ZN627_HUMAN
ID ZN627_HUMAN Reviewed; 461 AA.
AC Q7L945; O14846; Q4KMP9; Q6NT81; Q9BRG4;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Zinc finger protein 627;
GN Name=ZNF627;
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].
RC TISSUE=Teratocarcinoma;
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 MRNA].
RC TISSUE=Ovary, and Uterus;
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 [MRNA] OF 146-204.
RX PubMed=12016960;
RA Sun X.Y., Yu L., Wu G.J., Fan Y.X., Zheng Q.P., Hu P.R., Zhang M.,
RA Jiang Y., Liu S., Xu Y.F., Zhao S.Y.;
RT "Isolation of novel expression sequences of C2H2 type zinc finger protein
RT gene from human brain tissue according to the conservation of zinc finger
RT motif.";
RL Shi Yan Sheng Wu Xue Bao 31:377-378(1998).
RN [4]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-99 AND LYS-439, 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).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- INTERACTION:
CC Q7L945; O95273: CCNDBP1; NbExp=4; IntAct=EBI-2797561, EBI-748961;
CC Q7L945; Q13077: TRAF1; NbExp=3; IntAct=EBI-2797561, EBI-359224;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH06279.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH98416.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK074846; BAC11240.1; -; mRNA.
DR EMBL; BC006279; AAH06279.2; ALT_INIT; mRNA.
DR EMBL; BC069232; AAH69232.2; -; mRNA.
DR EMBL; BC098416; AAH98416.1; ALT_INIT; mRNA.
DR EMBL; AF024694; AAB81084.1; -; mRNA.
DR CCDS; CCDS42502.1; -.
DR RefSeq; NP_001277012.1; NM_001290083.1.
DR RefSeq; NP_001277013.1; NM_001290084.1.
DR RefSeq; NP_001277014.1; NM_001290085.1.
DR RefSeq; NP_660338.1; NM_145295.3.
DR AlphaFoldDB; Q7L945; -.
DR SMR; Q7L945; -.
DR BioGRID; 128262; 23.
DR IntAct; Q7L945; 9.
DR STRING; 9606.ENSP00000354414; -.
DR iPTMnet; Q7L945; -.
DR PhosphoSitePlus; Q7L945; -.
DR BioMuta; ZNF627; -.
DR DMDM; 74759019; -.
DR EPD; Q7L945; -.
DR jPOST; Q7L945; -.
DR MassIVE; Q7L945; -.
DR MaxQB; Q7L945; -.
DR PaxDb; Q7L945; -.
DR PeptideAtlas; Q7L945; -.
DR PRIDE; Q7L945; -.
DR ProteomicsDB; 68842; -.
DR Antibodypedia; 6931; 71 antibodies from 17 providers.
DR DNASU; 199692; -.
DR Ensembl; ENST00000361113.10; ENSP00000354414.4; ENSG00000198551.10.
DR GeneID; 199692; -.
DR KEGG; hsa:199692; -.
DR MANE-Select; ENST00000361113.10; ENSP00000354414.4; NM_145295.4; NP_660338.1.
DR UCSC; uc002msk.3; human.
DR CTD; 199692; -.
DR DisGeNET; 199692; -.
DR GeneCards; ZNF627; -.
DR HGNC; HGNC:30570; ZNF627.
DR HPA; ENSG00000198551; Low tissue specificity.
DR MalaCards; ZNF627; -.
DR MIM; 612248; gene.
DR neXtProt; NX_Q7L945; -.
DR OpenTargets; ENSG00000198551; -.
DR PharmGKB; PA134903355; -.
DR VEuPathDB; HostDB:ENSG00000198551; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000164244; -.
DR HOGENOM; CLU_002678_0_10_1; -.
DR InParanoid; Q7L945; -.
DR OMA; RSTYFRI; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q7L945; -.
DR TreeFam; TF338854; -.
DR PathwayCommons; Q7L945; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q7L945; -.
DR BioGRID-ORCS; 199692; 10 hits in 1095 CRISPR screens.
DR ChiTaRS; ZNF627; human.
DR GenomeRNAi; 199692; -.
DR Pharos; Q7L945; Tdark.
DR PRO; PR:Q7L945; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q7L945; protein.
DR Bgee; ENSG00000198551; Expressed in ganglionic eminence and 176 other tissues.
DR ExpressionAtlas; Q7L945; baseline and differential.
DR Genevisible; Q7L945; HS.
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: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: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; 5.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 11.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..461
FT /note="Zinc finger protein 627"
FT /id="PRO_0000280425"
FT DOMAIN 4..80
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 99..123
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 167..189
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 195..217
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 223..245
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 251..273
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 279..301
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 307..329
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 335..357
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 363..385
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 391..413
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 419..441
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 99
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 439
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 172
FT /note="C -> V (in Ref. 3; AAB81084)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="P -> T (in Ref. 3; AAB81084)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="H -> R (in Ref. 2; AAH98416)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 461 AA; 52853 MW; 3440788DBB79A24A CRC64;
MDSVAFEDVA VNFTLEEWAL LDPSQKNLYR DVMRETFRNL ASVGKQWEDQ NIEDPFKIPR
RNISHIPERL CESKEGGQGE ETFSQIPDGI LNKKTPGVKP CESSVCGEVG MGPSSLNRHI
RDHTGREPNE YQEYGKKSYT RNQCGRALSY HRSFPVRERT HPGGKPYDCK ECGETFISLV
SIRRHMLTHR GGVPYKCKVC GKAFDYPSLF RIHERSHTGE KPYECKQCGK AFSCSSYIRI
HERTHTGDKP YECKQCGKAF SCSKYIRIHE RTHTGEKPYE CKQCGKAFRC ASSVRSHERT
HTGEKLFECK ECGKALTCLA SVRRHMIKHT GNGPYKCKVC GKAFDFPSSF RIHERTHTGE
KPYDCKQCGK AFSCSSSFRK HERIHTGEKP YKCTKCGKAF SRSSYFRIHE RTHTGEKPYE
CKQCGKAFSR STYFRVHEKI HTGEKPYENP NPNASVVPVL S
