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Protein

Brevican core protein

Gene

BCAN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Hyaluronic acid, Lectin

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_120800. Dermatan sulfate biosynthesis.
REACT_120888. CS/DS degradation.
REACT_120989. Chondroitin sulfate biosynthesis.
REACT_121408. A tetrasaccharide linker sequence is required for GAG synthesis.
REACT_163906. ECM proteoglycans.
REACT_267648. Defective CHST3 causes SEDCJD.
REACT_267917. Defective CHST14 causes EDS, musculocontractural type.
REACT_268113. Defective CHSY1 causes TPBS.
REACT_268678. Defective B3GAT3 causes JDSSDHD.
REACT_268749. Defective B4GALT7 causes EDS, progeroid type.

Names & Taxonomyi

Protein namesi
Recommended name:
Brevican core protein
Alternative name(s):
Brain-enriched hyaluronan-binding protein
Short name:
BEHAB
Chondroitin sulfate proteoglycan 7
Gene namesi
Name:BCAN
Synonyms:BEHAB, CSPG7
ORF Names:UNQ2525/PRO6018
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:23059. BCAN.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134868393.

Polymorphism and mutation databases

BioMutaiBCAN.
DMDMi68067899.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 911889Brevican core proteinPRO_0000017511Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi57 ↔ 137By similarity
Glycosylationi130 – 1301N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi179 ↔ 250By similarity
Disulfide bondi203 ↔ 224By similarity
Disulfide bondi277 ↔ 352By similarity
Disulfide bondi301 ↔ 322By similarity
Glycosylationi337 – 3371N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi650 ↔ 661By similarity
Disulfide bondi655 ↔ 670By similarity
Disulfide bondi672 ↔ 681By similarity
Disulfide bondi688 ↔ 699By similarity
Disulfide bondi716 ↔ 808By similarity
Disulfide bondi784 ↔ 800By similarity
Disulfide bondi815 ↔ 858By similarity
Disulfide bondi844 ↔ 871By similarity
Glycosylationi905 – 9051O-linked (GalNAc...)1 Publication
Glycosylationi906 – 9061O-linked (GalNAc...)1 Publication

Post-translational modificationi

Contains mostly chondroitin sulfate (By similarity). O-glycosylated with a core 1 or possibly core 8 glycan.By similarity1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Proteoglycan

Proteomic databases

PaxDbiQ96GW7.
PeptideAtlasiQ96GW7.
PRIDEiQ96GW7.

PTM databases

PhosphoSiteiQ96GW7.

Expressioni

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiQ96GW7.
CleanExiHS_BCAN.
ExpressionAtlasiQ96GW7. baseline and differential.
GenevisibleiQ96GW7. HS.

Organism-specific databases

HPAiCAB025862.
HPA007865.

Interactioni

Subunit structurei

Interacts with TNR.By similarity

Protein-protein interaction databases

BioGridi121964. 12 interactions.
IntActiQ96GW7. 2 interactions.
MINTiMINT-4830140.
STRINGi9606.ENSP00000331210.

Structurei

3D structure databases

ProteinModelPortaliQ96GW7.
SMRiQ96GW7. Positions 42-146, 161-251, 267-353, 688-811.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 155120Ig-like V-typeAdd
BLAST
Domaini157 – 25296Link 1PROSITE-ProRule annotationAdd
BLAST
Domaini257 – 35498Link 2PROSITE-ProRule annotationAdd
BLAST
Domaini646 – 68237EGF-likePROSITE-ProRule annotationAdd
BLAST
Domaini695 – 809115C-type lectinPROSITE-ProRule annotationAdd
BLAST
Domaini813 – 87361SushiPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni520 – 53011O-glycosylated at two sitesAdd
BLAST
Regioni540 – 5456O-glycosylated at two sites
Regioni569 – 5757O-glycosylated at one site

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi385 – 47793Glu-richAdd
BLAST

Sequence similaritiesi

Contains 1 C-type lectin domain.PROSITE-ProRule annotation
Contains 1 EGF-like domain.PROSITE-ProRule annotation
Contains 2 Link domains.PROSITE-ProRule annotation
Contains 1 Sushi (CCP/SCR) domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Immunoglobulin domain, Repeat, Signal, Sushi

