Full text data of CHORDC1
CHORDC1
(CHP1)
[Confidence: low (only semi-automatic identification from reviews)]
Cysteine and histidine-rich domain-containing protein 1 (CHORD domain-containing protein 1; CHORD-containing protein 1; CHP-1; Protein morgana)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Cysteine and histidine-rich domain-containing protein 1 (CHORD domain-containing protein 1; CHORD-containing protein 1; CHP-1; Protein morgana)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9UHD1
ID CHRD1_HUMAN Reviewed; 332 AA.
AC Q9UHD1; B2R6P8; Q6IN49; Q8WVL9; Q9H3D6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-FEB-2008, sequence version 2.
DT 22-JAN-2014, entry version 88.
DE RecName: Full=Cysteine and histidine-rich domain-containing protein 1;
DE AltName: Full=CHORD domain-containing protein 1;
DE Short=CHORD-containing protein 1;
DE Short=CHP-1;
DE AltName: Full=Protein morgana;
GN Name=CHORDC1; Synonyms=CHP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASP-329.
RX PubMed=10571178; DOI=10.1016/S0092-8674(00)81522-6;
RA Shirasu K., Lahaye T., Tan M.-W., Zhou F., Azevedo C.,
RA Schulze-Lefert P.;
RT "A novel class of eukaryotic zinc-binding proteins is required for
RT disease resistance signaling in barley and development in C.
RT elegans.";
RL Cell 99:355-366(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT ASP-329.
RC TISSUE=Heart;
RA Zhao Y., Cao H., Jiang Y., Meng X., Zhao X., Liu D., Ding J.;
RT "Isolation and characterization the chymotrypsin-like protein gene
RT from human heart cDNA library.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP ASP-329.
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASP-329.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 2-8; 47-61; 108-121; 249-256; 282-289; 291-299 AND
RP 306-321, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Bilsland A.E., Keith W.N.;
RL Submitted (JAN-2010) to UniProtKB.
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47 AND SER-51, AND MASS
RP SPECTROMETRY.
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP FUNCTION, INTERACTION WITH ROCK1 AND ROCK2, AND TISSUE SPECIFICITY.
RX PubMed=20230755; DOI=10.1016/j.devcel.2009.12.020;
RA Ferretti R., Palumbo V., Di Savino A., Velasco S., Sbroggio M.,
RA Sportoletti P., Micale L., Turco E., Silengo L., Palumbo G.,
RA Hirsch E., Teruya-Feldstein J., Bonaccorsi S., Pandolfi P.P.,
RA Gatti M., Tarone G., Brancaccio M.;
RT "Morgana/chp-1, a ROCK inhibitor involved in centrosome duplication
RT and tumorigenesis.";
RL Dev. Cell 18:486-495(2010).
RN [11]
RP INTERACTION WITH HSP90AA1.
RX PubMed=19875381; DOI=10.1074/mcp.M900261-MCP200;
RA Gano J.J., Simon J.A.;
RT "A proteomic investigation of ligand-dependent HSP90 complexes reveals
RT CHORDC1 as a novel ADP-dependent HSP90-interacting protein.";
RL Mol. Cell. Proteomics 9:255-270(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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.,
RA Buerckstuemmer T., 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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP STRUCTURE BY NMR OF 1-68.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the CHORD domain of human CHORD-containing
RT protein 1.";
RL Submitted (APR-2008) to the PDB data bank.
CC -!- FUNCTION: Regulates centrosome duplication, probably by inhibiting
CC the kinase activity of ROCK2. Proposed to act as co-chaperone for
CC HSP90. May play a role in the regulation of NOD1 via a HSP90
CC chaperone complex. In vitro, has intrinsic chaperone activity.
CC This function may be achieved by inhibiting association of ROCK2
CC with NPM1. Involved in stress response. Prevents tumorigenesis.
