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Q9BY84

- DUS16_HUMAN

UniProt

Q9BY84 - DUS16_HUMAN

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Protein

Dual specificity protein phosphatase 16

Gene

DUSP16

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

Functioni

Dual specificity protein phosphatase involved in the inactivation of MAP kinases. Dephosphorylates MAPK10 bound to ARRB2.2 Publications

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 sitei244 – 2441Phosphocysteine intermediatePROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. dephosphorylation Source: UniProtKB
  2. inactivation of MAPK activity Source: UniProtKB
  3. MAPK export from nucleus Source: UniProtKB
  4. MAPK phosphatase export from nucleus, leptomycin B sensitive Source: UniProtKB
  5. protein dephosphorylation Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

SignaLinkiQ9BY84.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein phosphatase 16 (EC:3.1.3.16, EC:3.1.3.48)
Alternative name(s):
Mitogen-activated protein kinase phosphatase 7
Short name:
MAP kinase phosphatase 7
Short name:
MKP-7
Gene namesi
Name:DUSP16
Synonyms:KIAA1700, MKP7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:17909. DUSP16.

Subcellular locationi

Cytoplasm. Nucleus. Cytoplasmic vesicle
Note: After dissociation upon AGTR stimulation, re-associates with ARRB2 on endocytic vesicles.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic vesicle Source: UniProtKB-KW
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38475.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 665665Dual specificity protein phosphatase 16PRO_0000094826Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei446 – 4461Phosphoserine; by MAPK11 Publication
Modified residuei501 – 5011Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated at Ser-446 by MAPK1/ERK2, which prevents its degradation, and thereby stabilizes it and blocks JNK MAPK activity.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9BY84.
PaxDbiQ9BY84.
PRIDEiQ9BY84.

PTM databases

PhosphoSiteiQ9BY84.

Expressioni

Gene expression databases

BgeeiQ9BY84.
CleanExiHS_DUSP16.
ExpressionAtlasiQ9BY84. baseline and differential.
GenevestigatoriQ9BY84.

Organism-specific databases

HPAiHPA020326.

Interactioni

Subunit structurei

Interacts with ARRB2.1 Publication

Protein-protein interaction databases

BioGridi123321. 7 interactions.
IntActiQ9BY84. 1 interaction.
STRINGi9606.ENSP00000228862.

Structurei

Secondary structure

1
665
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 103Combined sources
Helixi12 – 198Combined sources
Beta strandi21 – 244Combined sources
Beta strandi26 – 305Combined sources
Helixi34 – 396Combined sources
Helixi52 – 598Combined sources
Helixi65 – 717Combined sources
Beta strandi83 – 886Combined sources
Helixi95 – 973Combined sources
Helixi103 – 11412Combined sources
Beta strandi118 – 1214Combined sources
Helixi124 – 1318Combined sources
Helixi133 – 1353Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VSWX-ray2.20A/B5-150[»]
3TG3X-ray2.68A/B/C/D5-138[»]
ProteinModelPortaliQ9BY84.
SMRiQ9BY84. Positions 5-138, 158-328.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BY84.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 137116RhodanesePROSITE-ProRule annotationAdd
BLAST
Domaini227 – 28963Tyrosine-protein phosphataseAdd
BLAST

