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Q61823

- PDCD4_MOUSE

UniProt

Q61823 - PDCD4_MOUSE

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Protein

Programmed cell death protein 4

Gene

Pdcd4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Inhibits translation initiation and cap-dependent translation. May excert its function by hindering the interaction between EIF4A1 and EIF4G. Inhibits the helicase activity of EIF4A. Modulates the activation of JUN kinase. Down-regulates the expression of MAP4K1, thus inhibiting events important in driving invasion, namely, MAPK85 activation and consequent JUN-dependent transcription. May play a role in apoptosis. Tumor suppressor. Inhibits tumor promoter-induced neoplastic transformation. Binds RNA.4 Publications

GO - Molecular functioni

  1. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cell aging Source: UniProtKB
  3. negative regulation of JUN kinase activity Source: UniProtKB
  4. negative regulation of transcription, DNA-templated Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Programmed cell death protein 4
Alternative name(s):
Protein MA-3
Topoisomerase-inhibitor suppressed protein
Gene namesi
Name:Pdcd4
Synonyms:Ma3, Tis
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:107490. Pdcd4.

Subcellular locationi

Nucleus. Cytoplasm
Note: Shuttles between the nucleus and cytoplasm. Predominantly nuclear under normal growth conditions, and when phosphorylated at Ser-457 (By similarity). Exported from the nucleus in the absence of serum.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Decreases benign tumor development and malignant progression.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi414 – 4141D → A: Strongly reduced interaction with EIF4A1. 1 Publication
Mutagenesisi418 – 4181D → A: Strongly reduced interaction with EIF4A1. 1 Publication
Mutagenesisi457 – 4571S → A or D: No effect on interaction with EIF4A1. 1 Publication

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 469469Programmed cell death protein 4PRO_0000256520Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei67 – 671Phosphoserine; by PKB and RPS6KB1By similarity
Modified residuei76 – 761PhosphoserineBy similarity
Modified residuei78 – 781PhosphoserineBy similarity
Modified residuei94 – 941PhosphoserineBy similarity
Modified residuei152 – 1521PhosphotyrosineBy similarity
Modified residuei457 – 4571Phosphoserine; by PKBBy similarity

Post-translational modificationi

Polyubiquitinated, leading to its proteasomal degradation. Rapidly degraded in response to mitogens. Phosphorylation of the phosphodegron promotes interaction with BTRC and proteasomal degradation (By similarity).By similarity
Phosphorylated at Ser-67 by RPS6KB1 in response to mitogens; phosphorylation promotes proteasomal degradation of PDCD4.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ61823.
PaxDbiQ61823.
PRIDEiQ61823.

PTM databases

PhosphoSiteiQ61823.

Expressioni

Tissue specificityi

Expressed ubiquitously. Highyly expressed in thymus and liver. Moderately expressed in brain, kidney and spleen; weakly in lung and heart. Expression is up- or down-regulated in response to apoptosis inducers. Regulated by many programmed cell death-inducing stimuli.2 Publications

Gene expression databases

BgeeiQ61823.
CleanExiMM_PDCD4.
GenevestigatoriQ61823.

Interactioni

Subunit structurei

Interacts (via MI domains) with EIF4A1 and EIF4A2 (via N-terminal domain). Heterotrimer with EIF4A1; one molecule of PDCD4 binds two molecules of EIF4A1. Interacts with EIF4G1. May form a complex with EIF4A1 and EIF4G1. The interaction between PDCD4 and EIF4A1 interferes with the interaction between EIF4A1 and EIF4G. When phosphorylated, interacts with BTRC and FBXW11 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Eif4a1P608434EBI-296473,EBI-6665935
Eif4g2Q624482EBI-296473,EBI-296494

Protein-protein interaction databases

BioGridi202070. 1 interaction.
IntActiQ61823. 4 interactions.
MINTiMINT-7012023.

Structurei

Secondary structure

1
469
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi162 – 17817
Helixi181 – 1899
Turni190 – 1923
Helixi195 – 1995
Helixi200 – 2089
Helixi213 – 22412
Turni225 – 2295
Helixi233 – 24513
Helixi247 – 2537
Helixi257 – 27014
Helixi280 – 2823
Helixi289 – 30214
Beta strandi320 – 3223
Helixi326 – 34116
Helixi344 – 35411
Helixi357 – 3593
Helixi360 – 37314
Beta strandi374 – 3774
Helixi378 – 39215
Helixi398 – 41821
Helixi422 – 43514
Helixi441 – 4455

