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Q13115

- DUS4_HUMAN

UniProt

Q13115 - DUS4_HUMAN

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Protein

Dual specificity protein phosphatase 4

Gene

DUSP4

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

Functioni

Regulates mitogenic signal transduction by dephosphorylating both Thr and Tyr residues on MAP kinases ERK1 and ERK2.

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 sitei280 – 2801Phosphocysteine intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. MAP kinase tyrosine/serine/threonine phosphatase activity Source: InterPro
  2. protein tyrosine/serine/threonine phosphatase activity Source: RefGenome
  3. protein tyrosine/threonine phosphatase activity Source: ProtInc
  4. protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. endoderm formation Source: RefGenome
  2. innate immune response Source: Reactome
  3. MAPK cascade Source: ProtInc
  4. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  5. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  6. neurotrophin TRK receptor signaling pathway Source: Reactome
  7. protein dephosphorylation Source: RefGenome
  8. stress-activated MAPK cascade Source: Reactome
  9. toll-like receptor 10 signaling pathway Source: Reactome
  10. toll-like receptor 2 signaling pathway Source: Reactome
  11. toll-like receptor 3 signaling pathway Source: Reactome
  12. toll-like receptor 4 signaling pathway Source: Reactome
  13. toll-like receptor 5 signaling pathway Source: Reactome
  14. toll-like receptor 9 signaling pathway Source: Reactome
  15. toll-like receptor signaling pathway Source: Reactome
  16. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  17. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  18. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

ReactomeiREACT_12436. ERKs are inactivated.
SignaLinkiQ13115.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein phosphatase 4 (EC:3.1.3.16, EC:3.1.3.48)
Alternative name(s):
Dual specificity protein phosphatase hVH2
Mitogen-activated protein kinase phosphatase 2
Short name:
MAP kinase phosphatase 2
Short name:
MKP-2
Gene namesi
Name:DUSP4
Synonyms:MKP2, VH2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:3070. DUSP4.

Subcellular locationi

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27527.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 394394Dual specificity protein phosphatase 4PRO_0000094798Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei386 – 3861Phosphoserine; by MAPK1 Publication
Modified residuei391 – 3911Phosphoserine; by MAPK1 Publication

Post-translational modificationi

Phosphorylation in the C-terminus by ERK1/2 inhibits proteasomal degradation and stabilizes the protein.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ13115.
PaxDbiQ13115.
PRIDEiQ13115.

PTM databases

PhosphoSiteiQ13115.

Expressioni

Gene expression databases

BgeeiQ13115.
CleanExiHS_DUSP4.
GenevestigatoriQ13115.

Interactioni

Subunit structurei

Hollow spherical complex composed of 24 subunits with pseudooctahedral symmetry, has a tetramer as the basic unit.1 Publication

Protein-protein interaction databases

BioGridi108179. 7 interactions.
IntActiQ13115. 5 interactions.
MINTiMINT-8217030.
STRINGi9606.ENSP00000240100.

Structurei

Secondary structure

1
394
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi197 – 2004Combined sources
Beta strandi203 – 2075Combined sources
Helixi208 – 2114Combined sources
Helixi214 – 2196Combined sources
Beta strandi224 – 2274Combined sources
Beta strandi229 – 2313Combined sources
Turni235 – 2395Combined sources
Beta strandi240 – 2445Combined sources
Beta strandi249 – 2524Combined sources
Turni255 – 2584Combined sources
Helixi259 – 27113Combined sources
Beta strandi276 – 28510Combined sources
Helixi286 – 29914Combined sources
Helixi303 – 3119Combined sources
Helixi321 – 33515Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EZZX-ray2.90A/B/C/D/E/F194-336[»]
ProteinModelPortaliQ13115.
SMRiQ13115. Positions 44-158, 194-336.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13115.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 159119RhodanesePROSITE-ProRule annotationAdd
BLAST
Domaini197 – 394198Tyrosine-protein phosphataseAdd
BLAST

Sequence similaritiesi

Contains 1 rhodanese domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118902.
HOVERGENiHBG007347.
InParanoidiQ13115.
KOiK04459.
OMAiHHSPITT.
OrthoDBiEOG75MVWD.
PhylomeDBiQ13115.
TreeFamiTF105122.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR008343. MKP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PIRSFiPIRSF000939. MAPK_Ptase. 1 hit.
PRINTSiPR01764. MAPKPHPHTASE.
SMARTiSM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
SSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13115-1) [UniParc]FASTAAdd to Basket

Also known as: MKP-2-L

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
MVTMEELREM DCSVLKRLMN RDENGGGAGG SGSHGTLGLP SGGKCLLLDC
60 70 80 90 100
RPFLAHSAGY ILGSVNVRCN TIVRRRAKGS VSLEQILPAE EEVRARLRSG
110 120 130 140 150
LYSAVIVYDE RSPRAESLRE DSTVSLVVQA LRRNAERTDI CLLKGGYERF
160 170 180 190 200
SSEYPEFCSK TKALAAIPPP VPPSATEPLD LGCSSCGTPL HDQGGPVEIL
210 220 230 240 250
PFLYLGSAYH AARRDMLDAL GITALLNVSS DCPNHFEGHY QYKCIPVEDN
260 270 280 290 300
HKADISSWFM EAIEYIDAVK DCRGRVLVHC QAGISRSATI CLAYLMMKKR
310 320 330 340 350
VRLEEAFEFV KQRRSIISPN FSFMGQLLQF ESQVLATSCA AEAASPSGPL
360 370 380 390
RERGKTPATP TSQFVFSFPV SVGVHSAPSS LPYLHSPITT SPSC
Length:394
Mass (Da):42,953
Last modified:November 1, 1996 - v1
Checksum:i0603971759B6952E
GO
Isoform 2 (identifier: Q13115-2) [UniParc]FASTAAdd to Basket

Also known as: MKP-2-S

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: MVTMEELREM...KCLLLDCRPF → MGRKVHSNGS...RSRCLCSESQ
     54-144: Missing.

Note: Does not bind to JNK or ERK, and is more susceptible to proteosomal degradation.

Show »
Length:303
Mass (Da):32,993
Checksum:i3BFB1126F4CF000A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti111 – 1111R → G in AAC50452. (PubMed:8626452)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5353MVTME…DCRPF → MGRKVHSNGSQFAEHSRSPR RTGRDCKPVRAPSMALGVSQ LAGRSRCLCSESQ in isoform 2. 1 PublicationVSP_044667Add
BLAST
Alternative sequencei54 – 14491Missing in isoform 2. 1 PublicationVSP_044668Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U21108 mRNA. Translation: AAA85119.1.
U48807 mRNA. Translation: AAC50452.1.
AK314820 mRNA. Translation: BAG37342.1.
AL137704 mRNA. No translation available.
AC084262 Genomic DNA. No translation available.
CH471080 Genomic DNA. Translation: EAW63481.1.
CH471080 Genomic DNA. Translation: EAW63482.1.
CH471080 Genomic DNA. Translation: EAW63483.1.
CH471080 Genomic DNA. Translation: EAW63484.1.
BC002671 mRNA. Translation: AAH02671.1.
BC014565 mRNA. Translation: AAH14565.1.
CCDSiCCDS6072.1. [Q13115-1]
CCDS6073.1. [Q13115-2]
RefSeqiNP_001385.1. NM_001394.6. [Q13115-1]
NP_476499.1. NM_057158.3. [Q13115-2]
UniGeneiHs.417962.

Genome annotation databases

EnsembliENST00000240100; ENSP00000240100; ENSG00000120875. [Q13115-1]
ENST00000240101; ENSP00000240101; ENSG00000120875. [Q13115-2]
GeneIDi1846.
KEGGihsa:1846.
UCSCiuc003xhl.3. human.
uc003xhm.3. human. [Q13115-1]

Polymorphism databases

DMDMi2499745.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U21108 mRNA. Translation: AAA85119.1 .
U48807 mRNA. Translation: AAC50452.1 .
AK314820 mRNA. Translation: BAG37342.1 .
AL137704 mRNA. No translation available.
AC084262 Genomic DNA. No translation available.
CH471080 Genomic DNA. Translation: EAW63481.1 .
CH471080 Genomic DNA. Translation: EAW63482.1 .
CH471080 Genomic DNA. Translation: EAW63483.1 .
CH471080 Genomic DNA. Translation: EAW63484.1 .
BC002671 mRNA. Translation: AAH02671.1 .
BC014565 mRNA. Translation: AAH14565.1 .
CCDSi CCDS6072.1. [Q13115-1 ]
CCDS6073.1. [Q13115-2 ]
RefSeqi NP_001385.1. NM_001394.6. [Q13115-1 ]
NP_476499.1. NM_057158.3. [Q13115-2 ]
UniGenei Hs.417962.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3EZZ X-ray 2.90 A/B/C/D/E/F 194-336 [» ]
ProteinModelPortali Q13115.
SMRi Q13115. Positions 44-158, 194-336.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108179. 7 interactions.
IntActi Q13115. 5 interactions.
MINTi MINT-8217030.
STRINGi 9606.ENSP00000240100.

