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O14594 (NCAN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neurocan core protein
Alternative name(s):
Chondroitin sulfate proteoglycan 3
Gene names
Name:NCAN
Synonyms:CSPG3, NEUR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1321 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May modulate neuronal adhesion and neurite growth during development by binding to neural cell adhesion molecules (NG-CAM and N-CAM). Chondroitin sulfate proteoglycan; binds to hyaluronic acid.

Subcellular location

Secreted By similarity.

Tissue specificity

Brain.

Post-translational modification

O-glycosylated. Ref.3

Sequence similarities

Belongs to the aggrecan/versican proteoglycan family.

Contains 1 C-type lectin domain.

Contains 2 EGF-like domains.

Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Contains 2 Link domains.

Contains 1 Sushi (CCP/SCR) domain.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainEGF-like domain
Immunoglobulin domain
Repeat
Signal
Sushi
   LigandCalcium
Hyaluronic acid
Lectin
   PTMDisulfide bond
Glycoprotein
Proteoglycan
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Traceable author statement. Source: Reactome

carbohydrate metabolic process

Traceable author statement. Source: Reactome

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

chondroitin sulfate biosynthetic process

Traceable author statement. Source: Reactome

chondroitin sulfate catabolic process

Traceable author statement. Source: Reactome

chondroitin sulfate metabolic process

Traceable author statement. Source: Reactome

dermatan sulfate biosynthetic process

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

glycosaminoglycan metabolic process

Traceable author statement. Source: Reactome

regulation of synapse structural plasticity

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi lumen

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

lysosomal lumen

Traceable author statement. Source: Reactome

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

carbohydrate binding

Inferred from electronic annotation. Source: InterPro

hyaluronic acid binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 13211299Neurocan core protein
PRO_0000017516

Regions

Domain38 – 153116Ig-like V-type
Domain160 – 25596Link 1
Domain259 – 35799Link 2
Domain1008 – 104437EGF-like 1
Domain1046 – 108237EGF-like 2; calcium-binding Potential
Domain1084 – 1213130C-type lectin
Domain1213 – 127361Sushi
Region708 – 7125O-glycosylated at one site

Amino acid modifications

Glycosylation1221N-linked (GlcNAc...) Potential
Glycosylation3401N-linked (GlcNAc...) Potential
Glycosylation10261N-linked (GlcNAc...) Potential
Glycosylation12231N-linked (GlcNAc...) Potential
Disulfide bond59 ↔ 140 By similarity
Disulfide bond182 ↔ 253 By similarity
Disulfide bond206 ↔ 227 By similarity
Disulfide bond280 ↔ 355 By similarity
Disulfide bond304 ↔ 325 By similarity
Disulfide bond1012 ↔ 1023 By similarity
Disulfide bond1017 ↔ 1032 By similarity
Disulfide bond1034 ↔ 1043 By similarity
Disulfide bond1050 ↔ 1061 By similarity
Disulfide bond1055 ↔ 1070 By similarity
Disulfide bond1072 ↔ 1081 By similarity
Disulfide bond1088 ↔ 1099 By similarity
Disulfide bond1116 ↔ 1208 By similarity
Disulfide bond1184 ↔ 1200 By similarity
Disulfide bond1215 ↔ 1258 By similarity
Disulfide bond1244 ↔ 1271 By similarity

Natural variations

Natural variant701A → T.
Corresponds to variant rs2228601 [ dbSNP | Ensembl ].
VAR_024521
Natural variant921P → S.
Corresponds to variant rs2228603 [ dbSNP | Ensembl ].
VAR_020213
Natural variant12541A → V. Ref.1
Corresponds to variant rs1064389 [ dbSNP | Ensembl ].
VAR_016176

Experimental info

Sequence conflict12341Y → N in AAC80576. Ref.1
Sequence conflict12821R → G in AAC80576. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O14594 [UniParc].

Last modified November 13, 2007. Version 3.
Checksum: 22E21FFA24CE9FB2

FASTA1,321143,093
        10         20         30         40         50         60 
MGAPFVWALG LLMLQMLLFV AGEQGTQDIT DASERGLHMQ KLGSGSVQAA LAELVALPCL 

        70         80         90        100        110        120 
FTLQPRPSAA RDAPRIKWTK VRTASGQRQD LPILVAKDNV VRVAKSWQGR VSLPSYPRRR 

       130        140        150        160        170        180 
ANATLLLGPL RASDSGLYRC QVVRGIEDEQ DLVPLEVTGV VFHYRSARDR YALTFAEAQE 

       190        200        210        220        230        240 
ACRLSSAIIA APRHLQAAFE DGFDNCDAGW LSDRTVRYPI TQSRPGCYGD RSSLPGVRSY 

       250        260        270        280        290        300 
GRRNPQELYD VYCFARELGG EVFYVGPARR LTLAGARAQC RRQGAALASV GQLHLAWHEG 

       310        320        330        340        350        360 
LDQCDPGWLA DGSVRYPIQT PRRRCGGPAP GVRTVYRFAN RTGFPSPAER FDAYCFRAHH 

       370        380        390        400        410        420 
PTSQHGDLET PSSGDEGEIL SAEGPPVREL EPTLEEEEVV TPDFQEPLVS SGEEETLILE 

       430        440        450        460        470        480 
EKQESQQTLS PTPGDPMLAS WPTGEVWLST VAPSPSDMGA GTAASSHTEV APTDPMPRRR 

       490        500        510        520        530        540 
GRFKGLNGRY FQQQEPEPGL QGGMEASAQP PTSEAAVNQM EPPLAMAVTE MLGSGQSRSP 

