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P55290 (CAD13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cadherin-13
Alternative name(s):
Heart cadherin
Short name=H-cadherin
P105
Truncated cadherin
Short name=T-cad
Short name=T-cadherin
Gene names
Name:CDH13
Synonyms:CDHH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length713 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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. May act as a negative regulator of neural cell growth. Ref.9

Subunit structure

By contrast to classical cadherins, homodimerization in trans is not mediated by cadherin EC1 domain strand-swapping, but instead through a homophilic adhesive interface which joins two elongated EC1-EC2 domains through a region near their Ca2+-binding sites to form a tetrahedral, X-like shape By similarity.

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor.

Tissue specificity

Highly expressed in heart. In the CNS, expressed in cerebral cortex, medulla, hippocampus, amygdala, thalamus and substantia nigra. No expression detected in cerebellum or spinal cord. Ref.2 Ref.9

Developmental stage

Expressed at higher levels in adult brain than in developing brain. Ref.9

Domain

Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain By similarity.

Sequence similarities

Contains 5 cadherin domains.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
   LigandCalcium
Metal-binding
   PTMCleavage on pair of basic residues
Glycoprotein
GPI-anchor
Lipoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRac protein signal transduction

Inferred from mutant phenotype PubMed 15703273. Source: BHF-UCL

Rho protein signal transduction

Inferred from mutant phenotype PubMed 15703273. Source: BHF-UCL

adherens junction organization

Traceable author statement. Source: Reactome

calcium-dependent cell-cell adhesion

Inferred from direct assay PubMed 10601632. Source: BHF-UCL

cell junction assembly

Traceable author statement. Source: Reactome

cell-cell junction organization

Traceable author statement. Source: Reactome

endothelial cell migration

Inferred from direct assay PubMed 14729458. Source: BHF-UCL

homophilic cell adhesion

Inferred from direct assay PubMed 10601632. Source: BHF-UCL

keratinocyte proliferation

Inferred from direct assay PubMed 15816843. Source: BHF-UCL

lamellipodium assembly

Inferred from direct assay PubMed 15703273. Source: BHF-UCL

localization within membrane

Inferred from mutant phenotype PubMed 17573778. Source: BHF-UCL

low-density lipoprotein particle mediated signaling

Inferred from direct assay PubMed 16013438. Source: BHF-UCL

mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell adhesion

Inferred from direct assay PubMed 14729458. Source: BHF-UCL

negative regulation of cell proliferation

Inferred from direct assay Ref.9. Source: BHF-UCL

positive regulation of calcium-mediated signaling

Inferred from direct assay PubMed 16013438. Source: BHF-UCL

positive regulation of cell migration

Inferred from direct assay PubMed 14729458. Source: BHF-UCL

positive regulation of cell-matrix adhesion

Inferred from mutant phenotype PubMed 17573778. Source: BHF-UCL

positive regulation of endothelial cell proliferation

Inferred from mutant phenotype PubMed 15364621. Source: BHF-UCL

positive regulation of positive chemotaxis

Inferred from direct assay PubMed 16013438. Source: BHF-UCL

positive regulation of smooth muscle cell proliferation

Inferred from mutant phenotype PubMed 15364621. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 16099944. Source: BHF-UCL

regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

regulation of endocytosis

Inferred from mutant phenotype PubMed 17573778. Source: BHF-UCL

regulation of epidermal growth factor receptor signaling pathway

Inferred from mutant phenotype PubMed 17573778. Source: BHF-UCL

sprouting angiogenesis

Inferred from direct assay PubMed 16873731. Source: BHF-UCL

   Cellular_componentanchored component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

caveola

Inferred from direct assay PubMed 9650591. Source: BHF-UCL

cytoplasm

Inferred from direct assay Ref.9. Source: BHF-UCL

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from direct assay PubMed 16873731. Source: BHF-UCL

neuron projection

Inferred from direct assay Ref.9. Source: BHF-UCL

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay Ref.9. Source: BHF-UCL

   Molecular_functionadiponectin binding

Inferred from sequence or structural similarity. Source: BHF-UCL

cadherin binding

Inferred from direct assay PubMed 10601632. Source: BHF-UCL

calcium ion binding

Inferred from electronic annotation. Source: InterPro

lipoprotein particle binding

Inferred from direct assay Ref.10. Source: UniProtKB

low-density lipoprotein particle binding

Inferred from direct assay PubMed 16013438. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P55290-1)

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: P55290-2)

The sequence of this isoform differs from the canonical sequence as follows:
     162-190: VVDSDRPERSKFRLTGKGVDQEPKGIFRI → RTHNPINSELLLNEGITADLNPCITILAI
     191-713: Missing.
Isoform 3 (identifier: P55290-3)

The sequence of this isoform differs from the canonical sequence as follows:
     162-175: VVDSDRPERSKFRL → MKIWQVLCLARWLT
     176-713: Missing.
Isoform 4 (identifier: P55290-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: MQPRTPLVLCVLLS → MKTPPGASSRTKCSRELRSFCAFSCPRAKQPTCTAWFPQQEHPSENGPQMPGRDPPAASTM
Note: Gene prediction based on EST data.
Isoform 5 (identifier: P55290-5)

The sequence of this isoform differs from the canonical sequence as follows:
     123-161: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Propeptide23 – 138116
PRO_0000003793
Chain139 – 693555Cadherin-13
PRO_0000003794
Propeptide694 – 71320Removed in mature form Probable
PRO_0000003795

Regions

Domain139 – 245107Cadherin 1
Domain246 – 363118Cadherin 2
Domain364 – 477114Cadherin 3
Domain478 – 585108Cadherin 4
Domain584 – 694111Cadherin 5

Amino acid modifications

Lipidation6931GPI-anchor amidated glycine Probable
Glycosylation521N-linked (GlcNAc...) Potential
Glycosylation861N-linked (GlcNAc...) Ref.11
Glycosylation3821N-linked (GlcNAc...) Potential
Glycosylation5001N-linked (GlcNAc...) Ref.11
Glycosylation5301N-linked (GlcNAc...) Ref.13
Glycosylation5981N-linked (GlcNAc...) Potential
Glycosylation6381N-linked (GlcNAc...) Ref.11 Ref.13
Glycosylation6711N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 1414MQPRT…CVLLS → MKTPPGASSRTKCSRELRSF CAFSCPRAKQPTCTAWFPQQ EHPSENGPQMPGRDPPAAST M in isoform 4.
VSP_046714
Alternative sequence123 – 16139Missing in isoform 5.
VSP_053739
Alternative sequence162 – 19029VVDSD…GIFRI → RTHNPINSELLLNEGITADL NPCITILAI in isoform 2.
VSP_042696
Alternative sequence162 – 17514VVDSD…SKFRL → MKIWQVLCLARWLT in isoform 3.
VSP_042794
Alternative sequence176 – 713538Missing in isoform 3.
VSP_042795
Alternative sequence191 – 713523Missing in isoform 2.
VSP_042697
Natural variant651R → C in a patient with amyotrophic lateral sclerosis. Ref.14
VAR_065747
Natural variant1031A → V in a patient with amyotrophic lateral sclerosis. Ref.14
VAR_065748
Natural variant1131G → R in a patient with amyotrophic lateral sclerosis. Ref.14
Corresponds to variant rs183971768 [ dbSNP | Ensembl ].
VAR_065749
Natural variant1211L → S.
Corresponds to variant rs7197352 [ dbSNP | Ensembl ].
VAR_030632
Natural variant2461R → W in a patient with amyotrophic lateral sclerosis. Ref.14
VAR_065750
Natural variant3671E → Q in a patient with amyotrophic lateral sclerosis. Ref.14
VAR_065751
Natural variant3761A → T. Ref.14
Corresponds to variant rs35549391 [ dbSNP | Ensembl ].
VAR_065752
Natural variant6431L → R. Ref.14
Corresponds to variant rs34106627 [ dbSNP | Ensembl ].
VAR_065753

Experimental info

Sequence conflict1991V → M in AAH28624. Ref.4
Sequence conflict1991V → M in AAH30653. Ref.4
Sequence conflict2881Q → R in AAH28624. Ref.4
Sequence conflict2881Q → R in AAH30653. Ref.4
Sequence conflict3921T → A in AAH28624. Ref.4
Sequence conflict3921T → A in AAH30653. Ref.4
Sequence conflict5441P → T in AAH28624. Ref.4
Sequence conflict5441P → T in AAH30653. Ref.4

Secondary structure

......................... 713
Helix Strand Turn

Details...

Sequences

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

Last modified October 1, 1996. Version 1.
Checksum: CEB662D77824CB60

FASTA71378,287
        10         20         30         40         50         60 
MQPRTPLVLC VLLSQVLLLT SAEDLDCTPG FQQKVFHINQ PAEFIEDQSI LNLTFSDCKG 

        70         80         90        100        110        120 
NDKLRYEVSS PYFKVNSDGG LVALRNITAV GKTLFVHART PHAEDMAELV IVGGKDIQGS 

       130        140        150        160        170        180 
LQDIFKFART SPVPRQKRSI VVSPILIPEN QRQPFPRDVG KVVDSDRPER SKFRLTGKGV 

       190        200        210        220        230        240 
DQEPKGIFRI NENTGSVSVT RTLDREVIAV YQLFVETTDV NGKTLEGPVP LEVIVIDQND 

       250        260        270        280        290        300 
NRPIFREGPY IGHVMEGSPT GTTVMRMTAF DADDPATDNA LLRYNIRQQT PDKPSPNMFY 

       310        320        330        340        350        360 
IDPEKGDIVT VVSPALLDRE TLENPKYELI IEAQDMAGLD VGLTGTATAT IMIDDKNDHS 

       370        380        390        400        410        420 
PKFTKKEFQA TVEEGAVGVI VNLTVEDKDD PTTGAWRAAY TIINGNPGQS FEIHTNPQTN 

       430        440        450        460        470        480 
EGMLSVVKPL DYEISAFHTL LIKVENEDPL VPDVSYGPSS TATVHITVLD VNEGPVFYPD 

       490        500        510        520        530        540 
PMMVTRQEDL SVGSVLLTVN ATDPDSLQHQ TIRYSVYKDP AGWLNINPIN GTVDTTAVLD 

       550        560        570        580        590        600 
RESPFVDNSV YTALFLAIDS GNPPATGTGT LLITLEDVND NAPFIYPTVA EVCDDAKNLS 

       610        620        630        640        650        660 
VVILGASDKD LHPNTDPFKF EIHKQAVPDK VWKISKINNT HALVSLLQNL NKANYNLPIM 

       670        680        690        700        710 
VTDSGKPPMT NITDLRVQVC SCRNSKVDCN AAGALRFSLP SVLLLSLFSL ACL 

« Hide

Isoform 2 [UniParc].

Checksum: C7DA89A2C0C036E9
Show »

FASTA19021,058
Isoform 3 [UniParc].

Checksum: 0038FABE744ECAE0
Show »

FASTA17519,660
Isoform 4 [UniParc].

Checksum: B4BB30012F3D4560
Show »

FASTA76083,397
Isoform 5 [UniParc].

Checksum: 4C15F7C62AE5B0AA
Show »

FASTA67473,787

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Fetal brain.
[2]"H-cadherin, a novel cadherin with growth inhibitory functions and diminished expression in human breast cancer."
Lee S.W.
Nat. Med. 2:776-782(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[3]"The H-cadherin (CDH13) gene is inactivated in human lung cancer."
Sato M., Mori Y., Sakurada A., Fujimura S., Horii A.
Hum. Genet. 103:96-101(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Differential alternative splicing of Cadherin 13 gene in aging and Alzheimer's disease."
Liu Q.-R., Liu J.J., Zhu X.-G., Uhl G.R.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
[6]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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 1).
Tissue: Brain and Testis.
[8]"Identification of an atypical lipoprotein-binding protein from human aortic smooth muscle as T-cadherin."
Tkachuk V.A., Bochkov V.N., Philippova M.P., Stambolsky D.V., Kuzmenko E.S., Sidorova M.V., Molokoedov A.S., Spirov V.G., Resink T.J.
FEBS Lett. 421:208-212(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 140-149; 162-169 AND 284-287 (ISOFORM 1).
Tissue: Aorta.
[9]"Expression of T-cadherin (CDH13, H-Cadherin) in human brain and its characteristics as a negative growth regulator of epidermal growth factor in neuroblastoma cells."
Takeuchi T., Misaki A., Liang S.-B., Tachibana A., Hayashi N., Sonobe H., Ohtsuki Y.
J. Neurochem. 74:1489-1497(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Brain.
[10]"The glycosyl phosphatidylinositol anchor of human T-cadherin binds lipoproteins."
Niermann T., Kern F., Erne P., Resink T.
Biochem. Biophys. Res. Commun. 276:1240-1247(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[11]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-86; ASN-500 AND ASN-638.
Tissue: Plasma.
[12]"Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment."
Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S., Brodbeck U., Peck S.C., Jensen O.N.
J. Proteome Res. 5:935-943(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-530 AND ASN-638.
Tissue: Liver.
[14]"Resequencing of 29 candidate genes in patients with familial and sporadic amyotrophic lateral sclerosis."
Daoud H., Valdmanis P.N., Gros-Louis F., Belzil V., Spiegelman D., Henrion E., Diallo O., Desjarlais A., Gauthier J., Camu W., Dion P.A., Rouleau G.A.
Arch. Neurol. 68:587-593(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CYS-65; VAL-103; ARG-113; TRP-246; GLN-367; THR-376 AND ARG-643.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L34058 mRNA. Translation: AAA35624.1.
U59289 mRNA. Translation: AAB18912.1.
U59288 mRNA. Translation: AAB18911.1.
AB001103 Genomic DNA. Translation: BAA32411.1.
EU190357 mRNA. Translation: ABW97440.1.
EU190358 mRNA. Translation: ABW97441.1.
AK298612 mRNA. Translation: BAH12826.1.
AC009028 Genomic DNA. No translation available.
AC009063 Genomic DNA. No translation available.
AC009119 Genomic DNA. No translation available.
AC009142 Genomic DNA. No translation available.
AC087189 Genomic DNA. No translation available.
AC092340 Genomic DNA. No translation available.
AC092351 Genomic DNA. No translation available.
AC098804 Genomic DNA. No translation available.
AC099506 Genomic DNA. No translation available.
AC106814 Genomic DNA. No translation available.
AC125793 Genomic DNA. No translation available.
BC028624 mRNA. Translation: AAH28624.1.
BC030653 mRNA. Translation: AAH30653.1.
PIRB38992.
RefSeqNP_001207418.1. NM_001220489.1.
NP_001207420.1. NM_001220491.1.
NP_001207421.1. NM_001220492.1.
NP_001248.1. NM_001257.4.
UniGeneHs.654386.
Hs.661776.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2V37NMR-A139-243[»]
ProteinModelPortalP55290.
SMRP55290. Positions 13-680.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107447. 1 interaction.
IntActP55290. 1 interaction.
MINTMINT-7004770.
STRING9606.ENSP00000268613.

PTM databases

PhosphoSiteP55290.

Polymorphism databases

DMDM1705552.

Proteomic databases

PaxDbP55290.
PeptideAtlasP55290.
PRIDEP55290.

Protocols and materials databases

DNASU1012.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000268613; ENSP00000268613; ENSG00000140945. [P55290-4]
ENST00000428848; ENSP00000394557; ENSG00000140945. [P55290-5]
ENST00000431540; ENSP00000408632; ENSG00000140945. [P55290-2]
ENST00000446376; ENSP00000388804; ENSG00000140945. [P55290-3]
ENST00000565636; ENSP00000456491; ENSG00000140945. [P55290-3]
ENST00000566620; ENSP00000454435; ENSG00000140945. [P55290-1]
GeneID1012.
KEGGhsa:1012.
UCSCuc002fgx.3. human. [P55290-1]
uc010chh.3. human. [P55290-2]
uc021tlw.1. human. [P55290-3]

Organism-specific databases

CTD1012.
GeneCardsGC16P082660.
HGNCHGNC:1753. CDH13.
HPACAB025863.
HPA001380.
MIM601364. gene.
neXtProtNX_P55290.
PharmGKBPA26287.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG304703.
HOGENOMHOG000169079.
HOVERGENHBG106438.
InParanoidP55290.
KOK06808.
OMATIATYQL.
OrthoDBEOG7MH0XG.
PhylomeDBP55290.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.

Gene expression databases

ArrayExpressP55290.
BgeeP55290.
CleanExHS_CDH13.
GenevestigatorP55290.

Family and domain databases

Gene3D2.60.40.60. 6 hits.
InterProIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR014868. Cadherin_pro_dom.
[Graphical view]
PfamPF00028. Cadherin. 5 hits.
PF08758. Cadherin_pro. 1 hit.
[Graphical view]
PRINTSPR00205. CADHERIN.
SMARTSM00112. CA. 5 hits.
SM01055. Cadherin_pro. 1 hit.
[Graphical view]
SUPFAMSSF49313. SSF49313. 6 hits.
PROSITEPS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCDH13. human.
EvolutionaryTraceP55290.
GeneWikiT-cadherin.
GenomeRNAi1012.
NextBio35534829.
PROP55290.
SOURCESearch...

Entry information

Entry nameCAD13_HUMAN
AccessionPrimary (citable) accession number: P55290
Secondary accession number(s): A8W476 expand/collapse secondary AC list , A8W477, B7Z590, C9JRI6, J3KN62, Q6GTW4, Q8TBX3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM