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Q71M36

- CSPG5_MOUSE

UniProt

Q71M36 - CSPG5_MOUSE

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Protein
Chondroitin sulfate proteoglycan 5
Gene
Cspg5, Caleb, Ngc
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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; 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.3 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 423393Extracellular Reviewed prediction
Add
BLAST
Transmembranei424 – 44421Helical; Reviewed prediction
Add
BLAST
Topological domaini445 – 566122Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

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 – 3030 Reviewed prediction
Add
BLAST
Chaini31 – 566536Chondroitin sulfate proteoglycan 5
PRO_0000042152Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi57 – 571N-linked (GlcNAc...) Reviewed prediction
Glycosylationi76 – 761O-linked (GalNAc...) Reviewed prediction
Glycosylationi123 – 1231O-linked (Xyl...) (chondroitin sulfate)1 Publication
Glycosylationi132 – 1321O-linked (GalNAc...) Reviewed prediction
Glycosylationi143 – 1431O-linked (GalNAc...) Reviewed prediction
Glycosylationi144 – 1441O-linked (GalNAc...) Reviewed prediction
Glycosylationi153 – 1531O-linked (GalNAc...) Reviewed prediction
Glycosylationi155 – 1551O-linked (GalNAc...) Reviewed prediction
Glycosylationi156 – 1561O-linked (GalNAc...) Reviewed prediction
Glycosylationi160 – 1601O-linked (GalNAc...) Reviewed prediction
Glycosylationi235 – 2351O-linked (GalNAc...) Reviewed prediction
Glycosylationi355 – 3551N-linked (GlcNAc...) Reviewed prediction
Glycosylationi367 – 3671N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi374 ↔ 387 By similarity
Disulfide bondi381 ↔ 397 By similarity
Disulfide bondi399 ↔ 412 By similarity

Post-translational modificationi

N-glycosylated By similarity.2 Publications
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.1 Publication

Protein-protein interaction databases

IntActiQ71M36. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ71M36.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni265 – 30137Interaction with TNC and TNR
Add
BLAST
Regioni442 – 46019Interaction with GOPC By similarity
Add
BLAST

Sequence similaritiesi

Contains 1 EGF-like domain.

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8181Missing in isoform 3.
VSP_015762Add
BLAST
Alternative sequencei487 – 51327Missing in isoform 2 and isoform 3.
VSP_015763Add
BLAST
Alternative sequencei514 – 56653DDPSA…QNNLT → VTYLPHISPFACLCPCLPLP PCPLALSQSRQSPNSFEDQL RATQWCRERCIDSLTV in isoform 4.
VSP_015764Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti317 – 3171T → N in AAF23362. 1 Publication
Sequence conflicti317 – 3171T → N in AAQ04777. 1 Publication
Sequence conflicti317 – 3171T → N in AAQ04778. 1 Publication
Sequence conflicti317 – 3171T → N in AAQ04779. 1 Publication
Sequence conflicti318 – 3181N → H in AAH55736. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 91 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

Similar proteinsi