ZN502_HUMAN
ID ZN502_HUMAN Reviewed; 544 AA.
AC Q8TBZ5;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Zinc finger protein 502;
GN Name=ZNF502;
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=Testis;
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 INTERACTION WITH HRSV MATRIX PROTEIN (MICROBIAL INFECTION).
RX PubMed=25556234; DOI=10.1074/mcp.m114.044107;
RA Kipper S., Hamad S., Caly L., Avrahami D., Bacharach E., Jans D.A.,
RA Gerber D., Bajorek M.;
RT "New host factors important for respiratory syncytial virus (RSV)
RT replication revealed by a novel microfluidics screen for interactors of
RT matrix (M) protein.";
RL Mol. Cell. Proteomics 14:532-543(2015).
RN [3]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-43, 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 -!- SUBUNIT: (Microbial infection) Interacts with human respiratory
CC syncytial virus (HRSV) matrix protein; this interaction probably
CC facilitates viral release. {ECO:0000269|PubMed:25556234}.
CC -!- INTERACTION:
CC Q8TBZ5; Q13077: TRAF1; NbExp=7; IntAct=EBI-10273699, EBI-359224;
CC Q8TBZ5; P0DOE7: M; Xeno; NbExp=3; IntAct=EBI-10273699, EBI-10042882;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; BC028377; AAH28377.1; -; mRNA.
DR CCDS; CCDS2719.1; -.
DR RefSeq; NP_001127912.1; NM_001134440.1.
DR RefSeq; NP_001127913.1; NM_001134441.1.
DR RefSeq; NP_001127914.1; NM_001134442.1.
DR RefSeq; NP_001269809.1; NM_001282880.1.
DR RefSeq; NP_149987.2; NM_033210.4.
DR RefSeq; XP_016862929.1; XM_017007440.1.
DR AlphaFoldDB; Q8TBZ5; -.
DR SMR; Q8TBZ5; -.
DR BioGRID; 124825; 3.
DR IntAct; Q8TBZ5; 3.
DR STRING; 9606.ENSP00000296091; -.
DR iPTMnet; Q8TBZ5; -.
DR PhosphoSitePlus; Q8TBZ5; -.
DR BioMuta; ZNF502; -.
DR DMDM; 45477319; -.
DR EPD; Q8TBZ5; -.
DR jPOST; Q8TBZ5; -.
DR MassIVE; Q8TBZ5; -.
DR MaxQB; Q8TBZ5; -.
DR PaxDb; Q8TBZ5; -.
DR PeptideAtlas; Q8TBZ5; -.
DR PRIDE; Q8TBZ5; -.
DR ProteomicsDB; 74060; -.
DR Antibodypedia; 29472; 118 antibodies from 17 providers.
DR DNASU; 91392; -.
DR Ensembl; ENST00000296091.8; ENSP00000296091.4; ENSG00000196653.12.
DR Ensembl; ENST00000436624.7; ENSP00000406469.2; ENSG00000196653.12.
DR Ensembl; ENST00000449836.5; ENSP00000397390.1; ENSG00000196653.12.
DR Ensembl; ENST00000626630.2; ENSP00000487139.1; ENSG00000281448.3.
DR Ensembl; ENST00000628995.3; ENSP00000485847.1; ENSG00000281448.3.
DR Ensembl; ENST00000630464.2; ENSP00000486576.1; ENSG00000281448.3.
DR GeneID; 91392; -.
DR KEGG; hsa:91392; -.
DR MANE-Select; ENST00000436624.7; ENSP00000406469.2; NM_001134442.3; NP_001127914.1.
DR UCSC; uc003cns.4; human.
DR CTD; 91392; -.
DR DisGeNET; 91392; -.
DR GeneCards; ZNF502; -.
DR HGNC; HGNC:23718; ZNF502.
DR HPA; ENSG00000196653; Low tissue specificity.
DR neXtProt; NX_Q8TBZ5; -.
DR OpenTargets; ENSG00000196653; -.
DR PharmGKB; PA134866656; -.
DR VEuPathDB; HostDB:ENSG00000196653; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000163095; -.
DR HOGENOM; CLU_002678_44_0_1; -.
DR InParanoid; Q8TBZ5; -.
DR OMA; WETSNIH; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8TBZ5; -.
DR TreeFam; TF341817; -.
DR PathwayCommons; Q8TBZ5; -.
DR SignaLink; Q8TBZ5; -.
DR BioGRID-ORCS; 91392; 4 hits in 1090 CRISPR screens.
DR GenomeRNAi; 91392; -.
DR Pharos; Q8TBZ5; Tbio.
DR PRO; PR:Q8TBZ5; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8TBZ5; protein.
DR Bgee; ENSG00000196653; Expressed in calcaneal tendon and 102 other tissues.
DR ExpressionAtlas; Q8TBZ5; baseline and differential.
DR Genevisible; Q8TBZ5; HS.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
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:0044794; P:positive regulation by host of viral process; IMP:AgBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0019076; P:viral release from host cell; IMP:AgBase.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 12.
DR SMART; SM00355; ZnF_C2H2; 14.
DR SUPFAM; SSF57667; SSF57667; 8.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 14.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 14.
PE 1: Evidence at protein level;
KW DNA-binding; Host-virus interaction; Isopeptide bond; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..544
FT /note="Zinc finger protein 502"
FT /id="PRO_0000047623"
FT ZN_FING 155..177
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 183..205
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 211..233
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 239..261
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 267..289
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 295..317
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 323..345
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 351..373
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 379..401
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 407..429
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 435..457
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 463..485
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 491..513
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 519..541
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 43
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 28
FT /note="L -> P (in dbSNP:rs6798400)"
FT /id="VAR_033574"
FT VARIANT 174
FT /note="Q -> R (in dbSNP:rs56084453)"
FT /id="VAR_061953"
FT VARIANT 243
FT /note="E -> A (in dbSNP:rs7640654)"
FT /id="VAR_024220"
SQ SEQUENCE 544 AA; 62920 MW; 63437B670A6B22D0 CRC64;
MLNMQGAEER DIRRETCPGW VNKNKPALEQ DVCKIDSSGI VVKRFQEDEY QDSTFEEKYA
CEGMKENSPR EIAESCLFQE GGFGRITFIH KEAPPEIISQ GYNFEKSLLL TSSLVTRLRV
STEESLHQWE TSNIQTNDIS DQSKCPTLCT QKKSWKCNEC GKTFTQSSSL TQHQRTHTGE
RPYTCEECGK AFSRSSFLVQ HQRIHTGVKP YGCEQCGKTF RCRSFLTQHQ RIHTGEKPYK
CNECGNSFRN HSHLTEHQRI HTGEKPYKCN RCGKAFNQNT HLIHHQRIHT GEKPYICSEC
GSSFRKHSNL TQHQRIHTGE KPHKCDECGK TFQTKANLSQ HQRIHSGEKP YKCKECGKAF
CQSPSLIKHQ RIHTGEKPYK CKECGKAFTQ STPLTKHQRI HTGERPYKCS ECGKAFIQSI
CLIRHQRSHT GEKPYKCNEC GKGFNQNTCL TQHMRIHTGE KPYKCKECGK AFAHSSSLTE
HHRTHTGEKL YKCSECEKTF RKYAHLSEHY RIHTGEKPYE CIECGKFFRH SSVLFRHQKL
HSGD
