ID   ZN770_HUMAN             Reviewed;         691 AA.
AC   Q6IQ21; Q6ZMZ6; Q9NWV2;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=Zinc finger protein 770;
GN   Name=ZNF770;
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=Placenta;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-181 AND 259-691.
RC   TISSUE=Carcinoma, and Synovium;
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   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-11; LYS-112; LYS-121; LYS-146;
RP   LYS-262; LYS-420; LYS-437 AND LYS-683, 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   -!- 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=BAD18579.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC071603; AAH71603.1; -; mRNA.
DR   EMBL; AK000589; BAA91274.1; ALT_TERM; mRNA.
DR   EMBL; AK131433; BAD18579.1; ALT_INIT; mRNA.
DR   CCDS; CCDS10042.1; -.
DR   RefSeq; NP_054825.2; NM_014106.3.
DR   RefSeq; XP_011520046.1; XM_011521744.2.
DR   AlphaFoldDB; Q6IQ21; -.
DR   SMR; Q6IQ21; -.
DR   BioGRID; 120324; 106.
DR   IntAct; Q6IQ21; 15.
DR   MINT; Q6IQ21; -.
DR   STRING; 9606.ENSP00000348673; -.
DR   iPTMnet; Q6IQ21; -.
DR   PhosphoSitePlus; Q6IQ21; -.
DR   SwissPalm; Q6IQ21; -.
DR   BioMuta; ZNF770; -.
DR   DMDM; 74757996; -.
DR   EPD; Q6IQ21; -.
DR   jPOST; Q6IQ21; -.
DR   MassIVE; Q6IQ21; -.
DR   MaxQB; Q6IQ21; -.
DR   PaxDb; 9606-ENSP00000348673; -.
DR   PeptideAtlas; Q6IQ21; -.
DR   ProteomicsDB; 66477; -.
DR   Pumba; Q6IQ21; -.
DR   Antibodypedia; 9792; 29 antibodies from 10 providers.
DR   DNASU; 54989; -.
DR   Ensembl; ENST00000356321.4; ENSP00000348673.4; ENSG00000198146.4.
DR   GeneID; 54989; -.
DR   KEGG; hsa:54989; -.
DR   MANE-Select; ENST00000356321.4; ENSP00000348673.4; NM_014106.4; NP_054825.2.
DR   UCSC; uc001ziw.4; human.
DR   AGR; HGNC:26061; -.
DR   CTD; 54989; -.
DR   GeneCards; ZNF770; -.
DR   HGNC; HGNC:26061; ZNF770.
DR   HPA; ENSG00000198146; Low tissue specificity.
DR   neXtProt; NX_Q6IQ21; -.
DR   OpenTargets; ENSG00000198146; -.
DR   PharmGKB; PA162410336; -.
DR   VEuPathDB; HostDB:ENSG00000198146; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000161963; -.
DR   HOGENOM; CLU_002678_44_7_1; -.
DR   InParanoid; Q6IQ21; -.
DR   OMA; ENIHTGH; -.
DR   OrthoDB; 5294752at2759; -.
DR   PhylomeDB; Q6IQ21; -.
DR   TreeFam; TF335560; -.
DR   PathwayCommons; Q6IQ21; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   SignaLink; Q6IQ21; -.
DR   BioGRID-ORCS; 54989; 9 hits in 1146 CRISPR screens.
DR   GenomeRNAi; 54989; -.
DR   Pharos; Q6IQ21; Tdark.
DR   PRO; PR:Q6IQ21; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q6IQ21; Protein.
DR   Bgee; ENSG00000198146; Expressed in upper arm skin and 196 other cell types or tissues.
DR   ExpressionAtlas; Q6IQ21; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 9.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR47772:SF4; REDUCED EXPRESSION 2-RELATED; 1.
DR   PANTHER; PTHR47772; ZINC FINGER PROTEIN 200; 1.
DR   Pfam; PF00096; zf-C2H2; 8.
DR   SMART; SM00355; ZnF_C2H2; 11.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 6.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
DR   Genevisible; Q6IQ21; HS.
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..691
FT                   /note="Zinc finger protein 770"
FT                   /id="PRO_0000280436"
FT   ZN_FING         27..49
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         55..77
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         81..103
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         160..182
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         188..210
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         216..238
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         294..318
FT                   /note="C2H2-type 7; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         475..497
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         503..525
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         625..647
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         653..675
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          258..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        11
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        112
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        121
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        146
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        262
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        420
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        437
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        683
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CONFLICT        22
FT                   /note="P -> L (in Ref. 2; BAA91274)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   691 AA;  80007 MW;  1DA3E337BAC06A67 CRC64;
     MMAENNLKML KIQQCVVANK LPRNRPYVCN ICFKHFETPS KLARHYLIHT GQKPFECDVC
     HKTFRQLVHL ERHQLTHSLP FKCSICQRHF KNLKTFVKHQ QLHNETYQNN VKQVRRLLEA
     KQEKSMYGVY NTFTTEERWA LHPCSKSDPM YSMKRRKNIH ACTICGKMFP SQSKLDRHVL
     IHTGQRPFKC VLCTKSFRQS THLKIHQLTH SEERPFQCCF CQKGFKIQSK LLKHKQIHTR
     NKAFRALLLK KRRTESRPLP NKLNANQGGF ENGEIGESEE NNPLDVHSIY IVPFQCPKCE
     KCFESEQILN EHSCFAARSG KIPSRFKRSY NYKTIVKKIL AKLKRARSKK LDNFQSEKKV
     FKKSFLRNCD LISGEQSSEQ TQRTFVGSLG KHGTYKTIGN RKKKTLTLPF SWQNMGKNLK
     GILTTENILS IDNSVNKKDL SICGSSGEEF FNNCEVLQCG FSVPRENIRT RHKICPCDKC
     EKVFPSISKL KRHYLIHTGQ RPFGCNICGK SFRQSAHLKR HEQTHNEKSP YASLCQVEFG
     NFNNLSNHSG NNVNYNASQQ CQAPGVQKYE VSESDQMSGV KAESQDFIPG STGQPCLPNV
     LLESEQSNPF CSYSEHQEKN DVFLYRCSVC AKSFRSPSKL ERHYLIHAGQ KPFECSVCGK
     TFRQAPHWKR HQLTHFKERP QGKVVALDSV M
//