ZFP1_HUMAN
ID ZFP1_HUMAN Reviewed; 407 AA.
AC Q6P2D0; A8K5Q7; B4DKG9; Q8N188; Q8N9F9;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Zinc finger protein 1 homolog;
DE Short=Zfp-1;
DE AltName: Full=Zinc finger protein 475;
GN Name=ZFP1; Synonyms=ZNF475;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Thalamus;
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].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [4]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-114 AND LYS-145, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-145, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-145, 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 [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-74; LYS-114 AND LYS-145, 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 Q6P2D0; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-2555749, EBI-3866279;
CC Q6P2D0; Q6NZI2: CAVIN1; NbExp=3; IntAct=EBI-2555749, EBI-2559016;
CC Q6P2D0; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-2555749, EBI-11977221;
CC Q6P2D0; Q96LK0: CEP19; NbExp=3; IntAct=EBI-2555749, EBI-741885;
CC Q6P2D0; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-2555749, EBI-739624;
CC Q6P2D0; Q96Q77: CIB3; NbExp=3; IntAct=EBI-2555749, EBI-10292696;
CC Q6P2D0; Q8IUI8: CRLF3; NbExp=3; IntAct=EBI-2555749, EBI-2872414;
CC Q6P2D0; P50402: EMD; NbExp=3; IntAct=EBI-2555749, EBI-489887;
CC Q6P2D0; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-2555749, EBI-5916454;
CC Q6P2D0; P54257: HAP1; NbExp=3; IntAct=EBI-2555749, EBI-712814;
CC Q6P2D0; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-2555749, EBI-10961706;
CC Q6P2D0; Q6A162: KRT40; NbExp=3; IntAct=EBI-2555749, EBI-10171697;
CC Q6P2D0; O95751: LDOC1; NbExp=3; IntAct=EBI-2555749, EBI-740738;
CC Q6P2D0; Q9NYL2-2: MAP3K20; NbExp=4; IntAct=EBI-2555749, EBI-10255081;
CC Q6P2D0; P55081: MFAP1; NbExp=3; IntAct=EBI-2555749, EBI-1048159;
CC Q6P2D0; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-2555749, EBI-11522433;
CC Q6P2D0; P78424: POU6F2; NbExp=3; IntAct=EBI-2555749, EBI-12029004;
CC Q6P2D0; Q86TI0: TBC1D1; NbExp=3; IntAct=EBI-2555749, EBI-1644036;
CC Q6P2D0; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-2555749, EBI-725997;
CC Q6P2D0; Q9H2G4: TSPYL2; NbExp=3; IntAct=EBI-2555749, EBI-947459;
CC Q6P2D0; P15622-3: ZNF250; NbExp=3; IntAct=EBI-2555749, EBI-10177272;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P08042}.
CC Note=Shows widespread expression throughout the nucleus, but appears to
CC be excluded from nucleoli. {ECO:0000250|UniProtKB:P08042}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P2D0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P2D0-2; Sequence=VSP_012682;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH33774.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK094761; BAC04417.1; -; mRNA.
DR EMBL; AK291372; BAF84061.1; -; mRNA.
DR EMBL; AK296560; BAG59181.1; -; mRNA.
DR EMBL; CH471114; EAW95663.1; -; Genomic_DNA.
DR EMBL; BC064604; AAH64604.1; -; mRNA.
DR EMBL; BC033774; AAH33774.1; ALT_INIT; mRNA.
DR CCDS; CCDS10914.2; -. [Q6P2D0-1]
DR RefSeq; NP_001305398.1; NM_001318469.1. [Q6P2D0-1]
DR RefSeq; NP_001305400.1; NM_001318471.1.
DR RefSeq; NP_001305401.1; NM_001318472.1.
DR RefSeq; NP_001305402.1; NM_001318473.1. [Q6P2D0-2]
DR RefSeq; NP_001305403.1; NM_001318474.1. [Q6P2D0-2]
DR RefSeq; NP_001305404.1; NM_001318475.1.
DR RefSeq; NP_001305405.1; NM_001318476.1.
DR RefSeq; NP_710155.2; NM_153688.3. [Q6P2D0-1]
DR RefSeq; XP_016878473.1; XM_017022984.1. [Q6P2D0-1]
DR RefSeq; XP_016878474.1; XM_017022985.1. [Q6P2D0-1]
DR RefSeq; XP_016878476.1; XM_017022987.1. [Q6P2D0-2]
DR AlphaFoldDB; Q6P2D0; -.
DR SMR; Q6P2D0; -.
DR BioGRID; 127811; 39.
DR IntAct; Q6P2D0; 32.
DR STRING; 9606.ENSP00000377080; -.
DR iPTMnet; Q6P2D0; -.
DR PhosphoSitePlus; Q6P2D0; -.
DR BioMuta; ZFP1; -.
DR DMDM; 59802892; -.
DR EPD; Q6P2D0; -.
DR jPOST; Q6P2D0; -.
DR MassIVE; Q6P2D0; -.
DR MaxQB; Q6P2D0; -.
DR PaxDb; Q6P2D0; -.
DR PeptideAtlas; Q6P2D0; -.
DR PRIDE; Q6P2D0; -.
DR ProteomicsDB; 66888; -. [Q6P2D0-1]
DR ProteomicsDB; 66889; -. [Q6P2D0-2]
DR Antibodypedia; 16789; 63 antibodies from 14 providers.
DR DNASU; 162239; -.
DR Ensembl; ENST00000393430.6; ENSP00000377080.2; ENSG00000184517.12. [Q6P2D0-1]
DR Ensembl; ENST00000570010.6; ENSP00000457044.1; ENSG00000184517.12. [Q6P2D0-1]
DR Ensembl; ENST00000642425.2; ENSP00000496743.1; ENSG00000285178.2. [Q6P2D0-1]
DR Ensembl; ENST00000642672.1; ENSP00000496712.1; ENSG00000285178.2. [Q6P2D0-1]
DR GeneID; 162239; -.
DR KEGG; hsa:162239; -.
DR MANE-Select; ENST00000570010.6; ENSP00000457044.1; NM_153688.4; NP_710155.2.
DR UCSC; uc002fdo.4; human. [Q6P2D0-1]
DR CTD; 162239; -.
DR DisGeNET; 162239; -.
DR GeneCards; ZFP1; -.
DR HGNC; HGNC:23328; ZFP1.
DR HPA; ENSG00000184517; Low tissue specificity.
DR MIM; 617230; gene.
DR neXtProt; NX_Q6P2D0; -.
DR OpenTargets; ENSG00000184517; -.
DR PharmGKB; PA134882678; -.
DR VEuPathDB; HostDB:ENSG00000184517; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161694; -.
DR HOGENOM; CLU_002678_0_2_1; -.
DR InParanoid; Q6P2D0; -.
DR OMA; YEKTLKC; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q6P2D0; -.
DR TreeFam; TF336987; -.
DR PathwayCommons; Q6P2D0; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q6P2D0; -.
DR BioGRID-ORCS; 162239; 56 hits in 1101 CRISPR screens.
DR ChiTaRS; ZFP1; human.
DR GenomeRNAi; 162239; -.
DR Pharos; Q6P2D0; Tbio.
DR PRO; PR:Q6P2D0; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q6P2D0; protein.
DR Bgee; ENSG00000184517; Expressed in cortical plate and 109 other tissues.
DR ExpressionAtlas; Q6P2D0; baseline and differential.
DR Genevisible; Q6P2D0; 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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
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; 6.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
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..407
FT /note="Zinc finger protein 1 homolog"
FT /id="PRO_0000047279"
FT DOMAIN 8..83
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 184..206
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 212..234
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 240..262
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 268..290
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 296..318
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 324..346
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 352..374
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 380..402
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 2..167
FT /note="Required for correct nuclear localization and
FT exclusion from the nucleoli"
FT /evidence="ECO:0000250|UniProtKB:P08042"
FT REGION 171..404
FT /note="Does not affect nuclear localization pattern"
FT /evidence="ECO:0000250|UniProtKB:P08042"
FT CROSSLNK 74
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 114
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 145
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..55
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012682"
SQ SEQUENCE 407 AA; 47516 MW; EAD9B780E65D618B CRC64;
MNKSQGSVSF TDVTVDFTQE EWEQLDPSQR ILYMDVMLEN YSNLLSVEVW KADDQMERDH
RNPDEQARQF LILKNQTPIE ERGDLFGKAL NLNTDFVSLR QVPYKYDLYE KTLKYNSDLL
NSNRSYAGKQ TDECNEFGKA LLYLKQEKTH SGVEYSEYNK SGKALSHKAA IFKHQKIKNL
VQPFICTYCD KAFSFKSLLI SHKRIHTGEK PYECNVCKKT FSHKANLIKH QRIHTGEKPF
ECPECGKAFT HQSNLIVHQR AHMEKKPYEC SECGKTFAQK FELTTHQRIH TGERPYECNE
CAKTFFKKSN LIIHQKIHTG EKRYECSECG KSFIQNSQLI IHMRTHTGEK PYECTECGKT
FSQRSTLRLH LRIHTGEKPY ECSECGKAFS RKSRLSVHQR VHIGEKP
