Q9P0K1 (ADA22_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	ADAM22
Synonyms:	MDC2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	906 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.6 Ref.8 Ref.9
Subunit structure	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. Ref.6 Ref.8
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	Highly expressed in the brain and in some high-grade but not low-grade gliomas. Detected slightly or not at all in other tissues. Ref.9
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.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	EGF-like domain Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adult locomotory behavior Inferred from electronic annotation. Source: Compara cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW central nervous system development Traceable author statement Ref.1. Source: ProtInc myelination in peripheral nervous system Inferred from electronic annotation. Source: Compara negative regulation of cell adhesion Non-traceable author statement Ref.1. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: InterPro
Cellular_component	integral to membrane Non-traceable author statement Ref.1. Source: UniProtKB
Molecular_function	integrin binding Non-traceable author statement Ref.1. Source: UniProtKB metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
YWHAB	P31946	2	EBI-1567267,EBI-359815
YWHAQ	P27348	2	EBI-1567267,EBI-359854
YWHAZ	P63104	3	EBI-1567267,EBI-347088

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9P0K1-1)

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.

Isoform 2 (identifier: Q9P0K1-2)

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.

Isoform 3 (identifier: Q9P0K1-3)

Also known as: Alpha;

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

Isoform 4 (identifier: Q9P0K1-4)

Also known as: Beta;

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

Isoform 5 (identifier: Q9P0K1-5)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Potential

Propeptide

26 – 222

197

By similarity

PRO_0000029112

Chain

223 – 906

684

Disintegrin and metalloproteinase domain-containing protein 22

PRO_0000029113

Regions

Topological domain

223 – 736

514

Extracellular Potential

Transmembrane

737 – 757

21

Helical; Potential

Topological domain

758 – 906

149

Cytoplasmic Potential

Domain

239 – 438

200

Peptidase M12B

Domain

444 – 531

88

Disintegrin

Domain

675 – 712

38

EGF-like

Compositional bias

532 – 678

147

Cys-rich

Amino acid modifications

Modified residue

834

1

Phosphoserine Ref.10

Modified residue

866

1

Phosphoserine By similarity

Modified residue

868

1

Phosphoserine By similarity

Glycosylation

175

1

N-linked (GlcNAc...) Potential

Glycosylation

519

1

N-linked (GlcNAc...) Ref.11

Glycosylation

634

1

N-linked (GlcNAc...) Ref.11

Glycosylation

675

1

N-linked (GlcNAc...) Ref.11

Disulfide bond

349 ↔ 433

Ref.11

Disulfide bond

392 ↔ 417

Ref.11

Disulfide bond

394 ↔ 401

Ref.11

Disulfide bond

447 ↔ 477

Ref.11

Disulfide bond

458 ↔ 474

Ref.11

Disulfide bond

460 ↔ 466

Ref.11

Disulfide bond

473 ↔ 494

Ref.11

Disulfide bond

485 ↔ 491

Ref.11

Disulfide bond

490 ↔ 516

Ref.11

Disulfide bond

503 ↔ 523

Ref.11

Disulfide bond

510 ↔ 542

Ref.11

Disulfide bond

535 ↔ 547

Ref.11

Disulfide bond

554 ↔ 605

Ref.11

Disulfide bond

569 ↔ 635

Ref.11

Disulfide bond

583 ↔ 593

Ref.11

Disulfide bond

600 ↔ 663

Ref.11

Disulfide bond

657 ↔ 668

Ref.11

Disulfide bond

679 ↔ 694

Ref.11

Disulfide bond

688 ↔ 700

Ref.11

Disulfide bond

702 ↔ 711

Ref.11

Natural variations

Alternative sequence

768 – 803

36

Missing in isoform 2, isoform 4 and isoform 5.

VSP_005482

Alternative sequence

859

1

E → EYLNPWFKRDYNVAKWVEDV NKNTEGPYFR in isoform 2.

VSP_005484

Alternative sequence

860 – 906

47

Missing in isoform 3 and isoform 4.

VSP_005483

Natural variant

81

1

P → R. Ref.3 Ref.5
Corresponds to variant rs2279542 [ dbSNP | Ensembl ].

VAR_020057

Natural variant

119

1

H → Y.
Corresponds to variant rs4728730 [ dbSNP | Ensembl ].

VAR_051589

Natural variant

207

1

V → I.
Corresponds to variant rs17255978 [ dbSNP | Ensembl ].

