Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9P2N4 (ATS9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 133. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 9

Short name=ADAM-TS 9
Short name=ADAM-TS9
Short name=ADAMTS-9
EC=3.4.24.-
Gene names
Name:ADAMTS9
Synonyms:KIAA1312
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1935 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleaves the large aggregating proteoglycans, aggrecan and versican. Has a protease-independent function in promoting the transport from the endoplasmic reticulum to the Golgi apparatus of a variety of secretory cargos. Ref.2 Ref.6

Catalytic activity

Cleaves aggrecan at the 1838-Glu-|-Ala-1839 site and versican at the 1428-Glu-|-Ala-1429 site.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity. Endoplasmic reticulum Ref.6.

Tissue specificity

Highly expressed in all fetal tissues. Expressed in a number of adult tissues with highest expression in heart, placenta and skeletal muscle.

Domain

The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix By similarity.

The ancillary domains, including the TSRs domain, are required for specific extracellular localization and for its versicanase and aggrecanase activities.

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.

The GON domain mediates protease-independent function in ER to Golgi transport.

Post-translational modification

The precursor is cleaved by a furin endopeptidase By similarity.

Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion By similarity.

Sequence similarities

Contains 1 disintegrin domain.

Contains 1 GON domain.

Contains 1 peptidase M12B domain.

Contains 15 TSP type-1 domains.

Ontologies

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9P2N4-3)

Also known as: ADAMTS-9B;

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: Q9P2N4-1)

Also known as: Long;

The sequence of this isoform differs from the canonical sequence as follows:
     1624-1629: CSVTCG → VPSWEL
     1630-1935: Missing.
Note: May result from the retention of an intron in the cDNA leading to a prematurate stop codon.
Isoform 3 (identifier: Q9P2N4-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     1064-1072: CLVTCGKGH → VRWEGCYFP
     1073-1935: Missing.
Isoform 4 (identifier: Q9P2N4-4)

The sequence of this isoform differs from the canonical sequence as follows:
     324-351: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 287269
PRO_0000029182
Chain288 – 19351648A disintegrin and metalloproteinase with thrombospondin motifs 9
PRO_0000029183

Regions

Domain293 – 499207Peptidase M12B
Domain509 – 58779Disintegrin
Domain588 – 64356TSP type-1 1
Domain878 – 93659TSP type-1 2
Domain939 – 99759TSP type-1 3
Domain998 – 104952TSP type-1 4
Domain1052 – 110958TSP type-1 5
Domain1110 – 116657TSP type-1 6
Domain1182 – 124059TSP type-1 7
Domain1241 – 129656TSP type-1 8
Domain1328 – 137952TSP type-1 9
Domain1382 – 144059TSP type-1 10
Domain1441 – 149454TSP type-1 11
Domain1497 – 155559TSP type-1 12
Domain1556 – 161156TSP type-1 13
Domain1612 – 167665TSP type-1 14
Domain1677 – 173458TSP type-1 15
Domain1735 – 1935201GON
Region753 – 877125Spacer
Motif221 – 2288Cysteine switch By similarity
Compositional bias88 – 969Poly-Ser
Compositional bias644 – 752109Cys-rich

Sites

Active site4351 By similarity
Metal binding2231Zinc; in inhibited form By similarity
Metal binding4341Zinc; catalytic By similarity
Metal binding4381Zinc; catalytic By similarity
Metal binding4441Zinc; catalytic By similarity

Amino acid modifications

Glycosylation1121N-linked (GlcNAc...) Potential
Glycosylation1351N-linked (GlcNAc...) Potential
Glycosylation2711N-linked (GlcNAc...) Potential
Glycosylation7491N-linked (GlcNAc...) Potential
Glycosylation8401N-linked (GlcNAc...) Potential
Glycosylation12131N-linked (GlcNAc...) Potential
Glycosylation12671N-linked (GlcNAc...) Potential
Glycosylation17881N-linked (GlcNAc...) Potential
Glycosylation18061N-linked (GlcNAc...) Potential
Disulfide bond368 ↔ 418 By similarity
Disulfide bond394 ↔ 400 By similarity
Disulfide bond412 ↔ 494 By similarity
Disulfide bond450 ↔ 478 By similarity
Disulfide bond521 ↔ 543 By similarity
Disulfide bond532 ↔ 553 By similarity
Disulfide bond538 ↔ 572 By similarity
Disulfide bond566 ↔ 577 By similarity
Disulfide bond600 ↔ 637 By similarity
Disulfide bond604 ↔ 642 By similarity
Disulfide bond615 ↔ 627 By similarity
Disulfide bond890 ↔ 931 By similarity
Disulfide bond894 ↔ 935 By similarity
Disulfide bond904 ↔ 918 By similarity
Disulfide bond1250 ↔ 1290 By similarity
Disulfide bond1254 ↔ 1295 By similarity
Disulfide bond1265 ↔ 1278 By similarity
Disulfide bond1624 ↔ 1670 By similarity
Disulfide bond1628 ↔ 1675 By similarity
Disulfide bond1639 ↔ 1659 By similarity

Natural variations

Alternative sequence324 – 35128Missing in isoform 4.
VSP_053399
Alternative sequence1064 – 10729CLVTCGKGH → VRWEGCYFP in isoform 3.
VSP_005499
Alternative sequence1073 – 1935863Missing in isoform 3.
VSP_005500
Alternative sequence1624 – 16296CSVTCG → VPSWEL in isoform 2.
VSP_007548
Alternative sequence1630 – 1935306Missing in isoform 2.
VSP_007549
Natural variant961S → P. Ref.2
Corresponds to variant rs36115950 [ dbSNP | Ensembl ].
VAR_047081
Natural variant961S → T.
Corresponds to variant rs36115950 [ dbSNP | Ensembl ].
VAR_051592
Natural variant15791K → E.
Corresponds to variant rs17071010 [ dbSNP | Ensembl ].
VAR_047082
Natural variant16741D → E. Ref.2
Corresponds to variant rs6787633 [ dbSNP | Ensembl ].
VAR_047083
Natural variant17401K → R.
Corresponds to variant rs17070967 [ dbSNP | Ensembl ].
VAR_047084
Natural variant17911E → Q.
Corresponds to variant rs3796381 [ dbSNP | Ensembl ].
VAR_047085
Natural variant19211K → E.
Corresponds to variant rs17070909 [ dbSNP | Ensembl ].
VAR_051593
Natural variant19331R → Q.
Corresponds to variant rs17070905 [ dbSNP | Ensembl ].
VAR_047086

Experimental info

Sequence conflict461S → G in AAF89106. Ref.1
Sequence conflict1821D → G in AAO15765. Ref.2
Sequence conflict3671F → L in AAF89106. Ref.1
Sequence conflict11171G → V in AAO15765. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (ADAMTS-9B) [UniParc].

Last modified November 4, 2008. Version 4.
Checksum: 150B78D4C5CC2CCC

FASTA1,935216,491
        10         20         30         40         50         60 
MQFVSWATLL TLLVRDLAEM GSPDAAAAVR KDRLHPRQVK LLETLSEYEI VSPIRVNALG 

        70         80         90        100        110        120 
EPFPTNVHFK RTRRSINSAT DPWPAFASSS SSSTSSQAHY RLSAFGQQFL FNLTANAGFI 

       130        140        150        160        170        180 
APLFTVTLLG TPGVNQTKFY SEEEAELKHC FYKGYVNTNS EHTAVISLCS GMLGTFRSHD 

       190        200        210        220        230        240 
GDYFIEPLQS MDEQEDEEEQ NKPHIIYRRS APQREPSTGR HACDTSEHKN RHSKDKKKTR 

       250        260        270        280        290        300 
ARKWGERINL AGDVAALNSG LATEAFSAYG NKTDNTREKR THRRTKRFLS YPRFVEVLVV 

       310        320        330        340        350        360 
ADNRMVSYHG ENLQHYILTL MSIVASIYKD PSIGNLINIV IVNLIVIHNE QDGPSISFNA 

       370        380        390        400        410        420 
QTTLKNFCQW QHSKNSPGGI HHDTAVLLTR QDICRAHDKC DTLGLAELGT ICDPYRSCSI 

       430        440        450        460        470        480 
SEDSGLSTAF TIAHELGHVF NMPHDDNNKC KEEGVKSPQH VMAPTLNFYT NPWMWSKCSR 

       490        500        510        520        530        540 
KYITEFLDTG YGECLLNEPE SRPYPLPVQL PGILYNVNKQ CELIFGPGSQ VCPYMMQCRR 

       550        560        570        580        590        600 
LWCNNVNGVH KGCRTQHTPW ADGTECEPGK HCKYGFCVPK EMDVPVTDGS WGSWSPFGTC 

       610        620        630        640        650        660 
SRTCGGGIKT AIRECNRPEP KNGGKYCVGR RMKFKSCNTE PCLKQKRDFR DEQCAHFDGK 

       670        680        690        700        710        720 
HFNINGLLPN VRWVPKYSGI LMKDRCKLFC RVAGNTAYYQ LRDRVIDGTP CGQDTNDICV 

       730        740        750        760        770        780 
QGLCRQAGCD HVLNSKARRD KCGVCGGDNS SCKTVAGTFN TVHYGYNTVV RIPAGATNID 

       790        800        810        820        830        840 
VRQHSFSGET DDDNYLALSS SKGEFLLNGN FVVTMAKREI RIGNAVVEYS GSETAVERIN 

       850        860        870        880        890        900 
STDRIEQELL LQVLSVGKLY NPDVRYSFNI PIEDKPQQFY WNSHGPWQAC SKPCQGERKR 

       910        920        930        940        950        960 
KLVCTRESDQ LTVSDQRCDR LPQPGHITEP CGTDCDLRWH VASRSECSAQ CGLGYRTLDI 

       970        980        990       1000       1010       1020 
YCAKYSRLDG KTEKVDDGFC SSHPKPSNRE KCSGECNTGG WRYSAWTECS KSCDGGTQRR 

      1030       1040       1050       1060       1070       1080 
RAICVNTRND VLDDSKCTHQ EKVTIQRCSE FPCPQWKSGD WSECLVTCGK GHKHRQVWCQ 

      1090       1100       1110       1120       1130       1140 
FGEDRLNDRM CDPETKPTSM QTCQQPECAS WQAGPWGQCS VTCGQGYQLR AVKCIIGTYM 

      1150       1160       1170       1180       1190       1200 
SVVDDNDCNA ATRPTDTQDC ELPSCHPPPA APETRRSTYS APRTQWRFGS WTPCSATCGK 

      1210       1220       1230       1240       1250       1260 
GTRMRYVSCR DENGSVADES ACATLPRPVA KEECSVTPCG QWKALDWSSC SVTCGQGRAT 

      1270       1280       1290       1300       1310       1320 
RQVMCVNYSD HVIDRSECDQ DYIPETDQDC SMSPCPQRTP DSGLAQHPFQ NEDYRPRSAS 

      1330       1340       1350       1360       1370       1380 
PSRTHVLGGN QWRTGPWGAC SSTCAGGSQR RVVVCQDENG YTANDCVERI KPDEQRACES 

      1390       1400       1410       1420       1430       1440 
GPCPQWAYGN WGECTKLCGG GIRTRLVVCQ RSNGERFPDL SCEILDKPPD REQCNTHACP 

      1450       1460       1470       1480       1490       1500 
HDAAWSTGPW SSCSVSCGRG HKQRNVYCMA KDGSHLESDY CKHLAKPHGH RKCRGGRCPK 

      1510       1520       1530       1540       1550       1560 
WKAGAWSQCS VSCGRGVQQR HVGCQIGTHK IARETECNPY TRPESERDCQ GPRCPLYTWR 

      1570       1580       1590       1600       1610       1620 
AEEWQECTKT CGEGSRYRKV VCVDDNKNEV HGARCDVSKR PVDRESCSLQ PCEYVWITGE 

      1630       1640       1650       1660       1670       1680 
WSECSVTCGK GYKQRLVSCS EIYTGKENYE YSYQTTINCP GTQPPSVHPC YLRDCPVSAT 

      1690       1700       1710       1720       1730       1740 
WRVGNWGSCS VSCGVGVMQR SVQCLTNEDQ PSHLCHTDLK PEERKTCRNV YNCELPQNCK 

      1750       1760       1770       1780       1790       1800 
EVKRLKGASE DGEYFLMIRG KLLKIFCAGM HSDHPKEYVT LVHGDSENFS EVYGHRLHNP 

      1810       1820       1830       1840       1850       1860 
TECPYNGSRR DDCQCRKDYT AAGFSSFQKI RIDLTSMQII TTDLQFARTS EGHPVPFATA 

      1870       1880       1890       1900       1910       1920 
GDCYSAAKCP QGRFSINLYG TGLSLTESAR WISQGNYAVS DIKKSPDGTR VVGKCGGYCG 

      1930 
KCTPSSGTGL EVRVL 

« Hide

Isoform 2 (Long) [UniParc].

Checksum: E72B933CEED67809
Show »

FASTA1,629182,680
Isoform 3 (Short) [UniParc].

Checksum: 85251C8E59449E0C
Show »

FASTA1,072120,717
Isoform 4 [UniParc].

Checksum: 24BD2199B1142022
Show »

FASTA1,907213,420

References

« Hide 'large scale' references
[1]"ADAMTS 9, a novel member of the ADAM-TS/Metallospondin gene family."
Clark M.E., Kelner G.S., Turbeville L.A., Boyer A., Arden K.A., Maki R.A.
Genomics 67:343-350(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Fetus.
[2]"Characterization of ADAMTS-9 and ADAMTS-20 as a distinct ADAMTS subfamily related to Caenorhabditis elegans GON-1."
Somerville R.P., Longpre J.-M., Jungers K.A., Engle J.M., Ross M., Evanko S., Wight T.N., Leduc R., Apte S.S.
J. Biol. Chem. 278:9503-9513(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, VARIANTS PRO-96 AND GLU-1674.
[3]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [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] (ISOFORMS 1 AND 4).
[5]"Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 159-1935 (ISOFORM 2).
Tissue: Brain.
[6]"Identification of a novel ADAMTS9/GON-1 function for protein transport from the ER to the Golgi."
Yoshina S., Sakaki K., Yonezumi-Hayashi A., Gengyo-Ando K., Inoue H., Iino Y., Mitani S.
Mol. Biol. Cell 23:1728-1741(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRANSPORT, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF261918 mRNA. Translation: AAF89106.1.
AF488803 mRNA. Translation: AAO15765.1.
AC096888 Genomic DNA. No translation available.
AC122178 Genomic DNA. No translation available.
BC130578 mRNA. Translation: AAI30579.1.
BC171764 mRNA. Translation: AAI71764.1.
AB037733 mRNA. Translation: BAA92550.1.
RefSeqNP_891550.1. NM_182920.1.
XP_005265386.1. XM_005265329.1.
UniGeneHs.656071.

3D structure databases

ProteinModelPortalQ9P2N4.
SMRQ9P2N4. Positions 293-872, 880-1555, 1561-1613, 1617-1734.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9P2N4. 1 interaction.
STRING9606.ENSP00000418735.

Protein family/group databases

MEROPSM12.021.

PTM databases

PhosphoSiteQ9P2N4.

Polymorphism databases

DMDM212276516.

Proteomic databases

PaxDbQ9P2N4.
PRIDEQ9P2N4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295903; ENSP00000295903; ENSG00000163638. [Q9P2N4-4]
ENST00000498707; ENSP00000418735; ENSG00000163638. [Q9P2N4-3]
GeneID56999.
KEGGhsa:56999.
UCSCuc003dmg.3. human. [Q9P2N4-3]
uc003dmh.1. human. [Q9P2N4-1]
uc003dmk.1. human. [Q9P2N4-2]
uc011bfo.2. human.

Organism-specific databases

CTD56999.
GeneCardsGC03M064501.
HGNCHGNC:13202. ADAMTS9.
HPAHPA028567.
HPA028577.
MIM605421. gene.
neXtProtNX_Q9P2N4.
PharmGKBPA24553.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG237764.
HOGENOMHOG000004798.
HOVERGENHBG037334.
InParanoidQ9P2N4.
KOK08624.
OMACQGERKR.
PhylomeDBQ9P2N4.
TreeFamTF331949.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ9P2N4.
BgeeQ9P2N4.
CleanExHS_ADAMTS9.
GenevestigatorQ9P2N4.

Family and domain databases

Gene3D3.40.390.10. 2 hits.
InterProIPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR012314. Pept_M12B_GON-ADAMTSs.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamPF05986. ADAM_spacer1. 1 hit.
PF08685. GON. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 13 hits.
[Graphical view]
PRINTSPR01857. ADAMTSFAMILY.
SMARTSM00209. TSP1. 15 hits.
[Graphical view]
SUPFAMSSF82895. SSF82895. 14 hits.
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS51046. GON. 1 hit.
PS50092. TSP1. 14 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiADAMTS9.
GenomeRNAi56999.
NextBio35481460.
PMAP-CutDBQ9P2N4.
PROQ9P2N4.
SOURCESearch...

Entry information

Entry nameATS9_HUMAN
AccessionPrimary (citable) accession number: Q9P2N4
Secondary accession number(s): A1L4L0 expand/collapse secondary AC list , B7ZVX9, B9ZVN0, Q9NR29
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 4, 2008
Last modified: March 19, 2014
This is version 133 of the entry and version 4 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 3

Human chromosome 3: entries, gene names and cross-references to MIM