Q9UHD1 (CHRD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	CHORDC1
Synonyms:	CHP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	332 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.9
Subunit structure	Interacts with HSP90AA1, ROCK1 and ROCK2. Interacts with HSP90AB1 and PPP5C By similarity. Ref.9 Ref.10
Tissue specificity	Underexpressed in many breast and lung cancers. Ref.9
Sequence similarities	Contains 2 CHORD domains. Contains 1 CS domain.
Sequence caution	The sequence AAH17789.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Stress response
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	Metal-binding Zinc
Molecular function	Chaperone
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	chaperone-mediated protein folding Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of Rho-dependent protein serine/threonine kinase activity Inferred from electronic annotation. Source: Compara regulation of centrosome duplication Inferred from electronic annotation. Source: Compara regulation of response to stress Inferred from sequence or structural similarity. Source: UniProtKB response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	zinc ion binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HSP90AA1	P07900	8	EBI-2550959,EBI-296047

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UHD1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9UHD1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     39-57: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7

Chain

2 – 332

331

Cysteine and histidine-rich domain-containing protein 1

PRO_0000317770

Regions

Domain

5 – 64

60

CHORD 1

Domain

157 – 216

60

CHORD 2

Domain

227 – 316

90

CS

Region

2 – 77

76

Interaction with PPP5C By similarity

Region

65 – 316

252

Interaction with HSP90AA1 and HSP90AB1 By similarity

Sites

Metal binding

5

1

Zinc 1

Metal binding

10

1

Zinc 1

Metal binding

24

1

Zinc 1

Metal binding

27

1

Zinc 2

Metal binding

42

1

Zinc 2

Metal binding

43

1

Zinc 2

Metal binding

59

1

Zinc 2

Metal binding

64

1

Zinc 1

Metal binding

157

1

Zinc 3 By similarity

Metal binding

162

1

Zinc 3 By similarity

Metal binding

176

1

Zinc 3 By similarity

Metal binding

179

1

Zinc 4 By similarity

Metal binding

194

1

Zinc 4 By similarity

Metal binding

195

1

Zinc 4 By similarity

Metal binding

211

1

Zinc 4 By similarity

Metal binding

216

1

Zinc 3 By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.7

Modified residue

47

1

Phosphothreonine Ref.8

Modified residue

51

1

Phosphoserine Ref.8

Modified residue

204

1

Phosphothreonine By similarity

Natural variations

Alternative sequence

39 – 57

19

Missing in isoform 2.

VSP_031150

Natural variant

329

1

A → D. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs1045861 [ dbSNP | Ensembl ].

VAR_038676

Experimental info

Sequence conflict

234

1

W → L in AAF18437. Ref.1

Sequence conflict

267

1

H → I in AAF18437. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

332

Helix Strand Turn

Details...

Turn

8 – 10

3

Turn

16 – 18

3

Turn

21 – 23

3

Beta strand

31 – 34

4

Beta strand

37 – 44

8

Beta strand

46 – 49

4

Helix

50 – 53

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 5, 2008. Version 2. Checksum: 3142D8EC8A879155	FASTA	332	37,490
	10 20 30 40 50 60 MALLCYNRGC GQRFDPETNS DDACTYHPGV PVFHDALKGW SCCKRRTTDF SDFLSIVGCT 70 80 90 100 110 120 KGRHNSEKPP EPVKPEVKTT EKKELCELKP KFQEHIIQAP KPVEAIKRPS PDEPMTNLEL 130 140 150 160 170 180 KISASLKQAL DKLKLSSGNE ENKKEEDNDE IKIGTSCKNG GCSKTYQGLE SLEEVCVYHS 190 200 210 220 230 240 GVPIFHEGMK YWSCCRRKTS DFNTFLAQEG CTKGKHMWTK KDAGKKVVPC RHDWHQTGGE 250 260 270 280 290 300 VTISVYAKNS LPELSRVEAN STLLNVHIVF EGEKEFDQNV KLWGVIDVKR SYVTMTATKI 310 320 330 EITMRKAEPM QWASLELPAA KKQEKQKDAT TD
	Isoform 2 [UniParc]. Checksum: 3347F35622425A90	FASTA	313	35,286
	10 20 30 40 50 60 MALLCYNRGC GQRFDPETNS DDACTYHPGV PVFHDALKGC TKGRHNSEKP PEPVKPEVKT 70 80 90 100 110 120 TEKKELCELK PKFQEHIIQA PKPVEAIKRP SPDEPMTNLE LKISASLKQA LDKLKLSSGN 130 140 150 160 170 180 EENKKEEDND EIKIGTSCKN GGCSKTYQGL ESLEEVCVYH SGVPIFHEGM KYWSCCRRKT 190 200 210 220 230 240 SDFNTFLAQE GCTKGKHMWT KKDAGKKVVP CRHDWHQTGG EVTISVYAKN SLPELSRVEA 250 260 270 280 290 300 NSTLLNVHIV FEGEKEFDQN VKLWGVIDVK RSYVTMTATK IEITMRKAEP MQWASLELPA 310 AKKQEKQKDA TTD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel class of eukaryotic zinc-binding proteins is required for disease resistance signaling in barley and development in C. elegans." Shirasu K., Lahaye T., Tan M.-W., Zhou F., Azevedo C., Schulze-Lefert P. Cell 99:355-366(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASP-329.
[2]	"Isolation and characterization the chymotrypsin-like protein gene from human heart cDNA library." Zhao Y., Cao H., Jiang Y., Meng X., Zhao X., Liu D., Ding J. Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ASP-329. Tissue: Heart.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASP-329. Tissue: Thalamus.
[4]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASP-329.
[6]	"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] (ISOFORM 1). Tissue: Brain and Uterus.
[7]	Bienvenut W.V., Bilsland A.E., Keith W.N. Submitted (JAN-2010) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-8; 47-61; 108-121; 249-256; 282-289; 291-299 AND 306-321, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Colon carcinoma.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47 AND SER-51, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Morgana/chp-1, a ROCK inhibitor involved in centrosome duplication and tumorigenesis." Ferretti R., Palumbo V., Di Savino A., Velasco S., Sbroggio M., Sportoletti P., Micale L., Turco E., Silengo L., Palumbo G., Hirsch E., Teruya-Feldstein J., Bonaccorsi S., Pandolfi P.P., Gatti M., Tarone G., Brancaccio M. Dev. Cell 18:486-495(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ROCK1 AND ROCK2, TISSUE SPECIFICITY.
[10]	"A proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting protein." Gano J.J., Simon J.A. Mol. Cell. Proteomics 9:255-270(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HSP90AA1.
[11]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"Solution structure of the CHORD domain of human CHORD-containing protein 1." RIKEN structural genomics initiative (RSGI) Submitted (APR-2008) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1-68.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF192466 mRNA. Translation: AAF18437.1.
AF123249 mRNA. Translation: AAG43237.1.
AK290231 mRNA. Translation: BAF82920.1.
AK312663 mRNA. Translation: BAG35545.1.
AP002364 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW66868.1.
CH471065 Genomic DNA. Translation: EAW66870.1.
BC017789 mRNA. Translation: AAH17789.1. Different initiation.
BC072461 mRNA. Translation: AAH72461.1.

IPI

IPI00015897.
IPI00885057.

RefSeq

NP_001137545.1. NM_001144073.1.
NP_036256.2. NM_012124.2.

UniGene

Hs.22857.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2YRT	NMR	-	A	1-68	[»]

ProteinModelPortal

Q9UHD1.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UHD1. 5 interactions.

STRING

9606.ENSP00000319255.

Polymorphism databases

DMDM

167008724.

Proteomic databases

PaxDb

Q9UHD1.

PeptideAtlas

Q6IN49.

PRIDE

Q9UHD1.

Protocols and materials databases

DNASU

26973.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000320585; ENSP00000319255; ENSG00000110172.
ENST00000457199; ENSP00000401080; ENSG00000110172.

GeneID

26973.

KEGG

hsa:26973.

UCSC

uc001pdg.2. human.
uc009yvz.2. human.

Organism-specific databases

CTD

26973.

GeneCards

GC11M089933.

H-InvDB

HIX0010016.

HGNC

HGNC:14525. CHORDC1.

HPA

HPA041040.

MIM

604353. gene.

neXtProt

NX_Q9UHD1.

PharmGKB

PA26476.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG282821.

HOGENOM

HOG000207093.

HOVERGEN

HBG052156.

InParanoid

Q9UHD1.

KO

K16729.

OMA

GCTKGKH.

OrthoDB

EOG43N7D5.

PhylomeDB

Q9UHD1.

Gene expression databases

ArrayExpress

Q9UHD1.

Bgee

Q9UHD1.

CleanEx

HS_CHORDC1.

Genevestigator

Q9UHD1.

Family and domain databases

InterPro

IPR007051. CHORD.
IPR007052. CS-like_domain.
IPR017447. CS_domain.
IPR008978. HSP20-like_chaperone.
[Graphical view]

Pfam

PF04968. CHORD. 2 hits.
PF04969. CS. 1 hit.
[Graphical view]

SUPFAM

SSF49764. HSP20_chap. 1 hit.

PROSITE

PS51401. CHORD. 2 hits.
PS51203. CS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CHORDC1. human.

EvolutionaryTrace

Q9UHD1.

GenomeRNAi

26973.

NextBio

49424.

SOURCE

Search...

Entry information

Entry name

CHRD1_HUMAN

Accession

Primary (citable) accession number: Q9UHD1
Secondary accession number(s): B2R6P8 , Q6IN49, Q8WVL9, Q9H3D6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	February 5, 2008
Last modified:	May 1, 2013
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.