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Q8VHY0

- CSPG4_MOUSE

UniProt

Q8VHY0 - CSPG4_MOUSE

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Protein

Chondroitin sulfate proteoglycan 4

Gene

Cspg4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Proteoglycan playing a role in cell proliferation and migration which stimulates endothelial cells motility during microvascular morphogenesis. May also inhibit neurite outgrowth and growth cone collapse during axon regeneration. Cell surface receptor for collagen alpha 2(VI) which may confer cells ability to migrate on that substrate. Binds through its extracellular N-terminus growth factors, extracellular matrix proteases modulating their activity. May regulate MPP16-dependent degradation and invasion of type I collagen participating in melanoma cells invasion properties. May modulate the plasminogen system by enhancing plasminogen activation and inhibiting angiostatin. Functions also as a signal transducing protein by binding through its cytoplasmic C-terminus scaffolding and signaling proteins. May promote retraction fiber formation and cell polarization through Rho GTPase activation. May stimulate alpha-4, beta-1 integrin-mediated adhesion and spreading by recruiting and activating a signaling cascade through CDC42, ACK1 and BCAR1. May activate FAK and ERK1/ERK2 signaling cascades.2 Publications

GO - Molecular functioni

  1. signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  1. activation of MAPK activity Source: MGI
  2. angiogenesis Source: UniProtKB-KW
  3. cell proliferation Source: MGI
  4. glial cell migration Source: MGI
  5. intracellular signal transduction Source: Ensembl
  6. positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
  7. tissue remodeling Source: UniProtKB-KW
  8. transmembrane receptor protein tyrosine kinase signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Transducer

Keywords - Biological processi

Angiogenesis, Differentiation, Tissue remodeling

Enzyme and pathway databases

ReactomeiREACT_196489. A tetrasaccharide linker sequence is required for GAG synthesis.
REACT_196514. Chondroitin sulfate biosynthesis.
REACT_196540. Dermatan sulfate biosynthesis.
REACT_198981. CS/DS degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Chondroitin sulfate proteoglycan 4
Alternative name(s):
Chondroitin sulfate proteoglycan NG2
Proteoglycan AN2
Gene namesi
Name:Cspg4
Synonyms:An2, Kiaa4232, Ng2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:2153093. Cspg4.

Subcellular locationi

Apical cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication; Extracellular side 1 Publication. Cell projectionlamellipodium membrane 1 Publication; Single-pass type I membrane protein 1 Publication; Extracellular side 1 Publication
Note: Localized at the apical plasma membrane it relocalizes to the lamellipodia of astrocytoma upon phosphorylation by PRKCA. Localizes to the retraction fibers. A fraction may undergo cell surface proteolysis and secretion (By similarity). Localizes to the plasma membrane of oligodendrocytes.By similarity

GO - Cellular componenti

  1. cell projection Source: UniProtKB-KW
  2. extracellular vesicular exosome Source: Ensembl
  3. integral component of membrane Source: UniProtKB-KW
  4. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice are unresponsive to PDGF-AA through PDGF-alpha receptor.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2324 – 23241Q → G: No effect on interaction with GRIP1 and GRIP2. 1 Publication
Mutagenesisi2325 – 23251Y → F: No effect on interaction with GRIP1 and GRIP2. 1 Publication
Mutagenesisi2325 – 23251Y → G: Loss of interaction with GRIP1 and GRIP2. 1 Publication
Mutagenesisi2326 – 23261W → G: Loss of interaction with GRIP1 and GRIP2. 1 Publication
Mutagenesisi2327 – 23271V → G: Loss of interaction with GRIP1 and GRIP2. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Sequence AnalysisAdd
BLAST
Chaini30 – 23272298Chondroitin sulfate proteoglycan 4PRO_0000041963Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi130 – 1301N-linked (GlcNAc...)1 Publication
Disulfide bondi170 ↔ 193PROSITE-ProRule annotation
Glycosylationi349 – 3491N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi355 ↔ 381PROSITE-ProRule annotation
Glycosylationi428 – 4281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi686 – 6861N-linked (GlcNAc...)Sequence Analysis
Glycosylationi773 – 7731N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1000 – 10001O-linked (Xyl...) (chondroitin sulfate)By similarity
Glycosylationi1136 – 11361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1207 – 12071N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1369 – 13691N-linked (GlcNAc...)1 Publication
Glycosylationi1454 – 14541N-linked (GlcNAc...)1 Publication
Glycosylationi1650 – 16501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1914 – 19141N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2021 – 20211N-linked (GlcNAc...)1 Publication
Glycosylationi2039 – 20391N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2045 – 20451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2080 – 20801N-linked (GlcNAc...)1 Publication
Modified residuei2257 – 22571Phosphothreonine; by PKC/PRKCABy similarity

