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Q96GW7 (PGCB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 104. Feed History...

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

Names and origin

Protein namesRecommended name:
Brevican core protein
Alternative name(s):
Brain-enriched hyaluronan-binding protein
Short name=BEHAB
Chondroitin sulfate proteoglycan 7
Gene names
Name:BCAN
Synonyms:BEHAB, CSPG7
ORF Names:UNQ2525/PRO6018
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length911 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 the terminally differentiating and the adult nervous system during postnatal development. Could stabilize interactions between hyaluronan (HA) and brain proteoglycans.

Subunit structure

Interacts with TNR By similarity.

Subcellular location

Isoform 1: Secreted › extracellular space › extracellular matrix.

Isoform 2: Membrane; Lipid-anchor › GPI-anchor.

Developmental stage

Isoform 1 is highly expressed from birth through 8 years of age and is down-regulated by 20 years of age to low levels that are maintained in the normal adult cortex. Isoform 2 is expressed at uniformly low levels throughout development. Ref.1

Post-translational modification

Contains mostly chondroitin sulfate By similarity. O-glycosylated with a core 1 or possibly core 8 glycan.

Sequence similarities

Belongs to the aggrecan/versican proteoglycan family.

Contains 1 C-type lectin domain.

Contains 1 EGF-like domain.

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

Contains 2 Link domains.

Contains 1 Sushi (CCP/SCR) domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96GW7-1)

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.
Isoform 2 (identifier: Q96GW7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     649-671: DCVPSPCHNGGTCLEEEEGVRCL → NSAQGSTALSILLLFFPLQLWVT
     672-911: Missing.
Note: GPI-anchor amidated asparagine on Asn-649 (Potential).

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 911889Brevican core protein
PRO_0000017511

Regions

Domain36 – 155120Ig-like V-type
Domain157 – 25296Link 1
Domain257 – 35498Link 2
Domain646 – 68237EGF-like
Domain695 – 809115C-type lectin
Domain813 – 87361Sushi
Region520 – 53011O-glycosylated at two sites
Region540 – 5456O-glycosylated at two sites
Region569 – 5757O-glycosylated at one site
Compositional bias385 – 47793Glu-rich

Amino acid modifications

Glycosylation1301N-linked (GlcNAc...) Potential
Glycosylation3371N-linked (GlcNAc...) Potential
Glycosylation9051O-linked (GalNAc...) Probable
Glycosylation9061O-linked (GalNAc...) Probable
Disulfide bond57 ↔ 137 By similarity
Disulfide bond179 ↔ 250 By similarity
Disulfide bond203 ↔ 224 By similarity
Disulfide bond277 ↔ 352 By similarity
Disulfide bond301 ↔ 322 By similarity
Disulfide bond650 ↔ 661 By similarity
Disulfide bond655 ↔ 670 By similarity
Disulfide bond672 ↔ 681 By similarity
Disulfide bond688 ↔ 699 By similarity
Disulfide bond716 ↔ 808 By similarity
Disulfide bond784 ↔ 800 By similarity
Disulfide bond815 ↔ 858 By similarity
Disulfide bond844 ↔ 871 By similarity

Natural variations

Alternative sequence649 – 67123DCVPS…GVRCL → NSAQGSTALSILLLFFPLQL WVT in isoform 2.
VSP_011184
Alternative sequence672 – 911240Missing in isoform 2.
VSP_011185
Natural variant3561S → L.
Corresponds to variant rs12065791 [ dbSNP | Ensembl ].
VAR_050123
Natural variant5041E → K. Ref.2
Corresponds to variant rs1056695 [ dbSNP | Ensembl ].
VAR_019551

Experimental info

Sequence conflict1751A → T in AAH22938. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 21, 2005. Version 2.
Checksum: 5268E796FA3938D2

FASTA91199,118
        10         20         30         40         50         60 
MAQLFLPLLA ALVLAQAPAA LADVLEGDSS EDRAFRVRIA GDAPLQGVLG GALTIPCHVH 

        70         80         90        100        110        120 
YLRPPPSRRA VLGSPRVKWT FLSRGREAEV LVARGVRVKV NEAYRFRVAL PAYPASLTDV 

       130        140        150        160        170        180 
SLALSELRPN DSGIYRCEVQ HGIDDSSDAV EVKVKGVVFL YREGSARYAF SFSGAQEACA 

       190        200        210        220        230        240 
RIGAHIATPE QLYAAYLGGY EQCDAGWLSD QTVRYPIQTP REACYGDMDG FPGVRNYGVV 

       250        260        270        280        290        300 
DPDDLYDVYC YAEDLNGELF LGDPPEKLTL EEARAYCQER GAEIATTGQL YAAWDGGLDH 

       310        320        330        340        350        360 
CSPGWLADGS VRYPIVTPSQ RCGGGLPGVK TLFLFPNQTG FPNKHSRFNV YCFRDSAQPS 

       370        380        390        400        410        420 
AIPEASNPAS NPASDGLEAI VTVTETLEEL QLPQEATESE SRGAIYSIPI MEDGGGGSST 

       430        440        450        460        470        480 
PEDPAEAPRT LLEFETQSMV PPTGFSEEEG KALEEEEKYE DEEEKEEEEE EEEVEDEALW 

       490        500        510        520        530        540 
AWPSELSSPG PEASLPTEPA AQEESLSQAP ARAVLQPGAS PLPDGESEAS RPPRVHGPPT 

       550        560        570        580        590        600 
ETLPTPRERN LASPSPSTLV EAREVGEATG GPELSGVPRG ESEETGSSEG APSLLPATRA 

       610        620        630        640        650        660 
PEGTRELEAP SEDNSGRTAP AGTSVQAQPV LPTDSASRGG VAVVPASGDC VPSPCHNGGT 

       670        680        690        700        710        720 
CLEEEEGVRC LCLPGYGGDL CDVGLRFCNP GWDAFQGACY KHFSTRRSWE EAETQCRMYG 

       730        740        750        760        770        780 
AHLASISTPE EQDFINNRYR EYQWIGLNDR TIEGDFLWSD GVPLLYENWN PGQPDSYFLS 

       790        800        810        820        830        840 
GENCVVMVWH DQGQWSDVPC NYHLSYTCKM GLVSCGPPPE LPLAQVFGRP RLRYEVDTVL 

       850        860        870        880        890        900 
RYRCREGLAQ RNLPLIRCQE NGRWEAPQIS CVPRRPARAL HPEEDPEGRQ GRLLGRWKAL 

       910 
LIPPSSPMPG P

« Hide

Isoform 2 [UniParc].

Checksum: BAD0E1959546D4B9
Show »

FASTA67171,671

References

« Hide 'large scale' references
[1]"cDNA cloning, chromosomal localization, and expression analysis of human BEHAB/brevican, a brain specific proteoglycan regulated during cortical development and in glioma."
Gary S.C., Zerillo C.A., Chiang V.L., Gaw J.U., Gray G., Hockfield S.
Gene 256:139-147(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), DEVELOPMENTAL STAGE.
Tissue: Brain cortex.
[2]"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] (ISOFORM 1), VARIANT LYS-504.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Brain.
[6]"Enrichment of glycopeptides for glycan structure and attachment site identification."
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT SER-905 AND SER-906, STRUCTURE OF CARBOHYDRATES, MASS SPECTROMETRY.
Tissue: Cerebrospinal fluid.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF228710 mRNA. Translation: AAG23134.1.
AF229053 mRNA. Translation: AAG23135.1.
AY358372 mRNA. Translation: AAQ88738.1.
AL365181, AL590666 Genomic DNA. Translation: CAI13056.1.
AL365181 Genomic DNA. Translation: CAI13060.1.
AL590666, AL365181 Genomic DNA. Translation: CAI16352.1.
CH471121 Genomic DNA. Translation: EAW52927.1.
CH471121 Genomic DNA. Translation: EAW52928.1.
CH471121 Genomic DNA. Translation: EAW52929.1.
CH471121 Genomic DNA. Translation: EAW52930.1.
BC009117 mRNA. Translation: AAH09117.1.
BC022938 mRNA. Translation: AAH22938.1.
BC027971 mRNA. Translation: AAH27971.1.
IPIIPI00456623.
IPI00456624.
RefSeqNP_068767.3. NM_021948.4.
NP_940819.1. NM_198427.1.
UniGeneHs.516904.

3D structure databases

ProteinModelPortalQ96GW7.
ModBaseSearch...

Protein-protein interaction databases

IntActQ96GW7. 1 interaction.
MINTMINT-4830140.
STRING9606.ENSP00000331210.

PTM databases

PhosphoSiteQ96GW7.

Polymorphism databases

DMDM68067899.

Proteomic databases

PaxDbQ96GW7.
PeptideAtlasQ96GW7.
PRIDEQ96GW7.

Protocols and materials databases

DNASU63827.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000329117; ENSP00000331210; ENSG00000132692.
ENST00000361588; ENSP00000354925; ENSG00000132692.
GeneID63827.
KEGGhsa:63827.
UCSCuc001fpo.3. human.
uc001fpp.3. human.

Organism-specific databases

CTD63827.
GeneCardsGC01P156611.
HGNCHGNC:23059. BCAN.
HPACAB025862.
HPA007865.
MIM600347. gene.
neXtProtNX_Q96GW7.
PharmGKBPA134868393.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG136696.
HOVERGENHBG008175.
InParanoidQ96GW7.
KOK06795.
OMAYCFRDSA.
OrthoDBEOG4XGZZW.
PhylomeDBQ96GW7.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

ArrayExpressQ96GW7.
BgeeQ96GW7.
CleanExHS_BCAN.
GenevestigatorQ96GW7.
GermOnlineENSG00000132692. Homo sapiens.

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.
IPR013032. EGF-like_CS.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR013106. Ig_V-set.
IPR003596. Ig_V-set_subgr.
IPR000538. Link.
IPR000436. Sushi_SCR_CCP.
[Graphical view]
PfamPF00008. EGF. 1 hit.
PF00059. 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.
SM00406. IGv. 1 hit.
SM00445. LINK. 2 hits.
[Graphical view]
SUPFAMSSF56436. C-type_lectin_fold. 3 hits.
SSF57535. Complement_control_module. 1 hit.
PROSITEPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
PS01241. LINK_1. 2 hits.
PS50963. LINK_2. 2 hits.
PS50923. SUSHI. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi63827.
NextBio65542.
SOURCESearch...

Entry information

Entry namePGCB_HUMAN
AccessionPrimary (citable) accession number: Q96GW7
Secondary accession number(s): D3DVC2 expand/collapse secondary AC list , Q5SZ10, Q5T3I5, Q8TBB9, Q9HBK1, Q9HBK4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: June 21, 2005
Last modified: May 1, 2013
This is version 104 of the entry and version 2 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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents