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Q9P0K1

- ADA22_HUMAN

UniProt

Q9P0K1 - ADA22_HUMAN

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Protein

Disintegrin and metalloproteinase domain-containing protein 22

Gene

ADAM22

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

Functioni

Probable ligand for integrin in the brain. This is a non catalytic metalloprotease-like protein. Involved in regulation of cell adhesion and spreading and in inhibition of cell proliferation. Neuronal receptor for LGI1.3 Publications

GO - Molecular functioni

  1. integrin binding Source: UniProtKB
  2. metalloendopeptidase activity Source: InterPro
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. adult locomotory behavior Source: Ensembl
  2. cell adhesion Source: UniProtKB-KW
  3. central nervous system development Source: ProtInc
  4. myelination in peripheral nervous system Source: Ensembl
  5. negative regulation of cell adhesion Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Cell adhesion

Protein family/group databases

MEROPSiM12.978.

Names & Taxonomyi

Protein namesi
Recommended name:
Disintegrin and metalloproteinase domain-containing protein 22
Short name:
ADAM 22
Alternative name(s):
Metalloproteinase-disintegrin ADAM22-3
Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 2
Gene namesi
Name:ADAM22
Synonyms:MDC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:201. ADAM22.

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi834 – 8341S → A: Abolishes interactions with YWHAB and YWHAZ; when associated with A-857. 2 Publications
Mutagenesisi857 – 8571S → A: Abolishes interactions with YWHAB and YWHAZ; when associated with A-834. 2 Publications

Organism-specific databases

PharmGKBiPA24518.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Propeptidei26 – 222197By similarityPRO_0000029112Add
BLAST
Chaini223 – 906684Disintegrin and metalloproteinase domain-containing protein 22PRO_0000029113Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi175 – 1751N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi349 ↔ 4331 Publication
Disulfide bondi392 ↔ 4171 Publication
Disulfide bondi394 ↔ 4011 Publication
Disulfide bondi447 ↔ 4771 Publication
Disulfide bondi458 ↔ 4741 Publication
Disulfide bondi460 ↔ 4661 Publication
Disulfide bondi473 ↔ 4941 Publication
Disulfide bondi485 ↔ 4911 Publication
Disulfide bondi490 ↔ 5161 Publication
Disulfide bondi503 ↔ 5231 Publication
Disulfide bondi510 ↔ 5421 Publication
Glycosylationi519 – 5191N-linked (GlcNAc...)1 Publication
Disulfide bondi535 ↔ 5471 Publication
Disulfide bondi554 ↔ 6051 Publication
Disulfide bondi569 ↔ 6351 Publication
Disulfide bondi583 ↔ 5931 Publication
Disulfide bondi600 ↔ 6631 Publication
Glycosylationi634 – 6341N-linked (GlcNAc...)1 Publication
Disulfide bondi657 ↔ 6681 Publication
Glycosylationi675 – 6751N-linked (GlcNAc...)1 Publication
Disulfide bondi679 ↔ 6941 Publication
Disulfide bondi688 ↔ 7001 Publication
Disulfide bondi702 ↔ 7111 Publication
Modified residuei834 – 8341Phosphoserine1 Publication

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

Proteomic databases

MaxQBiQ9P0K1.
PaxDbiQ9P0K1.
PRIDEiQ9P0K1.

PTM databases

PhosphoSiteiQ9P0K1.

Expressioni

Tissue specificityi

Highly expressed in the brain and in some high-grade but not low-grade gliomas. Detected slightly or not at all in other tissues.1 Publication

Gene expression databases

BgeeiQ9P0K1.
CleanExiHS_ADAM22.
ExpressionAtlasiQ9P0K1. baseline and differential.
GenevestigatoriQ9P0K1.

Organism-specific databases

HPAiHPA045282.