Phylogenomic databases

eggNOGiNOG136696.
GeneTreeiENSGT00760000119025.
HOVERGENiHBG008175.
InParanoidiQ96GW7.
KOiK06795.
OMAiDVGLRFC.
OrthoDBiEOG7PS1F3.
PhylomeDBiQ96GW7.
TreeFamiTF332134.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.10.100.10. 3 hits.
InterProiIPR001304. 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.
IPR000538. Link.
IPR000436. Sushi_SCR_CCP_dom.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF00059. Lectin_C. 1 hit.
PF00084. Sushi. 1 hit.
PF07686. V-set. 1 hit.
PF00193. Xlink. 2 hits.
[Graphical view]
PRINTSiPR01265. LINKMODULE.
SMARTiSM00032. CCP. 1 hit.
SM00034. CLECT. 1 hit.
SM00181. EGF. 1 hit.
SM00406. IGv. 1 hit.
SM00445. LINK. 2 hits.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 3 hits.
SSF57535. SSF57535. 1 hit.
PROSITEiPS00615. 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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96GW7-1) [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

        10         20         30         40         50
MAQLFLPLLA ALVLAQAPAA LADVLEGDSS EDRAFRVRIA GDAPLQGVLG
60 70 80 90 100
GALTIPCHVH YLRPPPSRRA VLGSPRVKWT FLSRGREAEV LVARGVRVKV
110 120 130 140 150
NEAYRFRVAL PAYPASLTDV SLALSELRPN DSGIYRCEVQ HGIDDSSDAV
160 170 180 190 200
EVKVKGVVFL YREGSARYAF SFSGAQEACA RIGAHIATPE QLYAAYLGGY
210 220 230 240 250
EQCDAGWLSD QTVRYPIQTP REACYGDMDG FPGVRNYGVV DPDDLYDVYC
260 270 280 290 300
YAEDLNGELF LGDPPEKLTL EEARAYCQER GAEIATTGQL YAAWDGGLDH
310 320 330 340 350
CSPGWLADGS VRYPIVTPSQ RCGGGLPGVK TLFLFPNQTG FPNKHSRFNV
360 370 380 390 400
YCFRDSAQPS AIPEASNPAS NPASDGLEAI VTVTETLEEL QLPQEATESE
410 420 430 440 450
SRGAIYSIPI MEDGGGGSST PEDPAEAPRT LLEFETQSMV PPTGFSEEEG
460 470 480 490 500
KALEEEEKYE DEEEKEEEEE EEEVEDEALW AWPSELSSPG PEASLPTEPA
510 520 530 540 550
AQEESLSQAP ARAVLQPGAS PLPDGESEAS RPPRVHGPPT ETLPTPRERN
560 570 580 590 600
LASPSPSTLV EAREVGEATG GPELSGVPRG ESEETGSSEG APSLLPATRA
610 620 630 640 650
PEGTRELEAP SEDNSGRTAP AGTSVQAQPV LPTDSASRGG VAVVPASGDC
660 670 680 690 700
VPSPCHNGGT CLEEEEGVRC LCLPGYGGDL CDVGLRFCNP GWDAFQGACY
710 720 730 740 750
KHFSTRRSWE EAETQCRMYG AHLASISTPE EQDFINNRYR EYQWIGLNDR
760 770 780 790 800
TIEGDFLWSD GVPLLYENWN PGQPDSYFLS GENCVVMVWH DQGQWSDVPC
810 820 830 840 850
NYHLSYTCKM GLVSCGPPPE LPLAQVFGRP RLRYEVDTVL RYRCREGLAQ
860 870 880 890 900
RNLPLIRCQE NGRWEAPQIS CVPRRPARAL HPEEDPEGRQ GRLLGRWKAL
910
LIPPSSPMPG P
Length:911
Mass (Da):99,118
Last modified:June 21, 2005 - v2
Checksum:i5268E796FA3938D2
GO
Isoform 2 (identifier: Q96GW7-2) [UniParc]FASTAAdd to basket

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.Curated
Show »
Length:671
Mass (Da):71,671
Checksum:iBAD0E1959546D4B9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti175 – 1751A → T in AAH22938 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti356 – 3561S → L.
Corresponds to variant rs12065791 [ dbSNP | Ensembl ].
VAR_050123
Natural varianti504 – 5041E → K.1 Publication
Corresponds to variant rs1056695 [ dbSNP | Ensembl ].
VAR_019551

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei649 – 67123DCVPS…GVRCL → NSAQGSTALSILLLFFPLQL WVT in isoform 2. 1 PublicationVSP_011184Add
BLAST
Alternative sequencei672 – 911240Missing in isoform 2. 1 PublicationVSP_011185Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1149.1. [Q96GW7-1]
CCDS1150.1. [Q96GW7-2]
RefSeqiNP_068767.3. NM_021948.4. [Q96GW7-1]
NP_940819.1. NM_198427.1. [Q96GW7-2]
UniGeneiHs.516904.

