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Q9NZV1

- CRIM1_HUMAN

UniProt

Q9NZV1 - CRIM1_HUMAN

Protein

Cysteine-rich motor neuron 1 protein

Gene

CRIM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    May play a role in CNS development by interacting with growth factors implicated in motor neuron differentiation and survival. May play a role in capillary formation and maintenance during angiogenesis. Modulates BMP activity by affecting its processing and delivery to the cell surface.2 Publications

    GO - Molecular functioni

    1. insulin-like growth factor-activated receptor activity Source: ProtInc
    2. PDZ domain binding Source: MGI
    3. serine-type endopeptidase inhibitor activity Source: InterPro

    GO - Biological processi

    1. insulin-like growth factor receptor signaling pathway Source: GOC
    2. nervous system development Source: ProtInc
    3. regulation of cell growth Source: InterPro

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cysteine-rich motor neuron 1 protein
    Short name:
    CRIM-1
    Alternative name(s):
    Cysteine-rich repeat-containing protein S52
    Cleaved into the following chain:
    Gene namesi
    Name:CRIM1
    Synonyms:S52
    ORF Names:UNQ1886/PRO4330
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:2359. CRIM1.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. integral component of membrane Source: ProtInc
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26877.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 1036Processed cysteine-rich motor neuron 1 proteinPRO_0000296243
    Signal peptidei1 – 34342 PublicationsAdd
    BLAST
    Chaini35 – 10361002Cysteine-rich motor neuron 1 proteinPRO_0000021001Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi71 – 711N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi113 – 1131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi330 – 3301N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi474 – 4741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi746 – 7461N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1035 – 10351Phosphothreonine1 Publication

    Post-translational modificationi

    N-glycosylated.2 Publications

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ9NZV1.
    PaxDbiQ9NZV1.
    PeptideAtlasiQ9NZV1.
    PRIDEiQ9NZV1.

    PTM databases

    PhosphoSiteiQ9NZV1.

    Miscellaneous databases

    PMAP-CutDBQ9NZV1.

    Expressioni

    Tissue specificityi

    Expressed in pancreas, kidney, skeletal muscle, lung, placenta, brain, heart, spleen, liver and small intestine. Expressed in blood vessels (at protein level).2 Publications

    Gene expression databases

    ArrayExpressiQ9NZV1.
    BgeeiQ9NZV1.
    CleanExiHS_CRIM1.
    GenevestigatoriQ9NZV1.

    Organism-specific databases

    HPAiHPA000556.

    Interactioni

    Subunit structurei

    Interacts with BMP4 and BMP7.1 Publication

    Protein-protein interaction databases

    BioGridi119395. 3 interactions.
    DIPiDIP-58932N.
    IntActiQ9NZV1. 5 interactions.
    STRINGi9606.ENSP00000280527.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NZV1.
    SMRiQ9NZV1. Positions 34-94, 332-393, 398-458, 471-530, 606-666, 681-738, 753-812, 816-881.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini35 – 939905ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini961 – 103676CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei940 – 96021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 11278IGFBP N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini334 – 39158VWFC 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini401 – 45757VWFC 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini469 – 49830Antistasin-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini505 – 53228Antistasin-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini539 – 56426Antistasin-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini567 – 59226Antistasin-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini606 – 66358VWFC 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini677 – 73559VWFC 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini751 – 80959VWFC 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini817 – 87458VWFC 6PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi314 – 3163Cell attachment siteSequence Analysis

    Sequence similaritiesi

    Contains 4 antistasin-like domains.PROSITE-ProRule annotation
    Contains 1 IGFBP N-terminal domain.PROSITE-ProRule annotation
    Contains 6 VWFC domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG283828.
    HOGENOMiHOG000063671.
    HOVERGENiHBG081345.
    InParanoidiQ9NZV1.
    OMAiWREDDCT.
    PhylomeDBiQ9NZV1.
    TreeFamiTF106451.

