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P78325 (ADAM8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length824 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainEGF-like domain
Signal
Transmembrane
Transmembrane helix
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation 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: Ensembl

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

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_componentalpha9-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 component of 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_functioncalcium 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 824808Disintegrin and metalloproteinase domain-containing protein 8
PRO_0000029060

Regions

Topological domain17 – 655639Extracellular Potential
Transmembrane656 – 67621Helical; Potential
Topological domain677 – 824148Cytoplasmic Potential
Domain200 – 400201Peptidase M12B
Domain408 – 49487Disintegrin
Domain609 – 64133EGF-like

Sites

Active site3351 By similarity
Metal binding3341Zinc; catalytic
Metal binding3381Zinc; catalytic
Metal binding3441Zinc; catalytic

Amino acid modifications

Glycosylation671N-linked (GlcNAc...) Potential
Glycosylation911N-linked (GlcNAc...) Potential
Glycosylation4361N-linked (GlcNAc...) Potential
Glycosylation6121N-linked (GlcNAc...) Potential
Disulfide bond310 ↔ 395 By similarity
Disulfide bond351 ↔ 379 By similarity
Disulfide bond353 ↔ 362 By similarity
Disulfide bond466 ↔ 486 By similarity
Disulfide bond613 ↔ 623 By similarity
Disulfide bond617 ↔ 629 By similarity
Disulfide bond631 ↔ 640 By similarity

Natural variations

Alternative sequence16 – 9277AIAPS…TAANG → GPAPREGELRPWGHRAQLHP PPAEEQGPAGLRLHRDLYGC QWLRGDGAASRAGPLLLPGP RRGVPGLSRQPQHLCRP in isoform 2.
VSP_046154
Alternative sequence93 – 13139Missing in isoform 2.
VSP_046155
Alternative sequence596 – 62126Missing in isoform 2.
VSP_046156
Alternative sequence650 – 74293ASGSL…HPASS → GCQPRAGQGRGSSPIQGPPR AGPHHPPGPARPTPGLLGGS EEAAPCSSGHCVQPTLPSSC LHPAGTKAGHQANVRTPSAP SQTRGWCGQPWSS in isoform 3.
VSP_046157
Alternative sequence743 – 82482Missing in isoform 3.
VSP_046158
Alternative sequence774 – 79926Missing in isoform 2.
VSP_046159
Natural variant351W → R. Ref.1 Ref.4
Corresponds to variant rs2275725 [ dbSNP | Ensembl ].
VAR_069144
Natural variant1011G → R.
Corresponds to variant rs11101675 [ dbSNP | Ensembl ].
VAR_059760
Natural variant1891R → W.
Corresponds to variant rs45451297 [ dbSNP | Ensembl ].
VAR_061735
Natural variant4331R → C.
Corresponds to variant rs12257830 [ dbSNP | Ensembl ].
VAR_061736
Natural variant6571F → L. Ref.2
Corresponds to variant rs2275720 [ dbSNP | Ensembl ].
VAR_069145
Natural variant7751I → T.
Corresponds to variant rs3008319 [ dbSNP | Ensembl ].
VAR_061737

Experimental info

Sequence conflict1061F → L in BAA05626. Ref.1
Sequence conflict3721F → L in BAG62738. Ref.2
Sequence conflict6481H → D in BAG62738. Ref.2
Isoform 2:
Sequence conflict461L → F in BAG62738. Ref.2
Isoform 3:
Sequence conflict6931A → S in BC064500. Ref.4

Secondary structure

.......................... 824
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: CE3D31330E153DB8

FASTA82488,771
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 56F70752E92C2FE4
Show »

FASTA73378,850
Isoform 3 [UniParc].

Checksum: F02B705D4AA89ED3
Show »

FASTA74280,262

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
RefSeqNP_001100.3. NM_001109.4.
NP_001157961.1. NM_001164489.1.
NP_001157962.1. NM_001164490.1.
UniGeneHs.501574.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4DD8X-ray2.10A/B/C/D196-403[»]
ProteinModelPortalP78325.
SMRP78325. Positions 50-76, 194-646.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP78325. 2 interactions.
STRING9606.ENSP00000390728.

Chemistry

BindingDBP78325.
ChEMBLCHEMBL5665.

Protein family/group databases

MEROPSM12.208.

PTM databases

PhosphoSiteP78325.

Polymorphism databases

DMDM2499914.

Proteomic databases

PaxDbP78325.
PRIDEP78325.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000415217; ENSP00000453855; ENSG00000151651. [P78325-3]
ENST00000445355; ENSP00000453302; ENSG00000151651. [P78325-1]
ENST00000485491; ENSP00000453043; ENSG00000151651. [P78325-2]
GeneID101.
KEGGhsa:101.
UCSCuc021qbe.1. human. [P78325-1]

Organism-specific databases

CTD101.
GeneCardsGC10M135075.
H-InvDBHIX0035404.
HGNCHGNC:215. ADAM8.
MIM602267. gene.
neXtProtNX_P78325.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG310718.
HOVERGENHBG006978.
InParanoidP78325.
KOK06540.
OMANGTPCPG.
OrthoDBEOG74N5G6.
TreeFamTF314733.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP78325.
CleanExHS_ADAM8.
GenevestigatorP78325.

Family and domain databases

Gene3D3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProIPR006586. 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]
PfamPF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
PRINTSPR00289. DISINTEGRIN.
SMARTSM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view]
SUPFAMSSF57552. SSF57552. 1 hit.
PROSITEPS50215. 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]
ProtoNetSearch...

Other

GeneWikiADAM8.
GenomeRNAi101.
NextBio381.
PROP78325.
SOURCESearch...

Entry information

Entry nameADAM8_HUMAN
AccessionPrimary (citable) accession number: P78325
Secondary accession number(s): B4DVM6 expand/collapse secondary AC list , H0YL36, H0YLR0, H0YN39
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 3, 2012
Last modified: March 19, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries