P78325 (ADAM8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Disintegrin and metalloproteinase domain-containing protein 8
Short name=ADAM 8
EC=3.4.24.-

Alternative name(s):
Cell surface antigen MS2
CD_antigen=CD156a

Gene names

Name:	ADAM8
Synonyms:	MS2

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	824 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	Possible involvement in extravasation of leukocytes.
Cofactor	Binds 1 zinc ion per subunit.
Subunit structure	Interacts with FST3. Ref.5
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	Expressed on neutrophils and monocytes.
Sequence similarities	Contains 1 disintegrin domain. Contains 1 EGF-like domain. Contains 1 peptidase M12B domain.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	EGF-like domain Signal Transmembrane Transmembrane helix
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of MAPK activity involved in innate immune response Inferred from sequence or structural similarity. Source: BHF-UCL angiogenesis Inferred from sequence or structural similarity. Source: BHF-UCL cell morphogenesis Inferred from sequence or structural similarity. Source: BHF-UCL cell-cell adhesion Inferred from electronic annotation. Source: Compara cellular response to hypoxia Inferred from direct assay PubMed 18566576. Source: BHF-UCL leukocyte migration involved in inflammatory response Inferred from sequence or structural similarity. Source: BHF-UCL lymphocyte chemotaxis Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of neuron apoptotic process Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of NF-kappaB transcription factor activity Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of T cell differentiation in thymus Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of acute inflammatory response Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of bone resorption Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of cell adhesion Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of eosinophil migration Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of fibronectin-dependent thymocyte migration Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of membrane protein ectodomain proteolysis Inferred from direct assay PubMed 15220135PubMed 17548643. Source: BHF-UCL positive regulation of neutrophil extravasation Inferred from direct assay PubMed 17548643. Source: BHF-UCL positive regulation of protein kinase B signaling cascade Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of protein processing Non-traceable author statement PubMed 17548643. Source: BHF-UCL positive regulation of protein secretion Inferred by curator PubMed 17548643. Source: BHF-UCL positive regulation of thymocyte apoptotic process Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of tumor necrosis factor (ligand) superfamily member 11 production Inferred from sequence or structural similarity. Source: BHF-UCL proteolysis Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell-cell adhesion Inferred from direct assay PubMed 17548643. Source: BHF-UCL
Cellular_component	alpha9-beta1 integrin-ADAM8 complex Inferred from sequence or structural similarity. Source: BHF-UCL cell surface Inferred from direct assay PubMed 17548643. Source: BHF-UCL dense core granule membrane Inferred from direct assay PubMed 17548643. Source: BHF-UCL integral to plasma membrane Inferred from direct assay PubMed 18397961. Source: BHF-UCL phagolysosome Inferred from direct assay PubMed 17548643. Source: BHF-UCL podosome Inferred from direct assay PubMed 15220135. Source: BHF-UCL specific granule Inferred from direct assay PubMed 17548643. Source: BHF-UCL tertiary granule Inferred from direct assay PubMed 17548643. Source: BHF-UCL
Molecular_function	calcium ion binding Inferred from sequence or structural similarity. Source: BHF-UCL metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro metallopeptidase activity Inferred from direct assay PubMed 12777399PubMed 15220135PubMed 17548643. Source: BHF-UCL protein self-association Traceable author statement PubMed 12777399. Source: BHF-UCL zinc ion binding Traceable author statement PubMed 18397961. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P78325-1)

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: P78325-2)

The sequence of this isoform differs from the canonical sequence as follows:
     16-92: AIAPSRPWAL...YTETYTAANG → GPAPREGELR...SRQPQHLCRP
     93-131: Missing.
     596-621: Missing.
     774-799: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: P78325-3)

The sequence of this isoform differs from the canonical sequence as follows:
     650-742: ASGSLPVFVV...GQPARHPASS → GCQPRAGQGR...RGWCGQPWSS
     743-824: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 16

