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CHRD1_PONAB
ID   CHRD1_PONAB             Reviewed;         332 AA.
AC   Q5RD91;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=Protein morgana;
GN   Name=CHORDC1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR858025; CAH90266.1; -; mRNA.
DR   RefSeq; NP_001125118.1; NM_001131646.1.
DR   AlphaFoldDB; Q5RD91; -.
DR   SMR; Q5RD91; -.
DR   STRING; 9601.ENSPPYP00000004308; -.
DR   PRIDE; Q5RD91; -.
DR   GeneID; 100172001; -.
DR   KEGG; pon:100172001; -.
DR   CTD; 26973; -.
DR   eggNOG; KOG1667; Eukaryota.
DR   InParanoid; Q5RD91; -.
DR   OrthoDB; 1163528at2759; -.
DR   Proteomes; UP000001595; 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_0000317772"
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..81
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..81
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;  37490 MW;  29AB2CA3591A3677 CRC64;
     MALLCYNRGC GQRFDPETNS DDACTYHPGV PVFHDALKGW SCCKRRTTDF SDFLSIVGCT
     KGRHNSEKPP ESVKPEVKTT EKKELSELKP KFQEHIIQAP KPVEAIKRPS PDEPMTNLEL
     KISASLKQAL DKLKLSSGNE ENKKEEDNDE IKIGTSCKNG GCSKTYRGLE SLEEVCVYHS
     GVPISHEGMK YWSCCRRKTS DFNTFLAQEG CTKGKHMWTK KDAGKKVVPC RHDWHQTGGE
     VTISVYAKNS LPELSRVEAN STLLNVHIVF EGEKEFEQNV KLWGVIDVKR SYVTMTATKI
     EITMRKAEPM QWASLELPAA KKQEKQKDDT TD
 
 
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