       550        560        570        580        590        600 
WADLTNEVDM PGAGSAGGKS SPEPWLWPPT MVPPSISGHS RAPVLELEKA EGPSARPATP 

       610        620        630        640        650        660 
DLFWSPLEAT VSAPSPAPWE AFPVATSPDL PMMAMLRGPK EWMLPHPTPI STEANRVEAH 

       670        680        690        700        710        720 
GEATATAPPS PAAETKVYSL PLSLTPTGQG GEAMPTTPES PRADFRETGE TSPAQVNKAE 

       730        740        750        760        770        780 
HSSSSPWPSV NRNVAVGFVP TETATEPTGL RGIPGSESGV FDTAESPTSG LQATVDEVQD 

       790        800        810        820        830        840 
PWPSVYSKGL DASSPSAPLG SPGVFLVPKV TPNLEPWVAT DEGPTVNPMD STVTPAPSDA 

       850        860        870        880        890        900 
SGIWEPGSQV FEEAESTTLS PQVALDTSIV TPLTTLEQGD KVGVPAMSTL GSSSSQPHPE 

       910        920        930        940        950        960 
PEDQVETQGT SGASVPPHQS SPLGKPAVPP GTPTAASVGE SASVSSGEPT VPWDPSSTLL 

       970        980        990       1000       1010       1020 
PVTLGIEDFE LEVLAGSPGV ESFWEEVASG EEPALPGTPM NAGAEEVHSD PCENNPCLHG 

      1030       1040       1050       1060       1070       1080 
GTCNANGTMY GCSCDQGFAG ENCEIDIDDC LCSPCENGGT CIDEVNGFVC LCLPSYGGSF 

      1090       1100       1110       1120       1130       1140 
CEKDTEGCDR GWHKFQGHCY RYFAHRRAWE DAEKDCRRRS GHLTSVHSPE EHSFINSFGH 

      1150       1160       1170       1180       1190       1200 
ENTWIGLNDR IVERDFQWTD NTGLQFENWR ENQPDNFFAG GEDCVVMVAH ESGRWNDVPC 

      1210       1220       1230       1240       1250       1260 
NYNLPYVCKK GTVLCGPPPA VENASLIGAR KAKYNVHATV RYQCNEGFAQ HHVATIRCRS 

      1270       1280       1290       1300       1310       1320 
NGKWDRPQIV CTKPRRSHRM RRHHHHHQHH HQHHHHKSRK ERRKHKKHPT EDWEKDEGNF 


C 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the human neurocan gene, CSPG3."
Prange C.K., Pennacchio L.A., Lieuallen K., Fan W., Lennon G.G.
Gene 221:199-205(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-1254.
[2]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
Halim A., Ruetschi U., Larson G., Nilsson J.
J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF026547 mRNA. Translation: AAC80576.1.
AC003110 Genomic DNA. Translation: AAB86655.1.
AC005254 Genomic DNA. Translation: AAC25581.1.
RefSeqNP_004377.2. NM_004386.2.
XP_005259802.1. XM_005259745.1.
XP_005259803.1. XM_005259746.1.
UniGeneHs.169047.

3D structure databases

ProteinModelPortalO14594.
SMRO14594. Positions 43-157, 161-254, 270-359, 1007-1273.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107845. 6 interactions.
IntActO14594. 1 interaction.
STRING9606.ENSP00000252575.

PTM databases

PhosphoSiteO14594.

Proteomic databases

PaxDbO14594.
PRIDEO14594.

Protocols and materials databases

DNASU1463.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000252575; ENSP00000252575; ENSG00000130287.
GeneID1463.
KEGGhsa:1463.
UCSCuc002nlz.3. human.

Organism-specific databases

CTD1463.
GeneCardsGC19P019322.
H-InvDBHIX0027449.
HGNCHGNC:2465. NCAN.
HPAHPA036814.
MIM600826. gene.
neXtProtNX_O14594.
PharmGKBPA162396986.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG147231.
HOVERGENHBG078994.
InParanoidO14594.
KOK06794.
OMACSPCENG.
OrthoDBEOG7FFMQR.
PhylomeDBO14594.
TreeFamTF332134.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressO14594.
BgeeO14594.
CleanExHS_NCAN.
GenevestigatorO14594.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
3.10.100.10. 3 hits.
InterProIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR000538. Link.
IPR000436. Sushi_SCR_CCP.
[Graphical view]
PfamPF00059. Lectin_C. 1 hit.
PF00084. Sushi. 1 hit.
PF07686. V-set. 1 hit.
PF00193. Xlink. 2 hits.
[Graphical view]
PRINTSPR01265. LINKMODULE.
SMARTSM00032. CCP. 1 hit.
SM00034. CLECT. 1 hit.
SM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00409. IG. 1 hit.
SM00445. LINK. 2 hits.
[Graphical view]
SUPFAMSSF56436. SSF56436. 3 hits.
SSF57535. SSF57535. 1 hit.
PROSITEPS00010. ASX_HYDROXYL. 1 hit.
PS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
PS00022. EGF_1. 3 hits.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 2 hits.
PS01187. EGF_CA. 1 hit.
PS50835. IG_LIKE. 1 hit.
PS01241. LINK_1. 2 hits.
PS50963. LINK_2. 2 hits.
PS50923. SUSHI. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiNeurocan.
GenomeRNAi1463.
NextBio6009.
PROO14594.
SOURCESearch...

Entry information

Entry nameNCAN_HUMAN
AccessionPrimary (citable) accession number: O14594
Secondary accession number(s): Q9UPK6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 27, 2003
Last sequence update: November 13, 2007
Last modified: April 16, 2014
This is version 130 of the entry and version 3 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 19

Human chromosome 19: entries, gene names and cross-references to MIM