Chemistry

BindingDBi Q13115.
ChEMBLi CHEMBL2146343.

PTM databases

PhosphoSitei Q13115.

Polymorphism databases

DMDMi 2499745.

Proteomic databases

MaxQBi Q13115.
PaxDbi Q13115.
PRIDEi Q13115.

Protocols and materials databases

DNASUi 1846.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000240100 ; ENSP00000240100 ; ENSG00000120875 . [Q13115-1 ]
ENST00000240101 ; ENSP00000240101 ; ENSG00000120875 . [Q13115-2 ]
GeneIDi 1846.
KEGGi hsa:1846.
UCSCi uc003xhl.3. human.
uc003xhm.3. human. [Q13115-1 ]

Organism-specific databases

CTDi 1846.
GeneCardsi GC08M029190.
HGNCi HGNC:3070. DUSP4.
MIMi 602747. gene.
neXtProti NX_Q13115.
PharmGKBi PA27527.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2453.
GeneTreei ENSGT00760000118902.
HOVERGENi HBG007347.
InParanoidi Q13115.
KOi K04459.
OMAi HHSPITT.
OrthoDBi EOG75MVWD.
PhylomeDBi Q13115.
TreeFami TF105122.

Enzyme and pathway databases

Reactomei REACT_12436. ERKs are inactivated.
SignaLinki Q13115.

Miscellaneous databases

ChiTaRSi DUSP4. human.
EvolutionaryTracei Q13115.
GeneWikii DUSP4.
GenomeRNAii 1846.
NextBioi 7559.
PROi Q13115.
SOURCEi Search...

Gene expression databases

Bgeei Q13115.
CleanExi HS_DUSP4.
Genevestigatori Q13115.

Family and domain databases

Gene3Di 3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProi IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR008343. MKP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view ]
PANTHERi PTHR10159. PTHR10159. 1 hit.
Pfami PF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view ]
PIRSFi PIRSF000939. MAPK_Ptase. 1 hit.
PRINTSi PR01764. MAPKPHPHTASE.
SMARTi SM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
SSF52821. SSF52821. 1 hit.
PROSITEi PS50206. RHODANESE_3. 1 hit.
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. "Isolation and characterization of a novel dual specific phosphatase, HVH2, which selectively dephosphorylates the mitogen-activated protein kinase."
    Guan K.-L., Butch E.
    J. Biol. Chem. 270:7197-7203(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "The mitogen-activated protein kinase phosphatases PAC1, MKP-1, and MKP-2 have unique substrate specificities and reduced activity in vivo toward the ERK2 sevenmaker mutation."
    Chu Y., Solski P.A., Khosravi-Far R., Der C.J., Kelly K.
    J. Biol. Chem. 271:6497-6501(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "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] (ISOFORM 1).
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Testis.
  5. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM 1).
    Tissue: Skin and Uterus.
  8. "Post-translational regulation of mitogen-activated protein kinase phosphatase-2 (MKP-2) by ERK."
    Peng D.J., Zhou J.Y., Wu G.S.
    Cell Cycle 9:4650-4655(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-386 AND SER-391.
  9. "Differential regulation of MAP kinase activation by a novel splice variant of human MAP kinase phosphatase-2."
    Cadalbert L.C., Sloss C.M., Cunningham M.R., Al-Mutairi M., McIntire A., Shipley J., Plevin R.
    Cell. Signal. 22:357-365(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Crystal structure of the catalytic domain of human MKP-2 reveals a 24-mer assembly."
    Jeong D.G., Jung S.K., Yoon T.S., Woo E.J., Kim J.H., Park B.C., Ryu S.E., Kim S.J.
    Proteins 76:763-767(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 194-336, SUBUNIT.

Entry informationi

Entry nameiDUS4_HUMAN
AccessioniPrimary (citable) accession number: Q13115
Secondary accession number(s): B2RBU5
, D3DSU4, G5E930, Q13524
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 142 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 8
    Human chromosome 8: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3