Q9BY67 (CADM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cell adhesion molecule 1

Alternative name(s):
Immunoglobulin superfamily member 4
Short name=IgSF4
Nectin-like protein 2
Short name=NECL-2
Spermatogenic immunoglobulin superfamily
Short name=SgIgSF
Synaptic cell adhesion molecule
Short name=SynCAM
Tumor suppressor in lung cancer 1
Short name=TSLC-1

Gene names

Name:	CADM1
Synonyms:	IGSF4, IGSF4A, NECL2, SYNCAM, TSLC1

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	442 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	Mediates homophilic cell-cell adhesion in a Ca2+-independent manner. Also mediates heterophilic cell-cell adhesion with CADM3 and PVRL3 in a Ca2+-independent manner. Acts as a tumor suppressor in non-small-cell lung cancer (NSCLC) cells. Interaction with CRTAM promotes natural killer (NK) cell cytotoxicity and interferon-gamma (IFN-gamma) secretion by CD8+ cells in vitro as well as NK cell-mediated rejection of tumors expressing CADM3 in vivo. May contribute to the less invasive phenotypes of lepidic growth tumor cells. In mast cells, may mediate attachment to and promote communication with nerves. CADM1, together with MITF, is essential for development and survival of mast cells in vivo. Acts as a synaptic cell adhesion molecule and plays a role in the formation of dendritic spines and in synapse assembly By similarity. May be involved in neuronal migration, axon growth, pathfinding, and fasciculation on the axons of differentiating neurons. May play diverse roles in the spermatogenesis including in the adhesion of spermatocytes and spermatids to Sertoli cells and for their normal differentiation into mature spermatozoa. Ref.4 Ref.5 Ref.6 Ref.9 Ref.12 Ref.14 UniProtKB Q8R5M8
Subunit structure	Homodimer. Interacts with FARP1 By similarity. Interacts with CRTAM and EPB41L3/DAL1. The interaction with EPB41L3/DAL1 may act to anchor CADM1 to the actin cytoskeleton. Interacts via its C-terminus with the PDZ domain of MPP3 and the PDZ domain of MPP6. Ref.5 Ref.6 Ref.10 Ref.12 Ref.13
Subcellular location	Cell membrane; Single-pass type I membrane protein. Cell junction › synapse By similarity. Note: Associates with perinuclear and plasma membranes in vivo. Localized to the basolateral plasma membrane of epithelial cells in gall bladder. Ref.4 UniProtKB Q8R5M8
Domain	The cytoplasmic domain appears to play a critical role in proapoptosis and tumor suppressor activity in NSCLC. Ref.7 Ref.11
Post-translational modification	Glycosylation at Asn-67 and Asn-101 promotes adhesive binding and synapse induction By similarity.
Sequence similarities	Belongs to the nectin family. Contains 2 Ig-like C2-type (immunoglobulin-like) domains. Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Ontologies

Keywords
Biological process	Apoptosis Cell adhesion Differentiation Immunity Spermatogenesis
Cellular component	Cell junction Cell membrane Membrane Synapse
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Tumor suppressor
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Molecular function	Developmental protein
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adherens junction organization Traceable author statement. Source: Reactome apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW brain development Inferred from electronic annotation. Source: Compara calcium-independent cell-cell adhesion Inferred from electronic annotation. Source: Compara cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW cell junction assembly Traceable author statement. Source: Reactome cell recognition Inferred from direct assay Ref.12. Source: UniProtKB detection of stimulus Inferred from direct assay Ref.12. Source: UniProtKB heterophilic cell-cell adhesion Inferred from sequence or structural similarity PubMed 12826663. Source: UniProtKB homophilic cell adhesion Inferred from sequence or structural similarity PubMed 12826663. Source: UniProtKB liver development Inferred from electronic annotation. Source: Compara positive regulation of cytokine secretion Inferred from direct assay Ref.12. Source: UniProtKB spermatogenesis Inferred from electronic annotation. Source: UniProtKB-KW susceptibility to natural killer cell mediated cytotoxicity Inferred from direct assay Ref.12. Source: UniProtKB synapse assembly Inferred from electronic annotation. Source: Compara unidimensional cell growth Inferred from electronic annotation. Source: Compara
Cellular_component	axon Inferred from electronic annotation. Source: Compara basolateral plasma membrane Inferred from sequence or structural similarity PubMed 12826663. Source: UniProtKB cell-cell junction Inferred from sequence or structural similarity PubMed 12826663. Source: UniProtKB dendrite Inferred from electronic annotation. Source: Compara integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW synaptic vesicle Inferred from electronic annotation. Source: Compara
Molecular_function	PDZ domain binding Inferred from sequence or structural similarity PubMed 12826663. Source: UniProtKB protein C-terminus binding Inferred from sequence or structural similarity PubMed 12826663. Source: UniProtKB protein homodimerization activity Inferred from sequence or structural similarity PubMed 12826663. Source: UniProtKB receptor binding Inferred from sequence or structural similarity PubMed 12826663. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 Ref.1 (identifier: Q9BY67-1)