16

Potential

Chain

17 – 824

808

Disintegrin and metalloproteinase domain-containing protein 8

PRO_0000029060

Regions

Topological domain

17 – 655

639

Extracellular Potential

Transmembrane

656 – 676

21

Helical; Potential

Topological domain

677 – 824

148

Cytoplasmic Potential

Domain

200 – 400

201

Peptidase M12B

Domain

408 – 494

87

Disintegrin

Domain

609 – 641

33

EGF-like

Sites

Active site

335

1

By similarity

Metal binding

334

1

Zinc; catalytic

Metal binding

338

1

Zinc; catalytic

Metal binding

344

1

Zinc; catalytic

Amino acid modifications

Glycosylation

67

1

N-linked (GlcNAc...) Potential

Glycosylation

91

1

N-linked (GlcNAc...) Potential

Glycosylation

436

1

N-linked (GlcNAc...) Potential

Glycosylation

612

1

N-linked (GlcNAc...) Potential

Disulfide bond

310 ↔ 395

By similarity

Disulfide bond

351 ↔ 379

By similarity

Disulfide bond

353 ↔ 362

By similarity

Disulfide bond

466 ↔ 486

By similarity

Disulfide bond

613 ↔ 623

By similarity

Disulfide bond

617 ↔ 629

By similarity

Disulfide bond

631 ↔ 640

By similarity

Natural variations

Alternative sequence

16 – 92

77

AIAPS…TAANG → GPAPREGELRPWGHRAQLHP PPAEEQGPAGLRLHRDLYGC QWLRGDGAASRAGPLLLPGP RRGVPGLSRQPQHLCRP in isoform 2.

VSP_046154

Alternative sequence

93 – 131

39

Missing in isoform 2.

VSP_046155

Alternative sequence

596 – 621

26

Missing in isoform 2.

VSP_046156

Alternative sequence

650 – 742

93

ASGSL…HPASS → GCQPRAGQGRGSSPIQGPPR AGPHHPPGPARPTPGLLGGS EEAAPCSSGHCVQPTLPSSC LHPAGTKAGHQANVRTPSAP SQTRGWCGQPWSS in isoform 3.

VSP_046157

Alternative sequence

743 – 824

82

Missing in isoform 3.

VSP_046158

Alternative sequence

774 – 799

26

Missing in isoform 2.

VSP_046159

Natural variant

35

1

W → R. Ref.1 Ref.4
Corresponds to variant rs2275725 [ dbSNP | Ensembl ].

VAR_069144

Natural variant

101

1

G → R.
Corresponds to variant rs11101675 [ dbSNP | Ensembl ].

VAR_059760

Natural variant

189

1

R → W.
Corresponds to variant rs45451297 [ dbSNP | Ensembl ].

VAR_061735

Natural variant

433

1

R → C.
Corresponds to variant rs12257830 [ dbSNP | Ensembl ].

VAR_061736

Natural variant

657

1

F → L. Ref.2
Corresponds to variant rs2275720 [ dbSNP | Ensembl ].

VAR_069145

Natural variant

775

1

I → T.
Corresponds to variant rs3008319 [ dbSNP | Ensembl ].

VAR_061737

Experimental info

Sequence conflict

106

1

F → L in BAA05626. Ref.1

Sequence conflict

372

1

F → L in BAG62738. Ref.2

Sequence conflict

648

1

H → D in BAG62738. Ref.2

Isoform 2:

Sequence conflict

46

1

L → F in BAG62738. Ref.2

Isoform 3:

Sequence conflict

693

1

A → S in BC064500. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

824

Helix Strand Turn

Details...

Beta strand

200 – 208

9

Helix

210 – 216

7

Helix

219 – 237

19

Helix

238 – 240

3

Beta strand

242 – 251

10

Helix

264 – 276

13

Beta strand

286 – 292

7

Beta strand

302 – 304

3

Beta strand

315 – 319

5

Helix

325 – 339

15

Helix

345 – 347

3

Helix

378 – 387

10

Helix

391 – 396

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 3, 2012. Version 2. Checksum: CE3D31330E153DB8	FASTA	824	88,771
	10 20 30 40 50 60 MRGLGLWLLG AMMLPAIAPS RPWALMEQYE VVLPWRLPGP RVRRALPSHL GLHPERVSYV 70 80 90 100 110 120 LGATGHNFTL HLRKNRDLLG SGYTETYTAA NGSEVTEQPR GQDHCFYQGH VEGYPDSAAS 130 140 150 160 170 180 LSTCAGLRGF FQVGSDLHLI EPLDEGGEGG RHAVYQAEHL LQTAGTCGVS DDSLGSLLGP 190 200 210 220 230 240 RTAAVFRPRP GDSLPSRETR YVELYVVVDN AEFQMLGSEA AVRHRVLEVV NHVDKLYQKL 250 260 270 280 290 300 NFRVVLVGLE IWNSQDRFHV SPDPSVTLEN LLTWQARQRT RRHLHDNVQL ITGVDFTGTT 310 320 330 340 350 360 VGFARVSAMC SHSSGAVNQD HSKNPVGVAC TMAHEMGHNL GMDHDENVQG CRCQERFEAG 370 380 390 400 410 420 RCIMAGSIGS SFPRMFSDCS QAYLESFLER PQSVCLANAP DLSHLVGGPV CGNLFVERGE 430 440 450 460 470 480 QCDCGPPEDC RNRCCNSTTC QLAEGAQCAH GTCCQECKVK PAGELCRPKK DMCDLEEFCD 490 500 510 520 530 540 GRHPECPEDA FQENGTPCSG GYCYNGACPT LAQQCQAFWG PGGQAAEESC FSYDILPGCK 550 560 570 580 590 600 ASRYRADMCG VLQCKGGQQP LGRAICIVDV CHALTTEDGT AYEPVPEGTR CGPEKVCWKG 610 620 630 640 650 660 RCQDLHVYRS SNCSAQCHNH GVCNHKQECH CHAGWAPPHC AKLLTEVHAA SGSLPVFVVV 670 680 690 700 710 720 VLVLLAVVLV TLAGIIVYRK ARSRILSRNV APKTTMGRSN PLFHQAASRV PAKGGAPAPS 730 740 750 760 770 780 RGPQELVPTT HPGQPARHPA SSVALKRPPP APPVTVSSPP FPVPVYTRQA PKQVIKPTFA 790 800 810 820 PPVPPVKPGA GAANPGPAEG AVGPKVALKP PIQRKQGAGA PTAP
	Isoform 2 [UniParc]. Checksum: 56F70752E92C2FE4	FASTA	733	78,850
	10 20 30 40 50 60 MRGLGLWLLG AMMLPGPAPR EGELRPWGHR AQLHPPPAEE QGPAGLRLHR DLYGCQWLRG 70 80 90 100 110 120 DGAASRAGPL LLPGPRRGVP GLSRQPQHLC RPQVGSDLHL IEPLDEGGEG GRHAVYQAEH 130 140 150 160 170 180 LLQTAGTCGV SDDSLGSLLG PRTAAVFRPR PGDSLPSRET RYVELYVVVD NAEFQMLGSE 190 200 210 220 230 240 AAVRHRVLEV VNHVDKLYQK LNFRVVLVGL EIWNSQDRFH VSPDPSVTLE NLLTWQARQR 250 260 270 280 290 300 TRRHLHDNVQ LITGVDFTGT TVGFARVSAM CSHSSGAVNQ DHSKNPVGVA CTMAHEMGHN 310 320 330 340 350 360 LGMDHDENVQ GCRCQERFEA GRCIMAGSIG SSFPRMFSDC SQAYLESFLE RPQSVCLANA 370 380 390 400 410 420 PDLSHLVGGP VCGNLFVERG EQCDCGPPED CRNRCCNSTT CQLAEGAQCA HGTCCQECKV 430 440 450 460 470 480 KPAGELCRPK KDMCDLEEFC DGRHPECPED AFQENGTPCS GGYCYNGACP TLAQQCQAFW 490 500 510 520 530 540 GPGGQAAEES CFSYDILPGC KASRYRADMC GVLQCKGGQQ PLGRAICIVD VCHALTTEDG 550 560 570 580 590 600 TAYEPVPEGT RCGPEKVCNH KQECHCHAGW APPHCAKLLT EVHAASGSLP VFVVVVLVLL 610 620 630 640 650 660 AVVLVTLAGI IVYRKARSRI LSRNVAPKTT MGRSNPLFHQ AASRVPAKGG APAPSRGPQE 670 680 690 700 710 720 LVPTTHPGQP ARHPASSVAL KRPPPAPPVT VSSPPFPVPV YTRQAPKQGA VGPKVALKPP 730 IQRKQGAGAP TAP
	Isoform 3 [UniParc]. Checksum: F02B705D4AA89ED3	FASTA	742	80,262
	10 20 30 40 50 60 MRGLGLWLLG AMMLPAIAPS RPWALMEQYE VVLPWRLPGP RVRRALPSHL GLHPERVSYV 70 80 90 100 110 120 LGATGHNFTL HLRKNRDLLG SGYTETYTAA NGSEVTEQPR GQDHCFYQGH VEGYPDSAAS 130 140 150 160 170 180 LSTCAGLRGF FQVGSDLHLI EPLDEGGEGG RHAVYQAEHL LQTAGTCGVS DDSLGSLLGP 190 200 210 220 230 240 RTAAVFRPRP GDSLPSRETR YVELYVVVDN AEFQMLGSEA AVRHRVLEVV NHVDKLYQKL 250 260 270 280 290 300 NFRVVLVGLE IWNSQDRFHV SPDPSVTLEN LLTWQARQRT RRHLHDNVQL ITGVDFTGTT 310 320 330 340 350 360 VGFARVSAMC SHSSGAVNQD HSKNPVGVAC TMAHEMGHNL GMDHDENVQG CRCQERFEAG 370 380 390 400 410 420 RCIMAGSIGS SFPRMFSDCS QAYLESFLER PQSVCLANAP DLSHLVGGPV CGNLFVERGE 430 440 450 460 470 480 QCDCGPPEDC RNRCCNSTTC QLAEGAQCAH GTCCQECKVK PAGELCRPKK DMCDLEEFCD 490 500 510 520 530 540 GRHPECPEDA FQENGTPCSG GYCYNGACPT LAQQCQAFWG PGGQAAEESC FSYDILPGCK 550 560 570 580 590 600 ASRYRADMCG VLQCKGGQQP LGRAICIVDV CHALTTEDGT AYEPVPEGTR CGPEKVCWKG 610 620 630 640 650 660 RCQDLHVYRS SNCSAQCHNH GVCNHKQECH CHAGWAPPHC AKLLTEVHAG CQPRAGQGRG 670 680 690 700 710 720 SSPIQGPPRA GPHHPPGPAR PTPGLLGGSE EAAPCSSGHC VQPTLPSSCL HPAGTKAGHQ 730 740 ANVRTPSAPS QTRGWCGQPW SS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"CD156 (human ADAM8): expression, primary amino acid sequence, and gene location." Yoshiyama K., Higuchi Y., Kataoka M., Matsuura K., Yamamoto S. Genomics 41:56-62(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-35. Tissue: Blood.
[2]	"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 2), VARIANT LEU-657. Tissue: Spleen.
[3]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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 3), VARIANT ARG-35. Tissue: Pancreatic cancer.
[5]	"FLRG, a new ADAM12-associated protein, modulates osteoclast differentiation." Bartholin L., Destaing O., Forissier S., Martel S., Maguer-Satta V., Jurdic P., Rimokh R. Biol. Cell 97:577-588(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FST3.
[6]	"Structure of human ADAM-8 catalytic domain complexed with batimastat." Hall T., Shieh H.S., Day J.E., Caspers N., Chrencik J.E., Williams J.M., Pegg L.E., Pauley A.M., Moon A.F., Krahn J.M., Fischer D.H., Kiefer J.R., Tomasselli A.G., Zack M.D. Acta Crystallogr. F 68:616-621(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 196-403 IN COMPLEX WITH INHIBITOR AND ZINC IONS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D26579 mRNA. Translation: BAA05626.1.
AK301147 mRNA. Translation: BAG62738.1.
AL592071 Genomic DNA. No translation available.
BC064500 mRNA. No translation available.

