Q13443 (ADAM9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Disintegrin and metalloproteinase domain-containing protein 9
Short name=ADAM 9
EC=3.4.24.-

Alternative name(s):
Cellular disintegrin-related protein
Meltrin-gamma
Metalloprotease/disintegrin/cysteine-rich protein 9
Myeloma cell metalloproteinase

Gene names

Name:	ADAM9
Synonyms:	KIAA0021, MCMP, MDC9, MLTNG

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	819 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	Probable zinc protease. May mediate cell-cell or cell-matrix interactions. Isoform 2 displays alpha-secretase activity for APP. Ref.3
Cofactor	Binds 1 zinc ion per subunit Probable.
Subcellular location	Isoform 1: Cell membrane; Single-pass type I membrane protein Ref.3. Isoform 2: Secreted Ref.3.
Tissue specificity	Widely expressed. Expressed in chondrocytes. Isoform 2 is highly expressed in liver and heart. Ref.1 Ref.3 Ref.4 Ref.8
Involvement in disease	Defects in ADAM9 are the cause of cone-rod dystrophy type 9 (CORD9) [MIM:612775]. An inherited retinal dystrophy characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa. Ref.12
Sequence similarities	Contains 1 disintegrin domain. Contains 1 EGF-like domain. Contains 1 peptidase M12B domain.
Caution	Has sometimes been referred to as ADAM-12.

Ontologies

Keywords
Cellular component	Cell membrane Membrane Secreted
Coding sequence diversity	Alternative splicing
Disease	Cone-rod dystrophy
Domain	Signal Transmembrane Transmembrane helix
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	PMA-inducible membrane protein ectodomain proteolysis Traceable author statement. Source: BHF-UCL activation of MAPKK activity Inferred from direct assay. Source: BHF-UCL cell-cell adhesion mediated by integrin Inferred from expression pattern. Source: BHF-UCL cell-matrix adhesion Inferred from mutant phenotype. Source: BHF-UCL integrin-mediated signaling pathway Inferred by curator. Source: BHF-UCL keratinocyte differentiation Inferred from expression pattern. Source: BHF-UCL monocyte activation Inferred from mutant phenotype. Source: BHF-UCL positive regulation of cell adhesion mediated by integrin Inferred from mutant phenotype. Source: BHF-UCL positive regulation of keratinocyte migration Inferred from mutant phenotype. Source: BHF-UCL positive regulation of macrophage fusion Inferred from mutant phenotype. Source: BHF-UCL positive regulation of membrane protein ectodomain proteolysis Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL positive regulation of protein secretion Inferred from direct assay. Source: BHF-UCL response to calcium ion Inferred from mutant phenotype. Source: BHF-UCL response to glucocorticoid stimulus Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL response to hydrogen peroxide Inferred from mutant phenotype. Source: BHF-UCL response to manganese ion Inferred from mutant phenotype. Source: BHF-UCL response to tumor necrosis factor Inferred from direct assay. Source: BHF-UCL transforming growth factor beta receptor signaling pathway Inferred from mutant phenotype. Source: BHF-UCL
Cellular component	extracellular space Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intrinsic to external side of plasma membrane Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL
Molecular function	SH3 domain binding Inferred from physical interaction. Source: BHF-UCL collagen binding Inferred from mutant phenotype. Source: BHF-UCL integrin binding Inferred from direct assay. Source: BHF-UCL laminin binding Inferred from mutant phenotype. Source: BHF-UCL metalloendopeptidase activity Inferred from direct assay. Source: BHF-UCL protein kinase C binding Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MAD2L2	Q9UI95	3	EBI-77903,EBI-77889
PACSIN3	Q9UKS6	2	EBI-77903,EBI-77926
SH3GL2	Q99962	2	EBI-77903,EBI-77938

Alternative products

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

Isoform 1 (identifier: Q13443-1)

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: Q13443-2)

The sequence of this isoform differs from the canonical sequence as follows:
     655-655: V → K
     656-819: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