Interactioni

Subunit structurei

Interacts with LGI1 and can bind to LGI4 (By similarity). Interacts through its C-terminal region with YWHAB/14-3-3 beta and YWHAZ/14-3-3 zeta but not with YWHAE/14-3-3 epsilon or YWHAH/14-3-3 eta.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
YWHABP319462EBI-1567267,EBI-359815
YWHAQP273482EBI-1567267,EBI-359854
YWHAZP631043EBI-1567267,EBI-347088

Protein-protein interaction databases

BioGridi119789. 6 interactions.
IntActiQ9P0K1. 11 interactions.
MINTiMINT-252818.
STRINGi9606.ENSP00000265727.

Structurei

Secondary structure

1
906
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi235 – 2373Combined sources
Beta strandi239 – 2479Combined sources
Helixi249 – 2535Combined sources
Turni254 – 2574Combined sources
Helixi259 – 28022Combined sources
Beta strandi281 – 29212Combined sources
Helixi305 – 31814Combined sources
Beta strandi325 – 3339Combined sources
Beta strandi336 – 3383Combined sources
Beta strandi341 – 3433Combined sources
Turni351 – 3533Combined sources
Beta strandi354 – 3596Combined sources
Helixi363 – 37816Combined sources
Helixi384 – 3896Combined sources
Helixi416 – 42712Combined sources
Helixi432 – 4354Combined sources
Helixi463 – 4664Combined sources
Turni467 – 4737Combined sources
Beta strandi486 – 4883Combined sources
Beta strandi491 – 4966Combined sources
Beta strandi502 – 5043Combined sources
Turni536 – 5394Combined sources
Beta strandi540 – 5434Combined sources
Beta strandi546 – 5483Combined sources
Helixi550 – 5589Combined sources
Helixi567 – 5737Combined sources
Turni574 – 5763Combined sources
Beta strandi585 – 5906Combined sources
Helixi595 – 5973Combined sources
Beta strandi600 – 6023Combined sources
Beta strandi605 – 6073Combined sources
Beta strandi613 – 6175Combined sources
Beta strandi622 – 6287Combined sources
Beta strandi631 – 6377Combined sources
Beta strandi640 – 6456Combined sources
Beta strandi656 – 6583Combined sources
Beta strandi661 – 6666Combined sources
Beta strandi668 – 6703Combined sources
Helixi671 – 6744Combined sources
Helixi688 – 6903Combined sources
Beta strandi692 – 6954Combined sources
Beta strandi700 – 7023Combined sources
Beta strandi706 – 7083Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3G5CX-ray2.36A/B233-736[»]
ProteinModelPortaliQ9P0K1.
SMRiQ9P0K1. Positions 233-718.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9P0K1.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini223 – 736514ExtracellularSequence AnalysisAdd
BLAST
Topological domaini758 – 906149CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei737 – 75721HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini239 – 438200Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini444 – 53188DisintegrinPROSITE-ProRule annotationAdd
BLAST
Domaini675 – 71238EGF-likeAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi532 – 678147Cys-richAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

EGF-like domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG256419.
GeneTreeiENSGT00760000119181.
HOGENOMiHOG000231962.
HOVERGENiHBG050456.
InParanoidiQ9P0K1.
KOiK16068.
OMAiFSGSQFE.
OrthoDBiEOG7B31M6.
PhylomeDBiQ9P0K1.
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.
PS00022. EGF_1. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9P0K1) [UniParc]FASTAAdd to Basket

