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Protein

Calcium-regulated heat stable protein 1

Gene

CARHSP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 Componenti: 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 mRNA processing body Source: UniProtKB-SubCell
  2. cytosol Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
  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 – 301Phosphoserine3 Publications
Modified residuei32 – 321Phosphoserine3 Publications
Modified residuei41 – 411Phosphoserine6 Publications
Modified residuei45 – 451Phosphothreonine1 Publication
Modified residuei52 – 521Phosphoserine5 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 similarity1 Publication

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. 18 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[»]
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.
OMAiAMSSEPP.
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 15, 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.
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi117124. 18 interactions.
IntActiQ9Y2V2. 6 interactions.
MINTiMINT-1432836.
STRINGi9606.ENSP00000311847.

PTM databases

PhosphoSiteiQ9Y2V2.

Polymorphism databases

DMDMi41016932.

Proteomic databases

MaxQBiQ9Y2V2.
PaxDbiQ9Y2V2.
PeptideAtlasiQ9Y2V2.
PRIDEiQ9Y2V2.

Protocols and materials databases

DNASUi23589.
Structural Biology KnowledgebaseSearch...

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.

Organism-specific databases

CTDi23589.
GeneCardsiGC16M008946.
HGNCiHGNC:17150. CARHSP1.
HPAiHPA051911.
neXtProtiNX_Q9Y2V2.
PharmGKBiPA38440.
GenAtlasiSearch...

Phylogenomic databases

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

Miscellaneous databases

ChiTaRSiCARHSP1. human.
GeneWikiiCARHSP1.
GenomeRNAii23589.
NextBioi46226.
PROiQ9Y2V2.

Gene expression databases

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

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]
ProtoNetiSearch...

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(1997) [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(2003) [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(2003) [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(2004) [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(2007) [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(2008) [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(2009) [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(2010) [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(2010) [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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-32; SER-41 AND SER-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "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(2010) [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 15, 2004
Last sequence update: January 15, 2004
Last modified: March 31, 2015
This is version 124 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

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 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.