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 Ref.7 (identifier: Q9BY67-2)

The sequence of this isoform differs from the canonical sequence as follows:
     332-333: DP → GT
     334-442: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 44

44

Potential

Chain

45 – 442

398

Cell adhesion molecule 1

PRO_0000291968

Regions

Topological domain

45 – 374

330

Extracellular Potential

Transmembrane

375 – 395

21

Helical; Potential

Topological domain

396 – 442

47

Cytoplasmic Potential

Domain

45 – 139

95

Ig-like V-type

Domain

144 – 238

95

Ig-like C2-type 1

Domain

243 – 329

87

Ig-like C2-type 2

Amino acid modifications

Modified residue

434

1

Phosphoserine By similarity

Glycosylation

67

1

N-linked (GlcNAc...) Potential

Glycosylation

101

1

N-linked (GlcNAc...) Ref.15 Ref.16 Ref.17

Glycosylation

113

1

N-linked (GlcNAc...) Ref.15 Ref.16 Ref.17

Glycosylation

165

1

N-linked (GlcNAc...) Potential

Glycosylation

301

1

N-linked (GlcNAc...) Ref.17

Glycosylation

302

1

N-linked (GlcNAc...) Ref.17

Glycosylation

304

1

N-linked (GlcNAc...) Potential

Glycosylation

308

1

N-linked (GlcNAc...) Potential

Disulfide bond

64 ↔ 124

By similarity

Disulfide bond

166 ↔ 220

By similarity

Disulfide bond

267 ↔ 313

By similarity

Natural variations

Alternative sequence

332 – 333

2

DP → GT in isoform 2. Ref.7

VSP_052461

Alternative sequence

334 – 442

109

Missing in isoform 2. Ref.7

VSP_052462

Natural variant

285

1

D → E.
Corresponds to variant rs45525440 [ dbSNP | Ensembl ].

VAR_061309

Experimental info

Sequence conflict

153

1

K → R in AAF69029. Ref.1

Sequence conflict

333 – 359

27

PPTTI…LTIIT → TTATTEPAVHGLTQLPNSAE ELDSEDLS in BAC11657. Ref.3

Secondary structure

1

.

.

.

442

Helix Strand Turn

Details...

