Q9Y2V2 (CHSP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Calcium-regulated heat stable protein 1

Alternative name(s):
Calcium-regulated heat-stable protein of 24 kDa
Short name=CRHSP-24

Gene names

Name:

CARHSP1

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	147 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	Binds mRNA and regulates the stability of target mRNA. Binds single-stranded DNA (in vitro). Ref.11 Ref.13
Subunit structure	Homodimer. Interacts with STYX By similarity. Ref.13
Subcellular location	Cytoplasm. Cytoplasm › P-body. Cytoplasmic granule. Note: Detected at cytoplasmic stress granules and P-bodies. Detected at exosome granules where mRNA is degraded By similarity. Ref.13
Post-translational modification	Dephosphorylated by calcineurin in a Ca2+ dependent manner By similarity. Can be phosphorylated by DYRK2 (in vitro). Ref.5
Sequence similarities	Contains 1 CSD (cold-shock) domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	RNA-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	intracellular signal transduction Traceable author statement Ref.1. Source: ProtInc regulation of mRNA stability Inferred from sequence or structural similarity. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro
Cellular_component	P granule Inferred from sequence or structural similarity. Source: UniProtKB cytoplasmic mRNA processing body Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro mRNA 3'-UTR binding Inferred from direct assay Ref.11. Source: UniProtKB phosphatase binding Non-traceable author statement PubMed 12801884. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.12

Chain

2 – 147

146

Calcium-regulated heat stable protein 1

PRO_0000100230

Regions

Domain

62 – 129

68

CSD

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.12

Modified residue

30

1

Phosphoserine Ref.5 Ref.8

Modified residue

32

1

Phosphoserine Ref.5 Ref.8

Modified residue

41

1

Phosphoserine Ref.5 Ref.7 Ref.8 Ref.9 Ref.12

Modified residue

45

1

Phosphothreonine Ref.12

Modified residue

52

1

Phosphoserine Ref.5 Ref.8 Ref.9 Ref.12

Modified residue

146

1

Phosphoserine Ref.8

Modified residue

147

1

Phosphoserine Ref.8

Experimental info

Mutagenesis

41

1

S → D: Reduced affinity for single-stranded DNA. Abolishes location at cytoplasmic stress granules. Ref.13

Mutagenesis

76

1

H → Q: Reduced affinity for single-stranded DNA. Ref.13

Sequence conflict

60

1

G → V in AAD25021. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

147

Helix Strand Turn

Details...

