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P78325

- ADAM8_HUMAN

UniProt

P78325 - ADAM8_HUMAN

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Protein

Disintegrin and metalloproteinase domain-containing protein 8

Gene

ADAM8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Possible involvement in extravasation of leukocytes.

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi334 – 3341Zinc; catalytic
Active sitei335 – 3351PROSITE-ProRule annotation
Metal bindingi338 – 3381Zinc; catalytic
Metal bindingi344 – 3441Zinc; catalytic

GO - Molecular functioni

  1. calcium ion binding Source: BHF-UCL
  2. cell adhesion molecule binding Source: BHF-UCL
  3. metalloendopeptidase activity Source: InterPro
  4. metallopeptidase activity Source: BHF-UCL
  5. protein self-association Source: BHF-UCL
  6. zinc ion binding Source: BHF-UCL

GO - Biological processi

  1. activation of MAPK activity involved in innate immune response Source: BHF-UCL
  2. angiogenesis Source: BHF-UCL
  3. cell morphogenesis Source: BHF-UCL
  4. cellular response to hypoxia Source: BHF-UCL
  5. extracellular matrix disassembly Source: Reactome
  6. extracellular matrix organization Source: Reactome
  7. inflammatory response Source: BHF-UCL
  8. leukocyte migration involved in inflammatory response Source: BHF-UCL
  9. lymphocyte chemotaxis Source: BHF-UCL
  10. negative regulation of neuron apoptotic process Source: BHF-UCL
  11. positive regulation of acute inflammatory response Source: BHF-UCL
  12. positive regulation of bone resorption Source: BHF-UCL
  13. positive regulation of cell adhesion Source: BHF-UCL
  14. positive regulation of eosinophil migration Source: BHF-UCL
  15. positive regulation of fibronectin-dependent thymocyte migration Source: BHF-UCL
  16. positive regulation of membrane protein ectodomain proteolysis Source: BHF-UCL
  17. positive regulation of neutrophil extravasation Source: BHF-UCL
  18. positive regulation of NF-kappaB transcription factor activity Source: BHF-UCL
  19. positive regulation of protein kinase B signaling Source: BHF-UCL
  20. positive regulation of protein processing Source: BHF-UCL
  21. positive regulation of protein secretion Source: BHF-UCL
  22. positive regulation of T cell differentiation in thymus Source: BHF-UCL
  23. positive regulation of thymocyte apoptotic process Source: BHF-UCL
  24. positive regulation of tumor necrosis factor (ligand) superfamily member 11 production Source: BHF-UCL
  25. regulation of cell-cell adhesion Source: BHF-UCL
  26. single organismal cell-cell adhesion Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.

Protein family/group databases

MEROPSiM12.208.

Names & Taxonomyi

Protein namesi
Recommended name:
Disintegrin and metalloproteinase domain-containing protein 8 (EC:3.4.24.-)
Short name:
ADAM 8
Alternative name(s):
Cell surface antigen MS2
CD_antigen: CD156a
Gene namesi
Name:ADAM8
Synonyms:MS2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:215. ADAM8.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini17 – 655639ExtracellularSequence AnalysisAdd
BLAST
Transmembranei656 – 67621HelicalSequence AnalysisAdd
BLAST
Topological domaini677 – 824148CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. alpha9-beta1 integrin-ADAM8 complex Source: BHF-UCL
  2. cell surface Source: BHF-UCL
  3. cytoplasm Source: BHF-UCL
  4. dense core granule membrane Source: BHF-UCL
  5. integral component of plasma membrane Source: BHF-UCL
  6. phagolysosome Source: BHF-UCL
  7. plasma membrane Source: BHF-UCL
  8. podosome Source: BHF-UCL
  9. specific granule Source: BHF-UCL
  10. tertiary granule Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence AnalysisAdd
BLAST
Chaini17 – 824808Disintegrin and metalloproteinase domain-containing protein 8PRO_0000029060Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi67 – 671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi91 – 911N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi310 ↔ 395By similarity
Disulfide bondi351 ↔ 379By similarity
Disulfide bondi353 ↔ 362By similarity
Glycosylationi436 – 4361N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi466 ↔ 486By similarity
Glycosylationi612 – 6121N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi613 ↔ 623By similarity
Disulfide bondi617 ↔ 629By similarity
Disulfide bondi631 ↔ 640By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP78325.
PaxDbiP78325.
PRIDEiP78325.

