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Q9Y2V2

- CHSP1_HUMAN

UniProt

Q9Y2V2 - CHSP1_HUMAN

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Protein

Calcium-regulated heat stable protein 1

Gene

CARHSP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Binds mRNA and regulates the stability of target mRNA. Binds single-stranded DNA (in vitro).2 Publications

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. mRNA 3'-UTR binding Source: UniProtKB
  3. phosphatase binding Source: UniProtKB

GO - Biological processi

  1. intracellular signal transduction Source: ProtInc
  2. regulation of mRNA stability Source: UniProtKB
  3. regulation of transcription, DNA-templated Source: InterPro
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium-regulated heat stable protein 1
Alternative name(s):
Calcium-regulated heat-stable protein of 24 kDa
Short name:
CRHSP-24
Gene namesi
Name:CARHSP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:17150. CARHSP1.

Subcellular locationi

Cytoplasm 1 Publication. CytoplasmP-body 1 Publication. Cytoplasmic granule 1 Publication
Note: Detected at cytoplasmic stress granules and P-bodies. Detected at exosome granules where mRNA is degraded (By similarity).By similarity

GO - Cellular componenti

  1. cytoplasmic exosome (RNase complex) Source: Ensembl
  2. cytosol Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProt
  4. P granule Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi41 – 411S → D: Reduced affinity for single-stranded DNA. Abolishes location at cytoplasmic stress granules. 1 Publication
Mutagenesisi76 – 761H → Q: Reduced affinity for single-stranded DNA. 1 Publication

Organism-specific databases

PharmGKBiPA38440.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 147146Calcium-regulated heat stable protein 1PRO_0000100230Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei30 – 301Phosphoserine2 Publications
Modified residuei32 – 321Phosphoserine2 Publications
Modified residuei41 – 411Phosphoserine5 Publications
Modified residuei45 – 451Phosphothreonine1 Publication
Modified residuei52 – 521Phosphoserine4 Publications
Modified residuei146 – 1461Phosphoserine1 Publication
Modified residuei147 – 1471Phosphoserine1 Publication

Post-translational modificationi

Dephosphorylated by calcineurin in a Ca2+ dependent manner (By similarity). Can be phosphorylated by DYRK2 (in vitro).By similarity5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Y2V2.
PaxDbiQ9Y2V2.
PeptideAtlasiQ9Y2V2.
PRIDEiQ9Y2V2.

PTM databases

PhosphoSiteiQ9Y2V2.

Expressioni

Gene expression databases

BgeeiQ9Y2V2.
CleanExiHS_CARHSP1.
ExpressionAtlasiQ9Y2V2. baseline and differential.
GenevestigatoriQ9Y2V2.

Organism-specific databases

HPAiHPA051911.

Interactioni

Subunit structurei

Homodimer. Interacts with STYX (By similarity).By similarity

Protein-protein interaction databases

BioGridi117124. 11 interactions.
IntActiQ9Y2V2. 6 interactions.
MINTiMINT-1432836.
STRINGi9606.ENSP00000311847.

Structurei

Secondary structure

1
147
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi51 – 599Combined sources
Beta strandi63 – 708Combined sources
Turni72 – 743Combined sources
Beta strandi75 – 8410Combined sources
Beta strandi88 – 914Combined sources
Helixi92 – 943Combined sources
Beta strandi95 – 995Combined sources
Beta strandi106 – 1138Combined sources
Beta strandi121 – 13010Combined sources
Beta strandi133 – 1353Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AQQX-ray2.80A/B/C/D1-147[»]
ProteinModelPortaliQ9Y2V2.
SMRiQ9Y2V2. Positions 43-141.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini62 – 12968CSDAdd
BLAST

Sequence similaritiesi

Contains 1 CSD (cold-shock) domain.Curated

Phylogenomic databases

eggNOGiNOG239041.
GeneTreeiENSGT00390000000022.
HOGENOMiHOG000059524.
HOVERGENiHBG050947.
InParanoidiQ9Y2V2.
OMAiWDAVSWL.
OrthoDBiEOG7N63PN.
PhylomeDBiQ9Y2V2.
TreeFamiTF324381.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR019844. Cold-shock_CS.
IPR011129. Cold_shock_prot.
IPR002059. CSP_DNA-bd.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PfamiPF00313. CSD. 1 hit.
[Graphical view]
SMARTiSM00357. CSP. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
PROSITEiPS00352. COLD_SHOCK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9Y2V2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSEPPPPPQ PPTHQASVGL LDTPRSRERS PSPLRGNVVP SPLPTRRTRT
60 70 80 90 100
FSATVRASQG PVYKGVCKCF CRSKGHGFIT PADGGPDIFL HISDVEGEYV
110 120 130 140
PVEGDEVTYK MCSIPPKNEK LQAVEVVITH LAPGTKHETW SGHVISS
Length:147
Mass (Da):15,892
Last modified:January 16, 2004 - v2
Checksum:i83D70DAE7B1FC573
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601G → V in AAD25021. (PubMed:9712905)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10537.1.
RefSeqiNP_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.
UniGeneiHs.632184.

