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ZNHI2_HUMAN
ID   ZNHI2_HUMAN             Reviewed;         403 AA.
AC   Q9UHR6; Q3SY14; Q8IUV0;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Zinc finger HIT domain-containing protein 2;
DE   AltName: Full=Protein FON;
GN   Name=ZNHIT2; Synonyms=C11orf5;
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 [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=10602999; DOI=10.1007/s003350010016;
RA   Lemmens I.H., Farnebo F., Piehl F., Merregaert J., Van de Ven W.J.M.,
RA   Larsson C., Kas K.;
RT   "Molecular characterization of human and murine c11orf5, a new member of
RT   the FAUNA gene cluster.";
RL   Mamm. Genome 11:78-80(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreas;
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH RUVBL2.
RX   PubMed=28561026; DOI=10.1038/ncomms15615;
RA   Cloutier P., Poitras C., Durand M., Hekmat O., Fiola-Masson E.,
RA   Bouchard A., Faubert D., Chabot B., Coulombe B.;
RT   "R2TP/Prefoldin-like component RUVBL1/RUVBL2 directly interacts with ZNHIT2
RT   to regulate assembly of U5 small nuclear ribonucleoprotein.";
RL   Nat. Commun. 8:15615-15615(2017).
RN   [9] {ECO:0007744|PDB:1X4S}
RP   STRUCTURE BY NMR OF 1-46.
RX   PubMed=17656577; DOI=10.1110/ps.062635107;
RA   He F., Umehara T., Tsuda K., Inoue M., Kigawa T., Matsuda T., Yabuki T.,
RA   Aoki M., Seki E., Terada T., Shirouzu M., Tanaka A., Sugano S., Muto Y.,
RA   Yokoyama S.;
RT   "Solution structure of the zinc finger HIT domain in protein FON.";
RL   Protein Sci. 16:1577-1587(2007).
RN   [10]
RP   VARIANT [LARGE SCALE ANALYSIS] PRO-59.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: May act as a bridging factor mediating the interaction
CC       between the R2TP/Prefoldin-like (R2TP/PFDL) complex and U5 small
CC       nuclear ribonucleoprotein (U5 snRNP) (PubMed:28561026). Required for
CC       the interaction of R2TP complex subunit RPAP3 and prefoldin-like
CC       subunit URI1 with U5 snRNP proteins EFTUD2 and PRPF8 (PubMed:28561026).
CC       May play a role in regulating the composition of the U5 snRNP complex
CC       (PubMed:28561026). {ECO:0000269|PubMed:28561026}.
CC   -!- SUBUNIT: Interacts (via HIT-type zinc finger) with RUVBL2 in the
CC       presence of ATP or ADP; shows a stronger interaction in the presence of
CC       ADP. {ECO:0000269|PubMed:28561026}.
CC   -!- INTERACTION:
CC       Q9UHR6; O95400: CD2BP2; NbExp=4; IntAct=EBI-2557592, EBI-768015;
CC       Q9UHR6; Q96N16: JAKMIP1; NbExp=3; IntAct=EBI-2557592, EBI-2680803;
CC       Q9UHR6; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-2557592, EBI-2341787;
CC       Q9UHR6; Q9Y265: RUVBL1; NbExp=6; IntAct=EBI-2557592, EBI-353675;
CC   -!- TISSUE SPECIFICITY: Low expression in most tissues; highly expressed in
CC       testis. {ECO:0000269|PubMed:10602999}.
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DR   EMBL; AF119497; AAF23591.1; -; mRNA.
DR   EMBL; BC038089; AAH38089.1; -; mRNA.
DR   EMBL; BC052240; AAH52240.1; -; mRNA.
DR   CCDS; CCDS8094.1; -.
DR   RefSeq; NP_055020.1; NM_014205.3.
DR   PDB; 1X4S; NMR; -; A=1-46.
DR   PDBsum; 1X4S; -.
DR   AlphaFoldDB; Q9UHR6; -.
DR   SMR; Q9UHR6; -.
DR   BioGRID; 107200; 128.
DR   IntAct; Q9UHR6; 27.
DR   STRING; 9606.ENSP00000308548; -.
DR   iPTMnet; Q9UHR6; -.
DR   PhosphoSitePlus; Q9UHR6; -.
DR   BioMuta; ZNHIT2; -.
DR   DMDM; 27734232; -.
DR   EPD; Q9UHR6; -.
DR   jPOST; Q9UHR6; -.
DR   MassIVE; Q9UHR6; -.
DR   MaxQB; Q9UHR6; -.
DR   PaxDb; Q9UHR6; -.
DR   PeptideAtlas; Q9UHR6; -.
DR   PRIDE; Q9UHR6; -.
DR   ProteomicsDB; 84405; -.
DR   Antibodypedia; 29668; 69 antibodies from 21 providers.