CC -!- SUBUNIT: Interacts with HSP90AA1, ROCK1 and ROCK2. Interacts with
CC HSP90AB1 and PPP5C (By similarity).
CC -!- INTERACTION:
CC P07900:HSP90AA1; NbExp=8; IntAct=EBI-2550959, EBI-296047;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UHD1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UHD1-2; Sequence=VSP_031150;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Underexpressed in many breast and lung
CC cancers.
CC -!- SIMILARITY: Contains 2 CHORD domains.
CC -!- SIMILARITY: Contains 1 CS domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17789.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF192466; AAF18437.1; -; mRNA.
DR EMBL; AF123249; AAG43237.1; -; mRNA.
DR EMBL; AK290231; BAF82920.1; -; mRNA.
DR EMBL; AK312663; BAG35545.1; -; mRNA.
DR EMBL; AP002364; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471065; EAW66868.1; -; Genomic_DNA.
DR EMBL; CH471065; EAW66870.1; -; Genomic_DNA.
DR EMBL; BC017789; AAH17789.1; ALT_INIT; mRNA.
DR EMBL; BC072461; AAH72461.1; -; mRNA.
DR RefSeq; NP_001137545.1; NM_001144073.1.
DR RefSeq; NP_036256.2; NM_012124.2.
DR UniGene; Hs.22857; -.
DR PDB; 2YRT; NMR; -; A=1-68.
DR PDBsum; 2YRT; -.
DR ProteinModelPortal; Q9UHD1; -.
DR SMR; Q9UHD1; 1-68, 157-216, 231-316.
DR IntAct; Q9UHD1; 5.
DR STRING; 9606.ENSP00000319255; -.
DR DMDM; 167008724; -.
DR PaxDb; Q9UHD1; -.
DR PeptideAtlas; Q6IN49; -.
DR PRIDE; Q9UHD1; -.
DR DNASU; 26973; -.
DR Ensembl; ENST00000320585; ENSP00000319255; ENSG00000110172.
DR Ensembl; ENST00000457199; ENSP00000401080; ENSG00000110172.
DR GeneID; 26973; -.
DR KEGG; hsa:26973; -.
DR UCSC; uc001pdg.2; human.
DR CTD; 26973; -.
DR GeneCards; GC11M089933; -.
DR H-InvDB; HIX0010016; -.
DR HGNC; HGNC:14525; CHORDC1.
DR HPA; HPA041040; -.
DR MIM; 604353; gene.
DR neXtProt; NX_Q9UHD1; -.
DR PharmGKB; PA26476; -.
DR eggNOG; NOG282821; -.
DR HOGENOM; HOG000207093; -.
DR HOVERGEN; HBG052156; -.
DR InParanoid; Q9UHD1; -.
DR KO; K16729; -.
DR OMA; WSCCKKK; -.
DR OrthoDB; EOG7X6M0X; -.
DR PhylomeDB; Q9UHD1; -.
DR ChiTaRS; CHORDC1; human.
DR EvolutionaryTrace; Q9UHD1; -.
DR GenomeRNAi; 26973; -.
DR NextBio; 49424; -.
DR PRO; PR:Q9UHD1; -.
DR ArrayExpress; Q9UHD1; -.
DR Bgee; Q9UHD1; -.
DR CleanEx; HS_CHORDC1; -.
DR Genevestigator; Q9UHD1; -.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
DR GO; GO:2000299; P:negative regulation of Rho-dependent protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:1900034; P:regulation of cellular response to heat; ISS:UniProtKB.
DR GO; GO:0010824; P:regulation of centrosome duplication; IEA:Ensembl.
DR GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR InterPro; IPR007051; CHORD.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chaperone;
KW Complete proteome; Direct protein sequencing; Metal-binding;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW Stress response; Zinc.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 332 Cysteine and histidine-rich domain-
FT containing protein 1.
FT /FTId=PRO_0000317770.
FT DOMAIN 5 64 CHORD 1.