28

Potential

Chain

29 – 819

791

Disintegrin and metalloproteinase domain-containing protein 9

PRO_0000029062

Regions

Topological domain

29 – 697

669

Extracellular Potential

Transmembrane

698 – 718

21

Helical; Potential

Topological domain

719 – 819

101

Cytoplasmic Potential

Domain

212 – 406

195

Peptidase M12B

Domain

414 – 501

88

Disintegrin

Domain

644 – 698

55

EGF-like

Compositional bias

505 – 634

130

Cys-rich

Compositional bias

790 – 795

6

Poly-Pro

Sites

Active site

348

1

By similarity

Metal binding

347

1

Zinc; catalytic By similarity

Metal binding

351

1

Zinc; catalytic By similarity

Metal binding

357

1

Zinc; catalytic By similarity

Amino acid modifications

Modified residue

758

1

Phosphoserine Ref.9 Ref.11

Modified residue

761

1

Phosphothreonine Ref.9 Ref.11

Modified residue

815

1

Phosphotyrosine Ref.10 Ref.13

Glycosylation

125

1

N-linked (GlcNAc...) Potential

Glycosylation

144

1

N-linked (GlcNAc...) Potential

Glycosylation

154

1

N-linked (GlcNAc...) Potential

Glycosylation

231

1

N-linked (GlcNAc...) Potential

Glycosylation

381

1

N-linked (GlcNAc...) Potential

Glycosylation

487

1

N-linked (GlcNAc...) Potential

Disulfide bond

322 ↔ 401

By similarity

Disulfide bond

363 ↔ 385

By similarity

Disulfide bond

365 ↔ 370

By similarity

Disulfide bond

473 ↔ 493

By similarity

Disulfide bond

644 ↔ 656

By similarity

Disulfide bond

650 ↔ 662

By similarity

Disulfide bond

664 ↔ 673

By similarity

Natural variations

Alternative sequence

655

1

V → K in isoform 2.

VSP_011057

Alternative sequence

656 – 819

164

Missing in isoform 2.

VSP_011058

Experimental info

Sequence conflict

1 – 118

118

Missing no nucleotide entry Ref.2

Sequence conflict

117

1

R → Q in BAA03499. Ref.4

Sequence conflict

119 – 135

17

YVEGV…SDCFG → MWREFIIHPLLLATVLD no nucleotide entry Ref.2

Sequence conflict

154

1

N → M no nucleotide entry Ref.2

Sequence conflict

566

1

G → GLSLKFHAPFLSTMLQEAVR QTGTYLGGSVCCMKSDCRIV TLVK no nucleotide entry Ref.2

Sequence conflict

713 – 735

23

AIFIF…KRSQT → DYFYLHQEGSTVEKLLQKEE ITN no nucleotide entry Ref.2

Sequence conflict

736 – 819

84

Missing no nucleotide entry Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

819

Helix Strand Turn

Details...

