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Q8VHY0

- CSPG4_MOUSE

UniProt

Q8VHY0 - CSPG4_MOUSE

Protein

Chondroitin sulfate proteoglycan 4

Gene

Cspg4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 3 (03 Oct 2012)
      Previous versions | rss
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    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. protein binding Source: IntAct
    2. 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

    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. apical plasma membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. lamellipodium membrane Source: UniProtKB-SubCell
    4. plasma membrane Source: MGI

    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

    ArrayExpressiQ8VHY0.
    CleanExiMM_CSPG4.
    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.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    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

    MLLGPGHPLS APALALALTL ALLVRSTAPA SFFGENHLEV PVPSALTRVD     50
    LLLQFSTSQP EALLLLAAGQ DDHLLLQLHS GCLQVRLALG QKELKLQTPA 100
    DTVLSDSAPH TVVLTVSDSW AVLSVDGVLN TSAPIPRASH LKATYGLFVG 150
    SSGSLDLPYL KGISRPLRGC LHSAILNGRN LLRPLTSDVH EGCAEEFSAG 200
    DEVGLGFSGP HSLAAFPAWS TREEGTLEFT LTTRSQQAPL AFQAGDKRGN 250
    FIYVDIFEGH LRAVVEKGQG TMLLRNSVPV ADGQPHEVSV HIDVHRLEIS 300
    VDQYPTRTFN RGVLSYLEPR GSLLLGGLDT EASRHLQEHR LGLAPGAANI 350
    SLVGCIEDFS VNGRRQGLRD AWLTRDMSAG CRPEEDEYEE EVYGPYETFS 400
    TLAPEAWPAM ELPEPCIPEP GLPAVFANFT QLLTISPLVV AEGGTAWLEW 450
    RHVQPTLDLT EAELRKSQVL FSVSQSARHG DLELDILGAQ TRKMFTLLDV 500
    VNRKARFVHD GSEDTSDQLM LEVSVTARAP VPSCLRRGQI YILPIQVNPV 550
    NDPPRIIFPH GSLMVILEHT QKPLGPEIFQ AYDPDSACEG LTFQLLGVSS 600
    GVPVEHRDQP GEPATEFSCR ELEVGDIVYV HRGGPAQDLT FRVSDGMQAS 650
    APATLKVVAV RPAIQILHNT GLHLAQGSAA AILPANLSVE TNAVGQDVSV 700
    LFRVTGTLQF GELQKQGAGG VEGTEWWDTL AFHQRDVEQG RVRYLSTDPQ 750
    HHTQDTVEDL ILEVQVGQET LSNLSFPVTI QRATVWMLRL EPLHTQNPHQ 800
    ETLTPAHLEA SLEEEEEEGS PQPHTFHYEL VQAPRRGNLL LQGTRLSDGE 850
    SFSQSDLQAG RVTYRATMRT SEAADDSFRF RVTSPPHFSP LYTFPIHIGG 900
    DPNAPVLTNV LLMVPEGGEG VLSADHLFVK SLNSASYLYE VMEQPHHGKL 950
    AWRDPKGKST PVTSFTNEDL LHGRLVYQHD DSETIEDDIP FVATRQGEGS 1000
    GDMAWEEVRG VFRVAIQPVN DHAPVQTISR VFHVARGGQR LLTTDDVAFS 1050
    DADSGFSDAQ LVLTRKDLLF GSIVAMEEPT RPIYRFTQED LRKKQVLFVH 1100
    SGADHGWLQL QVSDGQHQAT AMLEVQASEP YLHVANSSSL VVPQGGQGTI 1150
    DTAVLQLDTN LDIRSGNEVH YHVTAGPQWG QLLRDGQSVT SFSQRDLLDG 1200
    AILYSHNGSL SPQDTLAFSV AAGPVHTNTF LQVTIALEGP LAPLQLVQHK 1250
    KIYVFQGEAA EIRRDQLEVV QEAVLPADIM FSLRSPPNAG YLVMVSHGAS 1300
    AEEPPSLDPV QSFSQEAVNS GRVLYLHSRP GAWSDSFSLD VASGLGDPLE 1350
    GISVELEVLP TVIPLDVQNF SVPEGGTRTL APPLVQITGP YFPTLPGLVL 1400
    QVLEPPQHGA LQKEDHSQDG SLSTFSWREV EEQLIRYVHD GSETQTDAFV 1450
    LLANASEMDR QSQPVAFTIT ILPVNDQPPV LTTNTGLQIW EGAIVPIPPE 1500
    ALRGTDNDSG PEDLVYTIEQ PSNGRIALRV APDTEVHRFT QAQLDSGLVL 1550
    FSHRGALEGG FHFDLSDGAH TSPGHFFRVV AQKQALLSLE GTRKLTVCPE 1600
    SVQPLSSQSL SASSSTGADP RHLLYRVVRG PQLGRLLHAQ QGSAEEVLVN 1650
    FTQAEVNAGN ILYEHEMSSE PFWEAHDTIG LLLSSPPARD LAATLAVMVS 1700
    FDAACPQRPS RLWKNKGLWV PEGQRAKITV AALDAANLLA SVPASQRSRH 1750
    DVLFQVTQFP TRGQLLVSEE PLHARRPYFL QSELAAGQLV YAHGGGGTQQ 1800
    DGFRFRAHLQ GPTGTSVAGP QTSEAFVITV RDVNERPPQP QASIPLRVTR 1850
    GSRAPVSRAQ LSVVDPDSAP GEIEYEVQRA PHNGFLSLAG DNTGPVTHFT 1900
    QADVDAGRLA FVANGSSVAG VFQLSMSDGA SPPIPMSLAV DVLPSTIEVQ 1950
    LRAPLEVPQA LGRTSLSRQQ LQVISDREEP DVAYRLTQGP LYGQLLVGGQ 2000
    PASAFSQLQV DQGDVVFVFT NFSSSQDHFK VVALARGVNA SATVNVTVQA 2050
    LLHVWAGGPW PQGTTLRLDP TVLDASELAN RTGSMPHFRL LAGPRYGRVV 2100
    RVSQGRTESR SNQLVEHFTQ RDLEEGQLGL EVGKPEGRST GPAGDRLTLE 2150
    LWAKGVPPAV ALLDFATEPY HAAKSYSVAL LSVPEAVRTE TEKPGRSVPT 2200
    GQPGQAASSP VPTAAKGGFL GFLEANMFSI IIPVCLILLL LALILPLLFY 2250
    LRKRNKTGKH DVQVLTAKPR NGLAGDTETF RKVEPGQAIP LITVPGQGPP 2300
    PGGQPDPELL QFCRTPNPAL RNGQYWV 2327
    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

    ArrayExpressi Q8VHY0.
    CleanExi MM_CSPG4.
    Genevestigatori Q8VHY0.

    Family and domain databases

    Gene3Di 2.60.120.200. 2 hits.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    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

    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 1, 2014
    This is version 103 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