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P15882

- CHIN_HUMAN

UniProt

P15882 - CHIN_HUMAN

Protein

N-chimaerin

Gene

CHN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 3 (11 Jul 2002)
      Previous versions | rss
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    Functioni

    GTPase-activating protein for p21-rac and a phorbol ester receptor. Involved in the assembly of neuronal locomotor circuits as a direct effector of EPHA4 in axon guidance.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri205 – 25551Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. GTPase activator activity Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. SH3/SH2 adaptor activity Source: ProtInc

    GO - Biological processi

    1. ephrin receptor signaling pathway Source: UniProtKB
    2. motor neuron axon guidance Source: UniProtKB
    3. positive regulation of signal transduction Source: GOC
    4. regulation of axonogenesis Source: UniProtKB
    5. regulation of Rac GTPase activity Source: Ensembl
    6. regulation of small GTPase mediated signal transduction Source: Reactome
    7. small GTPase mediated signal transduction Source: Reactome

    Keywords - Molecular functioni

    GTPase activation

    Keywords - Biological processi

    Neurogenesis

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.
    SignaLinkiP15882.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-chimaerin
    Alternative name(s):
    A-chimaerin
    Alpha-chimerin
    N-chimerin
    Short name:
    NC
    Rho GTPase-activating protein 2
    Gene namesi
    Name:CHN1
    Synonyms:ARHGAP2, CHN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:1943. CHN1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Involvement in diseasei

    Duane retraction syndrome 2 (DURS2) [MIM:604356]: Duane retraction syndrome is a congenital eye movement disorder characterized by a failure of cranial nerve VI (the abducens nerve) to develop normally, resulting in restriction or absence of abduction, adduction, or both, and narrowing of the palpebral fissure and retraction of the globe on attempted adduction. Undiagnosed in children, it can lead to amblyopia, a permanent uncorrectable loss of vision.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti20 – 201L → F in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA). 1 Publication
    VAR_047940
    Natural varianti126 – 1261I → M in DURS2; behaves as a dominant gain-of -function allele that increases CHN1 activity in vitro. 1 Publication
    VAR_047941
    Natural varianti143 – 1431Y → H in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA). 1 Publication
    VAR_047942
    Natural varianti223 – 2231A → V in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA). 1 Publication
    VAR_047943
    Natural varianti228 – 2281G → S in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro. 1 Publication
    VAR_047944
    Natural varianti252 – 2521P → Q in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA). 1 Publication
    VAR_047945
    Natural varianti313 – 3131E → K in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro. 1 Publication
    VAR_047946

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi604356. phenotype.
    Orphaneti233. Duane retraction syndrome.
    PharmGKBiPA26473.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 459458N-chimaerinPRO_0000056694Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei340 – 3401PhosphothreonineBy similarity

    Post-translational modificationi

    Phosphorylated. Phosphorylation is EPHA4 kinase activity-dependent By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP15882.
    PaxDbiP15882.
    PRIDEiP15882.

    PTM databases

    PhosphoSiteiP15882.

    Expressioni

    Tissue specificityi

    In neurons in brain regions that are involved in learning and memory processes.

    Developmental stagei

    Increases in amount during brain development coincident with synaptogenesis.

    Gene expression databases

    ArrayExpressiP15882.
    BgeeiP15882.
    CleanExiHS_CHN1.
    GenevestigatoriP15882.

    Organism-specific databases

    HPAiHPA036111.

    Interactioni

    Subunit structurei

    Interacts with EPHA4; effector of EPHA4 in axon guidance linking EPHA4 activation to RAC1 regulation.By similarity

    Protein-protein interaction databases

    BioGridi107547. 6 interactions.
    DIPiDIP-42177N.
    IntActiP15882. 5 interactions.
    MINTiMINT-1173390.
    STRINGi9606.ENSP00000386741.

    Structurei

    Secondary structure

    1
    459
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi19 – 268
    Helixi56 – 638
    Beta strandi69 – 746
    Beta strandi76 – 783
    Beta strandi82 – 876
    Beta strandi89 – 968
    Beta strandi98 – 10710
    Helixi113 – 12917
    Helixi131 – 1366
    Turni143 – 1453
    Beta strandi146 – 1483
    Helixi164 – 1663
    Beta strandi208 – 2114
    Turni220 – 2223
    Beta strandi228 – 2303
    Beta strandi233 – 2364
    Turni237 – 2393
    Helixi245 – 2484
    Helixi257 – 2615
    Helixi270 – 2778
    Helixi283 – 29513
    Turni300 – 3045
    Helixi309 – 32214
    Helixi323 – 3253
    Turni330 – 3323
    Helixi336 – 34813
    Turni357 – 3593
    Helixi360 – 3689
    Helixi372 – 38413
    Helixi388 – 40619
    Helixi408 – 4114
    Helixi415 – 42612
    Helixi434 – 45320
    Helixi455 – 4584

