ZN770_HUMAN
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 03-AUG-2022, entry version 154.
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 101.
DR IntAct; Q6IQ21; 14.
DR STRING; 9606.ENSP00000348673; -.
DR iPTMnet; Q6IQ21; -.
DR PhosphoSitePlus; Q6IQ21; -.
DR BioMuta; ZNF770; -.
DR DMDM; 74757996; -.
DR EPD; Q6IQ21; -.
DR jPOST; Q6IQ21; -.
DR MassIVE; Q6IQ21; -.
DR MaxQB; Q6IQ21; -.
DR PaxDb; Q6IQ21; -.
DR PeptideAtlas; Q6IQ21; -.
DR PRIDE; Q6IQ21; -.
DR ProteomicsDB; 66477; -.
DR Antibodypedia; 9792; 19 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 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; 1318335at2759; -.
DR PhylomeDB; Q6IQ21; -.
DR TreeFam; TF335560; -.
DR PathwayCommons; Q6IQ21; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q6IQ21; -.
DR BioGRID-ORCS; 54989; 8 hits in 1067 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 194 other tissues.
DR ExpressionAtlas; Q6IQ21; baseline and differential.
DR Genevisible; Q6IQ21; HS.
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 InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 8.
DR SMART; SM00355; ZnF_C2H2; 11.
DR SUPFAM; SSF57667; SSF57667; 6.
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..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