Genome annotation databases

EnsembliENST00000329117; ENSP00000331210; ENSG00000132692. [Q96GW7-1]
ENST00000361588; ENSP00000354925; ENSG00000132692. [Q96GW7-2]
GeneIDi63827.
KEGGihsa:63827.
UCSCiuc001fpo.3. human. [Q96GW7-2]
uc001fpp.3. human. [Q96GW7-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

Brevican

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1149.1. [Q96GW7-1]
CCDS1150.1. [Q96GW7-2]
RefSeqiNP_068767.3. NM_021948.4. [Q96GW7-1]
NP_940819.1. NM_198427.1. [Q96GW7-2]
UniGeneiHs.516904.

3D structure databases

ProteinModelPortaliQ96GW7.
SMRiQ96GW7. Positions 42-146, 161-251, 267-353, 688-811.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121964. 12 interactions.
IntActiQ96GW7. 2 interactions.
MINTiMINT-4830140.
STRINGi9606.ENSP00000331210.

PTM databases

PhosphoSiteiQ96GW7.

Polymorphism and mutation databases

BioMutaiBCAN.
DMDMi68067899.

Proteomic databases

PaxDbiQ96GW7.
PeptideAtlasiQ96GW7.
PRIDEiQ96GW7.

Protocols and materials databases

DNASUi63827.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000329117; ENSP00000331210; ENSG00000132692. [Q96GW7-1]
ENST00000361588; ENSP00000354925; ENSG00000132692. [Q96GW7-2]
GeneIDi63827.
KEGGihsa:63827.
UCSCiuc001fpo.3. human. [Q96GW7-2]
uc001fpp.3. human. [Q96GW7-1]

Organism-specific databases

CTDi63827.
GeneCardsiGC01P156611.
HGNCiHGNC:23059. BCAN.
HPAiCAB025862.
HPA007865.
MIMi600347. gene.
neXtProtiNX_Q96GW7.
PharmGKBiPA134868393.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG136696.
GeneTreeiENSGT00760000119025.
HOVERGENiHBG008175.
InParanoidiQ96GW7.
KOiK06795.
OMAiDVGLRFC.
OrthoDBiEOG7PS1F3.
PhylomeDBiQ96GW7.
TreeFamiTF332134.

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_120800. Dermatan sulfate biosynthesis.
REACT_120888. CS/DS degradation.
REACT_120989. Chondroitin sulfate biosynthesis.
REACT_121408. A tetrasaccharide linker sequence is required for GAG synthesis.
REACT_163906. ECM proteoglycans.
REACT_267648. Defective CHST3 causes SEDCJD.
REACT_267917. Defective CHST14 causes EDS, musculocontractural type.
REACT_268113. Defective CHSY1 causes TPBS.
REACT_268678. Defective B3GAT3 causes JDSSDHD.
REACT_268749. Defective B4GALT7 causes EDS, progeroid type.

Miscellaneous databases

GeneWikiiBrevican.
GenomeRNAii63827.
NextBioi65542.
PROiQ96GW7.
SOURCEiSearch...

Gene expression databases

BgeeiQ96GW7.
CleanExiHS_BCAN.
ExpressionAtlasiQ96GW7. baseline and differential.
GenevisibleiQ96GW7. HS.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.10.100.10. 3 hits.
InterProiIPR001304. 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.
IPR000538. Link.
IPR000436. Sushi_SCR_CCP_dom.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF00059. Lectin_C. 1 hit.
PF00084. Sushi. 1 hit.
PF07686. V-set. 1 hit.
PF00193. Xlink. 2 hits.
[Graphical view]
PRINTSiPR01265. LINKMODULE.
SMARTiSM00032. CCP. 1 hit.
SM00034. CLECT. 1 hit.
SM00181. EGF. 1 hit.
SM00406. IGv. 1 hit.
SM00445. LINK. 2 hits.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 3 hits.
SSF57535. SSF57535. 1 hit.
PROSITEiPS00615. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. 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.
    Tissue: Cerebrospinal fluid.

Entry informationi

Entry nameiPGCB_HUMAN
AccessioniPrimary (citable) accession number: Q96GW7
Secondary accession number(s): D3DVC2
, Q5SZ10, Q5T3I5, Q8TBB9, Q9HBK1, Q9HBK4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: June 21, 2005
Last modified: June 24, 2015
This is version 126 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.