Post-translational modificationi

O-glycosylated; contains glycosaminoglycan chondroitin sulfate which are required for proper localization and function in stress fiber formation. Involved in interaction with MMP16 and ITGA4 (By similarity).By similarity
Phosphorylation by PRKCA regulates its subcellular location and function in cell motility.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Proteoglycan

Proteomic databases

PaxDbiQ8VHY0.
PRIDEiQ8VHY0.

PTM databases

PhosphoSiteiQ8VHY0.

Expressioni

Tissue specificityi

Expressed in microcascular pericytes and not endothelial cells.1 Publication

Gene expression databases

CleanExiMM_CSPG4.
ExpressionAtlasiQ8VHY0. baseline and differential.
GenevestigatoriQ8VHY0.

Interactioni

Subunit structurei

Interacts with ITGA4 through its chondroitin sulfate glycosaminoglycan. Interacts with BCAR1, CDC42 and ACK1. Interacts with MMP16. Interacts with the first PDZ domain of MPDZ. Interacts with PRKCA. Interacts with LGALS3 and the integrin composed of ITGB1 and ITGA3. Binds TNC, laminin-1, COL5A1 and COL6A2. Interacts with PLG and angiostatin. Binds FGF2 and PDGFA (By similarity). Interacts with GRIP1, GRIP2 and GRIA2. Forms a ternary complex with GRIP1 and GRIA2.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Gria2P238192EBI-8327479,EBI-77538
Grip1Q925T67EBI-8327479,EBI-537752
Grip2Q9WTW12EBI-8327479,EBI-936045From a different organism.

Protein-protein interaction databases

IntActiQ8VHY0. 5 interactions.
MINTiMINT-1787512.

Structurei

3D structure databases

ProteinModelPortaliQ8VHY0.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini30 – 22292200ExtracellularSequence AnalysisAdd
BLAST
Topological domaini2251 – 232777CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei2230 – 225021HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 193164Laminin G-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini203 – 381179Laminin G-like 2PROSITE-ProRule annotationAdd
BLAST
Repeati431 – 52494CSPG 1Add
BLAST
Repeati557 – 64488CSPG 2Add
BLAST
Repeati666 – 765100CSPG 3Add
BLAST
Repeati793 – 88391CSPG 4Add
BLAST
Repeati905 – 99490CSPG 5Add
BLAST
Repeati1025 – 111389CSPG 6Add
BLAST
Repeati1133 – 122189CSPG 7Add
BLAST
Repeati1246 – 134297CSPG 8Add
BLAST
Repeati1365 – 145490CSPG 9Add
BLAST
Repeati1481 – 156686CSPG 10Add
BLAST
Repeati1588 – 168497CSPG 11Add
BLAST
Repeati1712 – 180897CSPG 12Add
BLAST
Repeati1840 – 192788CSPG 13Add
BLAST
Repeati1949 – 203486CSPG 14Add
BLAST
Repeati2053 – 2152100CSPG 15Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 640611Globular or compact configuration stabilized by disulfide bondsAdd
BLAST
Regioni30 – 640611Neurite growth inhibitionBy similarityAdd
BLAST
Regioni575 – 1045471Interaction with COL6A2By similarityAdd
BLAST
Regioni632 – 1451820Interaction with COL5A1By similarityAdd
BLAST
Regioni1591 – 2226636Neurite growth inhibitionBy similarityAdd
BLAST
Regioni1592 – 2226635Cysteine-containingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi2325 – 23273PDZ-binding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi640 – 1591952Gly/Ser-rich (glycosaminoglycan attachment domain)Add
BLAST

Sequence similaritiesi

Contains 15 CSPG (NG2) repeats.Curated
Contains 2 laminin G-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG261397.
GeneTreeiENSGT00550000074429.
HOGENOMiHOG000170195.
HOVERGENiHBG081360.
InParanoidiQ8VHY0.
KOiK08115.
OMAiRPIYRFT.
OrthoDBiEOG77DJ56.
TreeFamiTF316876.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF00054. Laminin_G_1. 1 hit.
PF02210. Laminin_G_2. 1 hit.
[Graphical view]
SMARTiSM00282. LamG. 2 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 2 hits.
PROSITEiPS50025. LAM_G_DOMAIN. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8VHY0-1) [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
MLLGPGHPLS APALALALTL ALLVRSTAPA SFFGENHLEV PVPSALTRVD
60 70 80 90 100
LLLQFSTSQP EALLLLAAGQ DDHLLLQLHS GCLQVRLALG QKELKLQTPA
110 120 130 140 150
DTVLSDSAPH TVVLTVSDSW AVLSVDGVLN TSAPIPRASH LKATYGLFVG
160 170 180 190 200
SSGSLDLPYL KGISRPLRGC LHSAILNGRN LLRPLTSDVH EGCAEEFSAG
210 220 230 240 250
DEVGLGFSGP HSLAAFPAWS TREEGTLEFT LTTRSQQAPL AFQAGDKRGN
260 270 280 290 300
FIYVDIFEGH LRAVVEKGQG TMLLRNSVPV ADGQPHEVSV HIDVHRLEIS
310 320 330 340 350
VDQYPTRTFN RGVLSYLEPR GSLLLGGLDT EASRHLQEHR LGLAPGAANI
360 370 380 390 400
SLVGCIEDFS VNGRRQGLRD AWLTRDMSAG CRPEEDEYEE EVYGPYETFS
410 420 430 440 450
TLAPEAWPAM ELPEPCIPEP GLPAVFANFT QLLTISPLVV AEGGTAWLEW
460 470 480 490 500
RHVQPTLDLT EAELRKSQVL FSVSQSARHG DLELDILGAQ TRKMFTLLDV
510 520 530 540 550
VNRKARFVHD GSEDTSDQLM LEVSVTARAP VPSCLRRGQI YILPIQVNPV
560 570 580 590 600
NDPPRIIFPH GSLMVILEHT QKPLGPEIFQ AYDPDSACEG LTFQLLGVSS
610 620 630 640 650
GVPVEHRDQP GEPATEFSCR ELEVGDIVYV HRGGPAQDLT FRVSDGMQAS
660 670 680 690 700
APATLKVVAV RPAIQILHNT GLHLAQGSAA AILPANLSVE TNAVGQDVSV
710 720 730 740 750
LFRVTGTLQF GELQKQGAGG VEGTEWWDTL AFHQRDVEQG RVRYLSTDPQ
760 770 780 790 800
HHTQDTVEDL ILEVQVGQET LSNLSFPVTI QRATVWMLRL EPLHTQNPHQ
810 820 830 840 850
ETLTPAHLEA SLEEEEEEGS PQPHTFHYEL VQAPRRGNLL LQGTRLSDGE
860 870 880 890 900
SFSQSDLQAG RVTYRATMRT SEAADDSFRF RVTSPPHFSP LYTFPIHIGG
910 920 930 940 950
DPNAPVLTNV LLMVPEGGEG VLSADHLFVK SLNSASYLYE VMEQPHHGKL
960 970 980 990 1000
AWRDPKGKST PVTSFTNEDL LHGRLVYQHD DSETIEDDIP FVATRQGEGS
1010 1020 1030 1040 1050
GDMAWEEVRG VFRVAIQPVN DHAPVQTISR VFHVARGGQR LLTTDDVAFS
