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O43184

- ADA12_HUMAN

UniProt

O43184 - ADA12_HUMAN

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Protein

Disintegrin and metalloproteinase domain-containing protein 12

Gene

ADAM12

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

Functioni

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).By similarity

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi179 – 1791Zinc; in inhibited formBy similarity
Metal bindingi350 – 3501Zinc; catalytic
Active sitei351 – 3511
Metal bindingi354 – 3541Zinc; catalytic
Metal bindingi360 – 3601Zinc; catalytic

GO - Molecular functioni

  1. metalloendopeptidase activity Source: InterPro
  2. metallopeptidase activity Source: ProtInc
  3. SH3 domain binding Source: BHF-UCL
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
  2. epidermal growth factor receptor signaling pathway Source: Reactome
  3. myoblast fusion Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_9417. Signaling by EGFR.

Protein family/group databases

MEROPSiM12.212.

Names & Taxonomyi

Protein namesi
Recommended name:
Disintegrin and metalloproteinase domain-containing protein 12 (EC:3.4.24.-)
Short name:
ADAM 12
Alternative name(s):
Meltrin-alpha
Gene namesi
Name:ADAM12
Synonyms:MLTN
ORF Names:UNQ346/PRO545
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:190. ADAM12.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini208 – 708501ExtracellularSequence AnalysisAdd
BLAST
Transmembranei709 – 72921HelicalSequence AnalysisAdd
BLAST
Topological domaini730 – 909180CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. plasma membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24507.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence AnalysisAdd
BLAST
Propeptidei29 – 207179By similarityPRO_0000029078Add
BLAST
Chaini208 – 909702Disintegrin and metalloproteinase domain-containing protein 12PRO_0000029079Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi111 – 1111N-linked (GlcNAc...)Sequence Analysis
Glycosylationi149 – 1491N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi325 ↔ 411By similarity
Disulfide bondi367 ↔ 395By similarity
Disulfide bondi369 ↔ 378By similarity
Glycosylationi381 – 3811N-linked (GlcNAc...)Sequence Analysis
Glycosylationi452 – 4521N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi482 ↔ 502By similarity
Glycosylationi651 – 6511N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi660 ↔ 670By similarity
Disulfide bondi664 ↔ 676By similarity
Disulfide bondi678 ↔ 687By similarity
Modified residuei907 – 9071Phosphotyrosine; by SRCBy similarity

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

MaxQBiO43184.
PaxDbiO43184.
PRIDEiO43184.

PTM databases

PhosphoSiteiO43184.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiO43184.
CleanExiHS_ADAM12.
ExpressionAtlasiO43184. baseline and differential.
GenevestigatoriO43184.

Organism-specific databases

HPAiHPA030866.
HPA030867.
HPA030868.

Interactioni

Subunit structurei

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.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FSTL3O956334EBI-2625865,EBI-2625790

Protein-protein interaction databases

BioGridi113731. 4 interactions.
IntActiO43184. 2 interactions.
MINTiMINT-246189.
STRINGi9606.ENSP00000357668.

Structurei

3D structure databases

ProteinModelPortaliO43184.
SMRiO43184. Positions 213-690.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini214 – 416203Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini424 – 51087DisintegrinPROSITE-ProRule annotationAdd
BLAST
Domaini656 – 68833EGF-likePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi177 – 1848Cysteine switchBy similarity
Motifi828 – 8347SH3-binding; class IIBy similarity
Motifi834 – 8418SH3-binding; class IBy similarity
Motifi885 – 8917SH3-binding; class IBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi514 – 649136Cys-richAdd
BLAST

Domaini

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.

