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Q9Y2V2 (CHSP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length147 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds mRNA and regulates the stability of target mRNA. Binds single-stranded DNA (in vitro). Ref.12 Ref.14

Subunit structure

Homodimer. Interacts with STYX By similarity. Ref.14

Subcellular location

Cytoplasm. CytoplasmP-body. Cytoplasmic granule. Note: Detected at cytoplasmic stress granules and P-bodies. Detected at exosome granules where mRNA is degraded By similarity. Ref.14

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 147146Calcium-regulated heat stable protein 1
PRO_0000100230

Regions

Domain62 – 12968CSD

Amino acid modifications

Modified residue21N-acetylserine Ref.9 Ref.13
Modified residue301Phosphoserine Ref.5 Ref.8
Modified residue321Phosphoserine Ref.5 Ref.8
Modified residue411Phosphoserine Ref.5 Ref.7 Ref.8 Ref.10 Ref.13
Modified residue451Phosphothreonine Ref.13
Modified residue521Phosphoserine Ref.5 Ref.8 Ref.10 Ref.13
Modified residue1461Phosphoserine Ref.8
Modified residue1471Phosphoserine Ref.8

Experimental info

Mutagenesis411S → D: Reduced affinity for single-stranded DNA. Abolishes location at cytoplasmic stress granules. Ref.14
Mutagenesis761H → Q: Reduced affinity for single-stranded DNA. Ref.14
Sequence conflict601G → V in AAD25021. Ref.1

Secondary structure

.................. 147
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y2V2 [UniParc].

Last modified January 16, 2004. Version 2.
Checksum: 83D70DAE7B1FC573

FASTA14715,892
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[10]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
[12]"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, IDENTIFICATION BY MASS SPECTROMETRY.
[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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; THR-45 AND SER-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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.
RefSeqNP_001035941.1. NM_001042476.2.
NP_001265189.1. NM_001278260.1.
NP_001265190.1. NM_001278261.1.
NP_001265191.1. NM_001278262.1.
NP_001265192.1. NM_001278263.1.
NP_001265193.1. NM_001278264.1.
NP_001265194.1. NM_001278265.1.
NP_001265195.1. NM_001278266.1.
NP_055131.2. NM_014316.3.
XP_005255286.1. XM_005255229.2.
UniGeneHs.632184.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3AQQX-ray2.80A/B/C/D1-147[»]
ProteinModelPortalQ9Y2V2.
SMRQ9Y2V2. Positions 43-141.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117124. 11 interactions.
IntActQ9Y2V2. 6 interactions.
MINTMINT-1432836.
STRING9606.ENSP00000311847.

PTM databases

PhosphoSiteQ9Y2V2.

Polymorphism databases

DMDM41016932.

Proteomic databases

PaxDbQ9Y2V2.
PeptideAtlasQ9Y2V2.
PRIDEQ9Y2V2.

Protocols and materials databases

DNASU23589.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000311052; ENSP00000311847; ENSG00000153048.
ENST00000396593; ENSP00000379838; ENSG00000153048.
ENST00000561530; ENSP00000455284; ENSG00000153048.
ENST00000567554; ENSP00000455855; ENSG00000153048.
GeneID23589.
KEGGhsa:23589.
UCSCuc002czh.2. human.

Organism-specific databases

CTD23589.
GeneCardsGC16M008946.
HGNCHGNC:17150. CARHSP1.
HPAHPA051911.
neXtProtNX_Q9Y2V2.
PharmGKBPA38440.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG239041.
HOGENOMHOG000059524.
HOVERGENHBG050947.
InParanoidQ9Y2V2.
OMAAMSSEPP.
OrthoDBEOG7N63PN.
PhylomeDBQ9Y2V2.
TreeFamTF324381.

Gene expression databases

ArrayExpressQ9Y2V2.
BgeeQ9Y2V2.
CleanExHS_CARHSP1.
GenevestigatorQ9Y2V2.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
InterProIPR019844. Cold-shock_CS.
IPR011129. Cold_shock_prot.
IPR002059. CSP_DNA-bd.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PfamPF00313. CSD. 1 hit.
[Graphical view]
SMARTSM00357. CSP. 1 hit.
[Graphical view]
SUPFAMSSF50249. SSF50249. 1 hit.
PROSITEPS00352. COLD_SHOCK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCARHSP1.
GenomeRNAi23589.
NextBio46226.
PROQ9Y2V2.

Entry information

Entry nameCHSP1_HUMAN
AccessionPrimary (citable) accession number: Q9Y2V2
Secondary accession number(s): B2R4C3 expand/collapse secondary AC list , D3DUF5, Q2YDX5, Q9BQ53
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 16, 2004
Last modified: April 16, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM