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Protein

Cysteine and histidine-rich domain-containing protein 1

Gene

Chordc1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis (By similarity).By similarity3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi5 – 51Zinc 1PROSITE-ProRule annotation
Metal bindingi10 – 101Zinc 1PROSITE-ProRule annotation
Metal bindingi24 – 241Zinc 1PROSITE-ProRule annotation
Metal bindingi27 – 271Zinc 2PROSITE-ProRule annotation
Metal bindingi42 – 421Zinc 2PROSITE-ProRule annotation
Metal bindingi43 – 431Zinc 2PROSITE-ProRule annotation
Metal bindingi59 – 591Zinc 2PROSITE-ProRule annotation
Metal bindingi64 – 641Zinc 1PROSITE-ProRule annotation
Metal bindingi157 – 1571Zinc 3PROSITE-ProRule annotation
Metal bindingi162 – 1621Zinc 3PROSITE-ProRule annotation
Metal bindingi176 – 1761Zinc 3PROSITE-ProRule annotation
Metal bindingi179 – 1791Zinc 4PROSITE-ProRule annotation
Metal bindingi194 – 1941Zinc 4PROSITE-ProRule annotation
Metal bindingi195 – 1951Zinc 4PROSITE-ProRule annotation
Metal bindingi211 – 2111Zinc 4PROSITE-ProRule annotation
Metal bindingi216 – 2161Zinc 3PROSITE-ProRule annotation

GO - Molecular functioni

  • ADP binding Source: MGI
  • ATP binding Source: MGI
  • Hsp90 protein binding Source: MGI
  • zinc ion binding Source: MGI

GO - Biological processi

  • chaperone-mediated protein folding Source: UniProtKB
  • negative regulation of Rho-dependent protein serine/threonine kinase activity Source: UniProtKB
  • regulation of cellular response to heat Source: UniProtKB
  • regulation of centrosome duplication Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine and histidine-rich domain-containing protein 1
Alternative name(s):
CHORD domain-containing protein 1
Short name:
CHORD-containing protein 1
Short name:
Chp-1
Protein morgana
Gene namesi
Name:Chordc1
Synonyms:Chp1, Morgana
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1914167. Chordc1.

Pathology & Biotechi

Disruption phenotypei

Results in centrosome amplification and lethality. Cells become polyploid or undergo apoptosis. Embryos are no longer detected after 3.5 dpc.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 331330Cysteine and histidine-rich domain-containing protein 1PRO_0000317771Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei47 – 471PhosphothreonineBy similarity
Modified residuei51 – 511PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9D1P4.
MaxQBiQ9D1P4.
PaxDbiQ9D1P4.
PeptideAtlasiQ9D1P4.
PRIDEiQ9D1P4.

PTM databases

iPTMnetiQ9D1P4.
PhosphoSiteiQ9D1P4.

Expressioni

Tissue specificityi

Ubiquitously expressed. Highly expressed in spleen, lung and brain (at protein level). Expressed in proliferating myoblasts and its expression remained steady after. Its expression undergoes diurnal and circadian changes in hypothalamus. Highly expressed during the dark-light transition (ZT20.5 (zeitgeber time 20.5) and ZT2.5).2 Publications

Developmental stagei

Weakly expressed at ZT8.5 and highly expressed at ZT14.5 at P6. At P6 highly expressed at ZT14.5 in hippocampus, prefrontal cortex and cerebellum. First detected and widely distributed at P1 and that continued throughout postnatal development. Expression is evident in the cortical plate (CP) at E17. Lower levels of expression is also evident in intermediate (IZ) and subventricular (SVZ) zones at this age. A more diffuse expression pattern is evident in early postnatal cortex with only slight differences in intensity throughout cortical layers. By P14, a more laminated distribution pattern becomes evident with a punctate distribution apparent in deep cortical layers.1 Publication

Inductioni

By Heat shock in a HSF1-dependent manner.1 Publication

Gene expression databases

BgeeiQ9D1P4.
GenevisibleiQ9D1P4. MM.

Interactioni

Subunit structurei

Interacts with HSP90AA1, HSP90AB1 and PPP5C. Interacts with ROCK1 and ROCK2 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi211809. 9 interactions.
IntActiQ9D1P4. 3 interactions.
MINTiMINT-1215377.
STRINGi10090.ENSMUSP00000001825.

Structurei

3D structure databases

ProteinModelPortaliQ9D1P4.
SMRiQ9D1P4. Positions 1-68, 157-216, 231-316.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 6460CHORD 1PROSITE-ProRule annotationAdd
BLAST
Domaini157 – 21660CHORD 2PROSITE-ProRule annotationAdd
BLAST
Domaini227 – 31690CSPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 7776Interaction with PPP5CAdd
BLAST
Regioni65 – 316252Interaction with HSP90AA1 and HSP90AB1Add
BLAST

