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Q9H1R2

- DUS15_HUMAN

UniProt

Q9H1R2 - DUS15_HUMAN

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Protein

Dual specificity protein phosphatase 15

Gene
DUSP15, C20orf57, VHY
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei85 – 851Phosphocysteine intermediate By similarity

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. protein tyrosine/serine/threonine phosphatase activity Source: RefGenome
  3. protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. positive regulation of JNK cascade Source: RefGenome
  2. protein dephosphorylation Source: RefGenome
  3. regulation of cell proliferation Source: RefGenome
  4. transforming growth factor beta receptor signaling pathway Source: RefGenome
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: Chromosome 20

Organism-specific databases

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

Subcellular locationi

Cytoplasm Inferred 1 Publication
Isoform 3 : Cell membrane; Lipid-anchor; Cytoplasmic side 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. plasma membrane Source: UniProtKB-SubCell
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 295295Dual specificity protein phosphatase 15PRO_0000094824Add
BLAST

Keywords - PTMi

Lipoprotein, Myristate

Proteomic databases

PaxDbiQ9H1R2.
PRIDEiQ9H1R2.

PTM databases

PhosphoSiteiQ9H1R2.

Expressioni

Tissue specificityi

Highly expressed in testis.1 Publication

Gene expression databases

ArrayExpressiQ9H1R2.
BgeeiQ9H1R2.
CleanExiHS_C20orf57.
HS_DUSP15.
GenevestigatoriQ9H1R2.

Organism-specific databases

HPAiHPA031114.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi126164. 2 interactions.
IntActiQ9H1R2. 9 interactions.
MINTiMINT-7241177.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YZ4X-ray2.40A/B5-145[»]
ProteinModelPortaliQ9H1R2.
SMRiQ9H1R2. Positions 5-146.

Miscellaneous databases

EvolutionaryTraceiQ9H1R2.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
HOGENOMiHOG000007880.
HOVERGENiHBG054344.
InParanoidiQ9H1R2.
KOiK14165.
OMAiCRQGSAT.
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.

This entry describes 4 isoformsi produced by alternative splicing. Align

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

MTEGVLPGLY LGNFIDAKDL DQLGRNKITH IISIHESPQP LLQDITYLRI    50
PVADTPEVPI KKHFKECINF IHCCRLNGGN CLVHCFAGIS RSTTIVTAYV 100
MTVTGLGWRD VLEAIKATRP IANPNPGFRQ QLEEFGWASS QKGARHRTSK 150
TSGAQCPPMT SATCLLAARV ALLSAALVRE ATGRTAQRCR LSPRAAAERL 200
LGPPPHVAAG WSPDPKYQIC LCFGEEDPGP TQHPKEQLIM ADVQVQLRPG 250
SSSCTLSAST ERPDGSSTPG NPDGITHLQC SCLHPKRAAS SSCTR 295
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.

Note: Initiator Met-1 is removed. Myristoylated on Gly-2.

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. VSP_043107Add
BLAST
Alternative sequencei1 – 44MTEG → MGNGMTK in isoform 3. VSP_019228
Alternative sequencei143 – 23290GARHR…PGPTQ → LRRQLEERFGESPFRDEEEL RALLPLCKRCRQGSATSASS AGPHSAASEGTVQRLVPRTP REAHRPLPLLARVKQTFSCL PRCLSRKGGK in isoform 2, isoform 3 and isoform 4. VSP_007292Add
BLAST
Alternative sequencei233 – 29563Missing in isoform 2, isoform 3 and isoform 4. VSP_007293Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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. [Q9H1R2-1]
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]

Polymorphism databases

DMDMi30316387.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS13193.1. [Q9H1R2-3 ]
CCDS42862.1. [Q9H1R2-4 ]
RefSeqi NP_001012662.1. NM_001012644.1. [Q9H1R2-4 ]
NP_542178.2. NM_080611.3. [Q9H1R2-3 ]
NP_817130.1. NM_177991.1. [Q9H1R2-4 ]
UniGenei Hs.434108.
Hs.585017.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1YZ4 X-ray 2.40 A/B 5-145 [» ]
ProteinModelPortali Q9H1R2.
SMRi Q9H1R2. Positions 5-146.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 126164. 2 interactions.
IntActi Q9H1R2. 9 interactions.
MINTi MINT-7241177.

Chemistry

ChEMBLi CHEMBL2396507.

PTM databases

PhosphoSitei Q9H1R2.

Polymorphism databases

DMDMi 30316387.

Proteomic databases

PaxDbi Q9H1R2.
PRIDEi Q9H1R2.

Protocols and materials databases

DNASUi 128853.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000278979 ; ENSP00000278979 ; ENSG00000149599 . [Q9H1R2-1 ]
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 ]
GeneIDi 128853.
KEGGi hsa:128853.
UCSCi uc002wwu.1. human. [Q9H1R2-1 ]
uc002wwv.1. human. [Q9H1R2-4 ]
uc002wwx.1. human. [Q9H1R2-3 ]

Organism-specific databases

CTDi 128853.
GeneCardsi GC20M030443.
GC20U990068.
H-InvDB HIX0015716.
HGNCi HGNC:16190. C20orf57.
HGNC:16236. DUSP15.
HPAi HPA031114.
neXtProti NX_Q9H1R2.
PharmGKBi PA27524.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2453.
HOGENOMi HOG000007880.
HOVERGENi HBG054344.
InParanoidi Q9H1R2.
KOi K14165.
OMAi CRQGSAT.
OrthoDBi EOG7966HM.
PhylomeDBi Q9H1R2.
TreeFami TF105126.

Enzyme and pathway databases

SABIO-RK Q9H1R2.

Miscellaneous databases

EvolutionaryTracei Q9H1R2.
GeneWikii DUSP15.
GenomeRNAii 128853.
NextBioi 82475.
PROi Q9H1R2.

Gene expression databases

ArrayExpressi Q9H1R2.
Bgeei Q9H1R2.
CleanExi HS_C20orf57.
HS_DUSP15.
Genevestigatori Q9H1R2.

Family and domain databases

Gene3Di 2.60.200.10. 1 hit.
3.90.190.10. 1 hit.
InterProi IPR020417. 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 ]
PANTHERi PTHR10159. PTHR10159. 1 hit.
Pfami PF00782. DSPc. 1 hit.
[Graphical view ]
PRINTSi PR01908. ADSPHPHTASE.
SMARTi SM00195. DSPc. 1 hit.
[Graphical view ]
SUPFAMi SSF49879. SSF49879. 1 hit.
SSF52799. SSF52799. 1 hit.
PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 9, 2014
This is version 130 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

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

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