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Q9NZV1 (CRIM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. Processed cysteine-rich motor neuron 1 protein
Gene names
Name:CRIM1
Synonyms:S52
ORF Names:UNQ1886/PRO4330
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1036 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.7

Subunit structure

Interacts with BMP4 and BMP7. Ref.5

Subcellular location

Processed cysteine-rich motor neuron 1 protein: Secreted Ref.5.

Cell membrane; Single-pass type I membrane protein Ref.5.

Tissue specificity

Expressed in pancreas, kidney, skeletal muscle, lung, placenta, brain, heart, spleen, liver and small intestine. Expressed in blood vessels (at protein level). Ref.1 Ref.7

Post-translational modification

N-glycosylated. Ref.5 Ref.7

Sequence similarities

Contains 4 antistasin-like domains.

Contains 1 IGFBP N-terminal domain.

Contains 6 VWFC domains.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3434 Ref.5 Ref.6
Chain35 – 10361002Cysteine-rich motor neuron 1 protein
PRO_0000021001
Chain? – 1036Processed cysteine-rich motor neuron 1 proteinPRO_0000296243

Regions

Topological domain35 – 939905Extracellular Potential
Transmembrane940 – 96021Helical; Potential
Topological domain961 – 103676Cytoplasmic Potential
Domain35 – 11278IGFBP N-terminal
Domain334 – 39158VWFC 1
Domain401 – 45757VWFC 2
Domain469 – 49830Antistasin-like 1
Domain505 – 53228Antistasin-like 2
Domain539 – 56426Antistasin-like 3
Domain567 – 59226Antistasin-like 4
Domain606 – 66358VWFC 3
Domain677 – 73559VWFC 4
Domain751 – 80959VWFC 5
Domain817 – 87458VWFC 6
Motif314 – 3163Cell attachment site Potential

Amino acid modifications

Modified residue10351Phosphothreonine Ref.8
Glycosylation711N-linked (GlcNAc...) Potential
Glycosylation1131N-linked (GlcNAc...) Potential
Glycosylation3301N-linked (GlcNAc...) Potential
Glycosylation4741N-linked (GlcNAc...) Potential
Glycosylation7461N-linked (GlcNAc...) Potential

Natural variations

Natural variant5021E → K.
Corresponds to variant rs12997487 [ dbSNP | Ensembl ].
VAR_050907
Natural variant7811V → I.
Corresponds to variant rs59929305 [ dbSNP | Ensembl ].
VAR_061625

Experimental info

Sequence conflict4331C → F in BAD92376. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9NZV1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 10CBF02A5C579C27

FASTA1,036113,738
        10         20         30         40         50         60 
MYLVAGDRGL AGCGHLLVSL LGLLLLLARS GTRALVCLPC DESKCEEPRN CPGSIVQGVC 

        70         80         90        100        110        120 
GCCYTCASQR NESCGGTFGI YGTCDRGLRC VIRPPLNGDS LTEYEAGVCE DENWTDDQLL 

       130        140        150        160        170        180 
GFKPCNENLI AGCNIINGKC ECNTIRTCSN PFEFPSQDMC LSALKRIEEE KPDCSKARCE 

       190        200        210        220        230        240 
VQFSPRCPED SVLIEGYAPP GECCPLPSRC VCNPAGCLRK VCQPGNLNIL VSKASGKPGE 

       250        260        270        280        290        300 
CCDLYECKPV FGVDCRTVEC PPVQQTACPP DSYETQVRLT ADGCCTLPTR CECLSGLCGF 

       310        320        330        340        350        360 
PVCEVGSTPR IVSRGDGTPG KCCDVFECVN DTKPACVFNN VEYYDGDMFR MDNCRFCRCQ 

       370        380        390        400        410        420 
GGVAICFTAQ CGEINCERYY VPEGECCPVC EDPVYPFNNP AGCYANGLIL AHGDRWREDD 

       430        440        450        460        470        480 
CTFCQCVNGE RHCVATVCGQ TCTNPVKVPG ECCPVCEEPT IITVDPPACG ELSNCTLTGK 

       490        500        510        520        530        540 
DCINGFKRDH NGCRTCQCIN TEELCSERKQ GCTLNCPFGF LTDAQNCEIC ECRPRPKKCR 

       550        560        570        580        590        600 
PIICDKYCPL GLLKNKHGCD ICRCKKCPEL SCSKICPLGF QQDSHGCLIC KCREASASAG 

