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CHRD1_MACFA
ID   CHRD1_MACFA             Reviewed;         332 AA.
AC   Q4R7U2;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Cysteine and histidine-rich domain-containing protein 1;
DE   AltName: Full=CHORD domain-containing protein 1;
DE            Short=CHP-1;
DE   AltName: Full=Morgana;
GN   Name=CHORDC1; ORFNames=QtsA-14386;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulates centrosome duplication, probably by inhibiting the
CC       kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90.
CC       May play a role in the regulation of NOD1 via a HSP90 chaperone
CC       complex. In vitro, has intrinsic chaperone activity. This function may
CC       be achieved by inhibiting association of ROCK2 with NPM1. Plays a role
CC       in ensuring the localization of the tyrosine kinase receptor EGFR to
CC       the plasma membrane, and thus ensures the subsequent regulation of EGFR
CC       activity and EGF-induced actin cytoskeleton remodeling (By similarity).
CC       Involved in stress response. Prevents tumorigenesis (By similarity).
CC       {ECO:0000250, ECO:0000250|UniProtKB:Q9UHD1}.
CC   -!- SUBUNIT: Interacts with HSP90AA1, HSP90AB1, PPP5C, ROCK1 and ROCK2.
CC       {ECO:0000250}.
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DR   EMBL; AB168720; BAE00830.1; -; mRNA.
DR   RefSeq; NP_001270158.1; NM_001283229.1.
DR   AlphaFoldDB; Q4R7U2; -.
DR   SMR; Q4R7U2; -.
DR   STRING; 9541.XP_005579397.1; -.
DR   PRIDE; Q4R7U2; -.
DR   GeneID; 101925655; -.
DR   CTD; 26973; -.
DR   eggNOG; KOG1667; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
DR   GO; GO:1900034; P:regulation of cellular response to heat; ISS:UniProtKB.
DR   GO; GO:0010824; P:regulation of centrosome duplication; ISS:UniProtKB.
DR   Gene3D; 2.60.40.790; -; 1.
DR   InterPro; IPR007051; CHORD_dom.
DR   InterPro; IPR039790; CHORD_protein.
DR   InterPro; IPR007052; CS_dom.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   PANTHER; PTHR12621; PTHR12621; 1.
DR   Pfam; PF04968; CHORD; 2.
DR   Pfam; PF04969; CS; 1.
DR   SUPFAM; SSF49764; SSF49764; 1.
DR   PROSITE; PS51401; CHORD; 2.
DR   PROSITE; PS51203; CS; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Chaperone; Metal-binding; Phosphoprotein; Reference proteome;
KW   Repeat; Stress response; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHD1"
FT   CHAIN           2..332
FT                   /note="Cysteine and histidine-rich domain-containing
FT                   protein 1"
FT                   /id="PRO_0000402800"
FT   DOMAIN          5..64
FT                   /note="CHORD 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT   DOMAIN          157..216
FT                   /note="CHORD 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT   DOMAIN          227..316
FT                   /note="CS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT   REGION          2..77
FT                   /note="Interaction with PPP5C"
FT                   /evidence="ECO:0000250"
FT   REGION          62..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          65..316
FT                   /note="Interaction with HSP90AA1 and HSP90AB1"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        64..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         5
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT   BINDING         10
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT   BINDING         24
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT   BINDING         27
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT   BINDING         42
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT   BINDING         43
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT   BINDING         157
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT   BINDING         162
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT   BINDING         176
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT   BINDING         179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT   BINDING         194
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT   BINDING         195
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT   BINDING         211
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT   BINDING         216
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHD1"
FT   MOD_RES         47
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHD1"
FT   MOD_RES         51
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHD1"
SQ   SEQUENCE   332 AA;  37602 MW;  91546BFAF62D4DC5 CRC64;
     MALLCYNRAC GQRFDPETNS DDACTYHPGV PVFHDALKGW SCCKRRTTDF SDFLSIVGCT
     KGRHNSEKPP EPVKPEVKTT EKKELSELKP KFQEHIIQAP KPVEAIKRPS PDEPMTNLEL
     KISASLKQAL DKLKLSSGNE EDKKEEDNDE IKIGTSCKNG GCSKTYRGLE SLEEVCVYHS
     GVPIFHEGMK YWSCCRRKTS DFNTFLAQEG CTKGRHMWTK KDAGKKVVPC RHDWHQTGGE
     VTISVYAKNS LPELSRVEAN STLLNVHIVF EGEKEFDQNV KLWGVIDVKR SYVTMTATKI
     EINMRKAEPM QWASLELPAA KKQEKQKDDT TD
 
 
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