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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 6

Gene

ADAMTS6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi403 – 4031Zinc; catalyticBy similarity
Active sitei404 – 4041PROSITE-ProRule annotation
Metal bindingi407 – 4071Zinc; catalyticBy similarity
Metal bindingi413 – 4131Zinc; catalyticBy similarity

GO - Molecular functioni

  1. metalloendopeptidase activity Source: InterPro
  2. metallopeptidase activity Source: ProtInc
  3. zinc ion binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

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

Protein family/group databases

MEROPSiM12.230.

Names & Taxonomyi

Protein namesi
Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 6 (EC:3.4.24.-)
Short name:
ADAM-TS 6
Short name:
ADAM-TS6
Short name:
ADAMTS-6
Gene namesi
Name:ADAMTS6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:222. ADAMTS6.

Subcellular locationi

GO - Cellular componenti

  1. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24550.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Propeptidei22 – 244223By similarityPRO_0000029174Add
BLAST
Chaini245 – 1117873A disintegrin and metalloproteinase with thrombospondin motifs 6PRO_0000029175Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi99 – 991N-linked (GlcNAc...)Sequence Analysis
Glycosylationi172 – 1721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi222 – 2221N-linked (GlcNAc...)Sequence Analysis
Glycosylationi234 – 2341N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi326 ↔ 387By similarity
Disulfide bondi362 ↔ 369By similarity
Disulfide bondi381 ↔ 463By similarity
Disulfide bondi420 ↔ 447By similarity
Disulfide bondi490 ↔ 512By similarity
Disulfide bondi501 ↔ 519By similarity
Disulfide bondi507 ↔ 542By similarity
Disulfide bondi532 ↔ 547By similarity
Disulfide bondi570 ↔ 607By similarity
Disulfide bondi574 ↔ 612By similarity
Disulfide bondi585 ↔ 597By similarity
Glycosylationi724 – 7241N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi911 ↔ 954By similarity
Disulfide bondi915 ↔ 959By similarity
Disulfide bondi926 ↔ 943By similarity
Glycosylationi956 – 9561N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

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).By similarity

Keywords - PTMi

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

Proteomic databases

PaxDbiQ9UKP5.
PRIDEiQ9UKP5.

PTM databases

PhosphoSiteiQ9UKP5.

Expressioni

Tissue specificityi

Expressed at low levels in placenta and barely detectable in a number of other tissues.

Inductioni

Isoform 1 and isoform 2 expressions are up-regulated by TNF in retinal pigment epithelial cells.2 Publications

Gene expression databases

BgeeiQ9UKP5.
CleanExiHS_ADAMTS6.
ExpressionAtlasiQ9UKP5. baseline and differential.
GenevestigatoriQ9UKP5.

Organism-specific databases

HPAiHPA027216.
HPA043441.

Interactioni

Protein-protein interaction databases

BioGridi116345. 2 interactions.

Structurei

3D structure databases

SMRiQ9UKP5. Positions 247-729.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini250 – 468219Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini495 – 55763DisintegrinAdd
BLAST
Domaini558 – 61356TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini840 – 90061TSP type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini902 – 96059TSP type-1 3PROSITE-ProRule annotationAdd
BLAST
Domaini962 – 100746TSP type-1 4PROSITE-ProRule annotationAdd
BLAST
Domaini1018 – 107356TSP type-1 5PROSITE-ProRule annotationAdd
BLAST
Domaini1079 – 111739PLACPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni717 – 843127SpacerAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 disintegrin domain.Curated
Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
Contains 1 PLAC domain.PROSITE-ProRule annotation
Contains 5 TSP type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG237764.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000004800.
HOVERGENiHBG004315.
InParanoidiQ9UKP5.
KOiK08621.
OMAiDNEVGFM.
OrthoDBiEOG78WKQV.
PhylomeDBiQ9UKP5.
TreeFamiTF313537.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR010909. PLAC.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF08686. PLAC. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 5 hits.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 5 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 5 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 4 hits.
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. AlignAdd to basket