1060 1070 1080 1090 1100
DADSGFSDAQ LVLTRKDLLF GSIVAMEEPT RPIYRFTQED LRKKQVLFVH
1110 1120 1130 1140 1150
SGADHGWLQL QVSDGQHQAT AMLEVQASEP YLHVANSSSL VVPQGGQGTI
1160 1170 1180 1190 1200
DTAVLQLDTN LDIRSGNEVH YHVTAGPQWG QLLRDGQSVT SFSQRDLLDG
1210 1220 1230 1240 1250
AILYSHNGSL SPQDTLAFSV AAGPVHTNTF LQVTIALEGP LAPLQLVQHK
1260 1270 1280 1290 1300
KIYVFQGEAA EIRRDQLEVV QEAVLPADIM FSLRSPPNAG YLVMVSHGAS
1310 1320 1330 1340 1350
AEEPPSLDPV QSFSQEAVNS GRVLYLHSRP GAWSDSFSLD VASGLGDPLE
1360 1370 1380 1390 1400
GISVELEVLP TVIPLDVQNF SVPEGGTRTL APPLVQITGP YFPTLPGLVL
1410 1420 1430 1440 1450
QVLEPPQHGA LQKEDHSQDG SLSTFSWREV EEQLIRYVHD GSETQTDAFV
1460 1470 1480 1490 1500
LLANASEMDR QSQPVAFTIT ILPVNDQPPV LTTNTGLQIW EGAIVPIPPE
1510 1520 1530 1540 1550
ALRGTDNDSG PEDLVYTIEQ PSNGRIALRV APDTEVHRFT QAQLDSGLVL
1560 1570 1580 1590 1600
FSHRGALEGG FHFDLSDGAH TSPGHFFRVV AQKQALLSLE GTRKLTVCPE
1610 1620 1630 1640 1650
SVQPLSSQSL SASSSTGADP RHLLYRVVRG PQLGRLLHAQ QGSAEEVLVN
1660 1670 1680 1690 1700
FTQAEVNAGN ILYEHEMSSE PFWEAHDTIG LLLSSPPARD LAATLAVMVS
1710 1720 1730 1740 1750
FDAACPQRPS RLWKNKGLWV PEGQRAKITV AALDAANLLA SVPASQRSRH
1760 1770 1780 1790 1800
DVLFQVTQFP TRGQLLVSEE PLHARRPYFL QSELAAGQLV YAHGGGGTQQ
1810 1820 1830 1840 1850
DGFRFRAHLQ GPTGTSVAGP QTSEAFVITV RDVNERPPQP QASIPLRVTR
1860 1870 1880 1890 1900
GSRAPVSRAQ LSVVDPDSAP GEIEYEVQRA PHNGFLSLAG DNTGPVTHFT
1910 1920 1930 1940 1950
QADVDAGRLA FVANGSSVAG VFQLSMSDGA SPPIPMSLAV DVLPSTIEVQ
1960 1970 1980 1990 2000
LRAPLEVPQA LGRTSLSRQQ LQVISDREEP DVAYRLTQGP LYGQLLVGGQ
2010 2020 2030 2040 2050
PASAFSQLQV DQGDVVFVFT NFSSSQDHFK VVALARGVNA SATVNVTVQA
2060 2070 2080 2090 2100
LLHVWAGGPW PQGTTLRLDP TVLDASELAN RTGSMPHFRL LAGPRYGRVV
2110 2120 2130 2140 2150
RVSQGRTESR SNQLVEHFTQ RDLEEGQLGL EVGKPEGRST GPAGDRLTLE
2160 2170 2180 2190 2200
LWAKGVPPAV ALLDFATEPY HAAKSYSVAL LSVPEAVRTE TEKPGRSVPT
2210 2220 2230 2240 2250
GQPGQAASSP VPTAAKGGFL GFLEANMFSI IIPVCLILLL LALILPLLFY
2260 2270 2280 2290 2300
LRKRNKTGKH DVQVLTAKPR NGLAGDTETF RKVEPGQAIP LITVPGQGPP
2310 2320
PGGQPDPELL QFCRTPNPAL RNGQYWV
Length:2,327
Mass (Da):252,309
Last modified:October 3, 2012 - v3
Checksum:iC101DF60FCE3A7BC
GO
Isoform 2 (identifier: Q8VHY0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1666: Missing.

Note: No experimental confirmation available.

Show »
Length:661
Mass (Da):70,843
Checksum:iDA679F6CCF894532
GO
Isoform 3 (identifier: Q8VHY0-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1657-1694: NAGNILYEHE...SPPARDLAAT → RASLLSHHTD...ASLDPVPAQG
     1695-2327: Missing.

Note: No experimental confirmation available.

Show »
Length:1,694
Mass (Da):184,393
Checksum:i52625A76C5070FBB
GO

Sequence cautioni

The sequence BAC26150.1 differs from that shown. Reason: Frameshift at position 1889.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1058 – 10581D → V in AAL37505. (PubMed:12458226)Curated
Sequence conflicti1113 – 11131S → P in BAD90326. 1 PublicationCurated
Sequence conflicti1427 – 14271W → R in AAL37505. (PubMed:12458226)Curated
Sequence conflicti1520 – 15201Q → E in AAL37505. (PubMed:12458226)Curated
Sequence conflicti1546 – 15461S → G in AAL37505. (PubMed:12458226)Curated
Sequence conflicti1929 – 19291G → E in AAL37505. (PubMed:12458226)Curated
Sequence conflicti2000 – 20001Q → R in AAL37505. (PubMed:12458226)Curated
Sequence conflicti2011 – 20111D → H in BAC26150. (PubMed:16141072)Curated
Sequence conflicti2093 – 20931G → E in AAL37505. (PubMed:12458226)Curated
Sequence conflicti2248 – 22481L → H in AAL37505. (PubMed:12458226)Curated
Sequence conflicti2300 – 23001P → S in AAL37505. (PubMed:12458226)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 16661666Missing in isoform 2. 1 PublicationVSP_015656Add
BLAST
Alternative sequencei1657 – 169438NAGNI…DLAAT → RASLLSHHTDPNLTSGGCQL EHPPHWQLASLDPVPAQG in isoform 3. 1 PublicationVSP_015657Add
BLAST
Alternative sequencei1695 – 2327633Missing in isoform 3. 1 PublicationVSP_015658Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF352400 mRNA. Translation: AAL37505.1.
AK028844 mRNA. Translation: BAC26150.1. Sequence problems.
AK075625 mRNA. Translation: BAC35866.1.
AC126257 Genomic DNA. No translation available.
CH466522 Genomic DNA. Translation: EDL25876.1.
AK220559 mRNA. Translation: BAD90326.1.
CCDSiCCDS23211.1. [Q8VHY0-1]
RefSeqiNP_620570.2. NM_139001.2. [Q8VHY0-1]
UniGeneiMm.41329.

Genome annotation databases

EnsembliENSMUST00000035661; ENSMUSP00000038909; ENSMUSG00000032911. [Q8VHY0-1]
GeneIDi121021.
KEGGimmu:121021.
UCSCiuc009ptl.1. mouse.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF352400 mRNA. Translation: AAL37505.1 .
AK028844 mRNA. Translation: BAC26150.1 . Sequence problems.
AK075625 mRNA. Translation: BAC35866.1 .
AC126257 Genomic DNA. No translation available.
CH466522 Genomic DNA. Translation: EDL25876.1 .
AK220559 mRNA. Translation: BAD90326.1 .
CCDSi CCDS23211.1. [Q8VHY0-1 ]
RefSeqi NP_620570.2. NM_139001.2. [Q8VHY0-1 ]
UniGenei Mm.41329.