Genome annotation databases

EnsembliENST00000311052; ENSP00000311847; ENSG00000153048.
ENST00000396593; ENSP00000379838; ENSG00000153048.
ENST00000561530; ENSP00000455284; ENSG00000153048.
ENST00000567554; ENSP00000455855; ENSG00000153048.
ENST00000610831; ENSP00000478055; ENSG00000153048.
ENST00000611932; ENSP00000481550; ENSG00000153048.
ENST00000614449; ENSP00000480542; ENSG00000153048.
ENST00000618335; ENSP00000483591; ENSG00000153048.
ENST00000619881; ENSP00000480144; ENSG00000153048.
GeneIDi23589.
KEGGihsa:23589.
UCSCiuc002czh.2. human.

Polymorphism databases

DMDMi41016932.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS10537.1.
RefSeqi NP_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.
UniGenei Hs.632184.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3AQQ X-ray 2.80 A/B/C/D 1-147 [» ]
ProteinModelPortali Q9Y2V2.
SMRi Q9Y2V2. Positions 43-141.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117124. 11 interactions.
IntActi Q9Y2V2. 6 interactions.
MINTi MINT-1432836.
STRINGi 9606.ENSP00000311847.

PTM databases

PhosphoSitei Q9Y2V2.

Polymorphism databases

DMDMi 41016932.

Proteomic databases

MaxQBi Q9Y2V2.
PaxDbi Q9Y2V2.
PeptideAtlasi Q9Y2V2.
PRIDEi Q9Y2V2.

Protocols and materials databases

DNASUi 23589.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000311052 ; ENSP00000311847 ; ENSG00000153048 .
ENST00000396593 ; ENSP00000379838 ; ENSG00000153048 .
ENST00000561530 ; ENSP00000455284 ; ENSG00000153048 .
ENST00000567554 ; ENSP00000455855 ; ENSG00000153048 .
ENST00000610831 ; ENSP00000478055 ; ENSG00000153048 .
ENST00000611932 ; ENSP00000481550 ; ENSG00000153048 .
ENST00000614449 ; ENSP00000480542 ; ENSG00000153048 .
ENST00000618335 ; ENSP00000483591 ; ENSG00000153048 .
ENST00000619881 ; ENSP00000480144 ; ENSG00000153048 .
GeneIDi 23589.
KEGGi hsa:23589.
UCSCi uc002czh.2. human.

Organism-specific databases

CTDi 23589.
GeneCardsi GC16M008946.
HGNCi HGNC:17150. CARHSP1.
HPAi HPA051911.
neXtProti NX_Q9Y2V2.
PharmGKBi PA38440.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG239041.
GeneTreei ENSGT00390000000022.
HOGENOMi HOG000059524.
HOVERGENi HBG050947.
InParanoidi Q9Y2V2.
OMAi WDAVSWL.
OrthoDBi EOG7N63PN.
PhylomeDBi Q9Y2V2.
TreeFami TF324381.

Miscellaneous databases

ChiTaRSi CARHSP1. human.
GeneWikii CARHSP1.
GenomeRNAii 23589.
NextBioi 46226.
PROi Q9Y2V2.

Gene expression databases

Bgeei Q9Y2V2.
CleanExi HS_CARHSP1.
ExpressionAtlasi Q9Y2V2. baseline and differential.
Genevestigatori Q9Y2V2.

Family and domain databases

Gene3Di 2.40.50.140. 1 hit.
InterProi IPR019844. Cold-shock_CS.
IPR011129. Cold_shock_prot.
IPR002059. CSP_DNA-bd.
IPR012340. NA-bd_OB-fold.
[Graphical view ]
Pfami PF00313. CSD. 1 hit.
[Graphical view ]
SMARTi SM00357. CSP. 1 hit.
[Graphical view ]
SUPFAMi SSF50249. SSF50249. 1 hit.
PROSITEi PS00352. COLD_SHOCK. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  8. 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. 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.

Entry informationi

Entry nameiCHSP1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2V2
Secondary accession number(s): B2R4C3
, D3DUF5, Q2YDX5, Q9BQ53
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 16, 2004
Last modified: November 26, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3