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2OSAX-ray1.80A260-459[»]
    3CXLX-ray2.60A15-459[»]
    ProteinModelPortaliP15882.
    SMRiP15882. Positions 15-459.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15882.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini49 – 13587SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini268 – 459192Rho-GAPPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
    Contains 1 Rho-GAP domain.PROSITE-ProRule annotation
    Contains 1 SH2 domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri205 – 25551Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    SH2 domain, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG295484.
    HOGENOMiHOG000231926.
    HOVERGENiHBG080489.
    InParanoidiP15882.
    OMAiNREPAHK.
    OrthoDBiEOG73JKVC.
    PhylomeDBiP15882.
    TreeFamiTF342052.

    Family and domain databases

    Gene3Di1.10.555.10. 1 hit.
    3.30.505.10. 1 hit.
    InterProiIPR020454. DAG/PE-bd.
    IPR017356. N-chimaerin.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    IPR000980. SH2.
    [Graphical view]
    PfamiPF00130. C1_1. 1 hit.
    PF00620. RhoGAP. 1 hit.
    PF00017. SH2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038015. N-chimaerin. 1 hit.
    PRINTSiPR00008. DAGPEDOMAIN.
    SMARTiSM00109. C1. 1 hit.
    SM00324. RhoGAP. 1 hit.
    SM00252. SH2. 1 hit.
    [Graphical view]
    SUPFAMiSSF48350. SSF48350. 1 hit.
    SSF55550. SSF55550. 1 hit.
    PROSITEiPS50238. RHOGAP. 1 hit.
    PS50001. SH2. 1 hit.
    PS00479. ZF_DAG_PE_1. 1 hit.
    PS50081. ZF_DAG_PE_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform Alpha-2 (identifier: P15882-1) [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

    MALTLFDTDE YRPPVWKSYL YQLQQEAPHP RRITCTCEVE NRPKYYGREF    50
    HGMISREAAD QLLIVAEGSY LIRESQRQPG TYTLALRFGS QTRNFRLYYD 100
    GKHFVGEKRF ESIHDLVTDG LITLYIETKA AEYIAKMTIN PIYEHVGYTT 150
    LNREPAYKKH MPVLKETHDE RDSTGQDGVS EKRLTSLVRR ATLKENEQIP 200
    KYEKIHNFKV HTFRGPHWCE YCANFMWGLI AQGVKCADCG LNVHKQCSKM 250
    VPNDCKPDLK HVKKVYSCDL TTLVKAHTTK RPMVVDMCIR EIESRGLNSE 300
    GLYRVSGFSD LIEDVKMAFD RDGEKADISV NMYEDINIIT GALKLYFRDL 350
    PIPLITYDAY PKFIESAKIM DPDEQLETLH EALKLLPPAH CETLRYLMAH 400
    LKRVTLHEKE NLMNAENLGI VFGPTLMRSP ELDAMAALND IRYQRLVVEL 450
    LIKNEDILF 459
    Length:459
    Mass (Da):53,172
    Last modified:July 11, 2002 - v3
    Checksum:i04C4CC9BCC611389
    GO
    Isoform Alpha-1 (identifier: P15882-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-183: MALTLFDTDE...TGQDGVSEKR → MPSKESWSGR...QPLKLFAYSQ

    Show »
    Length:334
    Mass (Da):38,196
    Checksum:i2E5BF139A231D13C
    GO
    Isoform 3 (identifier: P15882-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         184-209: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:433
    Mass (Da):50,034
    Checksum:iEB3E22E1C704D1BF
    GO

    Sequence cautioni

    The sequence CAA35769.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti20 – 201L → F in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA). 1 Publication
    VAR_047940
    Natural varianti126 – 1261I → M in DURS2; behaves as a dominant gain-of -function allele that increases CHN1 activity in vitro. 1 Publication
    VAR_047941
    Natural varianti143 – 1431Y → H in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA). 1 Publication
    VAR_047942
    Natural varianti223 – 2231A → V in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA). 1 Publication
    VAR_047943
    Natural varianti228 – 2281G → S in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro. 1 Publication
    VAR_047944
    Natural varianti252 – 2521P → Q in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA). 1 Publication
    VAR_047945
    Natural varianti313 – 3131E → K in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro. 1 Publication
    VAR_047946

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 183183MALTL…VSEKR → MPSKESWSGRKTNRAAVHKS KQEGRQQDLLIAALGMKLGS PKSSVTIWQPLKLFAYSQ in isoform Alpha-1. 2 PublicationsVSP_001636Add
    BLAST
    Alternative sequencei184 – 20926Missing in isoform 3. 1 PublicationVSP_043297Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51408 mRNA. Translation: CAA35769.1. Different initiation.
    Z22641 mRNA. Translation: CAA80354.1.
    AK055060 mRNA. Translation: BAG51458.1.
    AK289941 mRNA. Translation: BAF82630.1.
    AK300890 mRNA. Translation: BAG62531.1.
    AC007435 Genomic DNA. No translation available.
    AC018890 Genomic DNA. Translation: AAY14688.1.
    AC020596 Genomic DNA. Translation: AAY14940.1.
    CH471058 Genomic DNA. Translation: EAX11117.1.
    CH471058 Genomic DNA. Translation: EAX11118.1.
    CH471058 Genomic DNA. Translation: EAX11119.1.
    BC011393 mRNA. Translation: AAH11393.1.
    S75654 Genomic DNA. Translation: AAB33506.1.
    CCDSiCCDS46454.1. [P15882-3]
    CCDS46455.1. [P15882-1]
    CCDS56147.1. [P15882-2]
    PIRiA48090.
    I53329.
    RefSeqiNP_001020372.2. NM_001025201.3. [P15882-3]
    NP_001193531.1. NM_001206602.1. [P15882-2]
    NP_001813.1. NM_001822.5. [P15882-1]
    UniGeneiHs.380138.

    Genome annotation databases

    EnsembliENST00000295497; ENSP00000295497; ENSG00000128656. [P15882-2]
    ENST00000409156; ENSP00000386470; ENSG00000128656. [P15882-3]
    ENST00000409900; ENSP00000386741; ENSG00000128656. [P15882-1]
    GeneIDi1123.
    KEGGihsa:1123.
    UCSCiuc002ujg.3. human. [P15882-2]
    uc002uji.3. human. [P15882-1]
    uc010zeq.2. human. [P15882-3]

    Polymorphism databases

    DMDMi21903393.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51408 mRNA. Translation: CAA35769.1 . Different initiation.
    Z22641 mRNA. Translation: CAA80354.1 .
    AK055060 mRNA. Translation: BAG51458.1 .
    AK289941 mRNA. Translation: BAF82630.1 .
    AK300890 mRNA. Translation: BAG62531.1 .
    AC007435 Genomic DNA. No translation available.
    AC018890 Genomic DNA. Translation: AAY14688.1 .
    AC020596 Genomic DNA. Translation: AAY14940.1 .
    CH471058 Genomic DNA. Translation: EAX11117.1 .
    CH471058 Genomic DNA. Translation: EAX11118.1 .
    CH471058 Genomic DNA. Translation: EAX11119.1 .
    BC011393 mRNA. Translation: AAH11393.1 .
    S75654 Genomic DNA. Translation: AAB33506.1 .
    CCDSi CCDS46454.1. [P15882-3 ]
    CCDS46455.1. [P15882-1 ]
    CCDS56147.1. [P15882-2 ]
    PIRi A48090.
    I53329.
    RefSeqi NP_001020372.2. NM_001025201.3. [P15882-3 ]
    NP_001193531.1. NM_001206602.1. [P15882-2 ]
    NP_001813.1. NM_001822.5. [P15882-1 ]
    UniGenei Hs.380138.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2OSA X-ray 1.80 A 260-459 [» ]
    3CXL X-ray 2.60 A 15-459 [» ]
    ProteinModelPortali P15882.
    SMRi P15882. Positions 15-459.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107547. 6 interactions.
    DIPi DIP-42177N.
    IntActi P15882. 5 interactions.
    MINTi MINT-1173390.
    STRINGi 9606.ENSP00000386741.

    PTM databases

    PhosphoSitei P15882.

    Polymorphism databases

    DMDMi 21903393.

    Proteomic databases

    MaxQBi P15882.
    PaxDbi P15882.
    PRIDEi P15882.

    Protocols and materials databases

    DNASUi 1123.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295497 ; ENSP00000295497 ; ENSG00000128656 . [P15882-2 ]
    ENST00000409156 ; ENSP00000386470 ; ENSG00000128656 . [P15882-3 ]
    ENST00000409900 ; ENSP00000386741 ; ENSG00000128656 . [P15882-1 ]
    GeneIDi 1123.
    KEGGi hsa:1123.
    UCSCi uc002ujg.3. human. [P15882-2 ]
    uc002uji.3. human. [P15882-1 ]
    uc010zeq.2. human. [P15882-3 ]

    Organism-specific databases

    CTDi 1123.
    GeneCardsi GC02M175664.
    GeneReviewsi CHN1.
    HGNCi HGNC:1943. CHN1.
    HPAi HPA036111.
    MIMi 118423. gene.
    604356. phenotype.
    neXtProti NX_P15882.
    Orphaneti 233. Duane retraction syndrome.
    PharmGKBi PA26473.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG295484.
    HOGENOMi HOG000231926.
    HOVERGENi HBG080489.
    InParanoidi P15882.
    OMAi NREPAHK.
    OrthoDBi EOG73JKVC.
    PhylomeDBi P15882.
    TreeFami TF342052.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.
    SignaLinki P15882.

    Miscellaneous databases

    EvolutionaryTracei P15882.
    GenomeRNAii 1123.
    NextBioi 4662.
    PROi P15882.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15882.
    Bgeei P15882.
    CleanExi HS_CHN1.
    Genevestigatori P15882.

    Family and domain databases

    Gene3Di 1.10.555.10. 1 hit.
    3.30.505.10. 1 hit.
    InterProi IPR020454. DAG/PE-bd.
    IPR017356. N-chimaerin.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    IPR000980. SH2.
    [Graphical view ]
    Pfami PF00130. C1_1. 1 hit.
    PF00620. RhoGAP. 1 hit.
    PF00017. SH2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038015. N-chimaerin. 1 hit.
    PRINTSi PR00008. DAGPEDOMAIN.
    SMARTi SM00109. C1. 1 hit.
    SM00324. RhoGAP. 1 hit.
    SM00252. SH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48350. SSF48350. 1 hit.
    SSF55550. SSF55550. 1 hit.
    PROSITEi PS50238. RHOGAP. 1 hit.
    PS50001. SH2. 1 hit.
    PS00479. ZF_DAG_PE_1. 1 hit.
    PS50081. ZF_DAG_PE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Novel human brain cDNA encoding a 34,000 Mr protein n-chimaerin, related to both the regulatory domain of protein kinase C and BCR, the product of the breakpoint cluster region gene."
      Hall C., Monfries C., Smith P., Lim H.H., Kozma R., Ahmed S., Vanniasingham V., Leung T., Lim L.
      J. Mol. Biol. 211:11-16(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1).
      Tissue: Retina.
    2. "Developmental regulation and neuronal expression of the mRNA of rat n-chimaerin, a p21rac GAP:cDNA sequence."
      Lim H.H., Michael G.J., Smith P., Lim L., Hall C.
      Biochem. J. 287:415-422(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    3. "Alpha 2-chimerin, an SH2-containing GTPase-activating protein for the ras-related protein p21rac derived by alternate splicing of the human n-chimerin gene, is selectively expressed in brain regions and testes."
      Hall C., Sin W.C., Teo M., Michael G.J., Smith P., Dong J.M., Lim H.H., Manser E., Spurr N.K., Jones T.A., Lim L.
      Mol. Cell. Biol. 13:4986-4998(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-2).
    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 ALPHA-1; ALPHA-2 AND 3).
      Tissue: Brain, Hippocampus and Small intestine.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 ALPHA-2).
      Tissue: Eye.
    8. "Promoter region of the transcriptional unit for human alpha 1-chimaerin, a neuron-specific GTPase-activating protein for p21rac."
      Dong J.M., Smith P., Hall C., Lim L.
      Eur. J. Biochem. 227:636-646(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA-1).
      Tissue: Fibroblast.
    9. "Human brain n-chimaerin cDNA encodes a novel phorbol ester receptor."
      Ahmed S., Kozma R., Monfries C., Hall C., Lim H.H., Smith P., Lim L.
      Biochem. J. 272:767-773(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHORBOL-ESTER BINDING.
    10. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    11. "Crystal structure of human chimerin 1 (CHN1)."
      Structural genomics consortium (SGC)
      Submitted (JUL-2011) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 15-459 IN COMPLEX WITH ZINC IONS.
    12. Cited for: VARIANTS DURS2 PHE-20; MET-126; HIS-143; VAL-223; SER-228; GLN-252 AND LYS-313, CHARACTERIZATION OF VARIANTS DURS2 PHE-20; MET-126; HIS-143; VAL-223; SER-228; GLN-252 AND LYS-313.

    Entry informationi

    Entry nameiCHIN_HUMAN
    AccessioniPrimary (citable) accession number: P15882
    Secondary accession number(s): A8K1M6
    , B3KNU6, B4DV19, Q53SD6, Q53SH5, Q96FB0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: July 11, 2002
    Last modified: October 1, 2014
    This is version 158 of the entry and version 3 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 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3