IPI

IPI00019158.
IPI00910688.

RefSeq

NP_001100.3. NM_001109.4.
NP_001157961.1. NM_001164489.1.
NP_001157962.1. NM_001164490.1.

UniGene

Hs.501574.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4DD8	X-ray	2.10	A/B/C/D	196-403	[»]

ProteinModelPortal

P78325.

SMR

P78325. Positions 50-76, 197-643.

ModBase

Search...

Protein-protein interaction databases

IntAct

P78325. 2 interactions.

STRING

9606.ENSP00000390728.

Protein family/group databases

MEROPS

M12.208.

PTM databases

PhosphoSite

P78325.

Polymorphism databases

DMDM

2499914.

Proteomic databases

PaxDb

P78325.

PRIDE

P78325.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000415217; ENSP00000453855; ENSG00000151651.
ENST00000445355; ENSP00000453302; ENSG00000151651.
ENST00000485491; ENSP00000453043; ENSG00000151651.

GeneID

101.

KEGG

hsa:101.

Organism-specific databases

CTD

101.

GeneCards

GC10M135075.

H-InvDB

HIX0035404.

HGNC

HGNC:215. ADAM8.

MIM

602267. gene.

neXtProt

NX_P78325.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG310718.

HOVERGEN

HBG006978.

InParanoid

P78325.

KO

K06540.

Gene expression databases

CleanEx

HS_ADAM8.

Genevestigator

P78325.

GermOnline

ENSG00000151651. Homo sapiens.

Family and domain databases

Gene3D

3.40.390.10. 1 hit.
4.10.70.10. 1 hit.

InterPro

IPR006586. ADAM_Cys-rich.
IPR001762. Blood-coag_inhib_Disintegrin.
IPR018358. Disintegrin_CS.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]

Pfam

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

PRINTS

PR00289. DISINTEGRIN.

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

BindingDB

P78325.

ChEMBL

CHEMBL5665.

GenomeRNAi

101.

NextBio

381.

SOURCE

Search...

Entry information

Entry name

ADAM8_HUMAN

Accession

Primary (citable) accession number: P78325
Secondary accession number(s): B4DVM6 , H0YL36, H0YLR0, H0YN39

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	October 3, 2012
Last modified:	May 1, 2013
This is version 129 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.