Sequence similaritiesi

Contains 2 CHORD domains.PROSITE-ProRule annotation
Contains 1 CS domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1667. Eukaryota.
ENOG410XPV6. LUCA.
GeneTreeiENSGT00390000005180.
HOGENOMiHOG000207093.
HOVERGENiHBG052156.
InParanoidiQ9D1P4.
KOiK16729.
OMAiCCQKRTS.
OrthoDBiEOG7X6M0X.
PhylomeDBiQ9D1P4.
TreeFamiTF105394.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR007051. CHORD_dom.
IPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PfamiPF04968. CHORD. 2 hits.
PF04969. CS. 1 hit.
[Graphical view]
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS51401. CHORD. 2 hits.
PS51203. CS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9D1P4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLCYNRGC GQRFDPEANS DDACTYHPGV PVFHDALKGW SCCKRRTTDF
60 70 80 90 100
SDFLSIVGCT KGRHNSEKPP EPVKPEVKTT EKKELSELKP KFQEHIIQAP
110 120 130 140 150
KPVEAIKRPS PDEPMTNLEL KISASLKQAL DKLKLSSGSE EDKKEEDSDE
160 170 180 190 200
IKIGTSCKNG GCSKTYQGLQ SLEEVCVYHS GVPIFHEGMK YWSCCRRKTS
210 220 230 240 250
DFNTFLAQEG CTRGKHVWTK KDAGKKVVPC RHDWHQTGGE VTISVYAKNS
260 270 280 290 300
LPELSQVEAN STLLNVHIVF EGEKEFHQNV KLWGVIDVKR SYVTMTATKI
310 320 330
EITMRKAEPM QWASLELPTT KKQEKQKDIA D
Length:331
Mass (Da):37,351
Last modified:June 1, 2001 - v1
Checksum:i8E02FD5F4EB89BB9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003259 mRNA. Translation: BAB22675.1.
AK012747 mRNA. Translation: BAB28444.1.
AK132696 mRNA. Translation: BAE21307.1.
BC018374 mRNA. Translation: AAH18374.1.
CCDSiCCDS22842.1.
RefSeqiNP_080120.1. NM_025844.2.
UniGeneiMm.103534.

Genome annotation databases

EnsembliENSMUST00000001825; ENSMUSP00000001825; ENSMUSG00000001774.
GeneIDi66917.
KEGGimmu:66917.
UCSCiuc009ogm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003259 mRNA. Translation: BAB22675.1.
AK012747 mRNA. Translation: BAB28444.1.
AK132696 mRNA. Translation: BAE21307.1.
BC018374 mRNA. Translation: AAH18374.1.
CCDSiCCDS22842.1.
RefSeqiNP_080120.1. NM_025844.2.
UniGeneiMm.103534.

3D structure databases

ProteinModelPortaliQ9D1P4.
SMRiQ9D1P4. Positions 1-68, 157-216, 231-316.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211809. 9 interactions.
IntActiQ9D1P4. 3 interactions.
MINTiMINT-1215377.
STRINGi10090.ENSMUSP00000001825.

PTM databases

iPTMnetiQ9D1P4.
PhosphoSiteiQ9D1P4.

Proteomic databases

EPDiQ9D1P4.
MaxQBiQ9D1P4.
PaxDbiQ9D1P4.
PeptideAtlasiQ9D1P4.
PRIDEiQ9D1P4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000001825; ENSMUSP00000001825; ENSMUSG00000001774.
GeneIDi66917.
KEGGimmu:66917.
UCSCiuc009ogm.1. mouse.

Organism-specific databases

CTDi26973.
MGIiMGI:1914167. Chordc1.

Phylogenomic databases

eggNOGiKOG1667. Eukaryota.
ENOG410XPV6. LUCA.
GeneTreeiENSGT00390000005180.
HOGENOMiHOG000207093.
HOVERGENiHBG052156.
InParanoidiQ9D1P4.
KOiK16729.
OMAiCCQKRTS.
OrthoDBiEOG7X6M0X.
PhylomeDBiQ9D1P4.
TreeFamiTF105394.

Miscellaneous databases

ChiTaRSiChordc1. mouse.
PROiQ9D1P4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D1P4.
GenevisibleiQ9D1P4. MM.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR007051. CHORD_dom.
IPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PfamiPF04968. CHORD. 2 hits.
PF04969. CS. 1 hit.
[Graphical view]
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS51401. CHORD. 2 hits.
PS51203. CS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Testis.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Kidney.
  3. "Chp-1 and melusin, two CHORD containing proteins in vertebrates."
    Brancaccio M., Menini N., Bongioanni D., Ferretti R., De Acetis M., Silengo L., Tarone G.
    FEBS Lett. 551:47-52(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  4. "Mammalian CHORD-containing protein 1 is a novel heat shock protein 90-interacting protein."
    Wu J., Luo S., Jiang H., Li H.
    FEBS Lett. 579:421-426(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSP90AB1.
  5. "Regulation of Nod1 by Hsp90 chaperone complex."
    Hahn J.-S.
    FEBS Lett. 579:4513-4519(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSP90AA1 AND PPP5C, FUNCTION, INDUCTION.
  6. "The zinc-binding protein chordc1 undergoes complex diurnal changes in mRNA expression during mouse brain development."
    Gerstner J.R., Landry C.F.
    Neurochem. Res. 32:241-250(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. Cited for: FUNCTION.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  10. Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiCHRD1_MOUSE
AccessioniPrimary (citable) accession number: Q9D1P4
Secondary accession number(s): Q9CSI5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.