Beta strand

212 – 220

9

Helix

222 – 227

6

Turn

228 – 230

3

Helix

232 – 250

19

Helix

251 – 253

3

Beta strand

255 – 264

10

Helix

277 – 290

14

Turn

291 – 295

5

Beta strand

299 – 305

7

Beta strand

311 – 316

6

Beta strand

327 – 331

5

Turn

337 – 339

3

Helix

340 – 352

13

Beta strand

369 – 374

6

Helix

384 – 397

14

Helix

400 – 402

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: BC186641833137FF	FASTA	819	90,556
	10 20 30 40 50 60 MGSGARFPSG TLRVRWLLLL GLVGPVLGAA RPGFQQTSHL SSYEIITPWR LTRERREAPR 70 80 90 100 110 120 PYSKQVSYVI QAEGKEHIIH LERNKDLLPE DFVVYTYNKE GTLITDHPNI QNHCHYRGYV 130 140 150 160 170 180 EGVHNSSIAL SDCFGLRGLL HLENASYGIE PLQNSSHFEH IIYRMDDVYK EPLKCGVSNK 190 200 210 220 230 240 DIEKETAKDE EEEPPSMTQL LRRRRAVLPQ TRYVELFIVV DKERYDMMGR NQTAVREEMI 250 260 270 280 290 300 LLANYLDSMY IMLNIRIVLV GLEIWTNGNL INIVGGAGDV LGNFVQWREK FLITRRRHDS 310 320 330 340 350 360 AQLVLKKGFG GTAGMAFVGT VCSRSHAGGI NVFGQITVET FASIVAHELG HNLGMNHDDG 370 380 390 400 410 420 RDCSCGAKSC IMNSGASGSR NFSSCSAEDF EKLTLNKGGN CLLNIPKPDE AYSAPSCGNK 430 440 450 460 470 480 LVDAGEECDC GTPKECELDP CCEGSTCKLK SFAECAYGDC CKDCRFLPGG TLCRGKTSEC 490 500 510 520 530 540 DVPEYCNGSS QFCQPDVFIQ NGYPCQNNKA YCYNGMCQYY DAQCQVIFGS KAKAAPKDCF 550 560 570 580 590 600 IEVNSKGDRF GNCGFSGNEY KKCATGNALC GKLQCENVQE IPVFGIVPAI IQTPSRGTKC 610 620 630 640 650 660 WGVDFQLGSD VPDPGMVNEG TKCGAGKICR NFQCVDASVL NYDCDVQKKC HGHGVCNSNK 670 680 690 700 710 720 NCHCENGWAP PNCETKGYGG SVDSGPTYNE MNTALRDGLL VFFFLIVPLI VCAIFIFIKR 730 740 750 760 770 780 DQLWRSYFRK KRSQTYESDG KNQANPSRQP GSVPRHVSPV TPPREVPIYA NRFAVPTYAA 790 800 810 KQPQQFPSRP PPPQPKVSSQ GNLIPARPAP APPLYSSLT
	Isoform 2 [UniParc]. Checksum: 1E99DD3A056B90B7	FASTA	655	72,359
	10 20 30 40 50 60 MGSGARFPSG TLRVRWLLLL GLVGPVLGAA RPGFQQTSHL SSYEIITPWR LTRERREAPR 70 80 90 100 110 120 PYSKQVSYVI QAEGKEHIIH LERNKDLLPE DFVVYTYNKE GTLITDHPNI QNHCHYRGYV 130 140 150 160 170 180 EGVHNSSIAL SDCFGLRGLL HLENASYGIE PLQNSSHFEH IIYRMDDVYK EPLKCGVSNK 190 200 210 220 230 240 DIEKETAKDE EEEPPSMTQL LRRRRAVLPQ TRYVELFIVV DKERYDMMGR NQTAVREEMI 250 260 270 280 290 300 LLANYLDSMY IMLNIRIVLV GLEIWTNGNL INIVGGAGDV LGNFVQWREK FLITRRRHDS 310 320 330 340 350 360 AQLVLKKGFG GTAGMAFVGT VCSRSHAGGI NVFGQITVET FASIVAHELG HNLGMNHDDG 370 380 390 400 410 420 RDCSCGAKSC IMNSGASGSR NFSSCSAEDF EKLTLNKGGN CLLNIPKPDE AYSAPSCGNK 430 440 450 460 470 480 LVDAGEECDC GTPKECELDP CCEGSTCKLK SFAECAYGDC CKDCRFLPGG TLCRGKTSEC 490 500 510 520 530 540 DVPEYCNGSS QFCQPDVFIQ NGYPCQNNKA YCYNGMCQYY DAQCQVIFGS KAKAAPKDCF 550 560 570 580 590 600 IEVNSKGDRF GNCGFSGNEY KKCATGNALC GKLQCENVQE IPVFGIVPAI IQTPSRGTKC 610 620 630 640 650 WGVDFQLGSD VPDPGMVNEG TKCGAGKICR NFQCVDASVL NYDCDVQKKC HGHGK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains." Weskamp G., Kraetzschmar J., Reid M.S., Blobel C.P. J. Cell Biol. 132:717-726(1996) [PubMed: 8647900] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY. Tissue: Mammary carcinoma.
[2]	"Cloning of a novel membrane-linked metalloproteinase from human myeloma cells." McKie N., Dallas D.J., Edwards T., Apperley J.F., Russell R.G.G., Croucher P.I. Biochem. J. 318:459-462(1996) [PubMed: 8809033] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Placenta.
[3]	"A secreted form of human ADAM9 has an alpha-secretase activity for APP." Hotoda N., Koike H., Sasagawa N., Ishiura S. Biochem. Biophys. Res. Commun. 293:800-805(2002) [PubMed: 12054541] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]	"Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1." Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S. DNA Res. 1:27-35(1994) [PubMed: 7584026] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), TISSUE SPECIFICITY. Tissue: Bone marrow.
[5]	Ohara O., Nagase T., Kikuno R., Nomura N. Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[6]	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. , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Lung.
[8]	"Expression of members of a novel membrane linked metalloproteinase family (ADAM) in human articular chondrocytes." McKie N., Edwards T., Dallas D.J., Houghton A., Stringer B., Graham R., Russell G., Croucher P.I. Biochem. Biophys. Res. Commun. 230:335-339(1997) [PubMed: 9016778] [Abstract] Cited for: TISSUE SPECIFICITY.
[9]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-758 AND THR-761, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-815, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-758 AND THR-761, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Loss of the metalloprotease ADAM9 leads to cone-rod dystrophy in humans and retinal degeneration in mice." Parry D.A., Toomes C., Bida L., Danciger M., Towns K.V., McKibbin M., Jacobson S.G., Logan C.V., Ali M., Bond J., Chance R., Swendeman S., Daniele L.L., Springell K., Adams M., Johnson C.A., Booth A.P., Jafri H. , Rashid Y., Banin E., Strom T.M., Farber D.B., Sharon D., Blobel C.P., Pugh E.N. Jr., Pierce E.A., Inglehearn C.F. Am. J. Hum. Genet. 84:683-691(2009) [PubMed: 19409519] [Abstract] Cited for: INVOLVEMENT IN CORD9.
[13]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-815, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[14]	"Exploring the substrate affinities of MMP-3, ADAM-9 and ADAM-10 using molecular modelling and dynamics simulations." Manzetti S., McCulloch D.R., Herington A.C. Submitted (JUN-2002) to the PDB data bank Cited for: 3D-STRUCTURE MODELING OF 208-404.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U41766 mRNA. Translation: AAC50403.1.
AF495383 mRNA. Translation: AAM49575.1.
D14665 mRNA. Translation: BAA03499.2.
CH471080 Genomic DNA. Translation: EAW63284.1.
BC143923 mRNA. Translation: AAI43924.1.

IPI

IPI00440932.
IPI00440933.

PIR

JC7850.
S71949.

RefSeq

NP_003807.1. NM_003816.2.

UniGene

Hs.591852.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M1V	model	-	A	208-404	[»]

ProteinModelPortal

Q13443.

SMR

Q13443. Positions 207-679.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q13443. 3 interactions.

MINT

MINT-108373.

STRING

Q13443.

Protein family/group databases

MEROPS

M12.209.

PTM databases

PhosphoSite

Q13443.

Polymorphism databases

DMDM

24211441.

Proteomic databases

PRIDE

Q13443.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000302458; ENSP00000305538; ENSG00000168615.

GeneID

8754.

KEGG

hsa:8754.

UCSC

uc003xmq.1. human.
uc003xmr.1. human.

Organism-specific databases

CTD

8754.

GeneCards

GC08P038871.

H-InvDB

HIX0021419.

HGNC

HGNC:216. ADAM9.

HPA

HPA004000.

MIM

602713. gene.
612775. phenotype.

neXtProt

NX_Q13443.

Orphanet

1872. Cone rod dystrophy.

PharmGKB

PA24534.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00590000082741.

HOGENOM

HBG507118.

HOVERGEN

HBG006978.

InParanoid

Q13443.

OMA

HDDGRDC.

PhylomeDB

Q13443.

Gene expression databases

ArrayExpress

Q13443.

Bgee

Q13443.

CleanEx

HS_ADAM9.

Genevestigator

Q13443.

Family and domain databases

InterPro

IPR006586. ADAM_Cys-rich.
IPR001762. Blood-coag_inhib_Disintegrin.
IPR018358. Disintegrin_CS.
IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000742. EGF_3.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]

Gene3D

G3DSA:4.10.70.10. Blood-coag_inhib_Disintegrin. 1 hit.
G3DSA:3.40.390.10. G3DSA:3.40.390.10. 1 hit.

KO

K06834.

Pfam

PF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]

SMART

SM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view]

SUPFAM

SSF57552. Disintegrin. 1 hit.

PROSITE

PS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS00022. EGF_1. False negative.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

32845.

SOURCE

Search...

Entry information

Entry name

ADAM9_HUMAN

Accession

Primary (citable) accession number: Q13443
Secondary accession number(s): B7ZLN7, Q10718, Q8NFM6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2002
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 123 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.