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Protein

Dual specificity protein phosphatase 22

Gene

DUSP22

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

Functioni

Activates the Jnk signaling pathway. Dephosphorylates and deactivates p38 and stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) (By similarity).By similarity

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 sitei88 – 881Phosphocysteine intermediateBy similarity

GO - Molecular functioni

  1. protein tyrosine/serine/threonine phosphatase activity Source: GO_Central
  2. protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. apoptotic process Source: ProtInc
  2. cell proliferation Source: ProtInc
  3. inactivation of MAPK activity Source: ProtInc
  4. multicellular organismal development Source: ProtInc
  5. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  6. positive regulation of JNK cascade Source: GO_Central
  7. protein dephosphorylation Source: GO_Central
  8. regulation of cell proliferation Source: GO_Central
  9. transforming growth factor beta receptor signaling pathway Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

SABIO-RKQ9NRW4.
SignaLinkiQ9NRW4.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein phosphatase 22 (EC:3.1.3.16, EC:3.1.3.48)
Alternative name(s):
JNK-stimulatory phosphatase-1
Short name:
JSP-1
Low molecular weight dual specificity phosphatase 2
Short name:
LMW-DSP2
Mitogen-activated protein kinase phosphatase x
Short name:
MAP kinase phosphatase x
Short name:
MKP-x
Gene namesi
Name:DUSP22
Synonyms:JSP1, LMWDSP2, MKPX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:16077. DUSP22.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134991025.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 184183Dual specificity protein phosphatase 22PRO_0000244751Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication

Post-translational modificationi

Myristoylation regulates subcellular location, and is necessary for activation of JNK.1 Publication

Keywords - PTMi

Lipoprotein, Myristate

Proteomic databases

MaxQBiQ9NRW4.
PaxDbiQ9NRW4.
PRIDEiQ9NRW4.

PTM databases

DEPODiQ9NRW4.

Expressioni

Tissue specificityi

Ubiquitous. Highest expression seen in heart, placenta, lung, liver, kidney and pancreas.1 Publication

Gene expression databases

BgeeiQ9NRW4.
CleanExiHS_DUSP22.
ExpressionAtlasiQ9NRW4. baseline and differential.
GenevestigatoriQ9NRW4.

Organism-specific databases

HPAiHPA031394.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi121264. 4 interactions.
IntActiQ9NRW4. 1 interaction.
STRINGi9606.ENSP00000345281.

Structurei

Secondary structure

1
184
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 94Combined sources
Beta strandi12 – 154Combined sources
Helixi19 – 213Combined sources
Helixi23 – 286Combined sources
Beta strandi31 – 366Combined sources
Beta strandi49 – 524Combined sources
Helixi64 – 663Combined sources
Helixi67 – 7913Combined sources
Beta strandi83 – 875Combined sources
Beta strandi89 – 935Combined sources
Helixi94 – 10512Combined sources
Helixi111 – 12111Combined sources
Helixi129 – 14113Combined sources
Helixi143 – 15311Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WRMX-ray1.50A1-163[»]
ProteinModelPortaliQ9NRW4.
SMRiQ9NRW4. Positions 1-154.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NRW4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini65 – 13369Tyrosine-protein phosphataseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118853.
HOGENOMiHOG000007880.
HOVERGENiHBG054344.
InParanoidiQ9NRW4.
KOiK14165.
OMAiLFIGNFK.
OrthoDBiEOG7966HM.
PhylomeDBiQ9NRW4.
TreeFamiTF105126.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSiPR01908. ADSPHPHTASE.
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NRW4-1) [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
MGNGMNKILP GLYIGNFKDA RDAEQLSKNK VTHILSVHDS ARPMLEGVKY
60 70 80 90 100
LCIPAADSPS QNLTRHFKES IKFIHECRLR GESCLVHCLA GVSRSVTLVI
110 120 130 140 150
AYIMTVTDFG WEDALHTVRA GRSCANPNVG FQRQLQEFEK HEVHQYRQWL
160 170 180
KEEYGESPLQ DAEEAKNILA APGILKFWAF LRRL
Length:184
Mass (Da):20,910
Last modified:October 1, 2000 - v1
Checksum:iB3F962A087C2BA20
GO
Isoform 2 (identifier: Q9NRW4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     170-184: AAPGILKFWAFLRRL → GKYKEQGRTEPQPGARRWSSFPALAPLTYDNYTTET

Show »
Length:205
Mass (Da):23,268
Checksum:i48334A97991FCFF8
GO

Sequence cautioni

The sequence AAH16844.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti119 – 1191R → H.
Corresponds to variant rs7768224 [ dbSNP | Ensembl ].
VAR_026912

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei170 – 18415AAPGI…FLRRL → GKYKEQGRTEPQPGARRWSS FPALAPLTYDNYTTET in isoform 2. 2 PublicationsVSP_019614Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF424702 mRNA. Translation: AAL18850.1.
AF165519 mRNA. Translation: AAF86649.1.
AY249859 mRNA. Translation: AAP76376.1.
AK296402 mRNA. Translation: BAG59068.1.
AL365272 Genomic DNA. Translation: CAH72534.1.
AL365272 Genomic DNA. Translation: CAH72535.1.
BC016844 mRNA. Translation: AAH16844.1. Different initiation.
BC022847 mRNA. Translation: AAH22847.1.
AB208997 mRNA. Translation: BAD92234.1.
CCDSiCCDS4468.1. [Q9NRW4-1]
CCDS69035.1. [Q9NRW4-2]
RefSeqiNP_001273484.1. NM_001286555.1. [Q9NRW4-2]
NP_064570.1. NM_020185.4. [Q9NRW4-1]
UniGeneiHs.29106.