Helix

51 – 59

9

Beta strand

63 – 70

8

Turn

72 – 74

3

Beta strand

75 – 84

10

Beta strand

88 – 91

4

Helix

92 – 94

3

Beta strand

95 – 99

5

Beta strand

106 – 113

8

Beta strand

121 – 130

10

Beta strand

133 – 135

3

Sequences

	Sequence		Length	Mass (Da)
	Q9Y2V2 [UniParc]. Last modified January 16, 2004. Version 2. Checksum: 83D70DAE7B1FC573	FASTA	147	15,892
	10 20 30 40 50 60 MSSEPPPPPQ PPTHQASVGL LDTPRSRERS PSPLRGNVVP SPLPTRRTRT FSATVRASQG 70 80 90 100 110 120 PVYKGVCKCF CRSKGHGFIT PADGGPDIFL HISDVEGEYV PVEGDEVTYK MCSIPPKNEK 130 140 LQAVEVVITH LAPGTKHETW SGHVISS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Purification and characterization of a novel physiological substrate for calcineurin in mammalian cells." Groblewski G.E., Yoshida M., Bragado M.J., Ernst S.A., Leykam J., Williams J.A. J. Biol. Chem. 273:22738-22744(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[2]	"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]. Tissue: Brain.
[3]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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]. Tissue: Placenta and Prostate.
[5]	"Identification of calcium-regulated heat-stable protein of 24 kDa (CRHSP24) as a physiological substrate for PKB and RSK using KESTREL." Auld G.C., Campbell D.G., Morrice N., Cohen P. Biochem. J. 389:775-783(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-30; SER-32; SER-41 AND SER-52.
[6]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[7]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, MASS SPECTROMETRY. Tissue: Platelet.
[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 SER-30; SER-32; SER-41; SER-52; SER-146 AND SER-147, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-52, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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].
[11]	"CARHSP1 is required for effective tumor necrosis factor alpha mRNA stabilization and localizes to processing bodies and exosomes." Pfeiffer J.R., McAvoy B.L., Fecteau R.E., Deleault K.M., Brooks S.A. Mol. Cell. Biol. 31:277-286(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, RNA-BINDING, MASS SPECTROMETRY.
[12]	"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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; THR-45 AND SER-52, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE.
[13]	"Structure-functional analyses of CRHSP-24 plasticity and dynamics in oxidative stress response." Hou H., Wang F., Zhang W., Wang D., Li X., Bartlam M., Shen Y., Yao X., Rao Z. J. Biol. Chem. 286:9623-9635(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SUBUNIT, FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, MUTAGENESIS OF SER-41 AND HIS-76.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF115345 mRNA. Translation: AAD25021.1.
AK311777 mRNA. Translation: BAG34720.1.
CH471112 Genomic DNA. Translation: EAW85196.1.
CH471112 Genomic DNA. Translation: EAW85197.1.
CH471112 Genomic DNA. Translation: EAW85198.1.
CH471112 Genomic DNA. Translation: EAW85199.1.
BC003366 mRNA. Translation: AAH03366.1.
BC108283 mRNA. Translation: AAI08284.1.

IPI

IPI00304409.

RefSeq

NP_001035941.1. NM_001042476.1.
NP_055131.2. NM_014316.2.

UniGene

Hs.632184.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3AQQ	X-ray	2.80	A/B/C/D	1-147	[»]

ProteinModelPortal

Q9Y2V2.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9Y2V2. 1 interaction.

MINT

MINT-1432836.

STRING

9606.ENSP00000311847.

PTM databases

PhosphoSite

Q9Y2V2.

Polymorphism databases

DMDM

41016932.

Proteomic databases

PaxDb

Q9Y2V2.

PeptideAtlas

Q9Y2V2.

PRIDE

Q9Y2V2.

Protocols and materials databases

DNASU

23589.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000311052; ENSP00000311847; ENSG00000153048.
ENST00000396593; ENSP00000379838; ENSG00000153048.
ENST00000561530; ENSP00000455284; ENSG00000153048.
ENST00000567554; ENSP00000455855; ENSG00000153048.

GeneID

23589.

KEGG

hsa:23589.

UCSC

uc002czh.1. human.

Organism-specific databases

CTD

23589.

GeneCards

GC16M008946.

HGNC

HGNC:17150. CARHSP1.

HPA

HPA051911.

neXtProt

NX_Q9Y2V2.

PharmGKB

PA38440.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG239041.

HOGENOM

HOG000059524.

HOVERGEN

HBG050947.

InParanoid

Q9Y2V2.

OMA

PDIFVHI.

OrthoDB

EOG4V4390.

PhylomeDB

Q9Y2V2.

Gene expression databases

ArrayExpress

Q9Y2V2.

Bgee

Q9Y2V2.

CleanEx

HS_CARHSP1.

Genevestigator

Q9Y2V2.

GermOnline

ENSG00000153048. Homo sapiens.

Family and domain databases

Gene3D

2.40.50.140. 1 hit.

InterPro

IPR019844. Cold-shock_CS.
IPR011129. Cold_shock_prot.
IPR002059. CSP_DNA-bd.
IPR012340. NA-bd_OB-fold.
[Graphical view]

Pfam

PF00313. CSD. 1 hit.
[Graphical view]

SMART

SM00357. CSP. 1 hit.
[Graphical view]

SUPFAM

SSF50249. Nucleic_acid_OB. 1 hit.

PROSITE

PS00352. COLD_SHOCK. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

GenomeRNAi

23589.

NextBio

46226.

Entry information

Entry name

CHSP1_HUMAN

Accession

Primary (citable) accession number: Q9Y2V2
Secondary accession number(s): B2R4C3 , D3DUF5, Q2YDX5, Q9BQ53

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	January 16, 2004
Last modified:	May 1, 2013
This is version 106 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.