Beta strand

405 – 407

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 26, 2007. Version 2. Checksum: CDEDE1E0C08BDD3A	FASTA	442	48,509
	10 20 30 40 50 60 MASVVLPSGS QCAAAAAAAA PPGLRLRLLL LLFSAAALIP TGDGQNLFTK DVTVIEGEVA 70 80 90 100 110 120 TISCQVNKSD DSVIQLLNPN RQTIYFRDFR PLKDSRFQLL NFSSSELKVS LTNVSISDEG 130 140 150 160 170 180 RYFCQLYTDP PQESYTTITV LVPPRNLMID IQKDTAVEGE EIEVNCTAMA SKPATTIRWF 190 200 210 220 230 240 KGNTELKGKS EVEEWSDMYT VTSQLMLKVH KEDDGVPVIC QVEHPAVTGN LQTQRYLEVQ 250 260 270 280 290 300 YKPQVHIQMT YPLQGLTREG DALELTCEAI GKPQPVMVTW VRVDDEMPQH AVLSGPNLFI 310 320 330 340 350 360 NNLNKTDNGT YRCEASNIVG KAHSDYMLYV YDPPTTIPPP TTTTTTTTTT TTTILTIITD 370 380 390 400 410 420 SRAGEEGSIR AVDHAVIGGV VAVVVFAMLC LLIILGRYFA RHKGTYFTHE AKGADDAADA 430 440 DTAIINAEGG QNNSEEKKEY FI
	Isoform 2 [UniParc]. Checksum: D7C1102F46D08492	FASTA	333	36,915
	10 20 30 40 50 60 MASVVLPSGS QCAAAAAAAA PPGLRLRLLL LLFSAAALIP TGDGQNLFTK DVTVIEGEVA 70 80 90 100 110 120 TISCQVNKSD DSVIQLLNPN RQTIYFRDFR PLKDSRFQLL NFSSSELKVS LTNVSISDEG 130 140 150 160 170 180 RYFCQLYTDP PQESYTTITV LVPPRNLMID IQKDTAVEGE EIEVNCTAMA SKPATTIRWF 190 200 210 220 230 240 KGNTELKGKS EVEEWSDMYT VTSQLMLKVH KEDDGVPVIC QVEHPAVTGN LQTQRYLEVQ 250 260 270 280 290 300 YKPQVHIQMT YPLQGLTREG DALELTCEAI GKPQPVMVTW VRVDDEMPQH AVLSGPNLFI 310 320 330 NNLNKTDNGT YRCEASNIVG KAHSDYMLYV YGT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nectin-like molecule 1 is a protein 4.1N associated protein and recruits protein 4.1N from cytoplasm to the plasma membrane." Zhou Y., Du G., Hu X., Yu S., Liu Y., Xu Y., Huang X., Liu J., Yin B., Fan M., Peng X., Qiang B., Yuan J. Biochim. Biophys. Acta 1669:142-154(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Cloning of a secretory isoform of SgIGSF/TSLC-1." Ito A., Koma Y., Nagano T. Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Lung.
[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. , 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 1). Tissue: Embryo.
[4]	"TSLC1 is a tumor-suppressor gene in human non-small-cell lung cancer." Kuramochi M., Fukuhara H., Nobukuni T., Kanbe T., Maruyama T., Ghosh H.P., Pletcher M., Isomura M., Onizuka M., Kitamura T., Sekiya T., Reeves R.H., Murakami Y. Nat. Genet. 27:427-430(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[5]	"Direct association of TSLC1 and DAL-1, two distinct tumor suppressor proteins in lung cancer." Yageta M., Kuramochi M., Masuda M., Fukami T., Fukuhara H., Maruyama T., Shibuya M., Murakami Y. Cancer Res. 62:5129-5133(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH EPB41L3.
[6]	"The tumor suppressor protein TSLC1 is involved in cell-cell adhesion." Masuda M., Yageta M., Fukuhara H., Kuramochi M., Maruyama T., Nomoto A., Murakami Y. J. Biol. Chem. 277:31014-31019(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, GLYCOSYLATION.
[7]	"The cytoplasmic domain is critical to the tumor suppressor activity of TSLC1 in non-small cell lung cancer." Mao X., Seidlitz E., Ghosh K., Murakami Y., Ghosh H.P. Cancer Res. 63:7979-7985(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN.
[8]	"Promoter methylation of the TSLC1 gene in advanced lung tumors and various cancer cell lines." Fukami T., Fukuhara H., Kuramochi M., Maruyama T., Isogai K., Sakamoto M., Takamoto S., Murakami Y. Int. J. Cancer 107:53-59(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DISEASE.
[9]	"Expression of the TSLC1 adhesion molecule in pulmonary epithelium and its down-regulation in pulmonary adenocarcinoma other than bronchioloalveolar carcinoma." Ito A., Okada M., Uchino K., Wakayama T., Koma Y., Iseki S., Tsubota N., Okita Y., Kitamura Y. Lab. Invest. 83:1175-1183(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"Association of a lung tumor suppressor TSLC1 with MPP3, a human homologue of Drosophila tumor suppressor Dlg." Fukuhara H., Masuda M., Yageta M., Fukami T., Kuramochi M., Maruyama T., Kitamura T., Murakami Y. Oncogene 22:6160-6165(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MPP3.
[11]	"Re-expression of TSLC1 in a non-small-cell lung cancer cell line induces apoptosis and inhibits tumor growth." Mao X., Seidlitz E., Truant R., Hitt M., Ghosh H.P. Oncogene 23:5632-5642(2004) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN.
[12]	"The tumor suppressor TSLC1/NECL-2 triggers NK-cell and CD8+ T-cell responses through the cell-surface receptor CRTAM." Boles K.S., Barchet W., Diacovo T., Cella M., Colonna M. Blood 106:779-786(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CRTAM.
[13]	"Nectin-like protein 2 defines a subset of T-cell zone dendritic cells and is a ligand for class-I-restricted T-cell-associated molecule." Galibert L., Diemer G.S., Liu Z., Johnson R.S., Smith J.L., Walzer T., Comeau M.R., Rauch C.T., Wolfson M.F., Sorensen R.A., Van der Vuurst de Vries A.-R., Branstetter D.G., Koelling R.M., Scholler J., Fanslow W.C., Baum P.R., Derry J.M., Yan W. J. Biol. Chem. 280:21955-21964(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CRTAM.
[14]	"The spermatogenic Ig superfamily/synaptic cell adhesion molecule mast-cell adhesion molecule promotes interaction with nerves." Furuno T., Ito A., Koma Y., Watabe K., Yokozaki H., Bienenstock J., Nakanishi M., Kitamura Y. J. Immunol. 174:6934-6942(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[15]	"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-101 AND ASN-113, MASS SPECTROMETRY. Tissue: Plasma.
[16]	"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-101 AND ASN-113, MASS SPECTROMETRY. Tissue: Liver.
[17]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-101; ASN-113; ASN-301 AND ASN-302, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[18]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF132811 mRNA. Translation: AAF69029.1.
AB094146 mRNA. Translation: BAC66178.1.
AK075502 mRNA. Translation: BAC11657.1.

IPI

IPI00003813.
IPI00166392.

RefSeq

NP_001091987.1. NM_001098517.1.
NP_055148.3. NM_014333.3.

UniGene

Hs.370510.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3BIN	X-ray	2.30	B	400-411	[»]

ProteinModelPortal

Q9BY67.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9BY67. 1 interaction.

MINT

MINT-1184987.

STRING

9606.ENSP00000329797.

PTM databases

PhosphoSite

Q9BY67.

Polymorphism databases

DMDM

150438862.

Proteomic databases

PaxDb

Q9BY67.

PRIDE

Q9BY67.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000452722; ENSP00000395359; ENSG00000182985.

GeneID

23705.

KEGG

hsa:23705.

UCSC

uc001ppi.4. human.
uc001ppl.3. human.

Organism-specific databases

CTD

23705.

GeneCards

GC11M115044.

HGNC

HGNC:5951. CADM1.

HPA

CAB037266.

MIM

605686. gene.

neXtProt

NX_Q9BY67.

PharmGKB

PA29764.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG69486.

HOGENOM

HOG000036057.

HOVERGEN

HBG057086.

KO

K06781.

OrthoDB

EOG4TMR2D.

Enzyme and pathway databases

Reactome

REACT_111155. Cell-Cell communication.

Gene expression databases

ArrayExpress

Q9BY67.

Bgee

Q9BY67.

CleanEx

HS_CADM1.

Genevestigator

Q9BY67.

Family and domain databases

Gene3D

2.60.40.10. 3 hits.

InterPro

IPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR003585. Neurexin-like.
[Graphical view]

Pfam

PF08205. C2-set_2. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]

SMART

SM00294. 4.1m. 1 hit.
SM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CADM1. human.

EvolutionaryTrace

Q9BY67.

GenomeRNAi

23705.

NextBio

46597.

SOURCE

Search...

Entry information

Entry name

CADM1_HUMAN

Accession

Primary (citable) accession number: Q9BY67
Secondary accession number(s): Q86WB8, Q8N2F4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	June 26, 2007
Last modified:	May 29, 2013
This is version 102 of the entry and version 2 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.