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, SH3-binding, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG294463.
GeneTreeiENSGT00760000118888.
HOGENOMiHOG000230883.
HOVERGENiHBG006978.
InParanoidiO43184.
KOiK06835.
OMAiPPFCDKF.
OrthoDBiEOG7F7W89.
PhylomeDBiO43184.
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.
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.
[Graphical view]
SUPFAMiSSF57552. SSF57552. 1 hit.
PROSITEiPS50215. 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]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O43184-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAARPLPVSP ARALLLALAG ALLAPCEARG VSLWNQGRAD EVVSASVGSG
60 70 80 90 100
DLWIPVKSFD SKNHPEVLNI RLQRESKELI INLERNEGLI ASSFTETHYL
110 120 130 140 150
QDGTDVSLAR NYTVILGHCY YHGHVRGYSD SAVSLSTCSG LRGLIVFENE
160 170 180 190 200
SYVLEPMKSA TNRYKLFPAK KLKSVRGSCG SHHNTPNLAA KNVFPPPSQT
210 220 230 240 250
WARRHKRETL KATKYVELVI VADNREFQRQ GKDLEKVKQR LIEIANHVDK
260 270 280 290 300
FYRPLNIRIV LVGVEVWNDM DKCSVSQDPF TSLHEFLDWR KMKLLPRKSH
310 320 330 340 350
DNAQLVSGVY FQGTTIGMAP IMSMCTADQS GGIVMDHSDN PLGAAVTLAH
360 370 380 390 400
ELGHNFGMNH DTLDRGCSCQ MAVEKGGCIM NASTGYPFPM VFSSCSRKDL
410 420 430 440 450
ETSLEKGMGV CLFNLPEVRE SFGGQKCGNR FVEEGEECDC GEPEECMNRC
460 470 480 490 500
CNATTCTLKP DAVCAHGLCC EDCQLKPAGT ACRDSSNSCD LPEFCTGASP
510 520 530 540 550
HCPANVYLHD GHSCQDVDGY CYNGICQTHE QQCVTLWGPG AKPAPGICFE
560 570 580 590 600
RVNSAGDPYG NCGKVSKSSF AKCEMRDAKC GKIQCQGGAS RPVIGTNAVS
610 620 630 640 650
IETNIPLQQG GRILCRGTHV YLGDDMPDPG LVLAGTKCAD GKICLNRQCQ
660 670 680 690 700
NISVFGVHEC AMQCHGRGVC NNRKNCHCEA HWAPPFCDKF GFGGSTDSGP
710 720 730 740 750
IRQADNQGLT IGILVTILCL LAAGFVVYLK RKTLIRLLFT NKKTTIEKLR
760 770 780 790 800
CVRPSRPPRG FQPCQAHLGH LGKGLMRKPP DSYPPKDNPR RLLQCQNVDI
810 820 830 840 850
SRPLNGLNVP QPQSTQRVLP PLHRAPRAPS VPARPLPAKP ALRQAQGTCK
860 870 880 890 900
PNPPQKPLPA DPLARTTRLT HALARTPGQW ETGLRLAPLR PAPQYPHQVP

RSTHTAYIK
Length:909
Mass (Da):99,542
Last modified:May 5, 2009 - v3
Checksum:iE28131C64C4304AB
GO
Isoform 2 (identifier: O43184-2) [UniParc]FASTAAdd to Basket

Also known as: 12S

The sequence of this isoform differs from the canonical sequence as follows:
     705-738: DNQGLTIGILVTILCLLAAGFVVYLKRKTLIRLL → EARQEAAESNRERGQGQEPVGSQEHASTASLTLI
     739-909: Missing.

Show »
Length:738
Mass (Da):80,403
Checksum:i19699D2852ED28F6
GO
Isoform 3 (identifier: O43184-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:735
Mass (Da):80,078
Checksum:i664D4EDA47F8B533
GO
Isoform 4 (identifier: O43184-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:737
Mass (Da):80,263
Checksum:iD86FE821BCBC62C6
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti48 – 481G → R.4 Publications
Corresponds to variant rs3740199 [ dbSNP | Ensembl ].
VAR_038542
Natural varianti301 – 3011D → H in a breast cancer sample; somatic mutation. 1 Publication
VAR_036143
Natural varianti479 – 4791G → E in a breast cancer sample; somatic mutation. 1 Publication
VAR_036144
Natural varianti712 – 7121G → E in a cutaneous metastatic melanoma sample; somatic mutation. 1 Publication
VAR_066310
Natural varianti792 – 7921L → F in a breast cancer sample; somatic mutation. 1 Publication
VAR_036145
Natural varianti893 – 8931P → S in a cutaneous metastatic melanoma sample; somatic mutation. 1 Publication
VAR_066311

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei114 – 1163Missing in isoform 3 and isoform 4. 2 PublicationsVSP_031001
Alternative sequencei705 – 74036DNQGL…RLLFT → GKEARQEAAESNRERGQGQE PVGSQEHASTASLTLI in isoform 4. 1 PublicationVSP_031002Add
BLAST
Alternative sequencei705 – 73834DNQGL…LIRLL → EARQEAAESNRERGQGQEPV GSQEHASTASLTLI in isoform 2 and isoform 3. 2 PublicationsVSP_005476Add
BLAST
Alternative sequencei739 – 909171Missing in isoform 2 and isoform 3. 2 PublicationsVSP_005477Add
BLAST
Alternative sequencei741 – 909169Missing in isoform 4. 1 PublicationVSP_031003Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF023476 mRNA. Translation: AAC08702.2.
AF023477 mRNA. Translation: AAC08703.2.
AY358878 mRNA. Translation: AAQ89237.1.
AL589787
, AC022015, AC026226, AC063963 Genomic DNA. Translation: CAI40682.1.
AL589787
, 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.
CCDSiCCDS7653.1. [O43184-1]
CCDS7654.1. [O43184-2]
RefSeqiNP_001275903.1. NM_001288974.1. [O43184-4]
NP_001275904.1. NM_001288975.1. [O43184-3]
NP_003465.3. NM_003474.5. [O43184-1]
NP_067673.2. NM_021641.4. [O43184-2]
UniGeneiHs.594351.
Hs.741333.

Genome annotation databases

EnsembliENST00000368676; ENSP00000357665; ENSG00000148848. [O43184-2]
ENST00000368679; ENSP00000357668; ENSG00000148848. [O43184-1]
GeneIDi8038.
KEGGihsa:8038.
UCSCiuc001ljk.2. human. [O43184-1]
uc001ljl.4. human. [O43184-4]
uc001ljm.3. human. [O43184-2]
uc001ljn.3. human. [O43184-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF023476 mRNA. Translation: AAC08702.2 .
AF023477 mRNA. Translation: AAC08703.2 .
AY358878 mRNA. Translation: AAQ89237.1 .
AL589787
, AC022015 , AC026226 , AC063963 Genomic DNA. Translation: CAI40682.1 .
AL589787
, 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 .
CCDSi CCDS7653.1. [O43184-1 ]
CCDS7654.1. [O43184-2 ]
RefSeqi NP_001275903.1. NM_001288974.1. [O43184-4 ]
NP_001275904.1. NM_001288975.1. [O43184-3 ]
NP_003465.3. NM_003474.5. [O43184-1 ]
NP_067673.2. NM_021641.4. [O43184-2 ]
UniGenei Hs.594351.
Hs.741333.

3D structure databases

ProteinModelPortali O43184.
SMRi O43184. Positions 213-690.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113731. 4 interactions.
IntActi O43184. 2 interactions.
MINTi MINT-246189.
STRINGi 9606.ENSP00000357668.

Chemistry

BindingDBi O43184.
ChEMBLi CHEMBL5030.

Protein family/group databases

MEROPSi M12.212.

PTM databases

PhosphoSitei O43184.

Proteomic databases

MaxQBi O43184.
PaxDbi O43184.
PRIDEi O43184.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000368676 ; ENSP00000357665 ; ENSG00000148848 . [O43184-2 ]
ENST00000368679 ; ENSP00000357668 ; ENSG00000148848 . [O43184-1 ]
GeneIDi 8038.
KEGGi hsa:8038.
UCSCi uc001ljk.2. human. [O43184-1 ]
uc001ljl.4. human. [O43184-4 ]
uc001ljm.3. human. [O43184-2 ]
uc001ljn.3. human. [O43184-3 ]

Organism-specific databases

CTDi 8038.
GeneCardsi GC10M127693.
H-InvDB HIX0009299.
HGNCi HGNC:190. ADAM12.
HPAi HPA030866.
HPA030867.
HPA030868.
MIMi 602714. gene.
neXtProti NX_O43184.
PharmGKBi PA24507.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG294463.
GeneTreei ENSGT00760000118888.
HOGENOMi HOG000230883.
HOVERGENi HBG006978.
InParanoidi O43184.
KOi K06835.
OMAi PPFCDKF.
OrthoDBi EOG7F7W89.
PhylomeDBi O43184.
TreeFami TF314733.

Enzyme and pathway databases

Reactomei REACT_9417. Signaling by EGFR.

Miscellaneous databases

ChiTaRSi ADAM12. human.
GeneWikii ADAM12.
GenomeRNAii 8038.
NextBioi 30628.
PROi O43184.
SOURCEi Search...

Gene expression databases

Bgeei O43184.
CleanExi HS_ADAM12.
ExpressionAtlasi O43184. baseline and differential.
Genevestigatori O43184.

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.
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.
[Graphical view ]
SUPFAMi SSF57552. SSF57552. 1 hit.
PROSITEi PS50215. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. 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. 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.

Entry informationi

Entry nameiADA12_HUMAN
AccessioniPrimary (citable) accession number: O43184
Secondary accession number(s): O60470
, Q5JRP0, Q5JRP1, Q6P9E3, Q6UWB0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 5, 2009
Last modified: November 26, 2014
This is version 149 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3