       610        620        630        640        650        660 
PPILSGTCLT VDGHHHKNEE SWHDGCRECY CLNGREMCAL ITCPVPACGN PTIHPGQCCP 

       670        680        690        700        710        720 
SCADDFVVQK PELSTPSICH APGGEYFVEG ETWNIDSCTQ CTCHSGRVLC ETEVCPPLLC 

       730        740        750        760        770        780 
QNPSRTQDSC CPQCTDQPFR PSLSRNNSVP NYCKNDEGDI FLAAESWKPD VCTSCICIDS 

       790        800        810        820        830        840 
VISCFSESCP SVSCERPVLR KGQCCPYCIE DTIPKKVVCH FSGKAYADEE RWDLDSCTHC 

       850        860        870        880        890        900 
YCLQGQTLCS TVSCPPLPCV EPINVEGSCC PMCPEMYVPE PTNIPIEKTN HRGEVDLEVP 

       910        920        930        940        950        960 
LWPTPSENDI VHLPRDMGHL QVDYRDNRLH PSEDSSLDSI ASVVVPIIIC LSIIIAFLFI 

       970        980        990       1000       1010       1020 
NQKKQWIPLL CWYRTPTKPS SLNNQLVSVD CKKGTRVQVD SSQRMLRIAE PDARFSGFYS 

      1030 
MQKQNHLQAD NFYQTV 

« Hide

References

« Hide 'large scale' references
[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]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1035, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_057525.1. NM_016441.2.
UniGeneHs.699247.

3D structure databases

ProteinModelPortalQ9NZV1.
SMRQ9NZV1. Positions 34-94, 332-393, 398-458, 471-530, 606-666, 681-738, 753-812, 816-881.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119395. 3 interactions.
DIPDIP-58932N.
IntActQ9NZV1. 4 interactions.
STRING9606.ENSP00000280527.

PTM databases

PhosphoSiteQ9NZV1.

Polymorphism databases

DMDM67460590.

Proteomic databases

PaxDbQ9NZV1.
PeptideAtlasQ9NZV1.
PRIDEQ9NZV1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000280527; ENSP00000280527; ENSG00000150938.
ENST00000574904; ENSP00000459137; ENSG00000261899.
GeneID51232.
KEGGhsa:51232.
UCSCuc002rpd.3. human.

Organism-specific databases

CTD51232.
GeneCardsGC02P036495.
H-InvDBHIX0030218.
HGNCHGNC:2359. CRIM1.
HPAHPA000556.
MIM606189. gene.
neXtProtNX_Q9NZV1.
PharmGKBPA26877.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG283828.
HOGENOMHOG000063671.
HOVERGENHBG081345.
InParanoidQ9NZV1.
OMAWREDDCT.
PhylomeDBQ9NZV1.
TreeFamTF106451.

Gene expression databases

ArrayExpressQ9NZV1.
BgeeQ9NZV1.
CleanExHS_CRIM1.
GenevestigatorQ9NZV1.

Family and domain databases

Gene3D2.10.22.10. 3 hits.
InterProIPR004094. Antistasin-like.
IPR009030. Growth_fac_rcpt_N_dom.
IPR011061. Hirudin/antistatin.
IPR000867. IGFBP-like.
IPR001007. VWF_C.
[Graphical view]
PfamPF02822. Antistasin. 4 hits.
PF00093. VWC. 6 hits.
[Graphical view]
SMARTSM00121. IB. 1 hit.
SM00214. VWC. 6 hits.
[Graphical view]
SUPFAMSSF57184. SSF57184. 1 hit.
SSF57262. SSF57262. 3 hits.
PROSITEPS51252. ANTISTASIN. 4 hits.
PS51323. IGFBP_N_2. 1 hit.
PS01208. VWFC_1. 6 hits.
PS50184. VWFC_2. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCRIM1. human.
GeneWikiCRIM1.
GenomeRNAi51232.
NextBio54338.
PMAP-CutDBQ9NZV1.
PROQ9NZV1.
SOURCESearch...

Entry information

Entry nameCRIM1_HUMAN
AccessionPrimary (citable) accession number: Q9NZV1
Secondary accession number(s): Q2M2G4 expand/collapse secondary AC list , Q59GH0, Q7LCQ5, Q9H318
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: October 1, 2000
Last modified: March 19, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM