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Q8VHY0 (CSPG4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chondroitin sulfate proteoglycan 4
Alternative name(s):
Chondroitin sulfate proteoglycan NG2
Proteoglycan AN2
Gene names
Name:Cspg4
Synonyms:An2, Kiaa4232, Ng2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2327 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7

Subunit structure

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. Ref.1

Subcellular location

Apical cell membrane; Single-pass type I membrane protein; Extracellular side. Cell projectionlamellipodium membrane; Single-pass type I membrane protein; Extracellular side. 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. Ref.1

Tissue specificity

Expressed in microcascular pericytes and not endothelial cells. Ref.7

Post-translational modification

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.

Phosphorylation by PRKCA regulates its subcellular location and function in cell motility By similarity.

Disruption phenotype

Mice are unresponsive to PDGF-AA through PDGF-alpha receptor. Ref.6

Miscellaneous

Valuable marker for several incompletely differentiated precursor cells.

Sequence similarities

Contains 15 CSPG (NG2) repeats.

Contains 2 laminin G-like domains.

Sequence caution

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

Ontologies

Keywords
   Biological processAngiogenesis
Differentiation
Tissue remodeling
   Cellular componentCell membrane
Cell projection
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
Transducer
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Proteoglycan
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of MAPK activity

Inferred from mutant phenotype PubMed 11668599. Source: MGI

angiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

cell proliferation

Inferred from mutant phenotype PubMed 11668599. Source: MGI

glial cell migration

Inferred from direct assay PubMed 10366628. Source: MGI

intracellular signal transduction

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

tissue remodeling

Inferred from electronic annotation. Source: UniProtKB-KW

transmembrane receptor protein tyrosine kinase signaling pathway

Inferred from mutant phenotype PubMed 11668599. Source: MGI

   Cellular_componentapical plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lamellipodium membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay PubMed 11668599. Source: MGI

   Molecular_functionprotein binding

Inferred from physical interaction Ref.1. Source: IntAct

signal transducer activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Gria2P238192EBI-8327479,EBI-77538
Grip1Q925T67EBI-8327479,EBI-537752
Grip2Q9WTW12EBI-8327479,EBI-936045From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8VHY0-1)

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: Q8VHY0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1666: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8VHY0-3)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Chain30 – 23272298Chondroitin sulfate proteoglycan 4
PRO_0000041963

Regions

Topological domain30 – 22292200Extracellular Potential
Transmembrane2230 – 225021Helical; Potential
Topological domain2251 – 232777Cytoplasmic Potential
Domain30 – 193164Laminin G-like 1
Domain203 – 381179Laminin G-like 2
Repeat431 – 52494CSPG 1
Repeat557 – 64488CSPG 2
Repeat666 – 765100CSPG 3
Repeat793 – 88391CSPG 4
Repeat905 – 99490CSPG 5
Repeat1025 – 111389CSPG 6
Repeat1133 – 122189CSPG 7
Repeat1246 – 134297CSPG 8
Repeat1365 – 145490CSPG 9
Repeat1481 – 156686CSPG 10
Repeat1588 – 168497CSPG 11
Repeat1712 – 180897CSPG 12
Repeat1840 – 192788CSPG 13
Repeat1949 – 203486CSPG 14
Repeat2053 – 2152100CSPG 15
Region30 – 640611Globular or compact configuration stabilized by disulfide bonds
Region30 – 640611Neurite growth inhibition By similarity
Region575 – 1045471Interaction with COL6A2 By similarity
Region632 – 1451820Interaction with COL5A1 By similarity
Region1591 – 2226636Neurite growth inhibition By similarity
Region1592 – 2226635Cysteine-containing
Motif2325 – 23273PDZ-binding
Compositional bias640 – 1591952Gly/Ser-rich (glycosaminoglycan attachment domain)

Amino acid modifications

Modified residue22571Phosphothreonine; by PKC/PRKCA By similarity
Glycosylation1301N-linked (GlcNAc...) Ref.8
Glycosylation3491N-linked (GlcNAc...) Potential
Glycosylation4281N-linked (GlcNAc...) Potential
Glycosylation6861N-linked (GlcNAc...) Potential
Glycosylation7731N-linked (GlcNAc...) Potential
Glycosylation10001O-linked (Xyl...) (chondroitin sulfate) By similarity
Glycosylation11361N-linked (GlcNAc...) Potential
Glycosylation12071N-linked (GlcNAc...) Potential
Glycosylation13691N-linked (GlcNAc...) Ref.8
Glycosylation14541N-linked (GlcNAc...) Ref.8
Glycosylation16501N-linked (GlcNAc...) Potential
Glycosylation19141N-linked (GlcNAc...) Potential
Glycosylation20211N-linked (GlcNAc...) Ref.8
Glycosylation20391N-linked (GlcNAc...) Potential
Glycosylation20451N-linked (GlcNAc...) Potential
Glycosylation20801N-linked (GlcNAc...) Ref.8
Disulfide bond170 ↔ 193 By similarity
Disulfide bond355 ↔ 381 By similarity

Natural variations

Alternative sequence1 – 16661666Missing in isoform 2.
VSP_015656
Alternative sequence1657 – 169438NAGNI…DLAAT → RASLLSHHTDPNLTSGGCQL EHPPHWQLASLDPVPAQG in isoform 3.
VSP_015657
Alternative sequence1695 – 2327633Missing in isoform 3.
VSP_015658

Experimental info

Mutagenesis23241Q → G: No effect on interaction with GRIP1 and GRIP2. Ref.1
Mutagenesis23251Y → F: No effect on interaction with GRIP1 and GRIP2. Ref.1
Mutagenesis23251Y → G: Loss of interaction with GRIP1 and GRIP2. Ref.1
Mutagenesis23261W → G: Loss of interaction with GRIP1 and GRIP2. Ref.1
Mutagenesis23271V → G: Loss of interaction with GRIP1 and GRIP2. Ref.1
Sequence conflict10581D → V in AAL37505. Ref.1
Sequence conflict11131S → P in BAD90326. Ref.5
Sequence conflict14271W → R in AAL37505. Ref.1
Sequence conflict15201Q → E in AAL37505. Ref.1
Sequence conflict15461S → G in AAL37505. Ref.1
Sequence conflict19291G → E in AAL37505. Ref.1
Sequence conflict20001Q → R in AAL37505. Ref.1
Sequence conflict20111D → H in BAC26150. Ref.2
Sequence conflict20931G → E in AAL37505. Ref.1
Sequence conflict22481L → H in AAL37505. Ref.1
Sequence conflict23001P → S in AAL37505. Ref.1

Sequences

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

Last modified October 3, 2012. Version 3.
Checksum: C101DF60FCE3A7BC

FASTA2,327252,309
        10         20         30         40         50         60 
MLLGPGHPLS APALALALTL ALLVRSTAPA SFFGENHLEV PVPSALTRVD LLLQFSTSQP 

        70         80         90        100        110        120 
EALLLLAAGQ DDHLLLQLHS GCLQVRLALG QKELKLQTPA DTVLSDSAPH TVVLTVSDSW 

       130        140        150        160        170        180 
AVLSVDGVLN TSAPIPRASH LKATYGLFVG SSGSLDLPYL KGISRPLRGC LHSAILNGRN 

       190        200        210        220        230        240 
LLRPLTSDVH EGCAEEFSAG DEVGLGFSGP HSLAAFPAWS TREEGTLEFT LTTRSQQAPL 

       250        260        270        280        290        300 
AFQAGDKRGN FIYVDIFEGH LRAVVEKGQG TMLLRNSVPV ADGQPHEVSV HIDVHRLEIS 

       310        320        330        340        350        360 
VDQYPTRTFN RGVLSYLEPR GSLLLGGLDT EASRHLQEHR LGLAPGAANI SLVGCIEDFS 

       370        380        390        400        410        420 
VNGRRQGLRD AWLTRDMSAG CRPEEDEYEE EVYGPYETFS TLAPEAWPAM ELPEPCIPEP 

       430        440        450        460        470        480 
GLPAVFANFT QLLTISPLVV AEGGTAWLEW RHVQPTLDLT EAELRKSQVL FSVSQSARHG 

       490        500        510        520        530        540 
DLELDILGAQ TRKMFTLLDV VNRKARFVHD GSEDTSDQLM LEVSVTARAP VPSCLRRGQI 

       550        560        570        580        590        600 
YILPIQVNPV NDPPRIIFPH GSLMVILEHT QKPLGPEIFQ AYDPDSACEG LTFQLLGVSS 

       610        620        630        640        650        660 
GVPVEHRDQP GEPATEFSCR ELEVGDIVYV HRGGPAQDLT FRVSDGMQAS APATLKVVAV 

       670        680        690        700        710        720 
RPAIQILHNT GLHLAQGSAA AILPANLSVE TNAVGQDVSV LFRVTGTLQF GELQKQGAGG 

       730        740        750        760        770        780 
VEGTEWWDTL AFHQRDVEQG RVRYLSTDPQ HHTQDTVEDL ILEVQVGQET LSNLSFPVTI 

       790        800        810        820        830        840 
QRATVWMLRL EPLHTQNPHQ ETLTPAHLEA SLEEEEEEGS PQPHTFHYEL VQAPRRGNLL 

       850        860        870        880        890        900 
LQGTRLSDGE SFSQSDLQAG RVTYRATMRT SEAADDSFRF RVTSPPHFSP LYTFPIHIGG 

       910        920        930        940        950        960 
DPNAPVLTNV LLMVPEGGEG VLSADHLFVK SLNSASYLYE VMEQPHHGKL AWRDPKGKST 

       970        980        990       1000       1010       1020 
PVTSFTNEDL LHGRLVYQHD DSETIEDDIP FVATRQGEGS GDMAWEEVRG VFRVAIQPVN 

      1030       1040       1050       1060       1070       1080 
DHAPVQTISR VFHVARGGQR LLTTDDVAFS DADSGFSDAQ LVLTRKDLLF GSIVAMEEPT 

      1090       1100       1110       1120       1130       1140 
RPIYRFTQED LRKKQVLFVH SGADHGWLQL QVSDGQHQAT AMLEVQASEP YLHVANSSSL 

      1150       1160       1170       1180       1190       1200 
VVPQGGQGTI DTAVLQLDTN LDIRSGNEVH YHVTAGPQWG QLLRDGQSVT SFSQRDLLDG 

      1210       1220       1230       1240       1250       1260 
AILYSHNGSL SPQDTLAFSV AAGPVHTNTF LQVTIALEGP LAPLQLVQHK KIYVFQGEAA 

      1270       1280       1290       1300       1310       1320 
EIRRDQLEVV QEAVLPADIM FSLRSPPNAG YLVMVSHGAS AEEPPSLDPV QSFSQEAVNS 

      1330       1340       1350       1360       1370       1380 
GRVLYLHSRP GAWSDSFSLD VASGLGDPLE GISVELEVLP TVIPLDVQNF SVPEGGTRTL 

      1390       1400       1410       1420       1430       1440 
APPLVQITGP YFPTLPGLVL QVLEPPQHGA LQKEDHSQDG SLSTFSWREV EEQLIRYVHD 

      1450       1460       1470       1480       1490       1500 
GSETQTDAFV LLANASEMDR QSQPVAFTIT ILPVNDQPPV LTTNTGLQIW EGAIVPIPPE 

      1510       1520       1530       1540       1550       1560 
ALRGTDNDSG PEDLVYTIEQ PSNGRIALRV APDTEVHRFT QAQLDSGLVL FSHRGALEGG 

      1570       1580       1590       1600       1610       1620 
FHFDLSDGAH TSPGHFFRVV AQKQALLSLE GTRKLTVCPE SVQPLSSQSL SASSSTGADP 

      1630       1640       1650       1660       1670       1680 
RHLLYRVVRG PQLGRLLHAQ QGSAEEVLVN FTQAEVNAGN ILYEHEMSSE PFWEAHDTIG 

      1690       1700       1710       1720       1730       1740 
LLLSSPPARD LAATLAVMVS FDAACPQRPS RLWKNKGLWV PEGQRAKITV AALDAANLLA 

      1750       1760       1770       1780       1790       1800 
SVPASQRSRH DVLFQVTQFP TRGQLLVSEE PLHARRPYFL QSELAAGQLV YAHGGGGTQQ 

      1810       1820       1830       1840       1850       1860 
DGFRFRAHLQ GPTGTSVAGP QTSEAFVITV RDVNERPPQP QASIPLRVTR GSRAPVSRAQ 

      1870       1880       1890       1900       1910       1920 
LSVVDPDSAP GEIEYEVQRA PHNGFLSLAG DNTGPVTHFT QADVDAGRLA FVANGSSVAG 

      1930       1940       1950       1960       1970       1980 
VFQLSMSDGA SPPIPMSLAV DVLPSTIEVQ LRAPLEVPQA LGRTSLSRQQ LQVISDREEP 

      1990       2000       2010       2020       2030       2040 
DVAYRLTQGP LYGQLLVGGQ PASAFSQLQV DQGDVVFVFT NFSSSQDHFK VVALARGVNA 

      2050       2060       2070       2080       2090       2100 
SATVNVTVQA LLHVWAGGPW PQGTTLRLDP TVLDASELAN RTGSMPHFRL LAGPRYGRVV 

      2110       2120       2130       2140       2150       2160 
RVSQGRTESR SNQLVEHFTQ RDLEEGQLGL EVGKPEGRST GPAGDRLTLE LWAKGVPPAV 

      2170       2180       2190       2200       2210       2220 
ALLDFATEPY HAAKSYSVAL LSVPEAVRTE TEKPGRSVPT GQPGQAASSP VPTAAKGGFL 

      2230       2240       2250       2260       2270       2280 
GFLEANMFSI IIPVCLILLL LALILPLLFY LRKRNKTGKH DVQVLTAKPR NGLAGDTETF 

      2290       2300       2310       2320 
RKVEPGQAIP LITVPGQGPP PGGQPDPELL QFCRTPNPAL RNGQYWV 

« Hide

Isoform 2 [UniParc].

Checksum: DA679F6CCF894532
Show »

FASTA66170,843
Isoform 3 [UniParc].

Checksum: 52625A76C5070FBB
Show »

FASTA1,694184,393

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS23211.1. [Q8VHY0-1]
RefSeqNP_620570.2. NM_139001.2. [Q8VHY0-1]
UniGeneMm.41329.

3D structure databases

ProteinModelPortalQ8VHY0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8VHY0. 5 interactions.
MINTMINT-1787512.

PTM databases

PhosphoSiteQ8VHY0.

Proteomic databases

PaxDbQ8VHY0.
PRIDEQ8VHY0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000035661; ENSMUSP00000038909; ENSMUSG00000032911. [Q8VHY0-1]
GeneID121021.
KEGGmmu:121021.
UCSCuc009ptl.1. mouse.

Organism-specific databases

CTD1464.
MGIMGI:2153093. Cspg4.
RougeSearch...

Phylogenomic databases

eggNOGNOG261397.
GeneTreeENSGT00550000074429.
HOGENOMHOG000170195.
HOVERGENHBG081360.
InParanoidQ8VHY0.
KOK08115.
OMARPIYRFT.
OrthoDBEOG77DJ56.
TreeFamTF316876.

Gene expression databases

ArrayExpressQ8VHY0.
CleanExMM_CSPG4.
GenevestigatorQ8VHY0.

Family and domain databases

Gene3D2.60.120.200. 2 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR001791. Laminin_G.
[Graphical view]
PfamPF00054. Laminin_G_1. 1 hit.
PF02210. Laminin_G_2. 1 hit.
[Graphical view]
SMARTSM00282. LamG. 2 hits.
[Graphical view]
SUPFAMSSF49899. SSF49899. 2 hits.
PROSITEPS50025. LAM_G_DOMAIN. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio369752.
PROQ8VHY0.
SOURCESearch...

Entry information

Entry nameCSPG4_MOUSE
AccessionPrimary (citable) accession number: Q8VHY0
Secondary accession number(s): G5E892 expand/collapse secondary AC list , Q5DTG1, Q8BPI8, Q8CE79
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: October 3, 2012
Last modified: July 9, 2014
This is version 101 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot