ZFP37_HUMAN
ID ZFP37_HUMAN Reviewed; 630 AA.
AC Q9Y6Q3; A0AVJ9; B4DVX4; G3V3L7; Q5T7Q4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Zinc finger protein 37 homolog;
DE Short=Zfp-37;
GN Name=ZFP37;
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).
RC TISSUE=Cartilage;
RX PubMed=9585434; DOI=10.1007/s003359900796;
RA Dreyer S.D., Zhou L., Machado M.A., Horton W.A., Zabel B., Winterpacht A.,
RA Lee B.;
RT "Cloning, characterization, and chromosomal assignment of the human
RT ortholog of murine Zfp-37, a candidate gene for Nager syndrome.";
RL Mamm. Genome 9:458-462(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ASP-7.
RC TISSUE=Spleen;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASP-7.
RC TISSUE=Brain;
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).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y6Q3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y6Q3-2; Sequence=VSP_037941;
CC Name=3;
CC IsoId=Q9Y6Q3-3; Sequence=VSP_055044;
CC -!- TISSUE SPECIFICITY: Expressed at low level in several tissues including
CC fetal cartilage.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-34 is the initiator.
CC Orthologous sequences start at a downstream Met. {ECO:0000305}.
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DR EMBL; AF022158; AAC28425.1; -; mRNA.
DR EMBL; AK301275; BAG62836.1; -; mRNA.
DR EMBL; AL162588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH878453; EAW50556.1; -; Genomic_DNA.
DR EMBL; BC126390; AAI26391.1; -; mRNA.
DR CCDS; CCDS65109.1; -. [Q9Y6Q3-3]
DR CCDS; CCDS65110.1; -. [Q9Y6Q3-2]
DR CCDS; CCDS6787.1; -. [Q9Y6Q3-1]
DR RefSeq; NP_001269444.1; NM_001282515.1. [Q9Y6Q3-2]
DR RefSeq; NP_001269447.1; NM_001282518.1. [Q9Y6Q3-3]
DR RefSeq; NP_003399.1; NM_003408.2. [Q9Y6Q3-1]
DR AlphaFoldDB; Q9Y6Q3; -.
DR SMR; Q9Y6Q3; -.
DR BioGRID; 113371; 4.
DR IntAct; Q9Y6Q3; 2.
DR STRING; 9606.ENSP00000452552; -.
DR iPTMnet; Q9Y6Q3; -.
DR PhosphoSitePlus; Q9Y6Q3; -.
DR BioMuta; ZFP37; -.
DR DMDM; 257051078; -.
DR EPD; Q9Y6Q3; -.
DR jPOST; Q9Y6Q3; -.
DR MassIVE; Q9Y6Q3; -.
DR MaxQB; Q9Y6Q3; -.
DR PaxDb; Q9Y6Q3; -.
DR PeptideAtlas; Q9Y6Q3; -.
DR PRIDE; Q9Y6Q3; -.
DR ProteomicsDB; 32981; -.
DR ProteomicsDB; 86761; -. [Q9Y6Q3-1]
DR ProteomicsDB; 86762; -. [Q9Y6Q3-2]
DR Antibodypedia; 29718; 115 antibodies from 17 providers.
DR DNASU; 7539; -.
DR Ensembl; ENST00000374227.8; ENSP00000363344.3; ENSG00000136866.14. [Q9Y6Q3-1]
DR Ensembl; ENST00000553380.1; ENSP00000452552.1; ENSG00000136866.14. [Q9Y6Q3-2]
DR Ensembl; ENST00000555206.5; ENSP00000451310.1; ENSG00000136866.14. [Q9Y6Q3-3]
DR GeneID; 7539; -.
DR KEGG; hsa:7539; -.
DR MANE-Select; ENST00000374227.8; ENSP00000363344.3; NM_003408.3; NP_003399.1.
DR UCSC; uc004bgm.3; human. [Q9Y6Q3-1]
DR CTD; 7539; -.
DR DisGeNET; 7539; -.
DR GeneCards; ZFP37; -.
DR HGNC; HGNC:12863; ZFP37.
DR HPA; ENSG00000136866; Low tissue specificity.
DR MIM; 602951; gene.
DR neXtProt; NX_Q9Y6Q3; -.
DR OpenTargets; ENSG00000136866; -.
DR PharmGKB; PA37452; -.
DR VEuPathDB; HostDB:ENSG00000136866; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162711; -.
DR HOGENOM; CLU_002678_44_5_1; -.
DR InParanoid; Q9Y6Q3; -.
DR OMA; QCGKAHS; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9Y6Q3; -.
DR TreeFam; TF350860; -.
DR PathwayCommons; Q9Y6Q3; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q9Y6Q3; -.
DR BioGRID-ORCS; 7539; 17 hits in 1093 CRISPR screens.
DR GenomeRNAi; 7539; -.
DR Pharos; Q9Y6Q3; Tbio.
DR PRO; PR:Q9Y6Q3; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9Y6Q3; protein.
DR Bgee; ENSG00000136866; Expressed in cortical plate and 121 other tissues.
DR Genevisible; Q9Y6Q3; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:UniProtKB.
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: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: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 GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS: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; 11.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 11.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE 2: Evidence at transcript level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..630
FT /note="Zinc finger protein 37 homolog"
FT /id="PRO_0000047293"
FT DOMAIN 32..103
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 293..315
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 321..343
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 349..367
FT /note="C2H2-type 3; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 377..399
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 405..427
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 433..455
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 461..483
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 489..511
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 517..539
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 545..567
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 573..595
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 601..623
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88553"
FT VAR_SEQ 44
FT /note="A -> AVSVTFKHVTMAFTQK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037941"
FT VAR_SEQ 44
FT /note="A -> AK (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_055044"
FT VARIANT 7
FT /note="V -> D (in dbSNP:rs2282076)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_058701"
FT CONFLICT 160
FT /note="K -> KK (in Ref. 2; BAG62836)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="K -> R (in Ref. 2; BAG62836)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="H -> R (in Ref. 2; BAG62836)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="C -> F (in Ref. 2; BAG62836)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 630 AA; 71209 MW; 91AB6D25BB0B9C9D CRC64;
MSVSSGVQIL TKPETVDRRR SAETTKEAGR PLEMAVSEPE ASAAEWKQLD PAQSNLYNDV
MLENYCNQAS MGCQAPKPDM ISKLEKGEAP WLGKGKRPSQ GCPSKIARPK QKETDGKVQK
DDDQLENIQK SQNKLLREVA VKKKTQAKKN GSDCGSLGKK NNLHKKHVPS KKRLLKFESC
GKILKQNLDL PDHSRNCVKR KSDAAKEHKK SFNHSLSDTR KGKKQTGKKH EKLSSHSSSD
KCNKTGKKHD KLCCHSSSHI KQDKIQTGEK HEKSPSLSSS TKHEKPQACV KPYECNQCGK
VLSHKQGLID HQRVHTGEKP YECNECGIAF SQKSHLVVHQ RTHTGEKPYE CIQCGKAHGH
KHALTDHLRI HTGEKPYECA ECGKTFRHSS NLIQHVRSHT GEKPYECKEC GKSFRYNSSL
TEHVRTHTGE IPYECNECGK AFKYSSSLTK HMRIHTGEKP FECNECGKAF SKKSHLIIHQ
RTHTKEKPYK CNECGKAFGH SSSLTYHMRT HTGESPFECN QCGKGFKQIE GLTQHQRVHT
GEKPYECNEC GKAFSQKSHL IVHQRTHTGE KPYECNECEK AFNAKSQLVI HQRSHTGEKP
YECNECGKTF KQNASLTKHV KTHSEDKSHE