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Protein

Dual specificity protein phosphatase 15

Gene

DUSP15

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

Functioni

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei85 – 851Phosphocysteine intermediatePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

SABIO-RKQ9H1R2.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein phosphatase 15 (EC:3.1.3.16, EC:3.1.3.48)
Alternative name(s):
VH1-related member Y
Vaccinia virus VH1-related dual-specific protein phosphatase Y
Gene namesi
Name:DUSP15
Synonyms:C20orf57, VHY
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:16190. C20orf57.
HGNC:16236. DUSP15.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi85 – 851C → S: Loss of phosphatase activity. 1 Publication

Organism-specific databases

PharmGKBiPA27524.

Polymorphism and mutation databases

DMDMi30316387.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 295295Dual specificity protein phosphatase 15PRO_0000094824Add
BLAST
Isoform 3 (identifier: Q9H1R2-3)
Initiator methioninei1 – 11Removed

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform 3 (identifier: Q9H1R2-3)
Lipidationi2 – 21N-myristoyl glycine

Keywords - PTMi

Lipoprotein, Myristate

Proteomic databases

PaxDbiQ9H1R2.
PRIDEiQ9H1R2.

PTM databases

DEPODiQ9H1R2.
PhosphoSiteiQ9H1R2.

Expressioni

Tissue specificityi

Highly expressed in testis.1 Publication

Gene expression databases

BgeeiQ9H1R2.
CleanExiHS_C20orf57.
HS_DUSP15.
ExpressionAtlasiQ9H1R2. baseline and differential.
GenevisibleiQ9H1R2. HS.

Organism-specific databases

HPAiHPA031114.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
NCK1P163332EBI-1752795,EBI-389883
PLCG1P191742EBI-1752795,EBI-79387

Protein-protein interaction databases

BioGridi126164. 1 interaction.
IntActiQ9H1R2. 9 interactions.
MINTiMINT-7241177.
STRINGi9606.ENSP00000341658.

Structurei

Secondary structure

1
295
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 124Combined sources
Helixi16 – 183Combined sources
Helixi20 – 256Combined sources
Beta strandi30 – 345Combined sources
Beta strandi46 – 505Combined sources
Helixi60 – 634Combined sources
Helixi64 – 7613Combined sources
Beta strandi81 – 855Combined sources
Beta strandi88 – 903Combined sources
Helixi91 – 10414Combined sources
Helixi108 – 11710Combined sources
Helixi126 – 13712Combined sources
Helixi139 – 1457Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YZ4X-ray2.40A/B5-145[»]
ProteinModelPortaliQ9H1R2.
SMRiQ9H1R2. Positions 5-146.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H1R2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini62 – 13271Tyrosine-protein phosphataseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118853.
HOGENOMiHOG000007880.
HOVERGENiHBG054344.
InParanoidiQ9H1R2.
KOiK14165.
OMAiSCIPACL.
OrthoDBiEOG7966HM.
PhylomeDBiQ9H1R2.
TreeFamiTF105126.

Family and domain databases

Gene3Di2.60.200.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR017855. SMAD_dom-like.
IPR008984. SMAD_FHA_domain.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSiPR01908. ADSPHPHTASE.
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 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: Q9H1R2-1) [UniParc]FASTAAdd to basket

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
MTEGVLPGLY LGNFIDAKDL DQLGRNKITH IISIHESPQP LLQDITYLRI
60 70 80 90 100
PVADTPEVPI KKHFKECINF IHCCRLNGGN CLVHCFAGIS RSTTIVTAYV
110 120 130 140 150
MTVTGLGWRD VLEAIKATRP IANPNPGFRQ QLEEFGWASS QKGARHRTSK
160 170 180 190 200
TSGAQCPPMT SATCLLAARV ALLSAALVRE ATGRTAQRCR LSPRAAAERL
210 220 230 240 250
LGPPPHVAAG WSPDPKYQIC LCFGEEDPGP TQHPKEQLIM ADVQVQLRPG
260 270 280 290
SSSCTLSAST ERPDGSSTPG NPDGITHLQC SCLHPKRAAS SSCTR
Length:295
Mass (Da):31,882
Last modified:April 30, 2003 - v4
Checksum:i28F8A687ECB5C219
GO
Isoform 2 (identifier: Q9H1R2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     143-232: GARHRTSKTS...FGEEDPGPTQ → LRRQLEERFG...PRCLSRKGGK
     233-295: Missing.

Note: Derived from EST data.
Show »
Length:232
Mass (Da):25,851
Checksum:i806EB3DFA4167D76
GO
Isoform 3 (identifier: Q9H1R2-3) [UniParc]FASTAAdd to basket

Also known as: A

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MTEG → MGNGMTK
     143-232: GARHRTSKTS...FGEEDPGPTQ → LRRQLEERFG...PRCLSRKGGK
     233-295: Missing.

Show »
Length:235
Mass (Da):26,152
Checksum:iA3AF26789894FECB
GO
Isoform 4 (identifier: Q9H1R2-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-100: Missing.
     143-232: GARHRTSKTS...FGEEDPGPTQ → LRRQLEERFG...PRCLSRKGGK
     233-295: Missing.

Show »
Length:132
Mass (Da):14,721
Checksum:iF1690DF488891012
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 100100Missing in isoform 4. 1 PublicationVSP_043107Add
BLAST
Alternative sequencei1 – 44MTEG → MGNGMTK in isoform 3. 1 PublicationVSP_019228
Alternative sequencei143 – 23290GARHR…PGPTQ → LRRQLEERFGESPFRDEEEL RALLPLCKRCRQGSATSASS AGPHSAASEGTVQRLVPRTP REAHRPLPLLARVKQTFSCL PRCLSRKGGK in isoform 2, isoform 3 and isoform 4. 2 PublicationsVSP_007292Add
BLAST
Alternative sequencei233 – 29563Missing in isoform 2, isoform 3 and isoform 4. 2 PublicationsVSP_007293Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK091960 mRNA. Translation: BAG52450.1.
AK097430 mRNA. Translation: BAC05048.1.
AL160175 Genomic DNA. Translation: CAI12819.1.
AL160175 Genomic DNA. Translation: CAI12821.1.
AL160175 Genomic DNA. Translation: CAI12822.1.
CH471077 Genomic DNA. Translation: EAW76410.1.
BC056911 mRNA. Translation: AAH56911.1.
BM554314 mRNA. No translation available.
CCDSiCCDS13193.1. [Q9H1R2-3]
CCDS42862.1. [Q9H1R2-4]
RefSeqiNP_001012662.1. NM_001012644.1. [Q9H1R2-4]
NP_542178.2. NM_080611.3. [Q9H1R2-3]
NP_817130.1. NM_177991.1. [Q9H1R2-4]
UniGeneiHs.434108.
Hs.585017.

Genome annotation databases

EnsembliENST00000278979; ENSP00000278979; ENSG00000149599.
ENST00000339738; ENSP00000341658; ENSG00000149599. [Q9H1R2-3]
ENST00000375966; ENSP00000365133; ENSG00000149599. [Q9H1R2-2]
ENST00000398083; ENSP00000381157; ENSG00000149599. [Q9H1R2-4]
ENST00000398084; ENSP00000381158; ENSG00000149599. [Q9H1R2-4]
ENST00000486996; ENSP00000419818; ENSG00000149599. [Q9H1R2-4]
GeneIDi128853.
KEGGihsa:128853.
UCSCiuc002wwu.1. human. [Q9H1R2-1]
uc002wwv.1. human. [Q9H1R2-4]
uc002wwx.1. human. [Q9H1R2-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK091960 mRNA. Translation: BAG52450.1.
AK097430 mRNA. Translation: BAC05048.1.
AL160175 Genomic DNA. Translation: CAI12819.1.
AL160175 Genomic DNA. Translation: CAI12821.1.
AL160175 Genomic DNA. Translation: CAI12822.1.
CH471077 Genomic DNA. Translation: EAW76410.1.
BC056911 mRNA. Translation: AAH56911.1.
BM554314 mRNA. No translation available.
CCDSiCCDS13193.1. [Q9H1R2-3]
CCDS42862.1. [Q9H1R2-4]
RefSeqiNP_001012662.1. NM_001012644.1. [Q9H1R2-4]
NP_542178.2. NM_080611.3. [Q9H1R2-3]
NP_817130.1. NM_177991.1. [Q9H1R2-4]
UniGeneiHs.434108.
Hs.585017.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YZ4X-ray2.40A/B5-145[»]
ProteinModelPortaliQ9H1R2.
SMRiQ9H1R2. Positions 5-146.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126164. 1 interaction.
IntActiQ9H1R2. 9 interactions.
MINTiMINT-7241177.
STRINGi9606.ENSP00000341658.