PTM databases

PhosphoSiteiP78325.

Expressioni

Tissue specificityi

Expressed on neutrophils and monocytes.

Gene expression databases

CleanExiHS_ADAM8.
ExpressionAtlasiP78325. baseline and differential.
GenevestigatoriP78325.

Interactioni

Subunit structurei

Interacts with FST3.2 Publications

Protein-protein interaction databases

IntActiP78325. 2 interactions.
STRINGi9606.ENSP00000390728.

Structurei

Secondary structure

1
824
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi200 – 2089Combined sources
Helixi210 – 2167Combined sources
Helixi219 – 23719Combined sources
Helixi238 – 2403Combined sources
Beta strandi242 – 25110Combined sources
Helixi264 – 27613Combined sources
Beta strandi286 – 2927Combined sources
Beta strandi302 – 3043Combined sources
Beta strandi315 – 3195Combined sources
Helixi325 – 33915Combined sources
Helixi345 – 3473Combined sources
Helixi378 – 38710Combined sources
Helixi391 – 3966Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DD8X-ray2.10A/B/C/D196-403[»]
ProteinModelPortaliP78325.
SMRiP78325. Positions 197-605.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini200 – 400201Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini408 – 49487DisintegrinPROSITE-ProRule annotationAdd
BLAST
Domaini609 – 64133EGF-likePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 disintegrin domain.PROSITE-ProRule annotation
Contains 1 EGF-like domain.PROSITE-ProRule annotation
Contains 1 peptidase M12B domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG310718.
GeneTreeiENSGT00760000118888.
HOVERGENiHBG006978.
InParanoidiP78325.
KOiK06540.
OMAiCYNGACP.
OrthoDBiEOG74N5G6.
TreeFamiTF314733.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProiIPR006586. 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]
PfamiPF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
PRINTSiPR00289. DISINTEGRIN.
SMARTiSM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view]
SUPFAMiSSF57552. SSF57552. 1 hit.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P78325-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MRGLGLWLLG AMMLPAIAPS RPWALMEQYE VVLPWRLPGP RVRRALPSHL
60 70 80 90 100
GLHPERVSYV LGATGHNFTL HLRKNRDLLG SGYTETYTAA NGSEVTEQPR
110 120 130 140 150
GQDHCFYQGH VEGYPDSAAS LSTCAGLRGF FQVGSDLHLI EPLDEGGEGG
160 170 180 190 200
RHAVYQAEHL LQTAGTCGVS DDSLGSLLGP RTAAVFRPRP GDSLPSRETR
210 220 230 240 250
YVELYVVVDN AEFQMLGSEA AVRHRVLEVV NHVDKLYQKL NFRVVLVGLE
260 270 280 290 300
IWNSQDRFHV SPDPSVTLEN LLTWQARQRT RRHLHDNVQL ITGVDFTGTT
310 320 330 340 350
VGFARVSAMC SHSSGAVNQD HSKNPVGVAC TMAHEMGHNL GMDHDENVQG
360 370 380 390 400
CRCQERFEAG RCIMAGSIGS SFPRMFSDCS QAYLESFLER PQSVCLANAP
410 420 430 440 450
DLSHLVGGPV CGNLFVERGE QCDCGPPEDC RNRCCNSTTC QLAEGAQCAH
460 470 480 490 500
GTCCQECKVK PAGELCRPKK DMCDLEEFCD GRHPECPEDA FQENGTPCSG
510 520 530 540 550
GYCYNGACPT LAQQCQAFWG PGGQAAEESC FSYDILPGCK ASRYRADMCG
560 570 580 590 600
VLQCKGGQQP LGRAICIVDV CHALTTEDGT AYEPVPEGTR CGPEKVCWKG
610 620 630 640 650
RCQDLHVYRS SNCSAQCHNH GVCNHKQECH CHAGWAPPHC AKLLTEVHAA
660 670 680 690 700
SGSLPVFVVV VLVLLAVVLV TLAGIIVYRK ARSRILSRNV APKTTMGRSN
710 720 730 740 750
PLFHQAASRV PAKGGAPAPS RGPQELVPTT HPGQPARHPA SSVALKRPPP
760 770 780 790 800
APPVTVSSPP FPVPVYTRQA PKQVIKPTFA PPVPPVKPGA GAANPGPAEG
810 820
AVGPKVALKP PIQRKQGAGA PTAP
Length:824
Mass (Da):88,771
Last modified:October 3, 2012 - v2
Checksum:iCE3D31330E153DB8
GO
Isoform 2 (identifier: P78325-2) [UniParc]FASTAAdd to Basket

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.Curated

Show »
Length:733
Mass (Da):78,850
Checksum:i56F70752E92C2FE4
GO
Isoform 3 (identifier: P78325-3) [UniParc]FASTAAdd to Basket

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.Curated

Show »
Length:742
Mass (Da):80,262
Checksum:iF02B705D4AA89ED3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1061F → L in BAA05626. (PubMed:9126482)Curated
Sequence conflicti372 – 3721F → L in BAG62738. (PubMed:14702039)Curated
Sequence conflicti648 – 6481H → D in BAG62738. (PubMed:14702039)Curated
Isoform 2 (identifier: P78325-2)
Sequence conflicti46 – 461L → F in BAG62738. (PubMed:14702039)Curated
Isoform 3 (identifier: P78325-3)
Sequence conflicti693 – 6931A → S in BC064500. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti35 – 351W → R.2 Publications
Corresponds to variant rs2275725 [ dbSNP | Ensembl ].
VAR_069144
Natural varianti101 – 1011G → R.
Corresponds to variant rs11101675 [ dbSNP | Ensembl ].
VAR_059760
Natural varianti189 – 1891R → W.
Corresponds to variant rs45451297 [ dbSNP | Ensembl ].
VAR_061735
Natural varianti433 – 4331R → C.
Corresponds to variant rs12257830 [ dbSNP | Ensembl ].
VAR_061736
Natural varianti657 – 6571F → L.1 Publication
Corresponds to variant rs2275720 [ dbSNP | Ensembl ].
VAR_069145
Natural varianti775 – 7751I → T.
Corresponds to variant rs3008319 [ dbSNP | Ensembl ].
VAR_061737

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei16 – 9277AIAPS…TAANG → GPAPREGELRPWGHRAQLHP PPAEEQGPAGLRLHRDLYGC QWLRGDGAASRAGPLLLPGP RRGVPGLSRQPQHLCRP in isoform 2. 1 PublicationVSP_046154Add
BLAST
Alternative sequencei93 – 13139Missing in isoform 2. 1 PublicationVSP_046155Add
BLAST
Alternative sequencei596 – 62126Missing in isoform 2. 1 PublicationVSP_046156Add
BLAST
Alternative sequencei650 – 74293ASGSL…HPASS → GCQPRAGQGRGSSPIQGPPR AGPHHPPGPARPTPGLLGGS EEAAPCSSGHCVQPTLPSSC LHPAGTKAGHQANVRTPSAP SQTRGWCGQPWSS in isoform 3. 1 PublicationVSP_046157Add
BLAST
Alternative sequencei743 – 82482Missing in isoform 3. 1 PublicationVSP_046158Add
BLAST
Alternative sequencei774 – 79926Missing in isoform 2. 1 PublicationVSP_046159Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26579 mRNA. Translation: BAA05626.1.
AK301147 mRNA. Translation: BAG62738.1.
AL592071 Genomic DNA. No translation available.
BC064500 mRNA. No translation available.
CCDSiCCDS31319.2. [P78325-1]
CCDS58102.1. [P78325-2]
CCDS58103.1. [P78325-3]
RefSeqiNP_001100.3. NM_001109.4. [P78325-1]
NP_001157961.1. NM_001164489.1. [P78325-3]
NP_001157962.1. NM_001164490.1. [P78325-2]
UniGeneiHs.501574.

Genome annotation databases

EnsembliENST00000415217; ENSP00000453855; ENSG00000151651. [P78325-3]
ENST00000445355; ENSP00000453302; ENSG00000151651. [P78325-1]
ENST00000485491; ENSP00000453043; ENSG00000151651. [P78325-2]
GeneIDi101.
KEGGihsa:101.
UCSCiuc021qbe.1. human. [P78325-1]

Polymorphism databases

DMDMi408359955.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26579 mRNA. Translation: BAA05626.1 .
AK301147 mRNA. Translation: BAG62738.1 .
AL592071 Genomic DNA. No translation available.
BC064500 mRNA. No translation available.
CCDSi CCDS31319.2. [P78325-1 ]
CCDS58102.1. [P78325-2 ]
CCDS58103.1. [P78325-3 ]
RefSeqi NP_001100.3. NM_001109.4. [P78325-1 ]
NP_001157961.1. NM_001164489.1. [P78325-3 ]
NP_001157962.1. NM_001164490.1. [P78325-2 ]
UniGenei Hs.501574.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4DD8 X-ray 2.10 A/B/C/D 196-403 [» ]
ProteinModelPortali P78325.
SMRi P78325. Positions 197-605.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P78325. 2 interactions.
STRINGi 9606.ENSP00000390728.

Chemistry

ChEMBLi CHEMBL5665.

Protein family/group databases

MEROPSi M12.208.

PTM databases

PhosphoSitei P78325.

Polymorphism databases

DMDMi 408359955.

Proteomic databases

MaxQBi P78325.
PaxDbi P78325.
PRIDEi P78325.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000415217 ; ENSP00000453855 ; ENSG00000151651 . [P78325-3 ]
ENST00000445355 ; ENSP00000453302 ; ENSG00000151651 . [P78325-1 ]
ENST00000485491 ; ENSP00000453043 ; ENSG00000151651 . [P78325-2 ]
GeneIDi 101.
KEGGi hsa:101.
UCSCi uc021qbe.1. human. [P78325-1 ]

Organism-specific databases

CTDi 101.
GeneCardsi GC10M135075.
H-InvDB HIX0035404.
HGNCi HGNC:215. ADAM8.
MIMi 602267. gene.
neXtProti NX_P78325.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG310718.
GeneTreei ENSGT00760000118888.
HOVERGENi HBG006978.
InParanoidi P78325.
KOi K06540.
OMAi CYNGACP.
OrthoDBi EOG74N5G6.
TreeFami TF314733.

Enzyme and pathway databases

Reactomei REACT_118572. Degradation of the extracellular matrix.

Miscellaneous databases

ChiTaRSi ADAM8. human.
GeneWikii ADAM8.
GenomeRNAii 101.
NextBioi 381.
PROi P78325.
SOURCEi Search...

Gene expression databases

CleanExi HS_ADAM8.
ExpressionAtlasi P78325. baseline and differential.
Genevestigatori P78325.

Family and domain databases

Gene3Di 3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProi 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 ]
Pfami PF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view ]
PRINTSi PR00289. DISINTEGRIN.
SMARTi SM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view ]
SUPFAMi SSF57552. SSF57552. 1 hit.
PROSITEi PS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 196-403 IN COMPLEX WITH INHIBITOR AND ZINC IONS.

Entry informationi

Entry nameiADAM8_HUMAN
AccessioniPrimary (citable) accession number: P78325
Secondary accession number(s): B4DVM6
, H0YL36, H0YLR0, H0YN39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 3, 2012
Last modified: November 26, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Peptidase families
    Classification of peptidase families and list of entries
  8. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3