Q71M36 (CSPG5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chondroitin sulfate proteoglycan 5

Alternative name(s):
Acidic leucine-rich EGF-like domain-containing brain protein
Neuroglycan C

Gene names

Name:	Cspg5
Synonyms:	Caleb, Ngc

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	566 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May function as a growth and differentiation factor involved in neuritogenesis. May induce ERBB3 activation. Ref.9
Subunit structure	Binds TNR and probably TNC By similarity. Interacts with ERBB3 and GOPC. Ref.6
Subcellular location	Cell membrane; Single-pass type I membrane protein By similarity. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Note: Partially enriched in lipid rafts By similarity. In neurons, localizes to synaptic junctions. Also detected in the endoplasmic reticulum and the Golgi. Ref.1 Ref.7 Ref.8
Tissue specificity	Expressed in olfactory bulb, hippocampus, brain stem, spinal cord, cerebrum and cerebellum. Expressed by Purkinje cells in the cerebellum (at protein level). Expressed in immature and mature cerebellum (isoform 1, isoform 2 and isoform 3). Ref.1 Ref.5 Ref.8
Developmental stage	The proteoglycan form decreases from birth to adulthood in the cerebellum concomitant with non-proteoglycan form increase. In the cerebrum the maximum of expression of the proteoglycan is detected 15 days after birth and then decreases gradually to reach half-level at adulthood (at protein level). Ref.1
Post-translational modification	N-glycosylated By similarity. Ref.1 Ref.8 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 tissues maturation. In the cerebellum the 2 forms coexist while in the cerebrum the proteoglycan form is predominant. Ref.1 Ref.8 Phosphorylated; in intracellular and extracellular parts By similarity.
Disruption phenotype	Altered synaptic transmission at early developmental stages. Ref.9
Miscellaneous	Different forms of various molecular weight have been observed. Such forms are possibly due to different levels of glycosylation, phosphorylation and/or protein cleavage.
Sequence similarities	Contains 1 EGF-like domain.
Sequence caution	The sequence AAQ04778.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAC35578.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Differentiation Growth regulation Neurogenesis
Cellular component	Cell membrane Endoplasmic reticulum Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing
Domain	EGF-like domain Signal Transmembrane Transmembrane helix
Molecular function	Developmental protein
PTM	Disulfide bond Glycoprotein Phosphoprotein Proteoglycan
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	axon regeneration Inferred from electronic annotation. Source: Compara regulation of growth Inferred from electronic annotation. Source: UniProtKB-KW regulation of synaptic transmission Inferred from mutant phenotype Ref.9. Source: MGI
Cellular_component	Golgi-associated vesicle membrane Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q71M36-1)

Also known as: NGC-III;

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: Q71M36-2)

Also known as: NGC-I;

The sequence of this isoform differs from the canonical sequence as follows:
     487-513: Missing.

Note: Major isoform.

Isoform 3 (identifier: Q71M36-3)

Also known as: NGC-II;

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: Missing.
     487-513: Missing.

Isoform 4 (identifier: Q71M36-4)

The sequence of this isoform differs from the canonical sequence as follows:
     514-566: DDPSAPHKIQ...GVNCLQNNLT → VTYLPHISPF...RERCIDSLTV

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 30	30	Potential
	Chain	31 – 566	536	Chondroitin sulfate proteoglycan 5		PRO_0000042152
Regions
	Topological domain	31 – 423	393	Extracellular Potential
	Transmembrane	424 – 444	21	Helical; Potential
	Topological domain	445 – 566	122	Cytoplasmic Potential
	Domain	371 – 413	43	EGF-like
	Region	265 – 301	37	Interaction with TNC and TNR
	Region	442 – 460	19	Interaction with GOPC By similarity
Amino acid modifications
	Glycosylation	57	1	N-linked (GlcNAc...) Potential
	Glycosylation	76	1	O-linked (GalNAc...) Potential
	Glycosylation	123	1	O-linked (Xyl...) (chondroitin sulfate) Ref.8
	Glycosylation	132	1	O-linked (GalNAc...) Potential
	Glycosylation	143	1	O-linked (GalNAc...) Potential
	Glycosylation	144	1	O-linked (GalNAc...) Potential
	Glycosylation	153	1	O-linked (GalNAc...) Potential
	Glycosylation	155	1	O-linked (GalNAc...) Potential
	Glycosylation	156	1	O-linked (GalNAc...) Potential
	Glycosylation	160	1	O-linked (GalNAc...) Potential
	Glycosylation	235	1	O-linked (GalNAc...) Potential
	Glycosylation	355	1	N-linked (GlcNAc...) Potential
	Glycosylation	367	1	N-linked (GlcNAc...) Potential
	Disulfide bond	374 ↔ 387		By similarity
	Disulfide bond	381 ↔ 397		By similarity
	Disulfide bond	399 ↔ 412		By similarity
Natural variations
	Alternative sequence	1 – 81	81	Missing in isoform 3.		VSP_015762
	Alternative sequence	487 – 513	27	Missing in isoform 2 and isoform 3.		VSP_015763
	Alternative sequence	514 – 566	53	DDPSA…QNNLT → VTYLPHISPFACLCPCLPLP PCPLALSQSRQSPNSFEDQL RATQWCRERCIDSLTV in isoform 4.		VSP_015764
Experimental info
	Mutagenesis	38	1	S → A: No effect on chondroitin sulfate attachment. Ref.8
	Mutagenesis	123	1	S → A: No chondroitin sulfate attachment. no effect on transport to the cell surface. Ref.8
	Sequence conflict	317	1	T → N in AAF23362. Ref.1
	Sequence conflict	317	1	T → N in AAQ04777. Ref.1
	Sequence conflict	317	1	T → N in AAQ04778. Ref.1
	Sequence conflict	317	1	T → N in AAQ04779. Ref.1
	Sequence conflict	318	1	N → H in AAH55736. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (NGC-III) [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 8AB75BA1ACB11BDE	FASTA	566	60,406
	10 20 30 40 50 60 MGRAGGGGPD WGPPPVLLLL GVTLVLTAGA VPARETGSAI EAEELVRSSL AWESRANDTR 70 80 90 100 110 120 EEAGLPAAGE DETSWTERGS EMAAVGPGVG PEEALEASAA VTGTAWLEAD GPGLGGVTAE 130 140 150 160 170 180 AGSGDAQTLP ATLQAPDEAL GSSTMPPAIP EATETSGPPS PAVHDKPSVG PELPKEIPLE 190 200 210 220 230 240 VRLNLGGSTP EPTFPLQGTL ETQPASDIID IDYFEGLDSE GRGADMGSFP GSPGTSENHP 250 260 270 280 290 300 DTEGETPSWS LLDLYDDFTP FDESDFYPTT SFYDDLEEEE EEEEDKDTVG GGDLEDENDL 310 320 330 340 350 360 LLPSQKPGVG PGTGQPTNRW HAVPPQHTLG MVPGSSISLR PRPGDPGKDL ASGENGTECR 370 380 390 400 410 420 VGFVRHNGSC RSVCDLFPSY CHNGGQCYLV ENIGAFCRCN TQDYIWHKGM RCESIITDFQ 430 440 450 460 470 480 VMCVAVGSAA LVLLLLFMMT VFFAKKLYLL KTENTKLRRT NKFRTPSELH NDNFSLSTIA 490 500 510 520 530 540 EGSHPNVRKF CDTPRVSSPH ARALAHYDNI VCQDDPSAPH KIQDPLKSRL KEEESFNIQN 550 560 SMSPKLEGGK GDQDDLGVNC LQNNLT
	Isoform 2 (NGC-I) [UniParc]. Checksum: 81B105D7803930A3	FASTA	539	57,339
