKH LKAHSGEKPF VCKECGRGYT NKSYFVVHKR IHSGEKPYRC QECGRGFSNK
SHLITHQRTH SGEKPFACRQ CKQSFSVKGS LLRHQRTHSG EKPFVCKDCE RSFSQKSTLV
YHQRTHSGEK PFVCRECGQG FIQKSTLVKH QITHSEEKPF VCKDCGRGFI QKSTFTLHQR
THSEEKPYGC RECGRRFRDK SSYNKHLRAH LGEKRFFCRD CGRGFTLKPN LTIHQRTHSG
EKPFMCKQCE KSFSLKANLL RHQWTHSGER PFNCKDCGRG FILKSTLLFH QKTHSGEKPF
ICSECGQGFI WKSNLVKHQL AHSGKQPFVC KECGRGFNWK GNLLTHQRTH SGEKPFVCNV
CGQGFSWKRS LTRHHWRIHS KEKPFVCQEC KRGYTSKSDL TVHERIHTGE RPYECQECGR
KFSNKSYYSK HLKRHLREKR FCTGSVGEAS S