Isoform 1 (identifier: Q9UKP5-1) [UniParc]FASTAAdd to basket

Also known as: Variant 2

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
MEILWKTLTW ILSLIMASSE FHSDHRLSYS SQEEFLTYLE HYQLTIPIRV
60 70 80 90 100
DQNGAFLSFT VKNDKHSRRR RSMDPIDPQQ AVSKLFFKLS AYGKHFHLNL
110 120 130 140 150
TLNTDFVSKH FTVEYWGKDG PQWKHDFLDN CHYTGYLQDQ RSTTKVALSN
160 170 180 190 200
CVGLHGVIAT EDEEYFIEPL KNTTEDSKHF SYENGHPHVI YKKSALQQRH
210 220 230 240 250
LYDHSHCGVS DFTRSGKPWW LNDTSTVSYS LPINNTHIHH RQKRSVSIER
260 270 280 290 300
FVETLVVADK MMVGYHGRKD IEHYILSVMN IVAKLYRDSS LGNVVNIIVA
310 320 330 340 350
RLIVLTEDQP NLEINHHADK SLDSFCKWQK SILSHQSDGN TIPENGIAHH
360 370 380 390 400
DNAVLITRYD ICTYKNKPCG TLGLASVAGM CEPERSCSIN EDIGLGSAFT
410 420 430 440 450
IAHEIGHNFG MNHDGIGNSC GTKGHEAAKL MAAHITANTN PFSWSACSRD
460 470 480 490 500
YITSFLDSGR GTCLDNEPPK RDFLYPAVAP GQVYDADEQC RFQYGATSRQ
510 520 530 540 550
CKYGEVCREL WCLSKSNRCV TNSIPAAEGT LCQTGNIEKG WCYQGDCVPF
560 570 580 590 600
GTWPQSIDGG WGPWSLWGEC SRTCGGGVSS SLRHCDSPAP SGGGKYCLGE
610 620 630 640 650
RKRYRSCNTD PCPLGSRDFR EKQCADFDNM PFRGKYYNWK PYTGGGVKPC
660 670 680 690 700
ALNCLAEGYN FYTERAPAVI DGTQCNADSL DICINGECKH VGCDNILGSD
710 720 730 740 750
AREDRCRVCG GDGSTCDAIE GFFNDSLPRG GYMEVVQIPR GSVHIEVREV
760 770 780 790 800
AMSKNYIALK SEGDDYYING AWTIDWPRKF DVAGTAFHYK RPTDEPESLE
810 820 830 840 850
ALGPTSENLI VMVLLQEQNL GIRYKFNVPI TRTGSGDNEV GFTWNHQPWS
860 870 880 890 900
ECSATCAGGV QRQEVVCKRL DDNSIVQNNY CDPDSKPPEN QRACNTEPCP
910 920 930 940 950
PEWFIGDWLE CSKTCDGGMR TRAVLCIRKI GPSEEETLDY SGCLTHRPVE
960 970 980 990 1000
KEPCNNQSCP PQWVALDWSE CTPKCGPGFK HRIVLCKSSD LSKTFPAAQC
1010 1020 1030 1040 1050
PEESKPPVRI RCSLGRCPPP RWVTGDWGQC SAQCGLGQQM RTVQCLSYTG
1060 1070 1080 1090 1100
QASSDCLETV RPPSMQQCES KCDSTPISNT EECKDVNKVA YCPLVLKFKF
1110
CSRAYFRQMC CKTCQGH
Length:1,117
Mass (Da):125,273
Last modified:May 4, 2009 - v2
Checksum:i5901E86BC82A9A87
GO
Isoform 2 (identifier: Q9UKP5-2) [UniParc]FASTAAdd to basket

Also known as: Variant 1

The sequence of this isoform differs from the canonical sequence as follows:
     422-504: TKGHEAAKLM...GATSRQCKYG → RKVMKQQNYGSSHYCEYQSFFLVCLQSRFHHQLFR
     860-908: VQRQEVVCKR...CPPEWFIGDW → KMPTRQPTQR...SCNLAKETLL
     909-1117: Missing.

Note: Contains critical point mutations in the region encoding the catalytic domain as well as 2 point mutations compared with genomic sequence. May either be a rare polymorphism or may have arisen through a combination of aberrant RNA editing and point mutation/sequencing error.

Show »
Length:860
Mass (Da):97,152
Checksum:iEA137275B9A465C2
GO
Isoform 3 (identifier: Q9UKP5-3) [UniParc]FASTAAdd to basket

Also known as: Variant 3

The sequence of this isoform differs from the canonical sequence as follows:
     457-468: DSGRGTCLDNEP → EFLKLGDSISGS
     469-1117: Missing.

Show »
Length:468
Mass (Da):53,165
Checksum:iE8D2E75EF8A1C468
GO
Isoform 4 (identifier: Q9UKP5-4) [UniParc]FASTAAdd to basket

Also known as: Variant 4

The sequence of this isoform differs from the canonical sequence as follows:
     283-292: AKLYRDSSLG → RLPNFTVIPA
     293-1117: Missing.

Show »
Length:292
Mass (Da):34,189
Checksum:i01A54680DCEFABD7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41L → S in AAW47399 (PubMed:16129570).Curated
Sequence conflicti24 – 241D → G in AAW47398 (PubMed:16129570).Curated
Sequence conflicti83 – 831S → P in AAW47398 (PubMed:16129570).Curated
Sequence conflicti229 – 2291Y → H in AAW47397 (PubMed:16129570).Curated
Sequence conflicti406 – 4061G → V in AAD56357 (PubMed:10464288).Curated
Sequence conflicti426 – 4261E → G in AAD56357 (PubMed:10464288).Curated
Sequence conflicti426 – 4261E → G in AAW47397 (PubMed:16129570).Curated
Sequence conflicti588 – 5892PA → LK in BAD92922 (Ref. 4) Curated
Sequence conflicti712 – 7121D → G in AAD56357 (PubMed:10464288).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei283 – 29210AKLYRDSSLG → RLPNFTVIPA in isoform 4. 1 PublicationVSP_037093
Alternative sequencei293 – 1117825Missing in isoform 4. 1 PublicationVSP_037094Add
BLAST
Alternative sequencei422 – 50483TKGHE…QCKYG → RKVMKQQNYGSSHYCEYQSF FLVCLQSRFHHQLFR in isoform 2. 1 PublicationVSP_037095Add
BLAST
Alternative sequencei457 – 46812DSGRG…LDNEP → EFLKLGDSISGS in isoform 3. 1 PublicationVSP_037096Add
BLAST
Alternative sequencei469 – 1117649Missing in isoform 3. 1 PublicationVSP_037097Add
BLAST
Alternative sequencei860 – 90849VQRQE…FIGDW → KMPTRQPTQRARWRTKHILS YALCLLKKLIGNISCRFASS CNLAKETLL in isoform 2. 1 PublicationVSP_037098Add
BLAST
Alternative sequencei909 – 1117209Missing in isoform 2. 1 PublicationVSP_037099Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF140674 mRNA. Translation: AAD56357.1.
AY692424 mRNA. Translation: AAW47397.1.
AY692425 mRNA. Translation: AAW47398.1.
AY692426 mRNA. Translation: AAW47399.1.
AC008847 Genomic DNA. No translation available.
AC008868 Genomic DNA. No translation available.
AC025176 Genomic DNA. No translation available.
AC025186 Genomic DNA. No translation available.
AC099505 Genomic DNA. No translation available.
AB209685 mRNA. Translation: BAD92922.1.
CR749356 mRNA. Translation: CAH18209.1.
CCDSiCCDS3983.2. [Q9UKP5-1]
RefSeqiNP_922932.2. NM_197941.2. [Q9UKP5-1]
UniGeneiHs.482291.

Genome annotation databases

EnsembliENST00000381052; ENSP00000424377; ENSG00000049192. [Q9UKP5-4]
ENST00000381055; ENSP00000370443; ENSG00000049192. [Q9UKP5-1]
GeneIDi11174.
KEGGihsa:11174.
UCSCiuc003jto.4. human. [Q9UKP5-1]

Polymorphism databases

DMDMi229462816.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF140674 mRNA. Translation: AAD56357.1.
AY692424 mRNA. Translation: AAW47397.1.
AY692425 mRNA. Translation: AAW47398.1.
AY692426 mRNA. Translation: AAW47399.1.
AC008847 Genomic DNA. No translation available.
AC008868 Genomic DNA. No translation available.
AC025176 Genomic DNA. No translation available.
AC025186 Genomic DNA. No translation available.
AC099505 Genomic DNA. No translation available.
AB209685 mRNA. Translation: BAD92922.1.
CR749356 mRNA. Translation: CAH18209.1.
CCDSiCCDS3983.2. [Q9UKP5-1]
RefSeqiNP_922932.2. NM_197941.2. [Q9UKP5-1]
UniGeneiHs.482291.

3D structure databases

SMRiQ9UKP5. Positions 247-729.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116345. 2 interactions.

Protein family/group databases

MEROPSiM12.230.

PTM databases

PhosphoSiteiQ9UKP5.

Polymorphism databases

DMDMi229462816.

Proteomic databases

PaxDbiQ9UKP5.
PRIDEiQ9UKP5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000381052; ENSP00000424377; ENSG00000049192. [Q9UKP5-4]
ENST00000381055; ENSP00000370443; ENSG00000049192. [Q9UKP5-1]
GeneIDi11174.
KEGGihsa:11174.
UCSCiuc003jto.4. human. [Q9UKP5-1]

Organism-specific databases

CTDi11174.
GeneCardsiGC05M064526.
HGNCiHGNC:222. ADAMTS6.
HPAiHPA027216.
HPA043441.
MIMi605008. gene.
neXtProtiNX_Q9UKP5.
PharmGKBiPA24550.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG237764.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000004800.
HOVERGENiHBG004315.
InParanoidiQ9UKP5.
KOiK08621.
OMAiDNEVGFM.
OrthoDBiEOG78WKQV.
PhylomeDBiQ9UKP5.
TreeFamiTF313537.

Enzyme and pathway databases

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

Miscellaneous databases

GenomeRNAii11174.
NextBioi42521.
PROiQ9UKP5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UKP5.
CleanExiHS_ADAMTS6.
ExpressionAtlasiQ9UKP5. baseline and differential.
GenevestigatoriQ9UKP5.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR010909. PLAC.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF08686. PLAC. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 5 hits.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 5 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 5 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases."
    Hurskainen T.L., Hirohata S., Seldin M.F., Apte S.S.
    J. Biol. Chem. 274:25555-25563(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "Analysis of full length ADAMTS6 transcript reveals alternative splicing and a role for the 5' untranslated region in translational control."
    Bevitt D.J., Li Z., Lindrop J.L., Barker M.D., Clarke M.P., McKie N.
    Gene 359:99-110(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), INDUCTION.
  3. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 588-1117 (ISOFORM 1).
    Tissue: Brain.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 804-1117 (ISOFORM 1).
    Tissue: Uterus.
  6. "Expression of ADAMTS metalloproteinases in the retinal pigment epithelium derived cell line ARPE-19: transcriptional regulation by TNFalpha."
    Bevitt D.J., Mohamed J., Catterall J.B., Li Z., Arris C.E., Hiscott P., Sheridan C., Langton K.P., Barker M.D., Clarke M.P., McKie N.
    Biochim. Biophys. Acta 1626:83-91(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiATS6_HUMAN
AccessioniPrimary (citable) accession number: Q9UKP5
Secondary accession number(s): Q59EX6
, Q5IR87, Q5IR88, Q5IR89, Q68DL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 30, 2000
Last sequence update: May 4, 2009
Last modified: March 31, 2015
This is version 138 of the entry and version 2 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 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. 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.