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P70232 (CHL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. 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:
Neural cell adhesion molecule L1-like protein
Alternative name(s):
Cell adhesion molecule with homology to L1CAM
Chl1-like protein
Close homolog of L1
Gene names
Name:Chl1
Synonyms:Call
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1209 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Extracellular matrix and cell adhesion protein that plays a role in nervous system development and in synaptic plasticity. Both soluble and membranous forms promote neurite outgrowth of cerebellar and hippocampal neurons and suppress neuronal cell death. Plays a role in neuronal positioning of pyramidal neurons as well as in regulation of both the number of interneurons and the efficacy of GABAergic synapses. May play a role in regulating cell migration in nerve regeneration and cortical development. Potentiates integrin-dependent cell migration towards extracellular matrix proteins. Recruits ANK3 to the plasma membrane. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14

Subunit structure

May interact with L1CAM. May interact with ITGB1/ITGA1 heterodimer and ITGB1/ITGA2 heterodimer as well as with ANK3.

Subcellular location

Cell membrane; Single-pass type I membrane protein. Note: Soluble forms produced by cleavage/shedding also exist.

Processed neural cell adhesion molecule L1-like protein: Secretedextracellular spaceextracellular matrix.

Tissue specificity

Expressed in the brain, in the cerebellum and in the spinal cord. Detected in the retina and the optic nerve. Expressed in neurons and glial cells in the central nervous system and by Schwann cells in the peripheral nervous system. Ref.1 Ref.7 Ref.13

Developmental stage

Not detectable in the forebrain at E11, weakly detectable at E13 with highest detection at E18 to postnatal day 7. Down-regulated at postnatal day 15 and further reduced in four-week-old animals. Ref.1 Ref.7 Ref.13

Domain

The FIG[AQ]Y motif seems to be an ankyrin recruitment region.

The DGEA motif seems to be a recognition site for integrin.

Post-translational modification

Cleavage by metalloprotease ADAM8 in the extracellular part generates 2 soluble forms (125 kDa and 165 kDa) in vitro and is inhibited by metalloprotease inhibitors. In brain extracts, these two soluble forms are also present and are dramatically reduced in mice lacking ADAM8.

N-glycosylated. Contains N-linked oligosaccharides with a sulfated carbohydrate structure type HNK-1 (SO4-3-GlcUABeta1,3GalBeta1,4GlcNAc). Ref.1

O-glycosylated. Ref.1

Disruption phenotype

Mice exhibit misguided axonal projections and aberrant axonal connectivity. They show alterations of hippocampal fiber organization and olfactory axon projections. Their exploratory behavior in novel environments is altered suggesting deficits in information processing and in attention. They also display signs of decreased stress and are more sociable and less aggressive. Heterozygous mice exhibit half levels of CHL1 expression in the hippocampus compared to their wild-type littermates, reflecting a gene dosage effect. Ref.6 Ref.9 Ref.10 Ref.14

Sequence similarities

Belongs to the immunoglobulin superfamily. L1/neurofascin/NgCAM family.

Contains 4 fibronectin type-III domains.

Contains 6 Ig-like C2-type (immunoglobulin-like) domains.

Sequence caution

The sequence BAC30699.1 differs from that shown. Reason: Frameshift at positions 616, 624, 631, 632, 642 and 645.

Ontologies

Keywords
   Biological processCell adhesion
Differentiation
Neurogenesis
   Cellular componentCell membrane
Extracellular matrix
Membrane
Secreted
   Coding sequence diversityAlternative splicing
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadult locomotory behavior

Inferred from mutant phenotype Ref.9. Source: MGI

axon guidance

Inferred from mutant phenotype Ref.6. Source: MGI

axon regeneration

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cognition

Inferred from mutant phenotype Ref.9. Source: MGI

exploration behavior

Inferred from mutant phenotype Ref.6. Source: MGI

negative regulation of neuron apoptotic process

Inferred from direct assay Ref.12. Source: BHF-UCL

neuron migration

Inferred from mutant phenotype Ref.13. Source: MGI

neuron projection development

Inferred from direct assay Ref.7. Source: MGI

   Cellular_componentapical part of cell

Inferred from direct assay Ref.13. Source: MGI

dendrite

Inferred from direct assay Ref.13. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Traceable author statement. Source: Reactome

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotease binding

Inferred from physical interaction Ref.12. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P70232-1)

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: P70232-2)

The sequence of this isoform differs from the canonical sequence as follows:
     227-227: S → LKHASDSSSSTEICSQA
     1016-1070: SKGIRKITEGVNVTQKIHPVEVLVPGAEHIVHLMTKNWGDNDSIFQDVIETRGRE → K
     1138-1209: SDSDEKPLKG...SSTATFPLRA → RKMVLKQKLL...LRYFSSNKHT

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 12091184Neural cell adhesion molecule L1-like protein
PRO_0000247897
Chain26 – ?Processed neural cell adhesion molecule L1-like protein PotentialPRO_0000314778

Regions

Topological domain26 – 10831058Extracellular Potential
Transmembrane1084 – 110421Helical; Potential
Topological domain1105 – 1209105Cytoplasmic Potential
Domain35 – 12490Ig-like C2-type 1
Domain128 – 22396Ig-like C2-type 2
Domain235 – 32894Ig-like C2-type 3
Domain331 – 41787Ig-like C2-type 4
Domain423 – 51088Ig-like C2-type 5
Domain515 – 60793Ig-like C2-type 6
Domain614 – 70996Fibronectin type-III 1
Domain714 – 80794Fibronectin type-III 2
Domain812 – 914103Fibronectin type-III 3
Domain918 – 101598Fibronectin type-III 4
Motif555 – 5584DGEA
Motif1182 – 11865FIG[AQ]Y

Sites

Site753 – 7542Cleavage; by ADAM8
Site1040 – 10412Cleavage; by ADAM8

Amino acid modifications

Glycosylation871N-linked (GlcNAc...) Potential
Glycosylation2251N-linked (GlcNAc...) Potential
Glycosylation2991N-linked (GlcNAc...) Potential
Glycosylation4761N-linked (GlcNAc...) Potential
Glycosylation5621N-linked (GlcNAc...) Potential
Glycosylation5801N-linked (GlcNAc...) Potential
Glycosylation7671N-linked (GlcNAc...) Potential
Glycosylation8221N-linked (GlcNAc...) Potential
Glycosylation9451N-linked (GlcNAc...) Potential
Glycosylation10271N-linked (GlcNAc...) Potential
Disulfide bond57 ↔ 109 By similarity
Disulfide bond153 ↔ 204 By similarity
Disulfide bond262 ↔ 310 By similarity
Disulfide bond352 ↔ 401 By similarity
Disulfide bond445 ↔ 494 By similarity
Disulfide bond536 ↔ 591 By similarity

Natural variations

Alternative sequence2271S → LKHASDSSSSTEICSQA in isoform 2.
VSP_020083
Alternative sequence1016 – 107055SKGIR…TRGRE → K in isoform 2.
VSP_020084
Alternative sequence1138 – 120972SDSDE…FPLRA → RKMVLKQKLLSWSSSRGRTF YSCTKNTLFDGSSVDMKTLQ PLRYFSSNKHT in isoform 2.
VSP_020085

Experimental info

Mutagenesis555 – 5584DGEA → AGEV: Inhibition of migration potentiation. Ref.11
Mutagenesis11861Y → A: Inhibition of migration potentiation. Ref.11
Sequence conflict501D → G in BAC35247. Ref.2
Sequence conflict771D → E in CAC88131. Ref.6
Sequence conflict4251I → V in BAC35247. Ref.2
Sequence conflict6021E → K in CAA63972. Ref.1
Sequence conflict6121P → G in CAA63972. Ref.1

Sequences

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

Last modified October 3, 2012. Version 2.
Checksum: 2C689475920AB84C

FASTA1,209135,074
        10         20         30         40         50         60 
MMELPLCGRG LILSLIFLLL KLSAAEIPLS VQQVPTIVKQ SYVQVAFPFD EYFQIECEAK 

        70         80         90        100        110        120 
GNPEPIFSWT KDDKPFDLSD PRIIAANNSG TFKIPNEGHI SHFQGKYRCF ASNRLGTAVS 

       130        140        150        160        170        180 
EEIEFIVPGV PKFPKEKIEP IDVEEGDSIV LPCNPPKGLP PLHIYWMNIE LEHIEQDERV 

       190        200        210        220        230        240 
YMSQRGDLYF ANVEENDSRN DYCCFAAFPK LRTIVQKMPM KLTVNSSNSI KQRKPKLLLP 

       250        260        270        280        290        300 
PAQMGSLSAK TVLKGDTLLL ECFAEGLPTP HIQWSKPGSE LPEGRATIEV HEKTLKIENI 

       310        320        330        340        350        360 
SYQDRGNYRC TANNLLGKAS HDFHVTVEEP PRWKKKPQSA VYSTGSSGIL LCEAEGEPQP 

       370        380        390        400        410        420 
TIKWRLNGLP IEKHPFPGDF MFPREISFTN LLPNHTGVYQ CEASNIHGTI LANANIDVID 

       430        440        450        460        470        480 
VIPLIKTKNE ENYATVVGYS AFLHCEYFAS PKATVVWEVA DETHPLEGDR YHTHENGTLE 

       490        500        510        520        530        540 
IYRTTEEDAG SYSCWVDNAM GKAVITANLD IRNATKLRVS PKNPRIPKSH VLELYCESQC 

       550        560        570        580        590        600 
DSHLKHSLKL SWSKDGEAFE MNGTEDGRIV IDGAYLTISN ITAEDQGVYS CSAQTSLDST 

       610        620        630        640        650        660 
SEKTQVTVLG VPDPPGNLHL SERQNRSVRL SWEAGDDHNS KISEYIVEFE GNREEPGKWE 

       670        680        690        700        710        720 
ELTRVQGEET DVVLSLAPYV RYQFRVTAVN EVGRSHASLP SDHHETPPAA PDKNPQNIRV 

       730        740        750        760        770        780 
QASQPKEMII KWEPLKSMEQ NGPGLEYKVS WKPQGAPEEW EEEIVTNHTL RVMTPTVYAP 

       790        800        810        820        830        840 
YDVKVQAINQ LGSSPDPQPV TLYSGEDYPS TAPVIQRVDV MNSTLVKVTW SSIPKETVHG 

       850        860        870        880        890        900 
LLRGYQINWW KTKSLLDGRT HPKEVNILRF SGQRNSGMVP SLDPFSEFHL TVLAYNSKGA 

       910        920        930        940        950        960 
GPESEPYIFQ TPEGVPEQPS FLKVIKVDKD TATLSWGLPK KLNGNLTGYL LQYQIINDTY 

       970        980        990       1000       1010       1020 
ELGELNEINV TTPSKSSWHL SNLNSTTKYK FYLRACTSRG CGKPISEEGA TLGEGSKGIR 

      1030       1040       1050       1060       1070       1080 
KITEGVNVTQ KIHPVEVLVP GAEHIVHLMT KNWGDNDSIF QDVIETRGRE YAGLYDDIST 

      1090       1100       1110       1120       1130       1140 
QGWFIGLMCA IALLTLILLT ICFVKRNRGG KYSVKEKEDL HPDPEVQSAK DETFGEYSDS 

      1150       1160       1170       1180       1190       1200 
DEKPLKGSLR SLNRNMQPTE SADSLVEYGE GDQSIFNEDG SFIGAYTGAK EKGSVESNGS 


STATFPLRA 

« Hide

Isoform 2 [UniParc].

Checksum: 6CF6C082529C7A99
Show »

FASTA1,150129,001

References

« Hide 'large scale' references
[1]"Structural features of a close homologue of L1 (CHL1) in the mouse: a new member of the L1 family of neural recognition molecules."
Holm J., Hillenbrand R., Steuber V., Bartsch U., Moos M., Luebbert H., Montag D., Schachner M.
Eur. J. Neurosci. 8:1613-1629(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, GLYCOSYLATION, DEVELOPMENTAL STAGE.
[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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-425 AND 666-1209 (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Aorta, Head and Vein.
[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]"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].
[6]"Misguided axonal projections, neural cell adhesion molecule 180 mRNA upregulation, and altered behavior in mice deficient for the close homolog of L1."
Montag-Sallaz M., Schachner M., Montag D.
Mol. Cell. Biol. 22:7967-7981(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-129, FUNCTION, DISRUPTION PHENOTYPE.
Strain: 129/Sv.
[7]"The close homologue of the neural adhesion molecule L1 (CHL1): patterns of expression and promotion of neurite outgrowth by heterophilic interactions."
Hillenbrand R., Molthagen M., Montag D., Schachner M.
Eur. J. Neurosci. 11:813-826(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DEVELOPMENTAL STAGE, INTERACTION WITH L1CAM, TISSUE SPECIFICITY.
[8]"Prevention of neuronal cell death by neural adhesion molecules L1 and CHL1."
Chen S., Mantei N., Dong L., Schachner M.
J. Neurobiol. 38:428-439(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Mice deficient for the close homologue of the neural adhesion cell L1 (CHL1) display alterations in emotional reactivity and motor coordination."
Pratte M., Rougon G., Schachner M., Jamon M.
Behav. Brain Res. 147:31-39(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[10]"CALL interrupted in a patient with non-specific mental retardation: gene dosage-dependent alteration of murine brain development and behavior."
Frints S.G.M., Marynen P., Hartmann D., Fryns J.-P., Steyaert J., Schachner M., Rolf B., Craessaerts K., Snellinx A., Hollanders K., D'Hooge R., De Deyn P.P., Froyen G.
Hum. Mol. Genet. 12:1463-1474(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[11]"Close homolog of L1 is an enhancer of integrin-mediated cell migration."
Buhusi M., Midkiff B.R., Gates A.M., Richter M., Schachner M., Maness P.F.
J. Biol. Chem. 278:25024-25031(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ANK3; ITGB1/ITGA1 HETERODIMER AND ITGB1/ITGA2 HETERODIMER, MOTIFS, MUTAGENESIS OF 555-ASP--ALA-558 AND TYR-1186.
[12]"Ectodomain shedding of the neural recognition molecule CHL1 by the metalloprotease-disintegrin ADAM8 promotes neurite outgrowth and suppresses neuronal cell death."
Naus S., Richter M., Wildeboer D., Moss M., Schachner M., Bartsch J.W.
J. Biol. Chem. 279:16083-16090(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CLEAVAGE BY ADAM8.
[13]"Close homolog of L1 modulates area-specific neuronal positioning and dendrite orientation in the cerebral cortex."
Demyanenko G.P., Schachner M., Anton E., Schmid R., Feng G., Sanes J., Maness P.F.
Neuron 44:423-437(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[14]"Enhanced perisomatic inhibition and impaired long-term potentiation in the CA1 region of juvenile CHL1-deficient mice."
Nikonenko A.G., Sun M., Lepsveridze E., Apostolova I., Petrova I., Irintchev A., Dityatev A., Schachner M.
Eur. J. Neurosci. 23:1839-1852(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X94310 mRNA. Translation: CAA63972.1.
AK040765 mRNA. Translation: BAC30699.1. Frameshift.
AK048639 mRNA. Translation: BAC33405.1.
AK053039 mRNA. Translation: BAC35247.2.
AC153595 Genomic DNA. No translation available.
AC153598 Genomic DNA. No translation available.
AC161824 Genomic DNA. No translation available.
CH466523 Genomic DNA. Translation: EDK99388.1.
BC131670 mRNA. Translation: AAI31671.1.
BC131671 mRNA. Translation: AAI31672.1.
AJ319655, AJ319656, AJ319657 Genomic DNA. Translation: CAC88131.1.
PIRT42718.
RefSeqNP_031723.2. NM_007697.2.
XP_006505535.1. XM_006505472.1.
UniGeneMm.251288.

3D structure databases

ProteinModelPortalP70232.
SMRP70232. Positions 31-1007.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP70232. 3 interactions.
MINTMINT-4106227.

PTM databases

PhosphoSiteP70232.

Proteomic databases

PaxDbP70232.
PRIDEP70232.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000066905; ENSMUSP00000063933; ENSMUSG00000030077. [P70232-1]
GeneID12661.
KEGGmmu:12661.
UCSCuc009dcj.1. mouse.

Organism-specific databases

CTD10752.
MGIMGI:1098266. Chl1.

Phylogenomic databases

eggNOGNOG256023.
GeneTreeENSGT00690000101868.
HOGENOMHOG000231380.
HOVERGENHBG000144.
KOK06758.
OMAYVRYQFR.
OrthoDBEOG7R56RM.
TreeFamTF351098.

Enzyme and pathway databases

ReactomeREACT_188576. Developmental Biology.

Gene expression databases

CleanExMM_CHL1.
GenevestigatorP70232.

Family and domain databases

Gene3D2.60.40.10. 10 hits.
InterProIPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR026966. Neurofascin/L1/NrCAM_C.
[Graphical view]
PfamPF13882. Bravo_FIGEY. 1 hit.
PF00041. fn3. 4 hits.
PF07679. I-set. 4 hits.
[Graphical view]
SMARTSM00060. FN3. 4 hits.
SM00409. IG. 2 hits.
SM00408. IGc2. 3 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 2 hits.
PROSITEPS50853. FN3. 4 hits.
PS50835. IG_LIKE. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio281890.
PROP70232.
SOURCESearch...

Entry information

Entry nameCHL1_MOUSE
AccessionPrimary (citable) accession number: P70232
Secondary accession number(s): A2RRK1 expand/collapse secondary AC list , Q8BS24, Q8C6W0, Q8C823, Q8VBY7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: October 3, 2012
Last modified: April 16, 2014
This is version 113 of the entry and version 2 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