ZN507_HUMAN
ID ZN507_HUMAN Reviewed; 953 AA.
AC Q8TCN5; A8K911; Q2TBF1; Q6MZU0; Q9UPR8;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Zinc finger protein 507;
GN Name=ZNF507; Synonyms=KIAA1084;
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] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 MRNA] (ISOFORM 1).
RC TISSUE=Testis, and Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 542-953.
RC TISSUE=Duodenum;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95 AND SER-427, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TCN5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TCN5-2; Sequence=VSP_035357, VSP_035358;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA83036.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAD28536.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD28536.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAE45937.1; 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; AB029007; BAA83036.2; ALT_INIT; mRNA.
DR EMBL; AK292526; BAF85215.1; -; mRNA.
DR EMBL; AL713775; CAD28536.1; ALT_SEQ; mRNA.
DR EMBL; BX640881; CAE45937.1; ALT_INIT; mRNA.
DR EMBL; BC110332; AAI10333.1; -; mRNA.
DR CCDS; CCDS32985.1; -. [Q8TCN5-1]
DR RefSeq; NP_001129628.1; NM_001136156.1. [Q8TCN5-1]
DR RefSeq; NP_055725.2; NM_014910.4. [Q8TCN5-1]
DR AlphaFoldDB; Q8TCN5; -.
DR BioGRID; 116519; 48.
DR DIP; DIP-47281N; -.
DR IntAct; Q8TCN5; 23.
DR MINT; Q8TCN5; -.
DR STRING; 9606.ENSP00000312277; -.
DR GlyGen; Q8TCN5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TCN5; -.
DR PhosphoSitePlus; Q8TCN5; -.
DR BioMuta; ZNF507; -.
DR DMDM; 205371823; -.
DR CPTAC; CPTAC-1215; -.
DR EPD; Q8TCN5; -.
DR jPOST; Q8TCN5; -.
DR MassIVE; Q8TCN5; -.
DR MaxQB; Q8TCN5; -.
DR PaxDb; Q8TCN5; -.
DR PeptideAtlas; Q8TCN5; -.
DR PRIDE; Q8TCN5; -.
DR ProteomicsDB; 74147; -. [Q8TCN5-1]
DR ProteomicsDB; 74148; -. [Q8TCN5-2]
DR Antibodypedia; 28867; 39 antibodies from 13 providers.
DR DNASU; 22847; -.
DR Ensembl; ENST00000311921.8; ENSP00000312277.2; ENSG00000168813.17. [Q8TCN5-1]
DR Ensembl; ENST00000355898.6; ENSP00000348162.4; ENSG00000168813.17. [Q8TCN5-1]
DR GeneID; 22847; -.
DR KEGG; hsa:22847; -.
DR MANE-Select; ENST00000355898.6; ENSP00000348162.4; NM_001136156.2; NP_001129628.1.
DR UCSC; uc002ntd.4; human. [Q8TCN5-1]
DR CTD; 22847; -.
DR DisGeNET; 22847; -.
DR GeneCards; ZNF507; -.
DR HGNC; HGNC:23783; ZNF507.
DR HPA; ENSG00000168813; Low tissue specificity.
DR neXtProt; NX_Q8TCN5; -.
DR OpenTargets; ENSG00000168813; -.
DR PharmGKB; PA134917055; -.
DR VEuPathDB; HostDB:ENSG00000168813; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00490000043434; -.
DR HOGENOM; CLU_013272_0_0_1; -.
DR InParanoid; Q8TCN5; -.
DR OMA; PICEHKA; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8TCN5; -.
DR TreeFam; TF331496; -.
DR PathwayCommons; Q8TCN5; -.
DR SignaLink; Q8TCN5; -.
DR BioGRID-ORCS; 22847; 11 hits in 1099 CRISPR screens.
DR ChiTaRS; ZNF507; human.
DR GenomeRNAi; 22847; -.
DR Pharos; Q8TCN5; Tdark.
DR PRO; PR:Q8TCN5; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8TCN5; protein.
DR Bgee; ENSG00000168813; Expressed in endothelial cell and 179 other tissues.
DR ExpressionAtlas; Q8TCN5; baseline and differential.
DR Genevisible; Q8TCN5; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..953
FT /note="Zinc finger protein 507"
FT /id="PRO_0000047625"
FT ZN_FING 125..147
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 155..185
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 248..270
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 641..663
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 669..691
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 697..720
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 758..780
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 786..808
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 911..933
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 470..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 750..764
FT /note="NKSSVQKQYRCDVCD -> IYVFCYAGCSDLHMT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10470851"
FT /id="VSP_035357"
FT VAR_SEQ 765..953
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10470851"
FT /id="VSP_035358"
FT CONFLICT 361
FT /note="M -> V (in Ref. 2; BAF85215)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="I -> M (in Ref. 2; BAF85215)"
FT /evidence="ECO:0000305"
FT CONFLICT 722
FT /note="L -> P (in Ref. 2; BAF85215)"
FT /evidence="ECO:0000305"
FT CONFLICT 941
FT /note="I -> T (in Ref. 2; BAF85215)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 953 AA; 105767 MW; 0842CAD019057CE4 CRC64;
MEESSSVAML VPDIGEQEAI LTAESIISPS LEIDEQRKTK PDPLIHVIQK LSKIVENEKS
QKCLLIGKKR PRSSAATHSL ETQELCEIPA KVIQSPAADT RRAEMSQTNF TPDTLAQNEG
KAMSYQCSLC KFLSSSFSVL KDHIKQHGQQ NEVILMCSEC HITSRSQEEL EAHVVNDHDN
DANIHTQSKA QQCVSPSSSL CRKTTERNET IPDIPVSVDN LQTHTVQTAS VAEMGRRKWY
AYEQYGMYRC LFCSYTCGQQ RMLKTHAWKH AGEVDCSYPI FENENEPLGL LDSSAAAAPG
GVDAVVIAIG ESELSIHNGP SVQVQICSSE QLSSSSPLEQ SAERGVHLSQ SVTLDPNEEE
MLEVISDAEE NLIPDSLLTS AQKIISSSPN KKGHVNVIVE RLPSAEETLS QKRFLMNTEM
EEGKDLSLTE AQIGREGMDD VYRADKCTVD IGGLIIGWSS SEKKDELMNK GLATDENAPP
GRRRTNSESL RLHSLAAEAL VTMPIRAAEL TRANLGHYGD INLLDPDTSQ RQVDSTLAAY
SKMMSPLKNS SDGLTSLNQS NSTLVALPEG RQELSDGQVK TGISMSLLTV IEKLRERTDQ
NASDDDILKE LQDNAQCQPN SDTSLSGNNV VEYIPNAERP YRCRLCHYTS GNKGYIKQHL
RVHRQRQPYQ CPICEHIADN SKDLESHMIH HCKTRIYQCK QCEESFHYKS QLRNHEREQH
SLPDTLSIAT SNEPRISSDT ADGKCVQEGN KSSVQKQYRC DVCDYTSTTY VGVRNHRRIH
NSDKPYRCSL CGYVCSHPPS LKSHMWKHAS DQNYNYEQVN KAINDAISQS GRVLGKSPGK
TQLKSSEESA DPVTGSSENA VSSSELMSQT PSEVLGTNEN EKLSPTSNTS YSLEKISSLA
PPSMEYCVLL FCCCICGFES TSKENLLDHM KEHEGEIVNI ILNKDHNTAL NTN