	10 20 30 40 50 60 MGRAGGGGPD WGPPPVLLLL GVTLVLTAGA VPARETGSAI EAEELVRSSL AWESRANDTR 70 80 90 100 110 120 EEAGLPAAGE DETSWTERGS EMAAVGPGVG PEEALEASAA VTGTAWLEAD GPGLGGVTAE 130 140 150 160 170 180 AGSGDAQTLP ATLQAPDEAL GSSTMPPAIP EATETSGPPS PAVHDKPSVG PELPKEIPLE 190 200 210 220 230 240 VRLNLGGSTP EPTFPLQGTL ETQPASDIID IDYFEGLDSE GRGADMGSFP GSPGTSENHP 250 260 270 280 290 300 DTEGETPSWS LLDLYDDFTP FDESDFYPTT SFYDDLEEEE EEEEDKDTVG GGDLEDENDL 310 320 330 340 350 360 LLPSQKPGVG PGTGQPTNRW HAVPPQHTLG MVPGSSISLR PRPGDPGKDL ASGENGTECR 370 380 390 400 410 420 VGFVRHNGSC RSVCDLFPSY CHNGGQCYLV ENIGAFCRCN TQDYIWHKGM RCESIITDFQ 430 440 450 460 470 480 VMCVAVGSAA LVLLLLFMMT VFFAKKLYLL KTENTKLRRT NKFRTPSELH NDNFSLSTIA 490 500 510 520 530 EGSHPNDDPS APHKIQDPLK SRLKEEESFN IQNSMSPKLE GGKGDQDDLG VNCLQNNLT
	Isoform 3 (NGC-II) [UniParc]. Checksum: 87CE103CCD23205E	FASTA	458	49,027
	10 20 30 40 50 60 MAAVGPGVGP EEALEASAAV TGTAWLEADG PGLGGVTAEA GSGDAQTLPA TLQAPDEALG 70 80 90 100 110 120 SSTMPPAIPE ATETSGPPSP AVHDKPSVGP ELPKEIPLEV RLNLGGSTPE PTFPLQGTLE 130 140 150 160 170 180 TQPASDIIDI DYFEGLDSEG RGADMGSFPG SPGTSENHPD TEGETPSWSL LDLYDDFTPF 190 200 210 220 230 240 DESDFYPTTS FYDDLEEEEE EEEDKDTVGG GDLEDENDLL LPSQKPGVGP GTGQPTNRWH 250 260 270 280 290 300 AVPPQHTLGM VPGSSISLRP RPGDPGKDLA SGENGTECRV GFVRHNGSCR SVCDLFPSYC 310 320 330 340 350 360 HNGGQCYLVE NIGAFCRCNT QDYIWHKGMR CESIITDFQV MCVAVGSAAL VLLLLFMMTV 370 380 390 400 410 420 FFAKKLYLLK TENTKLRRTN KFRTPSELHN DNFSLSTIAE GSHPNDDPSA PHKIQDPLKS 430 440 450 RLKEEESFNI QNSMSPKLEG GKGDQDDLGV NCLQNNLT
	Isoform 4 [UniParc]. Checksum: 62DADBBC033BF0E0	FASTA	569	60,857
	10 20 30 40 50 60 MGRAGGGGPD WGPPPVLLLL GVTLVLTAGA VPARETGSAI EAEELVRSSL AWESRANDTR 70 80 90 100 110 120 EEAGLPAAGE DETSWTERGS EMAAVGPGVG PEEALEASAA VTGTAWLEAD GPGLGGVTAE 130 140 150 160 170 180 AGSGDAQTLP ATLQAPDEAL GSSTMPPAIP EATETSGPPS PAVHDKPSVG PELPKEIPLE 190 200 210 220 230 240 VRLNLGGSTP EPTFPLQGTL ETQPASDIID IDYFEGLDSE GRGADMGSFP GSPGTSENHP 250 260 270 280 290 300 DTEGETPSWS LLDLYDDFTP FDESDFYPTT SFYDDLEEEE EEEEDKDTVG GGDLEDENDL 310 320 330 340 350 360 LLPSQKPGVG PGTGQPTNRW HAVPPQHTLG MVPGSSISLR PRPGDPGKDL ASGENGTECR 370 380 390 400 410 420 VGFVRHNGSC RSVCDLFPSY CHNGGQCYLV ENIGAFCRCN TQDYIWHKGM RCESIITDFQ 430 440 450 460 470 480 VMCVAVGSAA LVLLLLFMMT VFFAKKLYLL KTENTKLRRT NKFRTPSELH NDNFSLSTIA 490 500 510 520 530 540 EGSHPNVRKF CDTPRVSSPH ARALAHYDNI VCQVTYLPHI SPFACLCPCL PLPPCPLALS 550 560 QSRQSPNSFE DQLRATQWCR ERCIDSLTV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genomic organization and expression pattern of mouse neuroglycan C in the cerebellar development." Aono S., Keino H., Ono T., Yasuda Y., Tokita Y., Matsui F., Taniguchi M., Sonta S., Oohira A. J. Biol. Chem. 275:337-342(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY, GLYCOSYLATION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE. Strain: C57BL/6. Tissue: Brain.
[2]	"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. , 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.
[3]	"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 2). Strain: C57BL/6. Tissue: Brain.
[4]	"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] OF 202-566 (ISOFORM 4). Strain: C57BL/6J. Tissue: Eye.