Also known as: Epsilon

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
MQAAVAVSVP FLLLCVLGTC PPARCGQAGD ASLMELEKRK ENRFVERQSI
60 70 80 90 100
VPLRLIYRSG GEDESRHDAL DTRVRGDLGG PQLTHVDQAS FQVDAFGTSF
110 120 130 140 150
ILDVVLNHDL LSSEYIERHI EHGGKTVEVK GGEHCYYQGH IRGNPDSFVA
160 170 180 190 200
LSTCHGLHGM FYDGNHTYLI EPEENDTTQE DFHFHSVYKS RLFEFSLDDL
210 220 230 240 250
PSEFQQVNIT PSKFILKPRP KRSKRQLRRY PRNVEEETKY IELMIVNDHL
260 270 280 290 300
MFKKHRLSVV HTNTYAKSVV NMADLIYKDQ LKTRIVLVAM ETWATDNKFA
310 320 330 340 350
ISENPLITLR EFMKYRRDFI KEKSDAVHLF SGSQFESSRS GAAYIGGICS
360 370 380 390 400
LLKGGGVNEF GKTDLMAVTL AQSLAHNIGI ISDKRKLASG ECKCEDTWSG
410 420 430 440 450
CIMGDTGYYL PKKFTQCNIE EYHDFLNSGG GACLFNKPSK LLDPPECGNG
460 470 480 490 500
FIETGEECDC GTPAECVLEG AECCKKCTLT QDSQCSDGLC CKKCKFQPMG
510 520 530 540 550
TVCREAVNDC DIRETCSGNS SQCAPNIHKM DGYSCDGVQG ICFGGRCKTR
560 570 580 590 600
DRQCKYIWGQ KVTASDKYCY EKLNIEGTEK GNCGKDKDTW IQCNKRDVLC
610 620 630 640 650
GYLLCTNIGN IPRLGELDGE ITSTLVVQQG RTLNCSGGHV KLEEDVDLGY
660 670 680 690 700
VEDGTPCGPQ MMCLEHRCLP VASFNFSTCL SSKEGTICSG NGVCSNELKC
710 720 730 740 750
VCNRHWIGSD CNTYFPHNDD AKTGITLSGN GVAGTNIIIG IIAGTILVLA
760 770 780 790 800
LILGITAWGY KNYREQRQLP QGDYVKKPGD GDSFYSDIPP GVSTNSASSS
810 820 830 840 850
KKRSNGLSHS WSERIPDTKH ISDICENGRP RSNSWQGNLG GNKKKIRGKR
860 870 880 890 900
FRPRSNSTET LSPAKSPSSS TGSIASSRKY PYPMPPLPDE DKKVNRQSAR

LWETSI
Length:906
Mass (Da):100,433
Last modified:October 1, 2000 - v1
Checksum:i265ECCD0FA6C088B
GO
Isoform 2 (identifier: Q9P0K1-2) [UniParc]FASTAAdd to Basket

Also known as: Delta

The sequence of this isoform differs from the canonical sequence as follows:
     768-803: Missing.
     859-859: E → EYLNPWFKRDYNVAKWVEDVNKNTEGPYFR

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.Curated

Show »
Length:899
Mass (Da):100,269
Checksum:i5AB89C258ECE0736
GO
Isoform 3 (identifier: Q9P0K1-3) [UniParc]FASTAAdd to Basket

Also known as: Alpha

The sequence of this isoform differs from the canonical sequence as follows:
     860-906: Missing.

Show »
Length:859
Mass (Da):95,288
Checksum:i6105B681A1331D55
GO
Isoform 4 (identifier: Q9P0K1-4) [UniParc]FASTAAdd to Basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     768-803: Missing.
     860-906: Missing.

Show »
Length:823
Mass (Da):91,492
Checksum:iE9FD1A9BA99DE0DB
GO
Isoform 5 (identifier: Q9P0K1-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     768-803: Missing.

Show »
Length:870
Mass (Da):96,637
Checksum:iC236086AD0BCCA2F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform 2 (identifier: Q9P0K1-2)
Sequence conflicti848 – 8481G → E in AAF73288. (PubMed:11050470)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti81 – 811P → R.2 Publications
Corresponds to variant rs2279542 [ dbSNP | Ensembl ].
VAR_020057
Natural varianti119 – 1191H → Y.
Corresponds to variant rs4728730 [ dbSNP | Ensembl ].
VAR_051589
Natural varianti207 – 2071V → I.
Corresponds to variant rs17255978 [ dbSNP | Ensembl ].
VAR_051590

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei768 – 80336Missing in isoform 2, isoform 4 and isoform 5. 3 PublicationsVSP_005482Add
BLAST
Alternative sequencei859 – 8591E → EYLNPWFKRDYNVAKWVEDV NKNTEGPYFR in isoform 2. 1 PublicationVSP_005484
Alternative sequencei860 – 90647Missing in isoform 3 and isoform 4. 1 PublicationVSP_005483Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB009671 mRNA. Translation: BAA32349.1.
AB009671 mRNA. Translation: BAA32350.1.
AF155381 mRNA. Translation: AAF73288.1.
AF155382 mRNA. Translation: AAF73289.1.
AF073291 mRNA. Translation: AAF22476.2.
AC005075 Genomic DNA. No translation available.
AF158637 mRNA. Translation: AAD55251.1.
CCDSiCCDS43608.1. [Q9P0K1-2]
CCDS43609.1. [Q9P0K1-5]
CCDS43610.1. [Q9P0K1-3]
CCDS47637.1. [Q9P0K1-1]
RefSeqiNP_004185.1. NM_004194.3. [Q9P0K1-3]
NP_068367.1. NM_021721.3. [Q9P0K1-4]
NP_068368.2. NM_021722.4. [Q9P0K1-2]
NP_068369.1. NM_021723.3. [Q9P0K1-1]
UniGeneiHs.256398.

Genome annotation databases

EnsembliENST00000265727; ENSP00000265727; ENSG00000008277. [Q9P0K1-1]
ENST00000398201; ENSP00000381260; ENSG00000008277. [Q9P0K1-3]
ENST00000398204; ENSP00000381262; ENSG00000008277. [Q9P0K1-5]
ENST00000398209; ENSP00000381267; ENSG00000008277. [Q9P0K1-2]
GeneIDi53616.
KEGGihsa:53616.
UCSCiuc003ujk.2. human. [Q9P0K1-1]
uc003ujl.2. human. [Q9P0K1-4]
uc003ujm.3. human. [Q9P0K1-2]
uc003ujo.3. human. [Q9P0K1-5]

Polymorphism databases

DMDMi14423634.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB009671 mRNA. Translation: BAA32349.1 .
AB009671 mRNA. Translation: BAA32350.1 .
AF155381 mRNA. Translation: AAF73288.1 .
AF155382 mRNA. Translation: AAF73289.1 .
AF073291 mRNA. Translation: AAF22476.2 .
AC005075 Genomic DNA. No translation available.
AF158637 mRNA. Translation: AAD55251.1 .
CCDSi CCDS43608.1. [Q9P0K1-2 ]
CCDS43609.1. [Q9P0K1-5 ]
CCDS43610.1. [Q9P0K1-3 ]
CCDS47637.1. [Q9P0K1-1 ]
RefSeqi NP_004185.1. NM_004194.3. [Q9P0K1-3 ]
NP_068367.1. NM_021721.3. [Q9P0K1-4 ]
NP_068368.2. NM_021722.4. [Q9P0K1-2 ]
NP_068369.1. NM_021723.3. [Q9P0K1-1 ]
UniGenei Hs.256398.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3G5C X-ray 2.36 A/B 233-736 [» ]
ProteinModelPortali Q9P0K1.
SMRi Q9P0K1. Positions 233-718.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119789. 6 interactions.
IntActi Q9P0K1. 11 interactions.
MINTi MINT-252818.
STRINGi 9606.ENSP00000265727.

Protein family/group databases

MEROPSi M12.978.

PTM databases

PhosphoSitei Q9P0K1.

Polymorphism databases

DMDMi 14423634.

Proteomic databases

MaxQBi Q9P0K1.
PaxDbi Q9P0K1.
PRIDEi Q9P0K1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265727 ; ENSP00000265727 ; ENSG00000008277 . [Q9P0K1-1 ]
ENST00000398201 ; ENSP00000381260 ; ENSG00000008277 . [Q9P0K1-3 ]
ENST00000398204 ; ENSP00000381262 ; ENSG00000008277 . [Q9P0K1-5 ]
ENST00000398209 ; ENSP00000381267 ; ENSG00000008277 . [Q9P0K1-2 ]
GeneIDi 53616.
KEGGi hsa:53616.
UCSCi uc003ujk.2. human. [Q9P0K1-1 ]
uc003ujl.2. human. [Q9P0K1-4 ]
uc003ujm.3. human. [Q9P0K1-2 ]
uc003ujo.3. human. [Q9P0K1-5 ]

Organism-specific databases

CTDi 53616.
GeneCardsi GC07P087563.
HGNCi HGNC:201. ADAM22.
HPAi HPA045282.
MIMi 603709. gene.
neXtProti NX_Q9P0K1.
PharmGKBi PA24518.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG256419.
GeneTreei ENSGT00760000119181.
HOGENOMi HOG000231962.
HOVERGENi HBG050456.
InParanoidi Q9P0K1.
KOi K16068.
OMAi FSGSQFE.
OrthoDBi EOG7B31M6.
PhylomeDBi Q9P0K1.
TreeFami TF314733.

Miscellaneous databases

ChiTaRSi ADAM22. human.
EvolutionaryTracei Q9P0K1.
GeneWikii ADAM22.
GenomeRNAii 53616.
NextBioi 56096.
PROi Q9P0K1.
SOURCEi Search...

Gene expression databases

Bgeei Q9P0K1.
CleanExi HS_ADAM22.
ExpressionAtlasi Q9P0K1. baseline and differential.
Genevestigatori Q9P0K1.

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.
PS00022. EGF_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Metalloproteinase-like, disintegrin-like, cysteine-rich proteins MDC2 and MDC3: novel human cellular disintegrins highly expressed in the brain."
    Sagane K., Ohya Y., Hasegawa Y., Tanaka I.
    Biochem. J. 334:93-98(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
    Tissue: Brain.
  2. "The specific expression of three novel splice variant forms of human metalloprotease-like disintegrin-like cysteine-rich protein 2 gene in brain tissues and gliomas."
    Harada T., Nishie A., Torigoe K., Ikezaki K., Shono T., Maehara Y., Kuwano M., Wada M.
    Jpn. J. Cancer Res. 91:1001-1006(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  3. "Isolation and tissue specific expression of novel ADAM family from 7q21.1 region."
    Wada M., Torigoe K., Harada T., Kuwano M.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), VARIANT ARG-81.
    Tissue: Brain.
  4. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The identification of seven metalloproteinase-disintegrin (ADAM) genes from genomic libraries."
    Poindexter K., Nelson N., DuBose R.F., Black R.A., Cerretti D.P.
    Gene 237:61-70(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 40-906 (ISOFORM 1), VARIANT ARG-81.
    Tissue: Cerebellum.
  6. "The interaction between ADAM 22 and 14-3-3zeta: regulation of cell adhesion and spreading."
    Zhu P., Sun Y., Xu R., Sang Y., Zhao J., Liu G., Cai L., Li C., Zhao S.
    Biochem. Biophys. Res. Commun. 301:991-999(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH YWHAZ, MUTAGENESIS OF SER-834 AND SER-857.
  7. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
  8. "ADAM22 plays an important role in cell adhesion and spreading with the assistance of 14-3-3."
    Zhu P., Sang Y., Xu H., Zhao J., Xu R., Sun Y., Xu T., Wang X., Chen L., Feng H., Li C., Zhao S.
    Biochem. Biophys. Res. Commun. 331:938-946(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH YWHAB, MUTAGENESIS OF SER-834 AND SER-857.
  9. "ADAM22, expressed in normal brain but not in high-grade gliomas, inhibits cellular proliferation via the disintegrin domain."
    D'Abaco G.M., Ng K., Paradiso L., Godde N.J., Kaye A., Novak U.
    Neurosurgery 58:179-186(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-834, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function."
    Liu H., Shim A.H., He X.
    J. Biol. Chem. 284:29077-29086(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF 233-736, GLYCOSYLATION AT ASN-519; ASN-634 AND ASN-675, DISULFIDE BONDS.

Entry informationi

Entry nameiADA22_HUMAN
AccessioniPrimary (citable) accession number: Q9P0K1
Secondary accession number(s): O75075
, O75076, Q9P0K2, Q9UIA1, Q9UKK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: October 1, 2000
Last modified: October 29, 2014
This is version 137 of the entry and version 1 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 chromosome 7
    Human chromosome 7: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3