Sequence similaritiesi

Contains 1 rhodanese domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118902.
HOGENOMiHOG000082452.
HOVERGENiHBG005541.
InParanoidiQ9BY84.
KOiK04459.
OMAiQMEFGES.
OrthoDBiEOG747PJD.
PhylomeDBiQ9BY84.
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]
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: Q9BY84-1) [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
MAHEMIGTQI VTERLVALLE SGTEKVLLID SRPFVEYNTS HILEAININC
60 70 80 90 100
SKLMKRRLQQ DKVLITELIQ HSAKHKVDID CSQKVVVYDQ SSQDVASLSS
110 120 130 140 150
DCFLTVLLGK LEKSFNSVHL LAGGFAEFSR CFPGLCEGKS TLVPTCISQP
160 170 180 190 200
CLPVANIGPT RILPNLYLGC QRDVLNKELM QQNGIGYVLN ASNTCPKPDF
210 220 230 240 250
IPESHFLRVP VNDSFCEKIL PWLDKSVDFI EKAKASNGCV LVHCLAGISR
260 270 280 290 300
SATIAIAYIM KRMDMSLDEA YRFVKEKRPT ISPNFNFLGQ LLDYEKKIKN
310 320 330 340 350
QTGASGPKSK LKLLHLEKPN EPVPAVSEGG QKSETPLSPP CADSATSEAA
360 370 380 390 400
GQRPVHPASV PSVPSVQPSL LEDSPLVQAL SGLHLSADRL EDSNKLKRSF
410 420 430 440 450
SLDIKSVSYS ASMAASLHGF SSSEDALEYY KPSTTLDGTN KLCQFSPVQE
460 470 480 490 500
LSEQTPETSP DKEEASIPKK LQTARPSDSQ SKRLHSVRTS SSGTAQRSLL
510 520 530 540 550
SPLHRSGSVE DNYHTSFLFG LSTSQQHLTK SAGLGLKGWH SDILAPQTST
560 570 580 590 600
PSLTSSWYFA TESSHFYSAS AIYGGSASYS AYSCSQLPTC GDQVYSVRRR
610 620 630 640 650
QKPSDRADSR RSWHEESPFE KQFKRRSCQM EFGESIMSEN RSREELGKVG
660
SQSSFSGSME IIEVS
Length:665
Mass (Da):73,102
Last modified:June 1, 2001 - v1
Checksum:i1BD853FF08460DFF
GO
Isoform 2 (identifier: Q9BY84-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     124-143: GFAEFSRCFPGLCEGKSTLV → ADAAEWDWLCVKCQQYLSKA
     144-665: Missing.

Note: No experimental confirmation available

Show »
Length:143
Mass (Da):16,078
Checksum:i5213A213AA7E5974
GO

Sequence cautioni

The sequence BAB21791.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231T → M.
Corresponds to variant rs36049447 [ dbSNP | Ensembl ].
VAR_051753
Natural varianti366 – 3661V → M.
Corresponds to variant rs3809199 [ dbSNP | Ensembl ].
VAR_051754

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei124 – 14320GFAEF…KSTLV → ADAAEWDWLCVKCQQYLSKA in isoform 2. 1 PublicationVSP_056981Add
BLAST
Alternative sequencei144 – 665522Missing in isoform 2. 1 PublicationVSP_056982Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB052156 mRNA. Translation: BAB40814.1.
AF506796 mRNA. Translation: AAN75120.1.
AY038927 mRNA. Translation: AAK69770.1.
AB051487 mRNA. Translation: BAB21791.1. Different initiation.
AC007619 Genomic DNA. No translation available.
AC092824 Genomic DNA. No translation available.
BC109235 mRNA. Translation: AAI09236.1.
CCDSiCCDS8650.1.
RefSeqiNP_085143.1. NM_030640.2.
XP_006719218.1. XM_006719155.1.
UniGeneiHs.536535.

Genome annotation databases

EnsembliENST00000228862; ENSP00000228862; ENSG00000111266. [Q9BY84-2]
ENST00000298573; ENSP00000298573; ENSG00000111266. [Q9BY84-1]
GeneIDi80824.
KEGGihsa:80824.
UCSCiuc001ran.2. human. [Q9BY84-1]

Polymorphism databases

DMDMi20137933.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB052156 mRNA. Translation: BAB40814.1 .
AF506796 mRNA. Translation: AAN75120.1 .
AY038927 mRNA. Translation: AAK69770.1 .
AB051487 mRNA. Translation: BAB21791.1 . Different initiation.
AC007619 Genomic DNA. No translation available.
AC092824 Genomic DNA. No translation available.
BC109235 mRNA. Translation: AAI09236.1 .
CCDSi CCDS8650.1.
RefSeqi NP_085143.1. NM_030640.2.
XP_006719218.1. XM_006719155.1.
UniGenei Hs.536535.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2VSW X-ray 2.20 A/B 5-150 [» ]
3TG3 X-ray 2.68 A/B/C/D 5-138 [» ]
ProteinModelPortali Q9BY84.
SMRi Q9BY84. Positions 5-138, 158-328.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123321. 7 interactions.
IntActi Q9BY84. 1 interaction.
STRINGi 9606.ENSP00000228862.