VAR_051590

Experimental info

Mutagenesis

834

1

S → A: Abolishes interactions with YWHAB and YWHAZ; when associated with A-857. Ref.6 Ref.8

Mutagenesis

857

1

S → A: Abolishes interactions with YWHAB and YWHAZ; when associated with A-834. Ref.6 Ref.8

Isoform 2:

Sequence conflict

848

1

G → E in AAF73288. Ref.2

Secondary structure

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906

Helix Strand Turn

Details...

Beta strand

235 – 237

3

Beta strand

239 – 247

9

Helix

249 – 253

5

Turn

254 – 257

4

Helix

259 – 280

22

Beta strand

281 – 292

12

Helix

305 – 318

14

Beta strand

325 – 333

9

Beta strand

336 – 338

3

Beta strand

341 – 343

3

Turn

351 – 353

3

Beta strand

354 – 359

6

Helix

363 – 378

16

Helix

384 – 389

6

Helix

416 – 427

12

Helix

432 – 435

4

Helix

463 – 466

4

Turn

467 – 473

7

Beta strand

486 – 488

3

Beta strand

491 – 496

6

Beta strand

502 – 504

3

Turn

536 – 539

4

Beta strand

540 – 543

4

Beta strand

546 – 548

3

Helix

550 – 558

9

Helix

567 – 573

7

Turn

574 – 576

3

Beta strand

585 – 590

6

Helix

595 – 597

3

Beta strand

600 – 602

3

Beta strand

605 – 607

3

Beta strand

613 – 617

5

Beta strand

622 – 628

7

Beta strand

631 – 637

7

Beta strand

640 – 645

6

Beta strand

656 – 658

3

Beta strand

661 – 666

6

Beta strand

668 – 670

3

Helix

671 – 674

4

Helix

688 – 690

3

Beta strand

692 – 695

4

Beta strand

700 – 702

3

Beta strand

706 – 708

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Epsilon) [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 265ECCD0FA6C088B	FASTA	906	100,433
	10 20 30 40 50 60 MQAAVAVSVP FLLLCVLGTC PPARCGQAGD ASLMELEKRK ENRFVERQSI VPLRLIYRSG 70 80 90 100 110 120 GEDESRHDAL DTRVRGDLGG PQLTHVDQAS FQVDAFGTSF ILDVVLNHDL LSSEYIERHI 130 140 150 160 170 180 EHGGKTVEVK GGEHCYYQGH IRGNPDSFVA LSTCHGLHGM FYDGNHTYLI EPEENDTTQE 190 200 210 220 230 240 DFHFHSVYKS RLFEFSLDDL PSEFQQVNIT PSKFILKPRP KRSKRQLRRY PRNVEEETKY 250 260 270 280 290 300 IELMIVNDHL MFKKHRLSVV HTNTYAKSVV NMADLIYKDQ LKTRIVLVAM ETWATDNKFA 310 320 330 340 350 360 ISENPLITLR EFMKYRRDFI KEKSDAVHLF SGSQFESSRS GAAYIGGICS LLKGGGVNEF 370 380 390 400 410 420 GKTDLMAVTL AQSLAHNIGI ISDKRKLASG ECKCEDTWSG CIMGDTGYYL PKKFTQCNIE 430 440 450 460 470 480 EYHDFLNSGG GACLFNKPSK LLDPPECGNG FIETGEECDC GTPAECVLEG AECCKKCTLT 490 500 510 520 530 540 QDSQCSDGLC CKKCKFQPMG TVCREAVNDC DIRETCSGNS SQCAPNIHKM DGYSCDGVQG 550 560 570 580 590 600 ICFGGRCKTR DRQCKYIWGQ KVTASDKYCY EKLNIEGTEK GNCGKDKDTW IQCNKRDVLC 610 620 630 640 650 660 GYLLCTNIGN IPRLGELDGE ITSTLVVQQG RTLNCSGGHV KLEEDVDLGY VEDGTPCGPQ 670 680 690 700 710 720 MMCLEHRCLP VASFNFSTCL SSKEGTICSG NGVCSNELKC VCNRHWIGSD CNTYFPHNDD 730 740 750 760 770 780 AKTGITLSGN GVAGTNIIIG IIAGTILVLA LILGITAWGY KNYREQRQLP QGDYVKKPGD 790 800 810 820 830 840 GDSFYSDIPP GVSTNSASSS KKRSNGLSHS WSERIPDTKH ISDICENGRP RSNSWQGNLG 850 860 870 880 890 900 GNKKKIRGKR FRPRSNSTET LSPAKSPSSS TGSIASSRKY PYPMPPLPDE DKKVNRQSAR LWETSI
	Isoform 2 (Delta) [UniParc]. Checksum: 5AB89C258ECE0736	FASTA	899	100,269
	10 20 30 40 50 60 MQAAVAVSVP FLLLCVLGTC PPARCGQAGD ASLMELEKRK ENRFVERQSI VPLRLIYRSG 70 80 90 100 110 120 GEDESRHDAL DTRVRGDLGG PQLTHVDQAS FQVDAFGTSF ILDVVLNHDL LSSEYIERHI 130 140 150 160 170 180 EHGGKTVEVK GGEHCYYQGH IRGNPDSFVA LSTCHGLHGM FYDGNHTYLI EPEENDTTQE 190 200 210 220 230 240 DFHFHSVYKS RLFEFSLDDL PSEFQQVNIT PSKFILKPRP KRSKRQLRRY PRNVEEETKY 250 260 270 280 290 300 IELMIVNDHL MFKKHRLSVV HTNTYAKSVV NMADLIYKDQ LKTRIVLVAM ETWATDNKFA 310 320 330 340 350 360 ISENPLITLR EFMKYRRDFI KEKSDAVHLF SGSQFESSRS GAAYIGGICS LLKGGGVNEF 370 380 390 400 410 420 GKTDLMAVTL AQSLAHNIGI ISDKRKLASG ECKCEDTWSG CIMGDTGYYL PKKFTQCNIE 430 440 450 460 470 480 EYHDFLNSGG GACLFNKPSK LLDPPECGNG FIETGEECDC GTPAECVLEG AECCKKCTLT 490 500 510 520 530 540 QDSQCSDGLC CKKCKFQPMG TVCREAVNDC DIRETCSGNS SQCAPNIHKM DGYSCDGVQG 550 560 570 580 590 600 ICFGGRCKTR DRQCKYIWGQ KVTASDKYCY EKLNIEGTEK GNCGKDKDTW IQCNKRDVLC 610 620 630 640 650 660 GYLLCTNIGN IPRLGELDGE ITSTLVVQQG RTLNCSGGHV KLEEDVDLGY VEDGTPCGPQ 670 680 690 700 710 720 MMCLEHRCLP VASFNFSTCL SSKEGTICSG NGVCSNELKC VCNRHWIGSD CNTYFPHNDD 730 740 750 760 770 780 AKTGITLSGN GVAGTNIIIG IIAGTILVLA LILGITAWGY KNYREQRSNG LSHSWSERIP 790 800 810 820 830 840 DTKHISDICE NGRPRSNSWQ GNLGGNKKKI RGKRFRPRSN STEYLNPWFK RDYNVAKWVE 850 860 870 880 890 DVNKNTEGPY FRTLSPAKSP SSSTGSIASS RKYPYPMPPL PDEDKKVNRQ SARLWETSI
	Isoform 3 (Alpha) [UniParc]. Checksum: 6105B681A1331D55	FASTA	859	95,288
	10 20 30 40 50 60 MQAAVAVSVP FLLLCVLGTC PPARCGQAGD ASLMELEKRK ENRFVERQSI VPLRLIYRSG 70 80 90 100 110 120 GEDESRHDAL DTRVRGDLGG PQLTHVDQAS FQVDAFGTSF ILDVVLNHDL LSSEYIERHI 130 140 150 160 170 180 EHGGKTVEVK GGEHCYYQGH IRGNPDSFVA LSTCHGLHGM FYDGNHTYLI EPEENDTTQE 190 200 210 220 230 240 DFHFHSVYKS RLFEFSLDDL PSEFQQVNIT PSKFILKPRP KRSKRQLRRY PRNVEEETKY 250 260 270 280 290 300 IELMIVNDHL MFKKHRLSVV HTNTYAKSVV NMADLIYKDQ LKTRIVLVAM ETWATDNKFA 310 320 330 340 350 360 ISENPLITLR EFMKYRRDFI KEKSDAVHLF SGSQFESSRS GAAYIGGICS LLKGGGVNEF 370 380 390 400 410 420 GKTDLMAVTL AQSLAHNIGI ISDKRKLASG ECKCEDTWSG CIMGDTGYYL PKKFTQCNIE 430 440 450 460 470 480 EYHDFLNSGG GACLFNKPSK LLDPPECGNG FIETGEECDC GTPAECVLEG AECCKKCTLT 490 500 510 520 530 540 QDSQCSDGLC CKKCKFQPMG TVCREAVNDC DIRETCSGNS SQCAPNIHKM DGYSCDGVQG 550 560 570 580 590 600 ICFGGRCKTR DRQCKYIWGQ KVTASDKYCY EKLNIEGTEK GNCGKDKDTW IQCNKRDVLC 610 620 630 640 650 660 GYLLCTNIGN IPRLGELDGE ITSTLVVQQG RTLNCSGGHV KLEEDVDLGY VEDGTPCGPQ 670 680 690 700 710 720 MMCLEHRCLP VASFNFSTCL SSKEGTICSG NGVCSNELKC VCNRHWIGSD CNTYFPHNDD 730 740 750 760 770 780 AKTGITLSGN GVAGTNIIIG IIAGTILVLA LILGITAWGY KNYREQRQLP QGDYVKKPGD 790 800 810 820 830 840 GDSFYSDIPP GVSTNSASSS KKRSNGLSHS WSERIPDTKH ISDICENGRP RSNSWQGNLG 850 GNKKKIRGKR FRPRSNSTE
	Isoform 4 (Beta) [UniParc]. Checksum: E9FD1A9BA99DE0DB	FASTA	823	91,492
	10 20 30 40 50 60 MQAAVAVSVP FLLLCVLGTC PPARCGQAGD ASLMELEKRK ENRFVERQSI VPLRLIYRSG 70 80 90 100 110 120 GEDESRHDAL DTRVRGDLGG PQLTHVDQAS FQVDAFGTSF ILDVVLNHDL LSSEYIERHI 130 140 150 160 170 180 EHGGKTVEVK GGEHCYYQGH IRGNPDSFVA LSTCHGLHGM FYDGNHTYLI EPEENDTTQE 190 200 210 220 230 240 DFHFHSVYKS RLFEFSLDDL PSEFQQVNIT PSKFILKPRP KRSKRQLRRY PRNVEEETKY 250 260 270 280 290 300 IELMIVNDHL MFKKHRLSVV HTNTYAKSVV NMADLIYKDQ LKTRIVLVAM ETWATDNKFA 310 320 330 340 350 360 ISENPLITLR EFMKYRRDFI KEKSDAVHLF SGSQFESSRS GAAYIGGICS LLKGGGVNEF 370 380 390 400 410 420 GKTDLMAVTL AQSLAHNIGI ISDKRKLASG ECKCEDTWSG CIMGDTGYYL PKKFTQCNIE 430 440 450 460 470 480 EYHDFLNSGG GACLFNKPSK LLDPPECGNG FIETGEECDC GTPAECVLEG AECCKKCTLT 490 500 510 520 530 540 QDSQCSDGLC CKKCKFQPMG TVCREAVNDC DIRETCSGNS SQCAPNIHKM DGYSCDGVQG 550 560 570 580 590 600 ICFGGRCKTR DRQCKYIWGQ KVTASDKYCY EKLNIEGTEK GNCGKDKDTW IQCNKRDVLC 610 620 630 640 650 660 GYLLCTNIGN IPRLGELDGE ITSTLVVQQG RTLNCSGGHV KLEEDVDLGY VEDGTPCGPQ 670 680 690 700 710 720 MMCLEHRCLP VASFNFSTCL SSKEGTICSG NGVCSNELKC VCNRHWIGSD CNTYFPHNDD 730 740 750 760 770 780 AKTGITLSGN GVAGTNIIIG IIAGTILVLA LILGITAWGY KNYREQRSNG LSHSWSERIP 790 800 810 820 DTKHISDICE NGRPRSNSWQ GNLGGNKKKI RGKRFRPRSN STE
	Isoform 5 [UniParc]. Checksum: C236086AD0BCCA2F	FASTA	870	96,637
	10 20 30 40 50 60 MQAAVAVSVP FLLLCVLGTC PPARCGQAGD ASLMELEKRK ENRFVERQSI VPLRLIYRSG 70 80 90 100 110 120 GEDESRHDAL DTRVRGDLGG PQLTHVDQAS FQVDAFGTSF ILDVVLNHDL LSSEYIERHI 130 140 150 160 170 180 EHGGKTVEVK GGEHCYYQGH IRGNPDSFVA LSTCHGLHGM FYDGNHTYLI EPEENDTTQE 190 200 210 220 230 240 DFHFHSVYKS RLFEFSLDDL PSEFQQVNIT PSKFILKPRP KRSKRQLRRY PRNVEEETKY 250 260 270 280 290 300 IELMIVNDHL MFKKHRLSVV HTNTYAKSVV NMADLIYKDQ LKTRIVLVAM ETWATDNKFA 310 320 330 340 350 360 ISENPLITLR EFMKYRRDFI KEKSDAVHLF SGSQFESSRS GAAYIGGICS LLKGGGVNEF 370 380 390 400 410 420 GKTDLMAVTL AQSLAHNIGI ISDKRKLASG ECKCEDTWSG CIMGDTGYYL PKKFTQCNIE 430 440 450 460 470 480 EYHDFLNSGG GACLFNKPSK LLDPPECGNG FIETGEECDC GTPAECVLEG AECCKKCTLT 490 500 510 520 530 540 QDSQCSDGLC CKKCKFQPMG TVCREAVNDC DIRETCSGNS SQCAPNIHKM DGYSCDGVQG 550 560 570 580 590 600 ICFGGRCKTR DRQCKYIWGQ KVTASDKYCY EKLNIEGTEK GNCGKDKDTW IQCNKRDVLC 610 620 630 640 650 660 GYLLCTNIGN IPRLGELDGE ITSTLVVQQG RTLNCSGGHV KLEEDVDLGY VEDGTPCGPQ 670 680 690 700 710 720 MMCLEHRCLP VASFNFSTCL SSKEGTICSG NGVCSNELKC VCNRHWIGSD CNTYFPHNDD 730 740 750 760 770 780 AKTGITLSGN GVAGTNIIIG IIAGTILVLA LILGITAWGY KNYREQRSNG LSHSWSERIP 790 800 810 820 830 840 DTKHISDICE NGRPRSNSWQ GNLGGNKKKI RGKRFRPRSN STETLSPAKS PSSSTGSIAS 850 860 870 SRKYPYPMPP LPDEDKKVNR QSARLWETSI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"An unappreciated role for RNA surveillance." Hillman R.T., Green R.E., Brenner S.E. Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY.
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00220631.
IPI00220632.
IPI00220634.
IPI00220635.
IPI00941986.