DR   DNASU; 741; -.
DR   Ensembl; ENST00000310597.6; ENSP00000308548.4; ENSG00000174276.7.
DR   GeneID; 741; -.
DR   KEGG; hsa:741; -.
DR   MANE-Select; ENST00000310597.6; ENSP00000308548.4; NM_014205.4; NP_055020.1.
DR   UCSC; uc001ocw.4; human.
DR   CTD; 741; -.
DR   DisGeNET; 741; -.
DR   GeneCards; ZNHIT2; -.
DR   HGNC; HGNC:1177; ZNHIT2.
DR   HPA; ENSG00000174276; Tissue enhanced (testis).
DR   MIM; 604575; gene.
DR   neXtProt; NX_Q9UHR6; -.
DR   OpenTargets; ENSG00000174276; -.
DR   PharmGKB; PA25496; -.
DR   VEuPathDB; HostDB:ENSG00000174276; -.
DR   eggNOG; KOG4317; Eukaryota.
DR   GeneTree; ENSGT00390000017147; -.
DR   HOGENOM; CLU_039057_1_0_1; -.
DR   InParanoid; Q9UHR6; -.
DR   OMA; VPYCSLR; -.
DR   OrthoDB; 1599898at2759; -.
DR   PhylomeDB; Q9UHR6; -.
DR   TreeFam; TF324864; -.
DR   PathwayCommons; Q9UHR6; -.
DR   SignaLink; Q9UHR6; -.
DR   BioGRID-ORCS; 741; 701 hits in 1085 CRISPR screens.
DR   EvolutionaryTrace; Q9UHR6; -.
DR   GenomeRNAi; 741; -.
DR   Pharos; Q9UHR6; Tbio.
DR   PRO; PR:Q9UHR6; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q9UHR6; protein.
DR   Bgee; ENSG00000174276; Expressed in right testis and 95 other tissues.
DR   ExpressionAtlas; Q9UHR6; baseline and differential.
DR   Genevisible; Q9UHR6; HS.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR007529; Znf_HIT.
DR   InterPro; IPR039646; ZNHIT2.
DR   PANTHER; PTHR15555; PTHR15555; 1.
DR   Pfam; PF04438; zf-HIT; 1.
DR   PROSITE; PS51083; ZF_HIT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Metal-binding; Phosphoprotein;
KW   Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..403
FT                   /note="Zinc finger HIT domain-containing protein 2"
FT                   /id="PRO_0000173548"
FT   ZN_FING         7..41
FT                   /note="HIT-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT   REGION          72..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         7
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT   BINDING         10
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT   BINDING         22
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT   BINDING         25
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT   BINDING         30
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT   BINDING         34
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT   BINDING         38
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT   BINDING         41
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         161
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:23186163"
FT   VARIANT         59
FT                   /note="A -> P (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs1185334988)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035720"
FT   VARIANT         155
FT                   /note="E -> K (in dbSNP:rs11556920)"
FT                   /id="VAR_053757"
FT   VARIANT         176
FT                   /note="A -> V (in dbSNP:rs35983251)"
FT                   /id="VAR_053758"
FT   STRAND          5..7
FT                   /evidence="ECO:0007829|PDB:1X4S"
FT   STRAND          16..18
FT                   /evidence="ECO:0007829|PDB:1X4S"
FT   TURN            23..25
FT                   /evidence="ECO:0007829|PDB:1X4S"
FT   STRAND          28..31
FT                   /evidence="ECO:0007829|PDB:1X4S"
FT   HELIX           32..38
FT                   /evidence="ECO:0007829|PDB:1X4S"
FT   HELIX           41..44
FT                   /evidence="ECO:0007829|PDB:1X4S"
SQ   SEQUENCE   403 AA;  42884 MW;  2384BF806CC40E71 CRC64;
     MEPAGPCGFC PAGEVQPARY TCPRCNAPYC SLRCYRTHGT CAENFYRDQV LGELRGCSAP
     PSRLASALRR LRQQRETEDE PGEAGLSSGP APGGLSGLWE RLAPGEKAAF ERLLSRGEAG
     RLLPPWRPWW WNRGAGPQLL EELDNAPGSD AAELELAPAR TPPDSVKDAS AAEPAAAERV
     LGDVPGACTP VVPTRIPAIV SLSRGPVSPL VRFQLPNVLF AYAHTLALYH GGDDALLSDF
     CATLLGVSGA LGAQQVFASA EEALQAAAHV LEAGEHPPGP LGTRGAMHEV ARILLGEGPT
     NQKGYTLAAL GDLAQTLGRA RKQAVAREER DHLYRARKKC QFLLAWTNEN EAALTPLALD
     CARAHQAHAV VAEEVAALTG ELERLWGGPV PPAPRTLIEE LPS
 
 
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