    Family and domain databases

    Gene3Di2.10.22.10. 3 hits.
    InterProiIPR004094. Antistasin-like.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR011061. Hirudin/antistatin.
    IPR000867. IGFBP-like.
    IPR001007. VWF_C.
    [Graphical view]
    PfamiPF02822. Antistasin. 4 hits.
    PF00093. VWC. 6 hits.
    [Graphical view]
    SMARTiSM00121. IB. 1 hit.
    SM00214. VWC. 6 hits.
    [Graphical view]
    SUPFAMiSSF57184. SSF57184. 1 hit.
    SSF57262. SSF57262. 3 hits.
    PROSITEiPS51252. ANTISTASIN. 4 hits.
    PS51323. IGFBP_N_2. 1 hit.
    PS01208. VWFC_1. 6 hits.
    PS50184. VWFC_2. 6 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9NZV1-1 [UniParc]FASTAAdd to Basket

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    MYLVAGDRGL AGCGHLLVSL LGLLLLLARS GTRALVCLPC DESKCEEPRN     50
    CPGSIVQGVC GCCYTCASQR NESCGGTFGI YGTCDRGLRC VIRPPLNGDS 100
    LTEYEAGVCE DENWTDDQLL GFKPCNENLI AGCNIINGKC ECNTIRTCSN 150
    PFEFPSQDMC LSALKRIEEE KPDCSKARCE VQFSPRCPED SVLIEGYAPP 200
    GECCPLPSRC VCNPAGCLRK VCQPGNLNIL VSKASGKPGE CCDLYECKPV 250
    FGVDCRTVEC PPVQQTACPP DSYETQVRLT ADGCCTLPTR CECLSGLCGF 300
    PVCEVGSTPR IVSRGDGTPG KCCDVFECVN DTKPACVFNN VEYYDGDMFR 350
    MDNCRFCRCQ GGVAICFTAQ CGEINCERYY VPEGECCPVC EDPVYPFNNP 400
    AGCYANGLIL AHGDRWREDD CTFCQCVNGE RHCVATVCGQ TCTNPVKVPG 450
    ECCPVCEEPT IITVDPPACG ELSNCTLTGK DCINGFKRDH NGCRTCQCIN 500
    TEELCSERKQ GCTLNCPFGF LTDAQNCEIC ECRPRPKKCR PIICDKYCPL 550
    GLLKNKHGCD ICRCKKCPEL SCSKICPLGF QQDSHGCLIC KCREASASAG 600
    PPILSGTCLT VDGHHHKNEE SWHDGCRECY CLNGREMCAL ITCPVPACGN 650
    PTIHPGQCCP SCADDFVVQK PELSTPSICH APGGEYFVEG ETWNIDSCTQ 700
    CTCHSGRVLC ETEVCPPLLC QNPSRTQDSC CPQCTDQPFR PSLSRNNSVP 750
    NYCKNDEGDI FLAAESWKPD VCTSCICIDS VISCFSESCP SVSCERPVLR 800
    KGQCCPYCIE DTIPKKVVCH FSGKAYADEE RWDLDSCTHC YCLQGQTLCS 850
    TVSCPPLPCV EPINVEGSCC PMCPEMYVPE PTNIPIEKTN HRGEVDLEVP 900
    LWPTPSENDI VHLPRDMGHL QVDYRDNRLH PSEDSSLDSI ASVVVPIIIC 950
    LSIIIAFLFI NQKKQWIPLL CWYRTPTKPS SLNNQLVSVD CKKGTRVQVD 1000
    SSQRMLRIAE PDARFSGFYS MQKQNHLQAD NFYQTV 1036
    Length:1,036
    Mass (Da):113,738
    Last modified:October 1, 2000 - v1
    Checksum:i10CBF02A5C579C27
    GO

    Sequence cautioni

    The sequence BAD92376.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti433 – 4331C → F in BAD92376. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti502 – 5021E → K.
    Corresponds to variant rs12997487 [ dbSNP | Ensembl ].
    VAR_050907
    Natural varianti781 – 7811V → I.
    Corresponds to variant rs59929305 [ dbSNP | Ensembl ].
    VAR_061625

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF167706 mRNA. Translation: AAF34409.1.
    AF168681 Genomic DNA. Translation: AAG37011.1.
    AB209139 mRNA. Translation: BAD92376.1. Different initiation.
    AY358371 mRNA. Translation: AAQ88737.1.
    BC111989 mRNA. Translation: AAI11990.1.
    BC113371 mRNA. Translation: AAI13372.1.
    CCDSiCCDS1783.1.
    RefSeqiNP_057525.1. NM_016441.2.
    UniGeneiHs.699247.

    Genome annotation databases

    EnsembliENST00000280527; ENSP00000280527; ENSG00000150938.
    GeneIDi51232.
    KEGGihsa:51232.
    UCSCiuc002rpd.3. human.

    Polymorphism databases

    DMDMi67460590.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF167706 mRNA. Translation: AAF34409.1 .
    AF168681 Genomic DNA. Translation: AAG37011.1 .
    AB209139 mRNA. Translation: BAD92376.1 . Different initiation.
    AY358371 mRNA. Translation: AAQ88737.1 .
    BC111989 mRNA. Translation: AAI11990.1 .
    BC113371 mRNA. Translation: AAI13372.1 .
    CCDSi CCDS1783.1.
    RefSeqi NP_057525.1. NM_016441.2.
    UniGenei Hs.699247.

    3D structure databases

    ProteinModelPortali Q9NZV1.
    SMRi Q9NZV1. Positions 34-94, 332-393, 398-458, 471-530, 606-666, 681-738, 753-812, 816-881.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119395. 3 interactions.
    DIPi DIP-58932N.
    IntActi Q9NZV1. 5 interactions.
    STRINGi 9606.ENSP00000280527.

    PTM databases

    PhosphoSitei Q9NZV1.

    Polymorphism databases

    DMDMi 67460590.

    Proteomic databases

    MaxQBi Q9NZV1.
    PaxDbi Q9NZV1.
    PeptideAtlasi Q9NZV1.
    PRIDEi Q9NZV1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000280527 ; ENSP00000280527 ; ENSG00000150938 .
    GeneIDi 51232.
    KEGGi hsa:51232.
    UCSCi uc002rpd.3. human.

    Organism-specific databases

    CTDi 51232.
    GeneCardsi GC02P036495.
    H-InvDB HIX0030218.
    HGNCi HGNC:2359. CRIM1.
    HPAi HPA000556.
    MIMi 606189. gene.
    neXtProti NX_Q9NZV1.
    PharmGKBi PA26877.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG283828.
    HOGENOMi HOG000063671.
    HOVERGENi HBG081345.
    InParanoidi Q9NZV1.
    OMAi WREDDCT.
    PhylomeDBi Q9NZV1.
    TreeFami TF106451.

    Miscellaneous databases

    ChiTaRSi CRIM1. human.
    GeneWikii CRIM1.
    GenomeRNAii 51232.
    NextBioi 54338.
    PMAP-CutDB Q9NZV1.
    PROi Q9NZV1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NZV1.
    Bgeei Q9NZV1.
    CleanExi HS_CRIM1.
    Genevestigatori Q9NZV1.

    Family and domain databases

    Gene3Di 2.10.22.10. 3 hits.
    InterProi IPR004094. Antistasin-like.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR011061. Hirudin/antistatin.
    IPR000867. IGFBP-like.
    IPR001007. VWF_C.
    [Graphical view ]
    Pfami PF02822. Antistasin. 4 hits.
    PF00093. VWC. 6 hits.
    [Graphical view ]
    SMARTi SM00121. IB. 1 hit.
    SM00214. VWC. 6 hits.
    [Graphical view ]
    SUPFAMi SSF57184. SSF57184. 1 hit.
    SSF57262. SSF57262. 3 hits.
    PROSITEi PS51252. ANTISTASIN. 4 hits.
    PS51323. IGFBP_N_2. 1 hit.
    PS01208. VWFC_1. 6 hits.
    PS50184. VWFC_2. 6 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "CRIM1, a novel gene encoding a cysteine-rich repeat protein, is developmentally regulated and implicated in vertebrate CNS development and organogenesis."
      Kolle G.V., Georgas K., Holmes G.P., Little M.H., Yamada T.
      Mech. Dev. 90:181-193(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
    2. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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: Brain.
    5. "CRIM1 regulates the rate of processing and delivery of bone morphogenetic proteins to the cell surface."
      Wilkinson L., Kolle G.V., Wen D., Piper M., Scott J., Little M.H.
      J. Biol. Chem. 278:34181-34188(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 35-44, FUNCTION, GLYCOSYLATION, SUBCELLULAR LOCATION, INTERACTION WITH BMP4 AND BMP7, IDENTIFICATION OF A SOLUBLE FORM.
    6. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 35-49.
    7. "CRIM1 is involved in endothelial cell capillary formation in vitro and is expressed in blood vessels in vivo."
      Glienke J., Sturz A., Menrad A., Thierauch K.-H.
      Mech. Dev. 119:165-175(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, GLYCOSYLATION, TISSUE SPECIFICITY.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1035, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.

    Entry informationi

    Entry nameiCRIM1_HUMAN
    AccessioniPrimary (citable) accession number: Q9NZV1
    Secondary accession number(s): Q2M2G4
    , Q59GH0, Q7LCQ5, Q9H318
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 114 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

    Complete proteome, Direct protein sequencing, 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3