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Q9Y2V2

- CHSP1_HUMAN

UniProt

Q9Y2V2 - CHSP1_HUMAN

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
  1. 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

    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 mRNA processing body Source: UniProtKB-SubCell
    2. cytosol Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. P granule Source: UniProtKB

    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

    ArrayExpressiQ9Y2V2.
    BgeeiQ9Y2V2.
    CleanExiHS_CARHSP1.
    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 – 599
    Beta strandi63 – 708
    Turni72 – 743
    Beta strandi75 – 8410
    Beta strandi88 – 914
    Helixi92 – 943
    Beta strandi95 – 995
    Beta strandi106 – 1138
    Beta strandi121 – 13010
    Beta strandi133 – 1353

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MSSEPPPPPQ PPTHQASVGL LDTPRSRERS PSPLRGNVVP SPLPTRRTRT    50
    FSATVRASQG PVYKGVCKCF CRSKGHGFIT PADGGPDIFL HISDVEGEYV 100
    PVEGDEVTYK MCSIPPKNEK LQAVEVVITH LAPGTKHETW SGHVISS 147
    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:
    EMBL
    GenBank
    DDBJ
    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.
    GeneIDi23589.
    KEGGihsa:23589.
    UCSCiuc002czh.2. human.

    Polymorphism databases

    DMDMi41016932.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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 .
    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.
    HOGENOMi HOG000059524.
    HOVERGENi HBG050947.
    InParanoidi Q9Y2V2.
    OMAi WDAVSWL.
    OrthoDBi EOG7N63PN.
    PhylomeDBi Q9Y2V2.
    TreeFami TF324381.

    Miscellaneous databases

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

    Gene expression databases

    ArrayExpressi Q9Y2V2.
    Bgeei Q9Y2V2.
    CleanExi HS_CARHSP1.
    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

    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: October 1, 2014
    This is version 118 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