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Q71M36

- CSPG5_MOUSE

UniProt

Q71M36 - CSPG5_MOUSE

Protein

Chondroitin sulfate proteoglycan 5

Gene

Cspg5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    May function as a growth and differentiation factor involved in neuritogenesis. May induce ERBB3 activation.1 Publication

    GO - Biological processi

    1. axon regeneration Source: Ensembl
    2. regulation of growth Source: UniProtKB-KW
    3. regulation of synaptic transmission Source: MGI

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Differentiation, Growth regulation, Neurogenesis

    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 5
    Alternative name(s):
    Acidic leucine-rich EGF-like domain-containing brain protein
    Neuroglycan C
    Gene namesi
    Name:Cspg5
    Synonyms:Caleb, Ngc
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:1352747. Cspg5.

    Subcellular locationi

    Cell membrane By similarity; 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.By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. Golgi apparatus Source: UniProtKB
    3. Golgi-associated vesicle membrane Source: UniProtKB
    4. integral component of membrane Source: UniProtKB-KW
    5. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Golgi apparatus, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Altered synaptic transmission at early developmental stages.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi38 – 381S → A: No effect on chondroitin sulfate attachment. 1 Publication
    Mutagenesisi123 – 1231S → A: No chondroitin sulfate attachment. no effect on transport to the cell surface. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3030Sequence AnalysisAdd
    BLAST
    Chaini31 – 566536Chondroitin sulfate proteoglycan 5PRO_0000042152Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi57 – 571N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi76 – 761O-linked (GalNAc...)Sequence Analysis
    Glycosylationi123 – 1231O-linked (Xyl...) (chondroitin sulfate)2 Publications
    Glycosylationi132 – 1321O-linked (GalNAc...)Sequence Analysis
    Glycosylationi143 – 1431O-linked (GalNAc...)Sequence Analysis
    Glycosylationi144 – 1441O-linked (GalNAc...)Sequence Analysis
    Glycosylationi153 – 1531O-linked (GalNAc...)Sequence Analysis
    Glycosylationi155 – 1551O-linked (GalNAc...)Sequence Analysis
    Glycosylationi156 – 1561O-linked (GalNAc...)Sequence Analysis
    Glycosylationi160 – 1601O-linked (GalNAc...)Sequence Analysis
    Glycosylationi235 – 2351O-linked (GalNAc...)Sequence Analysis
    Glycosylationi355 – 3551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi367 – 3671N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi374 ↔ 387By similarity
    Disulfide bondi381 ↔ 397By similarity
    Disulfide bondi399 ↔ 412By similarity

    Post-translational modificationi

    N-glycosylated.By similarity
    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.2 Publications
    Phosphorylated; in intracellular and extracellular parts.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Proteoglycan

    Proteomic databases

    PaxDbiQ71M36.
    PRIDEiQ71M36.

    PTM databases

    PhosphoSiteiQ71M36.

    Expressioni

    Tissue specificityi

    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).3 Publications

    Developmental stagei

    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).1 Publication

    Gene expression databases

    BgeeiQ71M36.
    CleanExiMM_CSPG5.
    GenevestigatoriQ71M36.

    Interactioni

    Subunit structurei

    Binds TNR and probably TNC By similarity. Interacts with ERBB3 and GOPC.By similarity1 Publication

    Protein-protein interaction databases

    IntActiQ71M36. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ71M36.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini31 – 423393ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini445 – 566122CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei424 – 44421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini371 – 41343EGF-likeAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni265 – 30137Interaction with TNC and TNRAdd
    BLAST
    Regioni442 – 46019Interaction with GOPCBy similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 1 EGF-like domain.Curated

    Keywords - Domaini

    EGF-like domain, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG39505.
    GeneTreeiENSGT00440000034270.
    HOGENOMiHOG000112020.
    HOVERGENiHBG081361.
    InParanoidiQ71M36.
    KOiK08116.
    OMAiLEVNCLQ.
    OrthoDBiEOG7VX8WW.
    TreeFamiTF338636.

    Family and domain databases

    InterProiIPR010555. Chon_Sulph_att.
    IPR000742. EG-like_dom.
    IPR009505. Neural_ProG_Cyt.
    [Graphical view]
    PfamiPF06566. Chon_Sulph_att. 1 hit.
    PF06567. Neural_ProG_Cyt. 1 hit.
    [Graphical view]
    SMARTiSM00181. EGF. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q71M36-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MGRAGGGGPD WGPPPVLLLL GVTLVLTAGA VPARETGSAI EAEELVRSSL    50
    AWESRANDTR EEAGLPAAGE DETSWTERGS EMAAVGPGVG PEEALEASAA 100
    VTGTAWLEAD GPGLGGVTAE AGSGDAQTLP ATLQAPDEAL GSSTMPPAIP 150
    EATETSGPPS PAVHDKPSVG PELPKEIPLE VRLNLGGSTP EPTFPLQGTL 200
    ETQPASDIID IDYFEGLDSE GRGADMGSFP GSPGTSENHP DTEGETPSWS 250
    LLDLYDDFTP FDESDFYPTT SFYDDLEEEE EEEEDKDTVG GGDLEDENDL 300
    LLPSQKPGVG PGTGQPTNRW HAVPPQHTLG MVPGSSISLR PRPGDPGKDL 350
    ASGENGTECR VGFVRHNGSC RSVCDLFPSY CHNGGQCYLV ENIGAFCRCN 400
    TQDYIWHKGM RCESIITDFQ VMCVAVGSAA LVLLLLFMMT VFFAKKLYLL 450
    KTENTKLRRT NKFRTPSELH NDNFSLSTIA EGSHPNVRKF CDTPRVSSPH 500
    ARALAHYDNI VCQDDPSAPH KIQDPLKSRL KEEESFNIQN SMSPKLEGGK 550
    GDQDDLGVNC LQNNLT 566
    Length:566
    Mass (Da):60,406
    Last modified:July 27, 2011 - v2
    Checksum:i8AB75BA1ACB11BDE
    GO
    Isoform 2 (identifier: Q71M36-2) [UniParc]FASTAAdd to Basket

    Also known as: NGC-I

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

    Note: Major isoform.

    Show »
    Length:539
    Mass (Da):57,339
    Checksum:i81B105D7803930A3
    GO
    Isoform 3 (identifier: Q71M36-3) [UniParc]FASTAAdd to Basket

    Also known as: NGC-II

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

    Show »
    Length:458
    Mass (Da):49,027
    Checksum:i87CE103CCD23205E
    GO
    Isoform 4 (identifier: Q71M36-4) [UniParc]FASTAAdd to Basket

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

    Note: No experimental confirmation available.

    Show »
    Length:569
    Mass (Da):60,857
    Checksum:i62DADBBC033BF0E0
    GO

    Sequence cautioni

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti317 – 3171T → N in AAF23362. (PubMed:10617623)Curated
    Sequence conflicti317 – 3171T → N in AAQ04777. (PubMed:10617623)Curated
    Sequence conflicti317 – 3171T → N in AAQ04778. (PubMed:10617623)Curated
    Sequence conflicti317 – 3171T → N in AAQ04779. (PubMed:10617623)Curated
    Sequence conflicti318 – 3181N → H in AAH55736. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8181Missing in isoform 3. 1 PublicationVSP_015762Add
    BLAST
    Alternative sequencei487 – 51327Missing in isoform 2 and isoform 3. 2 PublicationsVSP_015763Add
    BLAST
    Alternative sequencei514 – 56653DDPSA…QNNLT → VTYLPHISPFACLCPCLPLP PCPLALSQSRQSPNSFEDQL RATQWCRERCIDSLTV in isoform 4. 1 PublicationVSP_015764Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS52936.1. [Q71M36-1]
    RefSeqiNP_001159745.1. NM_001166273.1. [Q71M36-1]
    NP_038912.3. NM_013884.3. [Q71M36-2]
    UniGeneiMm.38496.

    Genome annotation databases

    EnsembliENSMUST00000035058; ENSMUSP00000035058; ENSMUSG00000032482. [Q71M36-1]
    GeneIDi29873.
    KEGGimmu:29873.
    UCSCiuc009rtq.2. mouse. [Q71M36-1]
    uc009rtr.2. mouse. [Q71M36-2]
    uc009rtt.1. mouse. [Q71M36-3]
    uc009rtu.1. mouse. [Q71M36-4]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS52936.1. [Q71M36-1 ]
    RefSeqi NP_001159745.1. NM_001166273.1. [Q71M36-1 ]
    NP_038912.3. NM_013884.3. [Q71M36-2 ]
    UniGenei Mm.38496.

    3D structure databases

    ProteinModelPortali Q71M36.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q71M36. 1 interaction.

    PTM databases

    PhosphoSitei Q71M36.

    Proteomic databases

    PaxDbi Q71M36.
    PRIDEi Q71M36.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000035058 ; ENSMUSP00000035058 ; ENSMUSG00000032482 . [Q71M36-1 ]
    GeneIDi 29873.
    KEGGi mmu:29873.
    UCSCi uc009rtq.2. mouse. [Q71M36-1 ]
    uc009rtr.2. mouse. [Q71M36-2 ]
    uc009rtt.1. mouse. [Q71M36-3 ]
    uc009rtu.1. mouse. [Q71M36-4 ]

    Organism-specific databases

    CTDi 10675.
    MGIi MGI:1352747. Cspg5.

    Phylogenomic databases

    eggNOGi NOG39505.
    GeneTreei ENSGT00440000034270.
    HOGENOMi HOG000112020.
    HOVERGENi HBG081361.
    InParanoidi Q71M36.
    KOi K08116.
    OMAi LEVNCLQ.
    OrthoDBi EOG7VX8WW.
    TreeFami TF338636.

    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

    ChiTaRSi CSPG5. mouse.
    NextBioi 307106.
    PROi Q71M36.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q71M36.
    CleanExi MM_CSPG5.
    Genevestigatori Q71M36.

    Family and domain databases

    InterProi IPR010555. Chon_Sulph_att.
    IPR000742. EG-like_dom.
    IPR009505. Neural_ProG_Cyt.
    [Graphical view ]
    Pfami PF06566. Chon_Sulph_att. 1 hit.
    PF06567. Neural_ProG_Cyt. 1 hit.
    [Graphical view ]
    SMARTi SM00181. EGF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.

    Entry informationi

    Entry nameiCSPG5_MOUSE
    AccessioniPrimary (citable) accession number: Q71M36
    Secondary accession number(s): E9QN54
    , Q71M37, Q7TNT8, Q8BPJ5, Q9QY32
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2005
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 92 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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.

    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