FT DOMAIN 157 216 CHORD 2.
FT DOMAIN 227 316 CS.
FT REGION 2 77 Interaction with PPP5C (By similarity).
FT REGION 65 316 Interaction with HSP90AA1 and HSP90AB1
FT (By similarity).
FT METAL 5 5 Zinc 1.
FT METAL 10 10 Zinc 1.
FT METAL 24 24 Zinc 1.
FT METAL 27 27 Zinc 2.
FT METAL 42 42 Zinc 2.
FT METAL 43 43 Zinc 2.
FT METAL 59 59 Zinc 2.
FT METAL 64 64 Zinc 1.
FT METAL 157 157 Zinc 3 (By similarity).
FT METAL 162 162 Zinc 3 (By similarity).
FT METAL 176 176 Zinc 3 (By similarity).
FT METAL 179 179 Zinc 4 (By similarity).
FT METAL 194 194 Zinc 4 (By similarity).
FT METAL 195 195 Zinc 4 (By similarity).
FT METAL 211 211 Zinc 4 (By similarity).
FT METAL 216 216 Zinc 3 (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 47 47 Phosphothreonine.
FT MOD_RES 51 51 Phosphoserine.
FT VAR_SEQ 39 57 Missing (in isoform 2).
FT /FTId=VSP_031150.
FT VARIANT 329 329 A -> D (in dbSNP:rs1045861).
FT /FTId=VAR_038676.
FT CONFLICT 234 234 W -> L (in Ref. 1; AAF18437).
FT CONFLICT 267 267 H -> I (in Ref. 1; AAF18437).
FT TURN 8 10
FT TURN 16 18
FT TURN 21 23
FT STRAND 31 34
FT STRAND 37 44
FT STRAND 46 49
FT HELIX 50 53
SQ SEQUENCE 332 AA; 37490 MW; 3142D8EC8A879155 CRC64;
MALLCYNRGC GQRFDPETNS DDACTYHPGV PVFHDALKGW SCCKRRTTDF SDFLSIVGCT
KGRHNSEKPP EPVKPEVKTT EKKELCELKP KFQEHIIQAP KPVEAIKRPS PDEPMTNLEL
KISASLKQAL DKLKLSSGNE ENKKEEDNDE IKIGTSCKNG GCSKTYQGLE SLEEVCVYHS
GVPIFHEGMK YWSCCRRKTS DFNTFLAQEG CTKGKHMWTK KDAGKKVVPC RHDWHQTGGE
VTISVYAKNS LPELSRVEAN STLLNVHIVF EGEKEFDQNV KLWGVIDVKR SYVTMTATKI
EITMRKAEPM QWASLELPAA KKQEKQKDAT TD
//
ID CHRD1_HUMAN Reviewed; 332 AA.
AC Q9UHD1; B2R6P8; Q6IN49; Q8WVL9; Q9H3D6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-FEB-2008, sequence version 2.
DT 22-JAN-2014, entry version 88.
DE RecName: Full=Cysteine and histidine-rich domain-containing protein 1;
DE AltName: Full=CHORD domain-containing protein 1;
DE Short=CHORD-containing protein 1;
DE Short=CHP-1;
DE AltName: Full=Protein morgana;
GN Name=CHORDC1; Synonyms=CHP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASP-329.
RX PubMed=10571178; DOI=10.1016/S0092-8674(00)81522-6;
RA Shirasu K., Lahaye T., Tan M.-W., Zhou F., Azevedo C.,
RA Schulze-Lefert P.;
RT "A novel class of eukaryotic zinc-binding proteins is required for
RT disease resistance signaling in barley and development in C.
RT elegans.";
RL Cell 99:355-366(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT ASP-329.
RC TISSUE=Heart;
RA Zhao Y., Cao H., Jiang Y., Meng X., Zhao X., Liu D., Ding J.;
RT "Isolation and characterization the chymotrypsin-like protein gene
RT from human heart cDNA library.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP ASP-329.
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASP-329.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 2-8; 47-61; 108-121; 249-256; 282-289; 291-299 AND
RP 306-321, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Bilsland A.E., Keith W.N.;
RL Submitted (JAN-2010) to UniProtKB.
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47 AND SER-51, AND MASS
RP SPECTROMETRY.
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP FUNCTION, INTERACTION WITH ROCK1 AND ROCK2, AND TISSUE SPECIFICITY.
RX PubMed=20230755; DOI=10.1016/j.devcel.2009.12.020;
RA Ferretti R., Palumbo V., Di Savino A., Velasco S., Sbroggio M.,
RA Sportoletti P., Micale L., Turco E., Silengo L., Palumbo G.,
RA Hirsch E., Teruya-Feldstein J., Bonaccorsi S., Pandolfi P.P.,
RA Gatti M., Tarone G., Brancaccio M.;
RT "Morgana/chp-1, a ROCK inhibitor involved in centrosome duplication
RT and tumorigenesis.";
RL Dev. Cell 18:486-495(2010).
RN [11]
RP INTERACTION WITH HSP90AA1.
RX PubMed=19875381; DOI=10.1074/mcp.M900261-MCP200;
RA Gano J.J., Simon J.A.;
RT "A proteomic investigation of ligand-dependent HSP90 complexes reveals
RT CHORDC1 as a novel ADP-dependent HSP90-interacting protein.";
RL Mol. Cell. Proteomics 9:255-270(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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.,
RA Buerckstuemmer T., 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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP STRUCTURE BY NMR OF 1-68.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the CHORD domain of human CHORD-containing
RT protein 1.";
RL Submitted (APR-2008) to the PDB data bank.
CC -!- FUNCTION: Regulates centrosome duplication, probably by inhibiting
CC the kinase activity of ROCK2. Proposed to act as co-chaperone for
CC HSP90. May play a role in the regulation of NOD1 via a HSP90
CC chaperone complex. In vitro, has intrinsic chaperone activity.
CC This function may be achieved by inhibiting association of ROCK2
CC with NPM1. Involved in stress response. Prevents tumorigenesis.
CC -!- SUBUNIT: Interacts with HSP90AA1, ROCK1 and ROCK2. Interacts with
CC HSP90AB1 and PPP5C (By similarity).
CC -!- INTERACTION:
CC P07900:HSP90AA1; NbExp=8; IntAct=EBI-2550959, EBI-296047;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UHD1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UHD1-2; Sequence=VSP_031150;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Underexpressed in many breast and lung
CC cancers.
CC -!- SIMILARITY: Contains 2 CHORD domains.
CC -!- SIMILARITY: Contains 1 CS domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17789.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF192466; AAF18437.1; -; mRNA.
DR EMBL; AF123249; AAG43237.1; -; mRNA.
DR EMBL; AK290231; BAF82920.1; -; mRNA.
DR EMBL; AK312663; BAG35545.1; -; mRNA.
DR EMBL; AP002364; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471065; EAW66868.1; -; Genomic_DNA.
DR EMBL; CH471065; EAW66870.1; -; Genomic_DNA.
DR EMBL; BC017789; AAH17789.1; ALT_INIT; mRNA.
DR EMBL; BC072461; AAH72461.1; -; mRNA.
DR RefSeq; NP_001137545.1; NM_001144073.1.
DR RefSeq; NP_036256.2; NM_012124.2.
DR UniGene; Hs.22857; -.
DR PDB; 2YRT; NMR; -; A=1-68.
DR PDBsum; 2YRT; -.
DR ProteinModelPortal; Q9UHD1; -.
DR SMR; Q9UHD1; 1-68, 157-216, 231-316.
DR IntAct; Q9UHD1; 5.
DR STRING; 9606.ENSP00000319255; -.
DR DMDM; 167008724; -.