Chemistry

BindingDBiQ9H1R2.
ChEMBLiCHEMBL2396507.

PTM databases

DEPODiQ9H1R2.
PhosphoSiteiQ9H1R2.

Polymorphism and mutation databases

DMDMi30316387.

Proteomic databases

PaxDbiQ9H1R2.
PRIDEiQ9H1R2.

Protocols and materials databases

DNASUi128853.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000278979; ENSP00000278979; ENSG00000149599.
ENST00000339738; ENSP00000341658; ENSG00000149599. [Q9H1R2-3]
ENST00000375966; ENSP00000365133; ENSG00000149599. [Q9H1R2-2]
ENST00000398083; ENSP00000381157; ENSG00000149599. [Q9H1R2-4]
ENST00000398084; ENSP00000381158; ENSG00000149599. [Q9H1R2-4]
ENST00000486996; ENSP00000419818; ENSG00000149599. [Q9H1R2-4]
GeneIDi128853.
KEGGihsa:128853.
UCSCiuc002wwu.1. human. [Q9H1R2-1]
uc002wwv.1. human. [Q9H1R2-4]
uc002wwx.1. human. [Q9H1R2-3]

Organism-specific databases

CTDi128853.
GeneCardsiGC20M030446.
GC20U990068.
H-InvDBHIX0015716.
HGNCiHGNC:16190. C20orf57.
HGNC:16236. DUSP15.
HPAiHPA031114.
neXtProtiNX_Q9H1R2.
PharmGKBiPA27524.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118853.
HOGENOMiHOG000007880.
HOVERGENiHBG054344.
InParanoidiQ9H1R2.
KOiK14165.
OMAiSCIPACL.
OrthoDBiEOG7966HM.
PhylomeDBiQ9H1R2.
TreeFamiTF105126.

Enzyme and pathway databases

SABIO-RKQ9H1R2.

Miscellaneous databases

EvolutionaryTraceiQ9H1R2.
GeneWikiiDUSP15.
GenomeRNAii128853.
NextBioi82475.
PROiQ9H1R2.

Gene expression databases

BgeeiQ9H1R2.
CleanExiHS_C20orf57.
HS_DUSP15.
ExpressionAtlasiQ9H1R2. baseline and differential.
GenevisibleiQ9H1R2. HS.

Family and domain databases

Gene3Di2.60.200.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR017855. SMAD_dom-like.
IPR008984. SMAD_FHA_domain.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSiPR01908. ADSPHPHTASE.
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
    Tissue: Testis.
  2. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING.
  3. 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 2 AND 3).
    Tissue: Brain and PNS.
  5. "VHY, a novel myristoylated testis-restricted dual specificity protein phosphatase related to VHX."
    Alonso A., Narisawa S., Bogetz J., Tautz L., Hadzic R., Huynh H., Williams S., Gjoerloff-Wingren A., Bremer M.C.D., Holsinger L.J., Millan J.L., Mustelin T.
    J. Biol. Chem. 279:32586-32591(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-85, MYRISTOYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. "Crystal structure of the catalytic domain of human VHY, a dual-specificity protein phosphatase."
    Yoon T.-S., Jeong D.G., Kim J.H., Cho Y.H., Son J.H., Lee J.W., Ryu S.E., Kim S.J.
    Proteins 61:694-697(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-157 (ISOFORM 3).

Entry informationi

Entry nameiDUS15_HUMAN
AccessioniPrimary (citable) accession number: Q9H1R2
Secondary accession number(s): A6NH79
, A8MVC8, Q5QP62, Q5QP63, Q5QP65, Q6PGN7, Q8N826, Q9BX24
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: April 30, 2003
Last modified: July 22, 2015
This is version 138 of the entry and version 4 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

Caution

Although assigned as two separate genes (c20orf57 and DUSP15), it is probable that C20orf57 does not exist by itself and is a part of the DUSP15 gene.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.