[5]	"Cloning and chromosomal mapping of the human gene of neuroglycan C (NGC), a neural transmembrane chondroitin sulfate proteoglycan with an EGF module." Yasuda Y., Tokita Y., Aono S., Matsui F., Ono T., Sonta S., Watanabe E., Nakanishi Y., Oohira A. Neurosci. Res. 32:313-322(1998) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[6]	"CALEB binds via its acidic stretch to the fibrinogen-like domain of tenascin-C or tenascin-R and its expression is dynamically regulated after optic nerve lesion." Schumacher S., Jung M., Noerenberg U., Dorner A., Chiquet-Ehrismann R., Stuermer C.A.O., Rathjen F.G. J. Biol. Chem. 276:7337-7345(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TNR.
[7]	"CALEB/NGC interacts with the Golgi-associated protein PIST." Hassel B., Schreff M., Stuebe E.-M., Blaich U., Schumacher S. J. Biol. Chem. 278:40136-40143(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[8]	"Glycosylation site for chondroitin sulfate on the neural part-time proteoglycan, neuroglycan C." Aono S., Tokita Y., Shuo T., Yamauchi S., Matsui F., Nakanishi K., Hirano K., Sano M., Oohira A. J. Biol. Chem. 279:46536-46541(2004) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, MUTAGENESIS OF SER-38 AND SER-123, GLYCOSYLATION AT SER-123, SUBCELLULAR LOCATION.
[9]	"Impaired synapse function during postnatal development in the absence of CALEB, an EGF-like protein processed by neuronal activity." Juettner R., More M.I., Das D., Babich A., Meier J., Henning M., Erdmann B., Mueller E.-C., Otto A., Grantyn R., Rathjen F.G. Neuron 46:233-245(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF133700 mRNA. Translation: AAF23362.1. AF461090 mRNA. Translation: AAQ04777.1. AF461091 mRNA. Translation: AAQ04778.1. Different initiation. AF461092 mRNA. Translation: AAQ04779.1. AC159372 Genomic DNA. No translation available. AC160104 Genomic DNA. No translation available. BC055736 mRNA. Translation: AAH55736.1. AK053891 mRNA. Translation: BAC35578.1. Different initiation.
IPI	IPI00454159. IPI00652233. IPI00653847. IPI01008121.
RefSeq	NP_001159745.1. NM_001166273.1. NP_038912.3. NM_013884.3.
UniGene	Mm.38496.
3D structure databases
ProteinModelPortal	Q71M36.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q71M36. 1 interaction.
PTM databases
PhosphoSite	Q71M36.
Proteomic databases
PaxDb	Q71M36.
PRIDE	Q71M36.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000035058; ENSMUSP00000035058; ENSMUSG00000032482.
GeneID	29873.
KEGG	mmu:29873.
UCSC	uc009rtq.2. mouse. uc009rts.2. mouse. uc009rtt.1. mouse. uc009rtu.1. mouse.
Organism-specific databases
CTD	10675.
MGI	MGI:1352747. Cspg5.
Phylogenomic databases
eggNOG	NOG39505.
GeneTree	ENSGT00440000034270.
HOGENOM	HOG000112020.
HOVERGEN	HBG081361.
InParanoid	Q71M36.
KO	K08116.
OMA	LEVNCLQ.
OrthoDB	EOG4XWFXN.
Gene expression databases
Bgee	Q71M36.
CleanEx	MM_CSPG5.
Genevestigator	Q71M36.
GermOnline	ENSMUSG00000032482. Mus musculus.
Family and domain databases
InterPro	IPR010555. Chon_Sulph_att. IPR000742. EG-like_dom. IPR009505. Neural_ProG_Cyt. [Graphical view]
Pfam	PF06566. Chon_Sulph_att. 1 hit. PF06567. Neural_ProG_Cyt. 1 hit. [Graphical view]
SMART	SM00181. EGF. 1 hit. [Graphical view]
PROSITE	PS00022. EGF_1. False negative. PS01186. EGF_2. False negative. PS50026. EGF_3. False negative. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CSPG5. mouse.
NextBio	307106.
SOURCE	Search...

Entry information

Entry name

CSPG5_MOUSE

Accession

Primary (citable) accession number: Q71M36
Secondary accession number(s): E9QN54 , Q71M37, Q7TNT8, Q8BPJ5, Q9QY32

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2005
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program