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Reviewed, UniProtKB/Swiss-Prot P55289 (CAD12_HUMAN)

Last modified June 16, 2009. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Cadherin-12
Alternative name(s):
    Brain cadherin
      Short name=BR-cadherin
    Neural type cadherin 2
      Short name=N-cadherin 2
Gene names
Name: CDH12
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length794 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Cadherins are calcium dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.

Subcellular location

Cell membrane; Single-pass type I membrane protein.

Tissue specificity

Brain.

Sequence similarities

Contains 5 cadherin domains.

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Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
Transmembrane
   LigandCalcium
   PTMCleavage on pair of basic residues
Glycoprotein
Phosphoprotein
Gene Ontology (GO)
   Biological processhomophilic cell adhesion

Non-traceable author statement. Source: UniProtKB

   Cellular componentintegral to membrane

Non-traceable author statement. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Propeptide24 – 5431 Potential
PRO_0000003791
Chain55 – 794740Cadherin-12
PRO_0000003792

Regions

Topological domain55 – 609555Extracellular Potential
Transmembrane610 – 63728 Potential
Topological domain638 – 794157Cytoplasmic Potential
Domain55 – 160106Cadherin 1
Domain161 – 269109Cadherin 2
Domain270 – 384115Cadherin 3
Domain385 – 487103Cadherin 4
Domain488 – 609122Cadherin 5

Amino acid modifications

Modified residue2861Phosphoserine Ref.6
Glycosylation2561N-linked (GlcNAc...) Potential
Glycosylation4561N-linked (GlcNAc...) Potential
Glycosylation5371N-linked (GlcNAc...) Potential
Glycosylation5451N-linked (GlcNAc...) Potential

Natural variations

Natural variant681V → M: dbSNP rs4371716. Ref.2
VAR_048505
Natural variant861E → K: dbSNP rs7236.
VAR_014917
Natural variant2841I → V: dbSNP rs17328673.
VAR_048506
Natural variant4751I → T: dbSNP rs12108814.
VAR_048507

Experimental info

Sequence conflict3491E → D in AAB48539. Ref.2
Sequence conflict4161S → G in AAA35623. Ref.1
Sequence conflict6441D → H in AAA35623. Ref.1
Sequence conflict7331Y → I in AAA35623. Ref.1
Sequence conflict7611A → T in AAB48539. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
P55289-1 [UniParc].

Last modified August 21, 2007. Version 2.
Checksum: 76DF39AB56E7BC2D

FASTA79488,332
        10         20         30         40         50         60 
MLTRNCLSLL LWVLFDGGLL TPLQPQPQQT LATEPRENVI HLPGQRSHFQ RVKRGWVWNQ 

        70         80         90        100        110        120 
FFVLEEYVGS EPQYVGKLHS DLDKGEGTVK YTLSGDGAGT VFTIDETTGD IHAIRSLDRE 

       130        140        150        160        170        180 
EKPFYTLRAQ AVDIETRKPL EPESEFIIKV QDINDNEPKF LDGPYVATVP EMSPVGAYVL 

       190        200        210        220        230        240 
QVKATDADDP TYGNSARVVY SILQGQPYFS IDPKTGVIRT ALPNMDREVK EQYQVLIQAK 

       250        260        270        280        290        300 
DMGGQLGGLA GTTIVNITLT DVNDNPPRFP KSIFHLKVPE SSPIGSAIGR IRAVDPDFGQ 

       310        320        330        340        350        360 
NAEIEYNIVP GDGGNLFDIV TDEDTQEGVI KLKKPLDFET KKAYTFKVEA SNLHLDHRFH 

       370        380        390        400        410        420 
SAGPFKDTAT VKISVLDVDE PPVFSKPLYT MEVYEDTPVG TIIGAVTAQD LDVGSSAVRY 

       430        440        450        460        470        480 
FIDWKSDGDS YFTIDGNEGT IATNELLDRE STAQYNFSII ASKVSNPLLT SKVNILINVL 

       490        500        510        520        530        540 
DVNEFPPEIS VPYETAVCEN AKPGQIIQIV SAADRDLSPA GQQFSFRLSP EAAIKPNFTV 

       550        560        570        580        590        600 
RDFRNNTAGI ETRRNGYSRR QQELYFLPVV IEDSSYPVQS STNTMTIRVC RCDSDGTILS 

       610        620        630        640        650        660 
CNVEAIFLPV GLSTGALIAI LLCIVILLAI VVLYVALRRQ KKKDTLMTSK EDIRDNVIHY 

       670        680        690        700        710        720 
DDEGGGEEDT QAFDIGALRN PKVIEENKIR RDIKPDSLCL PRQRPPMEDN TDIRDFIHQR 

       730        740        750        760        770        780 
LQENDVDPTA PPYDSLATYA YEGSGSVAES LSSIDSLTTE ADQDYDYLTD WGPRFKVLAD 

       790 
MFGEEESYNP DKVT

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References

« Hide 'large scale' references
[1]"Cloning of five human cadherins clarifies characteristic features of cadherin extracellular domain and provides further evidence for two structurally different types of cadherin."
Tanihara H., Sano K., Heimark R.L., St John T., Suzuki S.
Cell Adhes. Commun. 2:15-26(1994) [PubMed: 7982033] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Expressed cadherin pseudogenes are localized to the critical region of the spinal muscular atrophy gene."
Selig S., Bruno S., Scharf J.M., Wang C.H., Vitale E., Gilliam T.C., Kunkel L.M.
Proc. Natl. Acad. Sci. U.S.A. 92:3702-3706(1995) [PubMed: 7731968] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT MET-68.
Tissue: Brain cortex.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[6]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286, MASS SPECTROMETRY.
Tissue: Epithelium.

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Cross-references

Sequence databases

L34057 mRNA. Translation: AAA35623.1.
L33477 mRNA. Translation: AAB48539.1.
AK314800 mRNA. Translation: BAG37328.1.
CH471118 Genomic DNA. Translation: EAX10736.1.
BC047608 mRNA. Translation: AAH47608.1.
IPIIPI00296942.
PIRI59372.
RefSeqNP_004052.2.
UniGeneHs.113684

3D structure databases

HSSPHSSP built from PDB template 1I7W based on UniProtKB P09803.
ModBaseSearch...

Proteomic databases

PRIDEP55289.

Genome annotation databases

EnsemblENSG00000154162. Homo sapiens. [Contig view]
GeneID1010.
KEGGhsa:1010.

Organism-specific databases

GeneCardsGC05M021786.
H-InvDBHIX0032687.
HIX0057563.
HIX0057564.
HIX0057700.
HIX0058607.
HGNCHGNC:1751. CDH12.
MIM600562. gene.
PharmGKBPA26285.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP55289.
HOVERGENP55289.
OMAP55289. FGQNAEI.

Gene expression databases

ArrayExpressP55289.
BgeeP55289.
CleanExHS_CDH12.
GermOnlineENSG00000154162. Homo sapiens.

Family and domain databases

InterProIPR002126. Cadherin.
IPR000233. Cadherin_C_term.
[Graphical view]
Gene3DG3DSA:2.60.40.60. Cadherin. 2 hits.
PfamPF00028. Cadherin. 5 hits.
PF01049. Cadherin_C. 1 hit.
[Graphical view]
PRINTSPR00205. CADHERIN.
SMARTSM00112. CA. 5 hits.
[Graphical view]
PROSITEPS00232. CADHERIN_1. 2 hits.
PS50268. CADHERIN_2. 5 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio4246.
SOURCESearch...

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Entry information

Entry nameCAD12_HUMAN
AccessionPrimary (citable) accession number: P55289
Secondary accession number(s): B2RBT1, Q86UD2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: August 21, 2007
Last modified: June 16, 2009
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents