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Protein

ADAMTS-like protein 2

Gene

ADAMTSL2

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

Functioni

GO - Molecular functioni

GO - Biological processi

  • negative regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCL
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_264269. O-glycosylation of TSR domain-containing proteins.
SignaLinkiQ86TH1.

Names & Taxonomyi

Protein namesi
Recommended name:
ADAMTS-like protein 2
Short name:
ADAMTSL-2
Gene namesi
Name:ADAMTSL2
Synonyms:KIAA0605
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:14631. ADAMTSL2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Geleophysic dysplasia 1 (GPHYSD1)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal recessive disorder characterized by severe short stature, short hands and feet, joint limitations, and skin thickening. Radiologic features include delayed bone age, cone-shaped epiphyses, shortened long tubular bones, and ovoid vertebral bodies. Affected individuals have characteristic facial features including a 'happy' face with full cheeks, shortened nose, hypertelorism, long and flat philtrum, and thin upper lip. Other distinctive features include progressive cardiac valvular thickening often leading to an early death, toe walking, tracheal stenosis, respiratory insufficiency, and lysosomal-like storage vacuoles in various tissues.

See also OMIM:231050
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti50 – 501W → C in GPHYSD1. 1 Publication
VAR_066543
Natural varianti72 – 721R → Q in GPHYSD1. 1 Publication
VAR_066544
Natural varianti113 – 1131R → H in GPHYSD1; leads to the reduced secretion of the mutated protein. 1 Publication
VAR_054874
Natural varianti114 – 1141E → K in GPHYSD1. 2 Publications
VAR_054875
Natural varianti147 – 1471P → L in GPHYSD1; leads to the reduced secretion of the mutated protein. 1 Publication
VAR_054876
Natural varianti159 – 1591R → W in GPHYSD1. 1 Publication
VAR_066545
Natural varianti165 – 1651A → T in GPHYSD1. 1 Publication
VAR_066546
Natural varianti171 – 1711C → R in GPHYSD1. 1 Publication
VAR_066547
Natural varianti221 – 2211R → C in GPHYSD1. 1 Publication
VAR_066548
Natural varianti239 – 2391A → T in GPHYSD1. 1 Publication
VAR_066549
Natural varianti383 – 39210Missing in GPHYSD1. 1 Publication
VAR_066550
Natural varianti593 – 5931R → C in GPHYSD1. 1 Publication
VAR_066551
Natural varianti635 – 6351S → L in GPHYSD1. 1 Publication
VAR_066552
Natural varianti811 – 8111G → R in GPHYSD1; leads to the reduced secretion of the mutated protein. 1 Publication
VAR_054877
Natural varianti906 – 9061P → L in GPHYSD1. 1 Publication
VAR_066553

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

MIMi231050. phenotype.
Orphaneti2623. Geleophysic dysplasia.
PharmGKBiPA134920655.

Polymorphism and mutation databases

BioMutaiADAMTSL2.
DMDMi74750384.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 951929ADAMTS-like protein 2PRO_0000249682Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi59 ↔ 100PROSITE-ProRule annotation
Disulfide bondi63 ↔ 105PROSITE-ProRule annotation
Disulfide bondi74 ↔ 90PROSITE-ProRule annotation
Glycosylationi87 – 871N-linked (GlcNAc...)Sequence Analysis
Glycosylationi367 – 3671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi428 – 4281N-linked (GlcNAc...) (complex)1 Publication
Glycosylationi475 – 4751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi511 – 5111N-linked (GlcNAc...)Sequence Analysis
Glycosylationi524 – 5241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi533 – 5331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi544 – 5441N-linked (GlcNAc...)Sequence Analysis
Glycosylationi731 – 7311N-linked (GlcNAc...)Sequence Analysis
Glycosylationi807 – 8071N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Glycosylated (By similarity). 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).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ86TH1.
PRIDEiQ86TH1.

PTM databases

PhosphoSiteiQ86TH1.

Expressioni

Gene expression databases

BgeeiQ86TH1.
CleanExiHS_ADAMTSL2.
ExpressionAtlasiQ86TH1. baseline and differential.
GenevisibleiQ86TH1. HS.

Organism-specific databases

HPAiHPA045634.
HPA053812.

Interactioni

Subunit structurei

Interacts with LTBP1.1 Publication

Protein-protein interaction databases

BioGridi115068. 1 interaction.
IntActiQ86TH1. 2 interactions.
MINTiMINT-8417703.
STRINGi9606.ENSP00000346478.

Structurei

3D structure databases

ProteinModelPortaliQ86TH1.
SMRiQ86TH1. Positions 50-236.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 10660TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini564 – 61855TSP type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini622 – 68665TSP type-1 3PROSITE-ProRule annotationAdd
BLAST
Domaini688 – 73649TSP type-1 4PROSITE-ProRule annotationAdd
BLAST
Domaini737 – 79559TSP type-1 5PROSITE-ProRule annotationAdd
BLAST
Domaini797 – 85155TSP type-1 6PROSITE-ProRule annotationAdd
BLAST
Domaini853 – 90856TSP type-1 7PROSITE-ProRule annotationAdd
BLAST
Domaini912 – 95039PLACPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PLAC domain.PROSITE-ProRule annotation
Contains 7 TSP type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG299441.
GeneTreeiENSGT00760000118885.
HOGENOMiHOG000116076.
HOVERGENiHBG079685.
InParanoidiQ86TH1.
OrthoDBiEOG74N5FZ.
PhylomeDBiQ86TH1.
TreeFamiTF316874.

Family and domain databases

InterProiIPR010294. ADAM_spacer1.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR010909. PLAC.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF08686. PLAC. 1 hit.
PF00090. TSP_1. 5 hits.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 7 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 7 hits.
PROSITEiPS50900. PLAC. 1 hit.
PS50092. TSP1. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q86TH1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDGRWQCSCW AWFLLVLAVV AGDTVSTGST DNSPTSNSLE GGTDATAFWW
60 70 80 90 100
GEWTKWTACS RSCGGGVTSQ ERHCLQQRRK SVPGPGNRTC TGTSKRYQLC
110 120 130 140 150
RVQECPPDGR SFREEQCVSF NSHVYNGRTH QWKPLYPDDY VHISSKPCDL
160 170 180 190 200
HCTTVDGQRQ LMVPARDGTS CKLTDLRGVC VSGKCEPIGC DGVLFSTHTL
210 220 230 240 250
DKCGICQGDG SSCTHVTGNY RKGNAHLGYS LVTHIPAGAR DIQIVERKKS
260 270 280 290 300
ADVLALADEA GYYFFNGNYK VDSPKNFNIA GTVVKYRRPM DVYETGIEYI
310 320 330 340 350
VAQGPTNQGL NVMVWNQNGK SPSITFEYTL LQPPHESRPQ PIYYGFSESA
360 370 380 390 400
ESQGLDGAGL MGFVPHNGSL YGQASSERLG LDNRLFGHPG LDMELGPSQG
410 420 430 440 450
QETNEVCEQA GGGACEGPPR GKGFRDRNVT GTPLTGDKDD EEVDTHFASQ
460 470 480 490 500
EFFSANAISD QLLGAGSDLK DFTLNETVNS IFAQGAPRSS LAESFFVDYE
510 520 530 540 550
ENEGAGPYLL NGSYLELSSD RVANSSSEAP FPNVSTSLLT SAGNRTHKAR
560 570 580 590 600
TRPKARKQGV SPADMYRWKL SSHEPCSATC TTGVMSAYAM CVRYDGVEVD
610 620 630 640 650
DSYCDALTRP EPVHEFCAGR ECQPRWETSS WSECSRTCGE GYQFRVVRCW
660 670 680 690 700
KMLSPGFDSS VYSDLCEAAE AVRPEERKTC RNPACGPQWE MSEWSECTAK
710 720 730 740 750
CGERSVVTRD IRCSEDEKLC DPNTRPVGEK NCTGPPCDRQ WTVSDWGPCS
760 770 780 790 800
GSCGQGRTIR HVYCKTSDGR VVPESQCQME TKPLAIHPCG DKNCPAHWLA
810 820 830 840 850
QDWERCNTTC GRGVKKRLVL CMELANGKPQ TRSGPECGLA KKPPEESTCF
860 870 880 890 900
ERPCFKWYTS PWSECTKTCG VGVRMRDVKC YQGTDIVRGC DPLVKPVGRQ
910 920 930 940 950
ACDLQPCPTE PPDDSCQDQP GTNCALAIKV NLCGHWYYSK ACCRSCRPPH

S
Length:951
Mass (Da):104,621
Last modified:June 1, 2003 - v1
Checksum:i93A9B0DC5BAB6CC7
GO

Sequence cautioni

The sequence BAA25531.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti59 – 591C → F in BAA25531 (PubMed:9628581).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti50 – 501W → C in GPHYSD1. 1 Publication
VAR_066543
Natural varianti72 – 721R → Q in GPHYSD1. 1 Publication
VAR_066544
Natural varianti113 – 1131R → H in GPHYSD1; leads to the reduced secretion of the mutated protein. 1 Publication
VAR_054874
Natural varianti114 – 1141E → K in GPHYSD1. 2 Publications
VAR_054875
Natural varianti147 – 1471P → L in GPHYSD1; leads to the reduced secretion of the mutated protein. 1 Publication
VAR_054876
Natural varianti159 – 1591R → W in GPHYSD1. 1 Publication
VAR_066545
Natural varianti165 – 1651A → T in GPHYSD1. 1 Publication
VAR_066546
Natural varianti171 – 1711C → R in GPHYSD1. 1 Publication
VAR_066547
Natural varianti221 – 2211R → C in GPHYSD1. 1 Publication
VAR_066548
Natural varianti239 – 2391A → T in GPHYSD1. 1 Publication
VAR_066549
Natural varianti364 – 3641V → I.1 Publication
Corresponds to variant rs35767802 [ dbSNP | Ensembl ].
VAR_046011
Natural varianti383 – 39210Missing in GPHYSD1. 1 Publication
VAR_066550
Natural varianti593 – 5931R → C in GPHYSD1. 1 Publication
VAR_066551
Natural varianti635 – 6351S → L in GPHYSD1. 1 Publication
VAR_066552
Natural varianti811 – 8111G → R in GPHYSD1; leads to the reduced secretion of the mutated protein. 1 Publication
VAR_054877
Natural varianti906 – 9061P → L in GPHYSD1. 1 Publication
VAR_066553

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011177 mRNA. Translation: BAA25531.2. Different initiation.
BX324209, BX629352, BX649571 Genomic DNA. Translation: CAI17317.1.
BX649571, BX324209, BX629352 Genomic DNA. Translation: CAI18773.1.
BX629352, BX324209, BX649571 Genomic DNA. Translation: CAI23592.1.
BC050544 mRNA. Translation: AAH50544.1.
CCDSiCCDS6976.1.
PIRiT00260.
RefSeqiNP_001138792.1. NM_001145320.1.
NP_055509.2. NM_014694.3.
XP_005272296.1. XM_005272239.2.
XP_006717400.1. XM_006717337.2.
UniGeneiHs.522543.

Genome annotation databases

EnsembliENST00000354484; ENSP00000346478; ENSG00000197859.
ENST00000393060; ENSP00000376780; ENSG00000197859.
GeneIDi9719.
KEGGihsa:9719.
UCSCiuc004cei.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011177 mRNA. Translation: BAA25531.2. Different initiation.
BX324209, BX629352, BX649571 Genomic DNA. Translation: CAI17317.1.
BX649571, BX324209, BX629352 Genomic DNA. Translation: CAI18773.1.
BX629352, BX324209, BX649571 Genomic DNA. Translation: CAI23592.1.
BC050544 mRNA. Translation: AAH50544.1.
CCDSiCCDS6976.1.
PIRiT00260.
RefSeqiNP_001138792.1. NM_001145320.1.
NP_055509.2. NM_014694.3.
XP_005272296.1. XM_005272239.2.
XP_006717400.1. XM_006717337.2.
UniGeneiHs.522543.

3D structure databases

ProteinModelPortaliQ86TH1.
SMRiQ86TH1. Positions 50-236.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115068. 1 interaction.
IntActiQ86TH1. 2 interactions.
MINTiMINT-8417703.
STRINGi9606.ENSP00000346478.

PTM databases

PhosphoSiteiQ86TH1.

Polymorphism and mutation databases

BioMutaiADAMTSL2.
DMDMi74750384.

Proteomic databases

PaxDbiQ86TH1.
PRIDEiQ86TH1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000354484; ENSP00000346478; ENSG00000197859.
ENST00000393060; ENSP00000376780; ENSG00000197859.
GeneIDi9719.
KEGGihsa:9719.
UCSCiuc004cei.3. human.

Organism-specific databases

CTDi9719.
GeneCardsiGC09P136397.
GeneReviewsiADAMTSL2.
H-InvDBHIX0170293.
HGNCiHGNC:14631. ADAMTSL2.
HPAiHPA045634.
HPA053812.
MIMi231050. phenotype.
612277. gene.
neXtProtiNX_Q86TH1.
Orphaneti2623. Geleophysic dysplasia.
PharmGKBiPA134920655.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG299441.
GeneTreeiENSGT00760000118885.
HOGENOMiHOG000116076.
HOVERGENiHBG079685.
InParanoidiQ86TH1.
OrthoDBiEOG74N5FZ.
PhylomeDBiQ86TH1.
TreeFamiTF316874.

Enzyme and pathway databases

ReactomeiREACT_264269. O-glycosylation of TSR domain-containing proteins.
SignaLinkiQ86TH1.

Miscellaneous databases

ChiTaRSiADAMTSL2. human.
GenomeRNAii9719.
NextBioi36549.
PROiQ86TH1.
SOURCEiSearch...

Gene expression databases

BgeeiQ86TH1.
CleanExiHS_ADAMTSL2.
ExpressionAtlasiQ86TH1. baseline and differential.
GenevisibleiQ86TH1. HS.

Family and domain databases

InterProiIPR010294. ADAM_spacer1.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR010909. PLAC.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF08686. PLAC. 1 hit.
PF00090. TSP_1. 5 hits.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 7 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 7 hits.
PROSITEiPS50900. PLAC. 1 hit.
PS50092. TSP1. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-364.
    Tissue: Brain.
  2. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
    Tissue: PNS.
  4. Cited for: GLYCOSYLATION AT ASN-428.
  5. "ADAMTSL2 mutations in geleophysic dysplasia demonstrate a role for ADAMTS-like proteins in TGF-beta bioavailability regulation."
    Le Goff C., Morice-Picard F., Dagoneau N., Wang L.W., Perrot C., Crow Y.J., Bauer F., Flori E., Prost-Squarcioni C., Krakow D., Ge G., Greenspan D.S., Bonnet D., Le Merrer M., Munnich A., Apte S.S., Cormier-Daire V.
    Nat. Genet. 40:1119-1123(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS GPHYSD1 HIS-113; LYS-114; LEU-147 AND ARG-811, CHARACTERIZATION OF VARIANTS HIS-113; LEU-147 AND ARG-811, INTERACTION WITH LTBP1.
  6. Cited for: VARIANTS GPHYSD1 CYS-50; GLN-72; LYS-114; TRP-159; THR-165; ARG-171; CYS-221; THR-239; 383-ASN--ASP-392 DEL; CYS-593; LEU-635 AND LEU-906.

Entry informationi

Entry nameiATL2_HUMAN
AccessioniPrimary (citable) accession number: Q86TH1
Secondary accession number(s): B1B0D5, O60345
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: June 1, 2003
Last modified: July 22, 2015
This is version 103 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

Miscellaneous

There is a significant increase in total and active TGFB1 in the culture medium as well as nuclear localization of phosphorylated SMAD2 in fibroblasts from individuals with geleophysic dysplasia.

Caution

Although strongly similar to members of the ADAMTS family it lacks the metalloprotease and disintegrin-like domains which are typical of that family.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.