RefSeq

NP_004185.1. NM_004194.3.
NP_068367.1. NM_021721.3.
NP_068368.2. NM_021722.4.
NP_068369.1. NM_021723.3.

UniGene

Hs.256398.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3G5C	X-ray	2.36	A/B	233-736	[»]

ProteinModelPortal

Q9P0K1.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9P0K1. 10 interactions.

MINT

MINT-252818.

STRING

9606.ENSP00000265727.

Protein family/group databases

MEROPS

M12.978.

PTM databases

PhosphoSite

Q9P0K1.

Polymorphism databases

DMDM

14423634.

Proteomic databases

PaxDb

Q9P0K1.

PRIDE

Q9P0K1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000265727; ENSP00000265727; ENSG00000008277.
ENST00000398201; ENSP00000381260; ENSG00000008277.
ENST00000398204; ENSP00000381262; ENSG00000008277.
ENST00000398209; ENSP00000381267; ENSG00000008277.

GeneID

53616.

KEGG

hsa:53616.

UCSC

uc003ujk.2. human.
uc003ujl.2. human.
uc003ujm.3. human.
uc003ujo.3. human.

Organism-specific databases

CTD

53616.

GeneCards

GC07P087563.

HGNC

HGNC:201. ADAM22.

HPA

HPA045282.

MIM

603709. gene.

neXtProt

NX_Q9P0K1.

PharmGKB

PA24518.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG256419.

HOGENOM

HOG000231962.

HOVERGEN

HBG050456.

InParanoid

Q9P0K1.

KO

K16068.

OMA

DRQCKYI.

Gene expression databases

ArrayExpress

Q9P0K1.

Bgee

Q9P0K1.

CleanEx

HS_ADAM22.

Genevestigator

Q9P0K1.

GermOnline

ENSG00000008277. Homo sapiens.

Family and domain databases

Gene3D

3.40.390.10. 1 hit.
4.10.70.10. 1 hit.

InterPro

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]

Pfam

PF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]

PRINTS

PR00289. DISINTEGRIN.

SMART

SM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view]

SUPFAM

SSF57552. Disintegrin. 1 hit.

PROSITE

PS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. False negative.
PS50026. EGF_3. False negative.
PS00142. ZINC_PROTEASE. False negative.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ADAM22. human.

EvolutionaryTrace

Q9P0K1.

GenomeRNAi

53616.

NextBio

56096.

SOURCE

Search...

Entry information

Entry name

ADA22_HUMAN

Accession

Primary (citable) accession number: Q9P0K1
Secondary accession number(s): O75075 , O75076, Q9P0K2, Q9UIA1, Q9UKK2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 123 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.