PTM databases

PhosphoSitei Q9BY84.

Polymorphism databases

DMDMi 20137933.

Proteomic databases

MaxQBi Q9BY84.
PaxDbi Q9BY84.
PRIDEi Q9BY84.

Protocols and materials databases

DNASUi 80824.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000228862 ; ENSP00000228862 ; ENSG00000111266 . [Q9BY84-2 ]
ENST00000298573 ; ENSP00000298573 ; ENSG00000111266 . [Q9BY84-1 ]
GeneIDi 80824.
KEGGi hsa:80824.
UCSCi uc001ran.2. human. [Q9BY84-1 ]

Organism-specific databases

CTDi 80824.
GeneCardsi GC12M012628.
HGNCi HGNC:17909. DUSP16.
HPAi HPA020326.
MIMi 607175. gene.
neXtProti NX_Q9BY84.
PharmGKBi PA38475.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2453.
GeneTreei ENSGT00760000118902.
HOGENOMi HOG000082452.
HOVERGENi HBG005541.
InParanoidi Q9BY84.
KOi K04459.
OMAi QMEFGES.
OrthoDBi EOG747PJD.
PhylomeDBi Q9BY84.
TreeFami TF105122.

Enzyme and pathway databases

SignaLinki Q9BY84.

Miscellaneous databases

ChiTaRSi DUSP16. human.
EvolutionaryTracei Q9BY84.
GeneWikii DUSP16.
GenomeRNAii 80824.
NextBioi 71232.
PROi Q9BY84.
SOURCEi Search...

Gene expression databases

Bgeei Q9BY84.
CleanExi HS_DUSP16.
ExpressionAtlasi Q9BY84. baseline and differential.
Genevestigatori Q9BY84.

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 ]
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. "MKP-7, a novel mitogen-activated protein kinase phosphatase, functions as a shuttle protein."
    Masuda K., Shima H., Watanabe M., Kikuchi K.
    J. Biol. Chem. 276:39002-39011(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION.
  2. "MAPK phosphatase DUSP16/MKP-7, a candidate tumor suppressor for chromosome region 12p12-13, reduces BCR-ABL-induced transformation."
    Hoornaert I., Marynen P., Goris J., Sciot R., Baens M.
    Oncogene 22:7728-7736(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  3. "A detailed transcriptional map of the chromosome 12p12 tumor suppressor locus."
    Montpetit A., Boily G., Sinnett D.
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  4. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
    DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  5. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. "Activation of ERK induces phosphorylation of MAPK phosphatase-7, a JNK specific phosphatase, at Ser-446."
    Masuda K., Shima H., Katagiri C., Kikuchi K.
    J. Biol. Chem. 278:32448-32456(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-446.
  8. "Dynamic interaction between the dual specificity phosphatase MKP7 and the JNK3 scaffold protein beta-arrestin 2."
    Willoughby E.A., Collins M.K.
    J. Biol. Chem. 280:25651-25658(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ARRB2.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "The structure of the rhodanese domain of the human 2 dual specificity phosphatase 16."
    Structural genomics consortium (SGC)
    Submitted (JUN-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 5-150.

Entry informationi

Entry nameiDUS16_HUMAN
AccessioniPrimary (citable) accession number: Q9BY84
Secondary accession number(s): Q547C7, Q96QS2, Q9C0G3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: June 1, 2001
Last modified: November 26, 2014
This is version 123 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 12
    Human chromosome 12: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3