Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P52943

- CRIP2_HUMAN

UniProt

P52943 - CRIP2_HUMAN

Protein

Cysteine-rich protein 2

Gene

CRIP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    GO - Molecular functioni

    1. zinc ion binding Source: ProtInc

    GO - Biological processi

    1. hemopoiesis Source: Ensembl
    2. positive regulation of cell proliferation Source: Ensembl

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cysteine-rich protein 2
    Short name:
    CRP-2
    Alternative name(s):
    Protein ESP1
    Gene namesi
    Name:CRIP2
    Synonyms:CRP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:2361. CRIP2.

    Subcellular locationi

    GO - Cellular componenti

    1. cell cortex Source: Ensembl

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26879.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 208208Cysteine-rich protein 2PRO_0000075710Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei23 – 231N6-acetyllysineBy similarity
    Modified residuei138 – 1381N6-acetyllysine1 Publication
    Modified residuei144 – 1441N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP52943.
    PaxDbiP52943.
    PeptideAtlasiP52943.
    PRIDEiP52943.

    PTM databases

    PhosphoSiteiP52943.

    Expressioni

    Tissue specificityi

    Widespread tissue expression; highest levels in the heart.

    Gene expression databases

    ArrayExpressiP52943.
    BgeeiP52943.
    CleanExiHS_CRIP2.
    GenevestigatoriP52943.

    Organism-specific databases

    HPAiHPA042664.

    Interactioni

    Subunit structurei

    Interacts with TGFB1I1.By similarity

    Protein-protein interaction databases

    BioGridi107787. 12 interactions.
    DIPiDIP-49905N.
    IntActiP52943. 10 interactions.
    MINTiMINT-2857785.
    STRINGi9606.ENSP00000328521.

    Structurei

    Secondary structure

    1
    208
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni6 – 83
    Turni14 – 163
    Beta strandi17 – 204
    Beta strandi23 – 264
    Turni27 – 293
    Beta strandi33 – 353
    Beta strandi45 – 473
    Beta strandi50 – 523
    Turni54 – 563
    Helixi57 – 615

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CU8NMR-A1-63[»]
    ProteinModelPortaliP52943.
    SMRiP52943. Positions 1-63, 126-184.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52943.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 5753LIM zinc-binding 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini126 – 17853LIM zinc-binding 2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi63 – 7311Gly-richAdd
    BLAST
    Compositional biasi180 – 19415Gly-richAdd
    BLAST

    Sequence similaritiesi

    Contains 2 LIM zinc-binding domains.PROSITE-ProRule annotation

    Keywords - Domaini

    LIM domain, Repeat

    Phylogenomic databases

    eggNOGiNOG246818.
    HOGENOMiHOG000111234.
    HOVERGENiHBG051143.
    InParanoidiP52943.
    OMAiIEGQTAP.
    OrthoDBiEOG7CK39M.
    PhylomeDBiP52943.
    TreeFamiTF313758.

    Family and domain databases

    Gene3Di2.10.110.10. 2 hits.
    InterProiIPR001781. Znf_LIM.
    [Graphical view]
    PfamiPF00412. LIM. 2 hits.
    [Graphical view]
    SMARTiSM00132. LIM. 2 hits.
    [Graphical view]
    PROSITEiPS00478. LIM_DOMAIN_1. 2 hits.
    PS50023. LIM_DOMAIN_2. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P52943-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MASKCPKCDK TVYFAEKVSS LGKDWHKFCL KCERCSKTLT PGGHAEHDGK    50
    PFCHKPCYAT LFGPKGVNIG GAGSYIYEKP LAEGPQVTGP IEVPAARAEE 100
    RKASGPPKGP SRASSVTTFT GEPNTCPRCS KKVYFAEKVT SLGKDWHRPC 150
    LRCERCGKTL TPGGHAEHDG QPYCHKPCYG ILFGPKGVNT GAVGSYIYDR 200
    DPEGKVQP 208
    Length:208
    Mass (Da):22,493
    Last modified:October 1, 1996 - v1
    Checksum:iD32B99F98D51D3B0
    GO
    Isoform 2 (identifier: P52943-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-14: MASKCPKCDKTVYF → MPPHHLLPWL...TCLVHQAEGT

    Show »
    Length:282
    Mass (Da):30,221
    Checksum:iFF8BB75C7912BE75
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1414MASKC…KTVYF → MPPHHLLPWLAQVPSAEGEL VRLVSRAGGRGACFWPAVTM EMAVAAGCVCKGGGCCHREP SQDHHESQEHRGPLVGSQTC LVHQAEGT in isoform 2. 1 PublicationVSP_047074Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D42123 mRNA. Translation: BAA07703.1.
    U36190 mRNA. Translation: AAB03194.1.
    BT019911 mRNA. Translation: AAV38714.1.
    AK300092 mRNA. Translation: BAH13206.1.
    AK315757 mRNA. Translation: BAG38110.1.
    AL928654 Genomic DNA. No translation available.
    BC000434 mRNA. Translation: AAH00434.1.
    BC001931 mRNA. Translation: AAH01931.1.
    BC034151 mRNA. Translation: AAH34151.1.
    BC128101 mRNA. Translation: AAI28102.1.
    CCDSiCCDS10003.1. [P52943-1]
    CCDS59246.1. [P52943-2]
    PIRiG02090.
    RefSeqiNP_001257766.1. NM_001270837.1. [P52943-2]
    NP_001257770.1. NM_001270841.1.
    NP_001303.1. NM_001312.3. [P52943-1]
    UniGeneiHs.534309.

    Genome annotation databases

    EnsembliENST00000329146; ENSP00000328521; ENSG00000182809. [P52943-1]
    ENST00000483017; ENSP00000426119; ENSG00000182809. [P52943-2]
    GeneIDi1397.
    KEGGihsa:1397.
    UCSCiuc001yrd.2. human. [P52943-1]

    Polymorphism databases

    DMDMi1706133.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D42123 mRNA. Translation: BAA07703.1 .
    U36190 mRNA. Translation: AAB03194.1 .
    BT019911 mRNA. Translation: AAV38714.1 .
    AK300092 mRNA. Translation: BAH13206.1 .
    AK315757 mRNA. Translation: BAG38110.1 .
    AL928654 Genomic DNA. No translation available.
    BC000434 mRNA. Translation: AAH00434.1 .
    BC001931 mRNA. Translation: AAH01931.1 .
    BC034151 mRNA. Translation: AAH34151.1 .
    BC128101 mRNA. Translation: AAI28102.1 .
    CCDSi CCDS10003.1. [P52943-1 ]
    CCDS59246.1. [P52943-2 ]
    PIRi G02090.
    RefSeqi NP_001257766.1. NM_001270837.1. [P52943-2 ]
    NP_001257770.1. NM_001270841.1.
    NP_001303.1. NM_001312.3. [P52943-1 ]
    UniGenei Hs.534309.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CU8 NMR - A 1-63 [» ]
    ProteinModelPortali P52943.
    SMRi P52943. Positions 1-63, 126-184.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107787. 12 interactions.
    DIPi DIP-49905N.
    IntActi P52943. 10 interactions.
    MINTi MINT-2857785.
    STRINGi 9606.ENSP00000328521.

    PTM databases

    PhosphoSitei P52943.

    Polymorphism databases

    DMDMi 1706133.

    Proteomic databases

    MaxQBi P52943.
    PaxDbi P52943.
    PeptideAtlasi P52943.
    PRIDEi P52943.

    Protocols and materials databases

    DNASUi 1397.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000329146 ; ENSP00000328521 ; ENSG00000182809 . [P52943-1 ]
    ENST00000483017 ; ENSP00000426119 ; ENSG00000182809 . [P52943-2 ]
    GeneIDi 1397.
    KEGGi hsa:1397.
    UCSCi uc001yrd.2. human. [P52943-1 ]

    Organism-specific databases

    CTDi 1397.
    GeneCardsi GC14P105939.
    HGNCi HGNC:2361. CRIP2.
    HPAi HPA042664.
    MIMi 601183. gene.
    neXtProti NX_P52943.
    PharmGKBi PA26879.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG246818.
    HOGENOMi HOG000111234.
    HOVERGENi HBG051143.
    InParanoidi P52943.
    OMAi IEGQTAP.
    OrthoDBi EOG7CK39M.
    PhylomeDBi P52943.
    TreeFami TF313758.

    Miscellaneous databases

    ChiTaRSi CRIP2. human.
    EvolutionaryTracei P52943.
    GeneWikii CRIP2.
    GenomeRNAii 1397.
    NextBioi 35479932.
    PROi P52943.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P52943.
    Bgeei P52943.
    CleanExi HS_CRIP2.
    Genevestigatori P52943.

    Family and domain databases

    Gene3Di 2.10.110.10. 2 hits.
    InterProi IPR001781. Znf_LIM.
    [Graphical view ]
    Pfami PF00412. LIM. 2 hits.
    [Graphical view ]
    SMARTi SM00132. LIM. 2 hits.
    [Graphical view ]
    PROSITEi PS00478. LIM_DOMAIN_1. 2 hits.
    PS50023. LIM_DOMAIN_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human ESP1/CRP2, a member of the LIM domain protein family: characterization of the cDNA and assignment of the gene locus to chromosome 14q32.3."
      Karim M.A., Ohta K., Egashira M., Jinno Y., Niikawa N., Matsuda I., Indo Y.
      Genomics 31:167-176(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "A novel cDNA encoding for a LIM domain protein located at human chromosome 14q32 as a candidate for leukemic translocation."
      Tsui S.K.W., Chan P.P.K., Cheuk C.W., Liew C.C., Waye M.M.Y., Fung K.P., Lee C.Y.
      Biochem. Mol. Biol. Int. 39:747-754(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Heart.
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "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] (ISOFORMS 1 AND 2).
      Tissue: Lung and Pericardium.
    5. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM 1).
      Tissue: Lung.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-138, IDENTIFICATION BY MASS SPECTROMETRY [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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Solution structure of the LIM domain of human cysteine-rich protein 2."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JAN-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1-63.

    Entry informationi

    Entry nameiCRIP2_HUMAN
    AccessioniPrimary (citable) accession number: P52943
    Secondary accession number(s): A1A4U1, B7Z6C0, E9PD13
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 123 of the entry and version 1 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 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3