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O43184 (ADA12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Disintegrin and metalloproteinase domain-containing protein 12

Short name=ADAM 12
EC=3.4.24.-
Alternative name(s):
Meltrin-alpha
Gene names
Name:ADAM12
Synonyms:MLTN
ORF Names:UNQ346/PRO545
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length909 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in skeletal muscle regeneration, specifically at the onset of cell fusion. Also involved in macrophage-derived giant cells (MGC) and osteoclast formation from mononuclear precursors By similarity.

Cofactor

Binds 1 zinc ion per subunit.

Subunit structure

Interacts with alpha-actinin-2 and with syndecans By similarity. Interacts with SH3PXD2A. Interacts with FST3. Interacts with GNB2L1/RACK1; the interaction is required for PKC-dependent translocation of ADAM12 to the cell membrane. Ref.8 Ref.9 Ref.10 Ref.11

Subcellular location

Isoform 1: Cell membrane; Single-pass type I membrane protein.

Isoform 2: Secreted.

Isoform 3: Secreted Potential.

Isoform 4: Secreted Potential.

Tissue specificity

Isoform 1 is expressed in placenta and skeletal, cardiac, and smooth muscle. Isoform 2 seems to be expressed only in placenta or in embryo and fetus. Both forms were expressed in some tumor cells lines. Not detected in brain, lung, liver, kidney or pancreas.

Domain

The cysteine-rich domain supports cell adhesion through syndecans and triggers signaling events that lead to beta-1 integrin-dependent cell spreading. In carcinomas cells the binding of this domain to syndecans does not allow the integrin-mediated cell spreading.

The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Post-translational modification

The precursor is cleaved by a furin endopeptidase By similarity.

Sequence similarities

Contains 1 disintegrin domain.

Contains 1 EGF-like domain.

Contains 1 peptidase M12B domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FSTL3O956334EBI-2625865,EBI-2625790

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43184-1)

Also known as: 12L;

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: O43184-2)

Also known as: 12S;

The sequence of this isoform differs from the canonical sequence as follows:
     705-738: DNQGLTIGILVTILCLLAAGFVVYLKRKTLIRLL → EARQEAAESNRERGQGQEPVGSQEHASTASLTLI
     739-909: Missing.
Isoform 3 (identifier: O43184-3)

The sequence of this isoform differs from the canonical sequence as follows:
     114-116: Missing.
     705-738: DNQGLTIGILVTILCLLAAGFVVYLKRKTLIRLL → EARQEAAESNRERGQGQEPVGSQEHASTASLTLI
     739-909: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: O43184-4)

The sequence of this isoform differs from the canonical sequence as follows:
     114-116: Missing.
     705-740: DNQGLTIGILVTILCLLAAGFVVYLKRKTLIRLLFT → GKEARQEAAESNRERGQGQEPVGSQEHASTASLTLI
     741-909: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Propeptide29 – 207179 By similarity
PRO_0000029078
Chain208 – 909702Disintegrin and metalloproteinase domain-containing protein 12
PRO_0000029079

Regions

Topological domain208 – 708501Extracellular Potential
Transmembrane709 – 72921Helical; Potential
Topological domain730 – 909180Cytoplasmic Potential
Domain214 – 416203Peptidase M12B
Domain424 – 51087Disintegrin
Domain656 – 68833EGF-like
Motif177 – 1848Cysteine switch By similarity
Motif828 – 8347SH3-binding; class II By similarity
Motif834 – 8418SH3-binding; class I By similarity
Motif885 – 8917SH3-binding; class I By similarity
Compositional bias514 – 649136Cys-rich

Sites

Active site3511
Metal binding1791Zinc; in inhibited form By similarity
Metal binding3501Zinc; catalytic
Metal binding3541Zinc; catalytic
Metal binding3601Zinc; catalytic

Amino acid modifications

Modified residue9071Phosphotyrosine; by SRC By similarity
Glycosylation1111N-linked (GlcNAc...) Potential
Glycosylation1491N-linked (GlcNAc...) Potential
Glycosylation3811N-linked (GlcNAc...) Potential
Glycosylation4521N-linked (GlcNAc...) Potential
Glycosylation6511N-linked (GlcNAc...) Potential
Disulfide bond325 ↔ 411 By similarity
Disulfide bond367 ↔ 395 By similarity
Disulfide bond369 ↔ 378 By similarity
Disulfide bond482 ↔ 502 By similarity
Disulfide bond660 ↔ 670 By similarity
Disulfide bond664 ↔ 676 By similarity
Disulfide bond678 ↔ 687 By similarity

Natural variations

Alternative sequence114 – 1163Missing in isoform 3 and isoform 4.
VSP_031001
Alternative sequence705 – 74036DNQGL…RLLFT → GKEARQEAAESNRERGQGQE PVGSQEHASTASLTLI in isoform 4.
VSP_031002
Alternative sequence705 – 73834DNQGL…LIRLL → EARQEAAESNRERGQGQEPV GSQEHASTASLTLI in isoform 2 and isoform 3.
VSP_005476
Alternative sequence739 – 909171Missing in isoform 2 and isoform 3.
VSP_005477
Alternative sequence741 – 909169Missing in isoform 4.
VSP_031003
Natural variant481G → R. Ref.1 Ref.3 Ref.5 Ref.6
Corresponds to variant rs3740199 [ dbSNP | Ensembl ].
VAR_038542
Natural variant3011D → H in a breast cancer sample; somatic mutation. Ref.12
VAR_036143
Natural variant4791G → E in a breast cancer sample; somatic mutation. Ref.12
VAR_036144
Natural variant7121G → E in a cutaneous metastatic melanoma sample; somatic mutation. Ref.13
VAR_066310
Natural variant7921L → F in a breast cancer sample; somatic mutation. Ref.12
VAR_036145
Natural variant8931P → S in a cutaneous metastatic melanoma sample; somatic mutation. Ref.13
VAR_066311

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (12L) [UniParc].

Last modified May 5, 2009. Version 3.
Checksum: E28131C64C4304AB

FASTA90999,542
        10         20         30         40         50         60 
MAARPLPVSP ARALLLALAG ALLAPCEARG VSLWNQGRAD EVVSASVGSG DLWIPVKSFD 

        70         80         90        100        110        120 
SKNHPEVLNI RLQRESKELI INLERNEGLI ASSFTETHYL QDGTDVSLAR NYTVILGHCY 

       130        140        150        160        170        180 
YHGHVRGYSD SAVSLSTCSG LRGLIVFENE SYVLEPMKSA TNRYKLFPAK KLKSVRGSCG 

       190        200        210        220        230        240 
SHHNTPNLAA KNVFPPPSQT WARRHKRETL KATKYVELVI VADNREFQRQ GKDLEKVKQR 

       250        260        270        280        290        300 
LIEIANHVDK FYRPLNIRIV LVGVEVWNDM DKCSVSQDPF TSLHEFLDWR KMKLLPRKSH 

       310        320        330        340        350        360 
DNAQLVSGVY FQGTTIGMAP IMSMCTADQS GGIVMDHSDN PLGAAVTLAH ELGHNFGMNH 

       370        380        390        400        410        420 
DTLDRGCSCQ MAVEKGGCIM NASTGYPFPM VFSSCSRKDL ETSLEKGMGV CLFNLPEVRE 

       430        440        450        460        470        480 
SFGGQKCGNR FVEEGEECDC GEPEECMNRC CNATTCTLKP DAVCAHGLCC EDCQLKPAGT 

       490        500        510        520        530        540 
ACRDSSNSCD LPEFCTGASP HCPANVYLHD GHSCQDVDGY CYNGICQTHE QQCVTLWGPG 

       550        560        570        580        590        600 
AKPAPGICFE RVNSAGDPYG NCGKVSKSSF AKCEMRDAKC GKIQCQGGAS RPVIGTNAVS 

       610        620        630        640        650        660 
IETNIPLQQG GRILCRGTHV YLGDDMPDPG LVLAGTKCAD GKICLNRQCQ NISVFGVHEC 

       670        680        690        700        710        720 
AMQCHGRGVC NNRKNCHCEA HWAPPFCDKF GFGGSTDSGP IRQADNQGLT IGILVTILCL 

       730        740        750        760        770        780 
LAAGFVVYLK RKTLIRLLFT NKKTTIEKLR CVRPSRPPRG FQPCQAHLGH LGKGLMRKPP 

       790        800        810        820        830        840 
DSYPPKDNPR RLLQCQNVDI SRPLNGLNVP QPQSTQRVLP PLHRAPRAPS VPARPLPAKP 

       850        860        870        880        890        900 
ALRQAQGTCK PNPPQKPLPA DPLARTTRLT HALARTPGQW ETGLRLAPLR PAPQYPHQVP 


RSTHTAYIK 

« Hide

Isoform 2 (12S) [UniParc].

Checksum: 19699D2852ED28F6
Show »

FASTA73880,403
Isoform 3 [UniParc].

Checksum: 664D4EDA47F8B533
Show »

FASTA73580,078
Isoform 4 [UniParc].

Checksum: D86FE821BCBC62C6
Show »

FASTA73780,263

References

« Hide 'large scale' references
[1]"A novel, secreted form of human ADAM 12 (meltrin alpha) provokes myogenesis in vivo."
Gilpin B.J., Loechel F., Mattei M.-G., Engvall E., Albrechtsen R., Wewer U.M.
J. Biol. Chem. 273:157-166(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT ARG-48.
Tissue: Placenta.
[2]Gilpin B.J., Loechel F., Mattei M.-G., Engvall E., Albrechtsen R., Wewer U.M.
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 36.
[3]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT ARG-48.
[4]"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].
[5]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. expand/collapse author list , 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], VARIANT ARG-48.
[6]"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 4), VARIANT ARG-48.
Tissue: Placenta.
[7]"Human ADAM 12 (meltrin alpha) is an active metalloprotease."
Loechel F., Gilpin B.J., Engvall E., Albrechtsen R., Wewer U.M.
J. Biol. Chem. 273:16993-16997(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[8]"The cysteine-rich domain of human ADAM 12 supports cell adhesion through syndecans and triggers signaling events that lead to beta1 integrin-dependent cell spreading."
Iba K., Albrechtsen R., Gilpin B.J., Froehlich C., Loechel F., Zolkiewska A., Ishiguro K., Kojima T., Liu W., Langford J.K., Sanderson R.D., Brakebusch C., Faessler R., Wewer U.M.
J. Cell Biol. 149:1143-1156(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SYNDECANS.
[9]"The adaptor protein fish associates with members of the ADAMs family and localizes to podosomes of Src-transformed cells."
Abram C.L., Seals D.F., Pass I., Salinsky D., Maurer L., Roth T.M., Courtneidge S.A.
J. Biol. Chem. 278:16844-16851(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SH3PXD2A.
[10]"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.
[11]"RACK1, a new ADAM12 interacting protein. Contribution to liver fibrogenesis."
Bourd-Boittin K., Le Pabic H., Bonnier D., L'Helgoualc'h A., Theret N.
J. Biol. Chem. 283:26000-26009(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GNB2L1.
[12]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] HIS-301; GLU-479 AND PHE-792.
[13]"Analysis of the disintegrin-metalloproteinases family reveals ADAM29 and ADAM7 are often mutated in melanoma."
Wei X., Moncada-Pazos A., Cal S., Soria-Valles C., Gartner J., Rudloff U., Lin J.C., Rosenberg S.A., Lopez-Otin C., Samuels Y.
Hum. Mutat. 32:E2148-E2175(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLU-712 AND SER-893.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF023476 mRNA. Translation: AAC08702.2.
AF023477 mRNA. Translation: AAC08703.2.
AY358878 mRNA. Translation: AAQ89237.1.
AL589787 expand/collapse EMBL AC list , AC022015, AC026226, AC063963 Genomic DNA. Translation: CAI40682.1.
AL589787 expand/collapse EMBL AC list , AC022015, AC026226, AC063963 Genomic DNA. Translation: CAI40683.1.
CH471066 Genomic DNA. Translation: EAW49206.1.
CH471066 Genomic DNA. Translation: EAW49209.1.
BC060804 mRNA. Translation: AAH60804.1.
RefSeqNP_001275903.1. NM_001288974.1.
NP_001275904.1. NM_001288975.1.
NP_003465.3. NM_003474.5.
NP_067673.2. NM_021641.4.
UniGeneHs.594351.
Hs.741333.

3D structure databases

ProteinModelPortalO43184.
SMRO43184. Positions 213-690.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113731. 4 interactions.
IntActO43184. 2 interactions.
MINTMINT-246189.
STRING9606.ENSP00000357668.

Chemistry

BindingDBO43184.
ChEMBLCHEMBL5030.

Protein family/group databases

MEROPSM12.212.

PTM databases

PhosphoSiteO43184.

Proteomic databases

PaxDbO43184.
PRIDEO43184.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368676; ENSP00000357665; ENSG00000148848. [O43184-2]
ENST00000368679; ENSP00000357668; ENSG00000148848. [O43184-1]
GeneID8038.
KEGGhsa:8038.
UCSCuc001ljk.2. human. [O43184-1]
uc001ljl.4. human. [O43184-4]
uc001ljm.3. human. [O43184-2]
uc001ljn.3. human. [O43184-3]

Organism-specific databases

CTD8038.
GeneCardsGC10M127693.
H-InvDBHIX0009299.
HGNCHGNC:190. ADAM12.
HPAHPA030866.
HPA030867.
HPA030868.
MIM602714. gene.
neXtProtNX_O43184.
PharmGKBPA24507.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG294463.
HOGENOMHOG000230883.
HOVERGENHBG006978.
InParanoidO43184.
KOK06835.
OMAPPFCDKF.
OrthoDBEOG7F7W89.
PhylomeDBO43184.
TreeFamTF314733.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

ArrayExpressO43184.
BgeeO43184.
CleanExHS_ADAM12.
GenevestigatorO43184.

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.
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.
[Graphical view]
SUPFAMSSF57552. SSF57552. 1 hit.
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSADAM12. human.
GeneWikiADAM12.
GenomeRNAi8038.
NextBio30628.
PROO43184.
SOURCESearch...

Entry information

Entry nameADA12_HUMAN
AccessionPrimary (citable) accession number: O43184
Secondary accession number(s): O60470 expand/collapse secondary AC list , Q5JRP0, Q5JRP1, Q6P9E3, Q6UWB0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 5, 2009
Last modified: April 16, 2014
This is version 142 of the entry and version 3 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

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