P55290 (CAD13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	713 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.8
Subcellular location	Cell membrane; Lipid-anchor › GPI-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.8
Developmental stage	Expressed at higher levels in adult brain than in developing brain. Ref.8
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 process	Cell adhesion
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal
Ligand	Calcium Metal-binding
PTM	Cleavage on pair of basic residues GPI-anchor Glycoprotein Lipoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Rac 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 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 negative regulation of cell adhesion Inferred from direct assay PubMed 14729458. Source: BHF-UCL negative regulation of cell proliferation Inferred from direct assay Ref.8. 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 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_component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW caveola Inferred from direct assay PubMed 9650591. Source: BHF-UCL cytoplasm Inferred from direct assay Ref.8. Source: BHF-UCL extracellular space Inferred from direct assay PubMed 16873731. Source: BHF-UCL neuron projection Inferred from direct assay Ref.8. Source: BHF-UCL
Molecular_function	adiponectin 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 low-density lipoprotein particle binding Inferred from direct assay PubMed 16013438. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 3 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Potential

Propeptide

23 – 138

116

PRO_0000003793

Chain

139 – 693

555

Cadherin-13

PRO_0000003794

Propeptide

694 – 713

20

Removed in mature form Probable

PRO_0000003795

Regions

Domain

139 – 245

107

Cadherin 1

Domain

246 – 363

118

Cadherin 2

Domain

364 – 477

114

Cadherin 3

Domain

478 – 585

108

Cadherin 4

Domain

584 – 694

111

Cadherin 5

Amino acid modifications

Lipidation

693

1

GPI-anchor amidated glycine Probable

Glycosylation

52

1

N-linked (GlcNAc...) Potential

Glycosylation

86

1

N-linked (GlcNAc...) Ref.10

Glycosylation

382

1

N-linked (GlcNAc...) Potential

Glycosylation

500

1

N-linked (GlcNAc...) Ref.10

Glycosylation

530

1

N-linked (GlcNAc...) Ref.12

Glycosylation

598

1

N-linked (GlcNAc...) Potential

Glycosylation

638

1

N-linked (GlcNAc...) Ref.10 Ref.12

Glycosylation

671

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

162 – 190

29

VVDSD…GIFRI → RTHNPINSELLLNEGITADL NPCITILAI in isoform 2.

VSP_042696

Alternative sequence

162 – 175

14

VVDSD…SKFRL → MKIWQVLCLARWLT in isoform 3.

VSP_042794

Alternative sequence

176 – 713

538

Missing in isoform 3.

VSP_042795

Alternative sequence

191 – 713

523

Missing in isoform 2.

VSP_042697

Natural variant

65

1

R → C in a patient with amyotrophic lateral sclerosis. Ref.13

VAR_065747

Natural variant

103

1

A → V in a patient with amyotrophic lateral sclerosis. Ref.13

VAR_065748

Natural variant

113

1

G → R in a patient with amyotrophic lateral sclerosis. Ref.13

VAR_065749

Natural variant

121

1

L → S.
Corresponds to variant rs7197352 [ dbSNP | Ensembl ].

VAR_030632

Natural variant

246

1

R → W in a patient with amyotrophic lateral sclerosis. Ref.13

VAR_065750

Natural variant

367

1

E → Q in a patient with amyotrophic lateral sclerosis. Ref.13

VAR_065751

Natural variant

376

1

A → T. Ref.13
Corresponds to variant rs35549391 [ dbSNP | Ensembl ].

VAR_065752

Natural variant

643

1

L → R. Ref.13
Corresponds to variant rs34106627 [ dbSNP | Ensembl ].

VAR_065753

Experimental info

Sequence conflict

199

1

V → M in AAH28624. Ref.4

Sequence conflict

199

1

V → M in AAH30653. Ref.4

Sequence conflict

288

1

Q → R in AAH28624. Ref.4

Sequence conflict

288

1

Q → R in AAH30653. Ref.4

Sequence conflict

392

1

T → A in AAH28624. Ref.4

Sequence conflict

392

1

T → A in AAH30653. Ref.4

Sequence conflict

544

1

P → T in AAH28624. Ref.4

Sequence conflict

544

1

P → T in AAH30653. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

713

Helix Strand Turn

Details...

Beta strand

145 – 148

4

Beta strand

157 – 161

5

Beta strand

163 – 167

5

Beta strand

172 – 178

7

Turn

179 – 181

3

Beta strand

182 – 184

3

Beta strand

187 – 190

4

Turn

192 – 194

3

Beta strand

196 – 199

4

Turn

205 – 207

3

Beta strand

209 – 218

10

Beta strand

224 – 236

13

Beta strand

238 – 241

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: CEB662D77824CB60	FASTA	713	78,287
	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
	Isoform 2 [UniParc]. Checksum: C7DA89A2C0C036E9	FASTA	190	21,058
	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 KRTHNPINSE LLLNEGITAD 190 LNPCITILAI
	Isoform 3 [UniParc]. Checksum: 0038FABE744ECAE0	FASTA	175	19,660
	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 LQDIFKFART SPVPRQKRSI VVSPILIPEN QRQPFPRDVG KMKIWQVLCL ARWLT

References

	« Hide 'large scale' referencesShow '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: 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]	"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. , 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].
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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, MASS SPECTROMETRY. Tissue: Plasma.
[11]	"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], MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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, MASS SPECTROMETRY. Tissue: Liver.
[13]	"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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.
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.

IPI

IPI01013272.

PIR

B38992.

RefSeq

NP_001207420.1. NM_001220491.1.
NP_001207421.1. NM_001220492.1.
NP_001248.1. NM_001257.4.

UniGene

Hs.654386.
Hs.661776.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2V37	NMR	-	A	139-243	[»]

ProteinModelPortal

P55290.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-7004770.

STRING

9606.ENSP00000268613.

PTM databases

PhosphoSite

P55290.

Polymorphism databases

DMDM

1705552.

Proteomic databases

PaxDb

P55290.

PeptideAtlas

P55290.

PRIDE

P55290.

Protocols and materials databases

DNASU

1012.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000431540; ENSP00000408632; ENSG00000140945.
ENST00000446376; ENSP00000388804; ENSG00000140945.
ENST00000565636; ENSP00000456491; ENSG00000140945.
ENST00000566620; ENSP00000454435; ENSG00000140945.

GeneID

1012.

KEGG

hsa:1012.

UCSC

uc002fgx.3. human.
uc010chh.3. human.
uc021tlw.1. human.

Organism-specific databases

CTD

1012.

GeneCards

GC16P082660.

HGNC

HGNC:1753. CDH13.

HPA

CAB025863.
HPA001380.

MIM

601364. gene.

neXtProt

NX_P55290.

PharmGKB

PA26287.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG304703.

HOGENOM

HOG000169079.

HOVERGEN

HBG106438.

InParanoid

P55290.

KO

K06808.

OrthoDB

EOG498V07.

Enzyme and pathway databases

Reactome

REACT_111155. Cell-Cell communication.

Gene expression databases

ArrayExpress

P55290.

Bgee

P55290.

CleanEx

HS_CDH13.

Genevestigator

P55290.

Family and domain databases

Gene3D

2.60.40.60. 6 hits.

InterPro

IPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR014868. Cadherin_pro_dom.
[Graphical view]

Pfam

PF00028. Cadherin. 5 hits.
PF08758. Cadherin_pro. 1 hit.
[Graphical view]

PRINTS

PR00205. CADHERIN.

SMART

SM00112. CA. 5 hits.
SM01055. Cadherin_pro. 1 hit.
[Graphical view]

SUPFAM

SSF49313. Cadherin. 6 hits.

PROSITE

PS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 5 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CDH13. human.

EvolutionaryTrace

P55290.

GenomeRNAi

1012.

NextBio

4253.

SOURCE

Search...

Entry information

Entry name

CAD13_HUMAN

Accession

Primary (citable) accession number: P55290
Secondary accession number(s): A8W476 , A8W477, Q6GTW4, Q8TBX3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 29, 2013
This is version 128 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.