Genome annotation databases

EnsembliENST00000344450; ENSP00000345281; ENSG00000112679. [Q9NRW4-1]
ENST00000419235; ENSP00000397459; ENSG00000112679. [Q9NRW4-2]
GeneIDi56940.
KEGGihsa:56940.
UCSCiuc003msx.3. human. [Q9NRW4-1]
uc011dhn.1. human. [Q9NRW4-2]

Polymorphism databases

DMDMi74752929.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF424702 mRNA. Translation: AAL18850.1.
AF165519 mRNA. Translation: AAF86649.1.
AY249859 mRNA. Translation: AAP76376.1.
AK296402 mRNA. Translation: BAG59068.1.
AL365272 Genomic DNA. Translation: CAH72534.1.
AL365272 Genomic DNA. Translation: CAH72535.1.
BC016844 mRNA. Translation: AAH16844.1. Different initiation.
BC022847 mRNA. Translation: AAH22847.1.
AB208997 mRNA. Translation: BAD92234.1.
CCDSiCCDS4468.1. [Q9NRW4-1]
CCDS69035.1. [Q9NRW4-2]
RefSeqiNP_001273484.1. NM_001286555.1. [Q9NRW4-2]
NP_064570.1. NM_020185.4. [Q9NRW4-1]
UniGeneiHs.29106.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WRMX-ray1.50A1-163[»]
ProteinModelPortaliQ9NRW4.
SMRiQ9NRW4. Positions 1-154.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121264. 4 interactions.
IntActiQ9NRW4. 1 interaction.
STRINGi9606.ENSP00000345281.

Chemistry

BindingDBiQ9NRW4.
ChEMBLiCHEMBL3924.

PTM databases

DEPODiQ9NRW4.

Polymorphism databases

DMDMi74752929.

Proteomic databases

MaxQBiQ9NRW4.
PaxDbiQ9NRW4.
PRIDEiQ9NRW4.

Protocols and materials databases

DNASUi56940.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000344450; ENSP00000345281; ENSG00000112679. [Q9NRW4-1]
ENST00000419235; ENSP00000397459; ENSG00000112679. [Q9NRW4-2]
GeneIDi56940.
KEGGihsa:56940.
UCSCiuc003msx.3. human. [Q9NRW4-1]
uc011dhn.1. human. [Q9NRW4-2]

Organism-specific databases

CTDi56940.
GeneCardsiGC06P000292.
HGNCiHGNC:16077. DUSP22.
HPAiHPA031394.
neXtProtiNX_Q9NRW4.
PharmGKBiPA134991025.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118853.
HOGENOMiHOG000007880.
HOVERGENiHBG054344.
InParanoidiQ9NRW4.
KOiK14165.
OMAiLFIGNFK.
OrthoDBiEOG7966HM.
PhylomeDBiQ9NRW4.
TreeFamiTF105126.

Enzyme and pathway databases

SABIO-RKQ9NRW4.
SignaLinkiQ9NRW4.

Miscellaneous databases

ChiTaRSiDUSP22. human.
EvolutionaryTraceiQ9NRW4.
GeneWikiiDUSP22.
GenomeRNAii56940.
NextBioi62505.
PROiQ9NRW4.

Gene expression databases

BgeeiQ9NRW4.
CleanExiHS_DUSP22.
ExpressionAtlasiQ9NRW4. baseline and differential.
GenevestigatoriQ9NRW4.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSiPR01908. ADSPHPHTASE.
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Activation of the Jnk signaling pathway by a dual-specificity phosphatase, JSP-1."
    Shen Y., Luche R., Wei B., Gordon M.L., Diltz C.D., Tonks N.K.
    Proc. Natl. Acad. Sci. U.S.A. 98:13613-13618(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY.
  2. "Novel genes expressed in hematopoietic stem/progenitor cells from myelodysplastic syndromes patient."
    Gu J., Huang Q., Yu Y., Xu S., Wang Y., Han Z., Chen Z., Zhou J., Tu Y., Gu W., Fu G., Huang C.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Hematopoietic stem cell.
  3. "Cloning and characterization of human LMW-DSP2 gene."
    Mao Y., Xie Y., Cheng H.
    Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Thalamus.
  5. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung and Pancreas.
  7. 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 56-184 (ISOFORM 2).
    Tissue: Myeloid.
  8. "Myristoylation of the dual-specificity phosphatase c-JUN N-terminal kinase (JNK) stimulatory phosphatase 1 is necessary for its activation of JNK signaling and apoptosis."
    Schwertassek U., Buckley D.A., Xu C.F., Lindsay A.J., McCaffrey M.W., Neubert T.A., Tonks N.K.
    FEBS J. 277:2463-2473(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2.
  9. "Crystal structure of human dual specificity phosphatase, JNK stimulatory phosphatase-1, at 1.5 A resolution."
    Yokota T., Nara Y., Kashima A., Matsubara K., Misawa S., Kato R., Sugio S.
    Proteins 66:272-278(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-163, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiDUS22_HUMAN
AccessioniPrimary (citable) accession number: Q9NRW4
Secondary accession number(s): B4DK56
, Q59GW2, Q5VWR2, Q96AR1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: October 1, 2000
Last modified: February 4, 2015
This is version 124 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.