Cspg5
entrez
29873
canonical
uniprot
Q71M36
canonical
ensembl
ENSMUSG00000032482
resolver
ensp
ENSMUSP00000035058
resolver
ensp
ENSMUSP00000143164
resolver
genesymbol
Cspg5
resolver
genesymbol_syn
Caleb
resolver
genesymbol_syn
Ngc
resolver
uniprot
E9QN54
resolver
uniprot
Q71M37
resolver
uniprot
Q7TNT8
resolver
uniprot
Q8BPJ5
resolver
uniprot
Q9QY32
resolver
uniprot_entry
CSPG5_MOUSE
resolver
uniprot_sec
E9QN54
resolver
uniprot_sec
Q71M37
resolver
uniprot_sec
Q7TNT8
resolver
uniprot_sec
Q8BPJ5
resolver
uniprot_sec
Q9QY32
resolver
amino_acid_sequence
MGRAGGGGPDWGPPPVLLLLGVTLVLTAGAVPARETGSAIEAEELVRSSLAWESRANDTREEAGLPAAGEDETSWTERGSEMAAVGPGVGPEEALEASAAVTGTAWLEADGPGLGGVTAEAGSGDAQTLPATLQAPDEALGSSTMPPAIPEATETSGPPSPAVHDKPSVGPELPKEIPLEVRLNLGGSTPEPTFPLQGTLETQPASDIIDIDYFEGLDSEGRGADMGSFPGSPGTSENHPDTEGETPSWSLLDLYDDFTPFDESDFYPTTSFYDDLEEEEEEEEDKDTVGGGDLEDENDLLLPSQKPGVGPGTGQPTNRWHAVPPQHTLGMVPGSSISLRPRPGDPGKDLASGENGTECRVGFVRHNGSCRSVCDLFPSYCHNGGQCYLVENIGAFCRCNTQDYIWHKGMRCESIITDFQVMCVAVGSAALVLLLLFMMTVFFAKKLYLLKTENTKLRRTNKFRTPSELHNDNFSLSTIAEGSHPNVRKFCDTPRVSSPHARALAHYDNIVCQDDPSAPHKIQDPLKSRLKEEESFNIQNSMSPKLEGGKGDQDDLGVNCLQNNLT
uniprot
proteins
function
FUNCTION: May function as a growth and differentiation factor involved in neuritogenesis. May induce ERBB3 activation. {ECO:0000269|PubMed:15848802}.
uniprot
proteins
mass_dalton
60406
uniprot
proteins
mutagenesis
MUTAGEN 38; /note="S->A: No effect on chondroitin sulfate attachment."; /evidence="ECO:0000269|PubMed:15331613"; MUTAGEN 123; /note="S->A: No chondroitin sulfate attachment. no effect on transport to the cell surface."; /evidence="ECO:0000269|PubMed:15331613
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000250}.; PTM: O-glycosylated; contains chondroitin sulfate glycans. Part-time proteoglycan, expressed in part as a proteoglycan exhibiting chondroitin sulfate glycans and in part as a non-proteoglycan form. The relative amount of both forms depends on tissues and tissue maturation. In the cerebellum the 2 forms coexist while in the cerebrum the proteoglycan form is predominant. {ECO:0000269|PubMed:10617623, ECO:0000269|PubMed:15331613}.; PTM: Phosphorylated; in intracellular and extracellular parts. {ECO:0000250}.
uniprot
proteins
pubmed
10617623
uniprot
proteins
pubmed
11069908
uniprot
proteins
pubmed
12885772
uniprot
proteins
pubmed
15331613
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15848802
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
9950058
uniprot
proteins
sequence_length
566
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10617623}; Single-pass type I membrane protein {ECO:0000305}. Synaptic cell membrane {ECO:0000269|PubMed:21183079}; Single-pass type I membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:10617623}; Single-pass type I membrane protein {ECO:0000305}. Golgi apparatus membrane {ECO:0000269|PubMed:10617623, ECO:0000269|PubMed:12885772}; Single-pass type I membrane protein {ECO:0000305}. Cell surface {ECO:0000269|PubMed:15331613}. Secreted {ECO:0000250|UniProtKB:O95196}. Note=Partially enriched in lipid rafts (By similarity). Also detected in the endoplasmic reticulum and the Golgi (PubMed:10617623). {ECO:0000250|UniProtKB:Q9ERQ6, ECO:0000269|PubMed:10617623}.
uniprot
proteins
transmembrane_region
TRANSMEM 424..444; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins