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ZSC25_HUMAN
ID   ZSC25_HUMAN             Reviewed;         544 AA.
AC   Q6NSZ9; A4D290; D6W5T5; Q14C82; Q14C99; Q5EBM9; Q6DJZ0; Q6N032; Q6ZML3;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 3.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=Zinc finger and SCAN domain-containing protein 25;
DE   AltName: Full=Zinc finger protein 498;
GN   Name=ZSCAN25; Synonyms=ZNF498;
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 3).
RC   TISSUE=Spleen;
RA   Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT   "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Fetal brain;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [4]
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   [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-544 (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 7-544 (ISOFORMS 2 AND 4).
RC   TISSUE=Lung, and Lymph;
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   [7]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-128, 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   [8]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-3; LYS-22; LYS-128; LYS-278 AND
RP   LYS-285, AND 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. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q6NSZ9-2; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-14650477, EBI-3866279;
CC       Q6NSZ9-2; P68400: CSNK2A1; NbExp=3; IntAct=EBI-14650477, EBI-347804;
CC       Q6NSZ9-2; Q92997: DVL3; NbExp=3; IntAct=EBI-14650477, EBI-739789;
CC       Q6NSZ9-2; P57086: SCAND1; NbExp=3; IntAct=EBI-14650477, EBI-745846;
CC       Q6NSZ9-2; P10073: ZSCAN22; NbExp=3; IntAct=EBI-14650477, EBI-10178224;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q6NSZ9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6NSZ9-2; Sequence=VSP_029147;
CC       Name=3;
CC         IsoId=Q6NSZ9-3; Sequence=VSP_029145;
CC       Name=4;
CC         IsoId=Q6NSZ9-4; Sequence=VSP_029146;
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI14574.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAI14942.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC       Sequence=BAD18712.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=EAL23869.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AK160369; BAD18712.1; ALT_INIT; mRNA.
DR   EMBL; BX640720; CAE45839.1; -; mRNA.
DR   EMBL; CH236956; EAL23869.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CH471091; EAW76643.1; -; Genomic_DNA.
DR   EMBL; CH471091; EAW76646.1; -; Genomic_DNA.
DR   EMBL; CH471091; EAW76647.1; -; Genomic_DNA.
DR   EMBL; BC069644; AAH69644.2; -; mRNA.
DR   EMBL; BC074902; AAH74902.3; -; mRNA.
DR   EMBL; BC074903; AAH74903.3; -; mRNA.
DR   EMBL; BC089402; AAH89402.1; -; mRNA.
DR   EMBL; BC114573; AAI14574.1; ALT_INIT; mRNA.
DR   EMBL; BC114941; AAI14942.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS5671.2; -. [Q6NSZ9-1]
DR   RefSeq; NP_660090.2; NM_145115.2. [Q6NSZ9-1]
DR   RefSeq; XP_005250251.1; XM_005250194.2.
DR   RefSeq; XP_011514207.1; XM_011515905.2. [Q6NSZ9-1]
DR   RefSeq; XP_011514208.1; XM_011515906.2.
DR   RefSeq; XP_011514209.1; XM_011515907.2. [Q6NSZ9-1]
DR   RefSeq; XP_011514210.1; XM_011515908.2.
DR   RefSeq; XP_016867313.1; XM_017011824.1. [Q6NSZ9-1]
DR   RefSeq; XP_016867314.1; XM_017011825.1.
DR   RefSeq; XP_016867315.1; XM_017011826.1.
DR   AlphaFoldDB; Q6NSZ9; -.
DR   SMR; Q6NSZ9; -.
DR   BioGRID; 128753; 73.
DR   IntAct; Q6NSZ9; 29.
DR   STRING; 9606.ENSP00000377708; -.
DR   iPTMnet; Q6NSZ9; -.
DR   PhosphoSitePlus; Q6NSZ9; -.
DR   BioMuta; ZSCAN25; -.
DR   DMDM; 160359044; -.
DR   EPD; Q6NSZ9; -.
DR   jPOST; Q6NSZ9; -.
DR   MassIVE; Q6NSZ9; -.
DR   MaxQB; Q6NSZ9; -.
DR   PaxDb; Q6NSZ9; -.
DR   PeptideAtlas; Q6NSZ9; -.
DR   PRIDE; Q6NSZ9; -.
DR   ProteomicsDB; 66645; -. [Q6NSZ9-1]
DR   ProteomicsDB; 66646; -. [Q6NSZ9-2]
DR   ProteomicsDB; 66647; -. [Q6NSZ9-3]
DR   ProteomicsDB; 66648; -. [Q6NSZ9-4]
DR   ABCD; Q6NSZ9; 2 sequenced antibodies.
DR   Antibodypedia; 30418; 197 antibodies from 25 providers.
DR   DNASU; 221785; -.
DR   Ensembl; ENST00000334715.7; ENSP00000334800.3; ENSG00000197037.11. [Q6NSZ9-1]
DR   Ensembl; ENST00000394150.5; ENSP00000377706.1; ENSG00000197037.11. [Q6NSZ9-4]
DR   Ensembl; ENST00000394152.7; ENSP00000377708.2; ENSG00000197037.11. [Q6NSZ9-1]
DR   GeneID; 221785; -.
DR   KEGG; hsa:221785; -.
DR   MANE-Select; ENST00000394152.7; ENSP00000377708.2; NM_145115.3; NP_660090.2.
DR   UCSC; uc003url.1; human. [Q6NSZ9-1]
DR   CTD; 221785; -.
DR   DisGeNET; 221785; -.
DR   GeneCards; ZSCAN25; -.
DR   HGNC; HGNC:21961; ZSCAN25.
DR   HPA; ENSG00000197037; Low tissue specificity.
DR   neXtProt; NX_Q6NSZ9; -.
DR   OpenTargets; ENSG00000197037; -.
DR   PharmGKB; PA134962723; -.
DR   VEuPathDB; HostDB:ENSG00000197037; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000162113; -.
DR   HOGENOM; CLU_002678_53_4_1; -.
DR   InParanoid; Q6NSZ9; -.
DR   OMA; VNTRDQE; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q6NSZ9; -.
DR   TreeFam; TF350842; -.
DR   PathwayCommons; Q6NSZ9; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   SignaLink; Q6NSZ9; -.
DR   BioGRID-ORCS; 221785; 14 hits in 1093 CRISPR screens.
DR   ChiTaRS; ZSCAN25; human.
DR   GenomeRNAi; 221785; -.
DR   Pharos; Q6NSZ9; Tdark.
DR   PRO; PR:Q6NSZ9; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q6NSZ9; protein.
DR   Bgee; ENSG00000197037; Expressed in tibialis anterior and 158 other tissues.
DR   ExpressionAtlas; Q6NSZ9; baseline and differential.
DR   Genevisible; Q6NSZ9; HS.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd07765; KRAB_A-box; 1.
DR   CDD; cd07936; SCAN; 1.
DR   Gene3D; 1.10.4020.10; -; 1.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR036051; KRAB_dom_sf.
DR   InterPro; IPR003309; SCAN_dom.
DR   InterPro; IPR038269; SCAN_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF02023; SCAN; 1.
DR   Pfam; PF00096; zf-C2H2; 7.
DR   SMART; SM00431; SCAN; 1.
DR   SMART; SM00355; ZnF_C2H2; 7.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 4.
DR   PROSITE; PS50804; SCAN_BOX; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
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..544
FT                   /note="Zinc finger and SCAN domain-containing protein 25"
FT                   /id="PRO_0000309332"
FT   DOMAIN          42..124
FT                   /note="SCAN box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT   ZN_FING         348..370
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         375..397
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         403..425
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         431..453
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         459..480
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         486..508
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         514..536
FT                   /note="C2H2-type 7; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          157..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        3
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        22
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        128
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25755297,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        278
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        285
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         1..216
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_029145"
FT   VAR_SEQ         130..544
FT                   /note="VPCHRQGEQEETALCRGAWEPGIQLGPVEVKPEWGMPPGEGVQGPDPGTEEQ
FT                   LSQDPGDETRAFQEQALPVLQAGPGLPAVNPRDQEMAAGFFTAGSQGLGPFKDMALAFP
FT                   EEEWRHVTPAQIDCFGEYVEPQDCRVSPGGGSKEKEAKPPQEDLKGALVALTSERFGEA
FT                   SLQGPGLGRVCEQEPGGPAGSAPGLPPPQHGAIPLPDEVKTHSSFWKPFQCPECGKGFS
FT                   RSSNLVRHQRTHEEKSYGCVECGKGFTLREYLMKHQRTHLGKRPYVCSECWKTFSQRHH
FT                   LEVHQRSHTGEKPYKCGDCWKSFSRRQHLQVHRRTHTGEKPYTCECGKSFSRNANLAVH
FT                   RRAHTGEKPYGCQVCGKRFSKGERLVRHQRIHTGEKPYHCPACGRSFNQRSILNRHQKT
FT                   QHRQEPLVQ -> VGSMPQAGRAGGNSTLQRRLGARHPAGASGGQA (in isoform
FT                   4)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:17974005"
FT                   /id="VSP_029146"
FT   VAR_SEQ         197..268
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_029147"
FT   VARIANT         325
FT                   /note="P -> A (in dbSNP:rs10239632)"
FT                   /id="VAR_036931"
SQ   SEQUENCE   544 AA;  61474 MW;  E63AA7ACDA7E7E8B CRC64;
     MLKEHPEMAE APQQQLGIPV VKLEKELPWG RGREDPSPET FRLRFRQFRY QEAAGPQEAL
     RELQELCRRW LRPELHTKEQ ILELLVLEQF LTILPREFYA WIREHGPESG KALAAMVEDL
     TERALEAKAV PCHRQGEQEE TALCRGAWEP GIQLGPVEVK PEWGMPPGEG VQGPDPGTEE
     QLSQDPGDET RAFQEQALPV LQAGPGLPAV NPRDQEMAAG FFTAGSQGLG PFKDMALAFP
     EEEWRHVTPA QIDCFGEYVE PQDCRVSPGG GSKEKEAKPP QEDLKGALVA LTSERFGEAS
     LQGPGLGRVC EQEPGGPAGS APGLPPPQHG AIPLPDEVKT HSSFWKPFQC PECGKGFSRS
     SNLVRHQRTH EEKSYGCVEC GKGFTLREYL MKHQRTHLGK RPYVCSECWK TFSQRHHLEV
     HQRSHTGEKP YKCGDCWKSF SRRQHLQVHR RTHTGEKPYT CECGKSFSRN ANLAVHRRAH
     TGEKPYGCQV CGKRFSKGER LVRHQRIHTG EKPYHCPACG RSFNQRSILN RHQKTQHRQE
     PLVQ
 
 
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