DR PaxDb; Q9UHD1; -.
DR PeptideAtlas; Q6IN49; -.
DR PRIDE; Q9UHD1; -.
DR DNASU; 26973; -.
DR Ensembl; ENST00000320585; ENSP00000319255; ENSG00000110172.
DR Ensembl; ENST00000457199; ENSP00000401080; ENSG00000110172.
DR GeneID; 26973; -.
DR KEGG; hsa:26973; -.
DR UCSC; uc001pdg.2; human.
DR CTD; 26973; -.
DR GeneCards; GC11M089933; -.
DR H-InvDB; HIX0010016; -.
DR HGNC; HGNC:14525; CHORDC1.
DR HPA; HPA041040; -.
DR MIM; 604353; gene.
DR neXtProt; NX_Q9UHD1; -.
DR PharmGKB; PA26476; -.
DR eggNOG; NOG282821; -.
DR HOGENOM; HOG000207093; -.
DR HOVERGEN; HBG052156; -.
DR InParanoid; Q9UHD1; -.
DR KO; K16729; -.
DR OMA; WSCCKKK; -.
DR OrthoDB; EOG7X6M0X; -.
DR PhylomeDB; Q9UHD1; -.
DR ChiTaRS; CHORDC1; human.
DR EvolutionaryTrace; Q9UHD1; -.
DR GenomeRNAi; 26973; -.
DR NextBio; 49424; -.
DR PRO; PR:Q9UHD1; -.
DR ArrayExpress; Q9UHD1; -.
DR Bgee; Q9UHD1; -.
DR CleanEx; HS_CHORDC1; -.
DR Genevestigator; Q9UHD1; -.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
DR GO; GO:2000299; P:negative regulation of Rho-dependent protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:1900034; P:regulation of cellular response to heat; ISS:UniProtKB.
DR GO; GO:0010824; P:regulation of centrosome duplication; IEA:Ensembl.
DR GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR InterPro; IPR007051; CHORD.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chaperone;
KW Complete proteome; Direct protein sequencing; Metal-binding;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW Stress response; Zinc.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 332 Cysteine and histidine-rich domain-
FT containing protein 1.
FT /FTId=PRO_0000317770.
FT DOMAIN 5 64 CHORD 1.
FT DOMAIN 157 216 CHORD 2.
FT DOMAIN 227 316 CS.
FT REGION 2 77 Interaction with PPP5C (By similarity).
FT REGION 65 316 Interaction with HSP90AA1 and HSP90AB1
FT (By similarity).
FT METAL 5 5 Zinc 1.
FT METAL 10 10 Zinc 1.
FT METAL 24 24 Zinc 1.
FT METAL 27 27 Zinc 2.
FT METAL 42 42 Zinc 2.
FT METAL 43 43 Zinc 2.
FT METAL 59 59 Zinc 2.
FT METAL 64 64 Zinc 1.
FT METAL 157 157 Zinc 3 (By similarity).
FT METAL 162 162 Zinc 3 (By similarity).
FT METAL 176 176 Zinc 3 (By similarity).
FT METAL 179 179 Zinc 4 (By similarity).
FT METAL 194 194 Zinc 4 (By similarity).
FT METAL 195 195 Zinc 4 (By similarity).
FT METAL 211 211 Zinc 4 (By similarity).
FT METAL 216 216 Zinc 3 (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 47 47 Phosphothreonine.
FT MOD_RES 51 51 Phosphoserine.
FT VAR_SEQ 39 57 Missing (in isoform 2).
FT /FTId=VSP_031150.
FT VARIANT 329 329 A -> D (in dbSNP:rs1045861).
FT /FTId=VAR_038676.
FT CONFLICT 234 234 W -> L (in Ref. 1; AAF18437).
FT CONFLICT 267 267 H -> I (in Ref. 1; AAF18437).
FT TURN 8 10
FT TURN 16 18
FT TURN 21 23
FT STRAND 31 34
FT STRAND 37 44
FT STRAND 46 49
FT HELIX 50 53
SQ SEQUENCE 332 AA; 37490 MW; 3142D8EC8A879155 CRC64;
MALLCYNRGC GQRFDPETNS DDACTYHPGV PVFHDALKGW SCCKRRTTDF SDFLSIVGCT
KGRHNSEKPP EPVKPEVKTT EKKELCELKP KFQEHIIQAP KPVEAIKRPS PDEPMTNLEL
KISASLKQAL DKLKLSSGNE ENKKEEDNDE IKIGTSCKNG GCSKTYQGLE SLEEVCVYHS
GVPIFHEGMK YWSCCRRKTS DFNTFLAQEG CTKGKHMWTK KDAGKKVVPC RHDWHQTGGE
VTISVYAKNS LPELSRVEAN STLLNVHIVF EGEKEFDQNV KLWGVIDVKR SYVTMTATKI
EITMRKAEPM QWASLELPAA KKQEKQKDAT TD
//
MIM
604353
*RECORD*
*FIELD* NO
604353
*FIELD* TI
*604353 CYSTEINE- AND HISTIDINE-RICH DOMAIN-CONTAINING PROTEIN 1; CHORDC1
;;CHORD DOMAIN-CONTAINING PROTEIN 1; CHP1
read more*FIELD* TX
CLONING
Shirasu et al. (1999) cloned the cDNA of a human gene, designated CHP1,
that encodes a 332-amino acid protein containing 2 CHORD domains. CHORD
was defined as a 60-amino acid, cysteine- and histidine-rich,
Zn(2+)-binding domain that is conserved in tandem organization in
protozoa, plants, and metazoa.
GENE FUNCTION
Shirasu et al. (1999) found that silencing of the C. elegans
CHORD-containing gene, chp, resulted in semisterility and embryo
lethality, suggesting an essential function of the wildtype gene in
nematode development.
*FIELD* RF
1. Shirasu, K.; Lahaye, T.; Tan, M.-W.; Zhou, F.; Azevedo, C.; Schulze-Lefert,
P.: A novel class of eukaryotic zinc-binding proteins is required
for disease resistance signaling in barley and development in C. elegans. Cell 99:
355-366, 1999.
*FIELD* CD
Stylianos E. Antonarakis: 12/21/1999
*FIELD* ED
mgross: 11/20/2006
mgross: 3/1/2001
mgross: 12/21/1999
*RECORD*
*FIELD* NO
604353
*FIELD* TI
*604353 CYSTEINE- AND HISTIDINE-RICH DOMAIN-CONTAINING PROTEIN 1; CHORDC1
;;CHORD DOMAIN-CONTAINING PROTEIN 1; CHP1
read more*FIELD* TX
CLONING
Shirasu et al. (1999) cloned the cDNA of a human gene, designated CHP1,
that encodes a 332-amino acid protein containing 2 CHORD domains. CHORD
was defined as a 60-amino acid, cysteine- and histidine-rich,
Zn(2+)-binding domain that is conserved in tandem organization in
protozoa, plants, and metazoa.
GENE FUNCTION
Shirasu et al. (1999) found that silencing of the C. elegans
CHORD-containing gene, chp, resulted in semisterility and embryo
lethality, suggesting an essential function of the wildtype gene in
nematode development.
*FIELD* RF
1. Shirasu, K.; Lahaye, T.; Tan, M.-W.; Zhou, F.; Azevedo, C.; Schulze-Lefert,
P.: A novel class of eukaryotic zinc-binding proteins is required
for disease resistance signaling in barley and development in C. elegans. Cell 99:
355-366, 1999.
*FIELD* CD
Stylianos E. Antonarakis: 12/21/1999
*FIELD* ED
mgross: 11/20/2006
mgross: 3/1/2001
mgross: 12/21/1999