3D structure databases

ProteinModelPortali Q8VHY0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8VHY0. 5 interactions.
MINTi MINT-1787512.

PTM databases

PhosphoSitei Q8VHY0.

Proteomic databases

PaxDbi Q8VHY0.
PRIDEi Q8VHY0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000035661 ; ENSMUSP00000038909 ; ENSMUSG00000032911 . [Q8VHY0-1 ]
GeneIDi 121021.
KEGGi mmu:121021.
UCSCi uc009ptl.1. mouse.

Organism-specific databases

CTDi 1464.
MGIi MGI:2153093. Cspg4.
Rougei Search...

Phylogenomic databases

eggNOGi NOG261397.
GeneTreei ENSGT00550000074429.
HOGENOMi HOG000170195.
HOVERGENi HBG081360.
InParanoidi Q8VHY0.
KOi K08115.
OMAi RPIYRFT.
OrthoDBi EOG77DJ56.
TreeFami TF316876.

Enzyme and pathway databases

Reactomei REACT_196489. A tetrasaccharide linker sequence is required for GAG synthesis.
REACT_196514. Chondroitin sulfate biosynthesis.
REACT_196540. Dermatan sulfate biosynthesis.
REACT_198981. CS/DS degradation.

Miscellaneous databases

NextBioi 369752.
PROi Q8VHY0.
SOURCEi Search...

Gene expression databases

CleanExi MM_CSPG4.
ExpressionAtlasi Q8VHY0. baseline and differential.
Genevestigatori Q8VHY0.

Family and domain databases

Gene3Di 2.60.120.200. 2 hits.
InterProi IPR013320. ConA-like_dom.
IPR001791. Laminin_G.
[Graphical view ]
Pfami PF00054. Laminin_G_1. 1 hit.
PF02210. Laminin_G_2. 1 hit.
[Graphical view ]
SMARTi SM00282. LamG. 2 hits.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 2 hits.
PROSITEi PS50025. LAM_G_DOMAIN. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The proteoglycan NG2 is complexed with alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors by the PDZ glutamate receptor interaction protein (GRIP) in glial progenitor cells. Implications for glial-neuronal signaling."
    Stegmueller J., Werner H., Nave K.-A., Trotter J.
    J. Biol. Chem. 278:3590-3598(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH GRIP1; GRIP2 AND GRIA2, MUTAGENESIS OF GLN-2324; TYR-2325; TRP-2326 AND VAL-2327, DOMAIN, SUBCELLULAR LOCATION.
    Tissue: Oligodendrocyte.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Embryo and Skin.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 999-2327 (ISOFORM 3).
    Tissue: Fetal brain.
  6. "PDGF (alpha)-receptor is unresponsive to PDGF-AA in aortic smooth muscle cells from the NG2 knockout mouse."
    Grako K.A., Ochiya T., Barritt D., Nishiyama A., Stallcup W.B.
    J. Cell Sci. 112:905-915(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. "NG2 proteoglycan promotes endothelial cell motility and angiogenesis via engagement of galectin-3 and alpha3beta1 integrin."
    Fukushi J., Makagiansar I.T., Stallcup W.B.
    Mol. Biol. Cell 15:3580-3590(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, FUNCTION.
  8. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
    Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
    Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-130; ASN-1369; ASN-1454; ASN-2021 AND ASN-2080.
    Tissue: Myoblast.

Entry informationi

Entry nameiCSPG4_MOUSE
AccessioniPrimary (citable) accession number: Q8VHY0
Secondary accession number(s): G5E892
, Q5DTG1, Q8BPI8, Q8CE79
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: October 3, 2012
Last modified: October 29, 2014
This is version 104 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Valuable marker for several incompletely differentiated precursor cells.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3