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HM8NMR-A319-449[»]
2IOLX-ray2.00A/B320-469[»]
2IONX-ray1.57A320-467[»]
2IOSX-ray1.76A320-469[»]
2KZTNMR-B319-449[»]
2NSZX-ray1.15A322-450[»]
3EIQX-ray3.50C120-469[»]
ProteinModelPortaliQ61823.
SMRiQ61823. Positions 157-450.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ61823.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini163 – 284122MI 1PROSITE-ProRule annotationAdd
BLAST
Domaini326 – 449124MI 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi58 – 647Nuclear localization signalSequence Analysis
Motifi70 – 767PhosphodegronBy similarity
Motifi448 – 4547Nuclear localization signalSequence Analysis

Domaini

Binds EIF4A1 via both MI domains.1 Publication

Sequence similaritiesi

Belongs to the PDCD4 family.Curated
Contains 2 MI domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG249108.
GeneTreeiENSGT00390000015948.
HOGENOMiHOG000261612.
HOVERGENiHBG052841.
InParanoidiQ61823.
KOiK16865.
OMAiLSMSKGG.
OrthoDBiEOG7X9G6X.
PhylomeDBiQ61823.
TreeFamiTF323207.

Family and domain databases

Gene3Di1.25.40.180. 2 hits.
InterProiIPR016024. ARM-type_fold.
IPR003891. Initiation_fac_eIF4g_MI.
IPR016021. MIF4-like_typ_1/2/3.
[Graphical view]
PfamiPF02847. MA3. 2 hits.
[Graphical view]
SMARTiSM00544. MA3. 2 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
PROSITEiPS51366. MI. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q61823-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDIENEQTLN VNPTDPDNLS DSLFSGDEEN AGTEEIKNEI NGNWISASTI
60 70 80 90 100
NEARINAKAK RRLRKNSSRD SGRGDSVSDN GSEAVRSGVA VPTSPKGRLL
110 120 130 140 150
DRRSRSGKGR GLPKKGGAGG KGVWGTPGQV YDVEEVDVKD PNYDDDQENC
160 170 180 190 200
VYETVVLPLD ETAFEKTLTP IIQEYFEHGD TNEVAEMLRD LNLGEMKSGV
210 220 230 240 250
PVLAVSLALE GKASHREMTS KLLSDLCGTV MSTNDVEKSF DKLLKDLPEL
260 270 280 290 300
ALDTPRAPQL VGQFIARAVG DGILCNTYID SYKGTVDCVQ ARAALDKATV
310 320 330 340 350
LLSMSKGGKR KDSVWGSGGG QQPVNHLVKE IDMLLKEYLL SGDISEAEHC
360 370 380 390 400
LKELEVPHFH HELVYEAIVM VLESTGESAF KMILDLLKSL WKSSTITIDQ
410 420 430 440 450
MKRGYERIYN EIPDINLDVP HSYSVLERFV EECFQAGIIS KQLRDLCPSR
460
GRKRFVSEGD GGRLKPESY
Length:469
Mass (Da):51,702
Last modified:November 1, 1996 - v1
Checksum:i6883BCE5011692F1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti232 – 2321S → I in BAA32356. (PubMed:8912629)Curated
Sequence conflicti232 – 2321S → I in BAA13072. (PubMed:9714845)Curated
Sequence conflicti369 – 3691V → I in BAA32356. (PubMed:8912629)Curated
Sequence conflicti369 – 3691V → I in BAA13072. (PubMed:9714845)Curated
Sequence conflicti414 – 4141D → G in BAE43115. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D50465 mRNA. Translation: BAA09056.1.
D86344 mRNA. Translation: BAA13072.1.
AB010139 Genomic DNA. Translation: BAA32356.1.
DQ479921 Genomic DNA. Translation: ABF51670.1.
CT010188 mRNA. Translation: CAJ18396.1.
AK134366 mRNA. Translation: BAE22118.1.
AK172654 mRNA. Translation: BAE43115.1.
BC055739 mRNA. Translation: AAH55739.1.
CCDSiCCDS29903.1.
PIRiJC4523.
RefSeqiNP_001161963.1. NM_001168491.1.
NP_001161964.1. NM_001168492.1.
NP_035180.2. NM_011050.4.
XP_006526825.1. XM_006526762.1.
UniGeneiMm.1605.

Genome annotation databases

EnsembliENSMUST00000025931; ENSMUSP00000025931; ENSMUSG00000024975.
ENSMUST00000074371; ENSMUSP00000073975; ENSMUSG00000024975.
ENSMUST00000165617; ENSMUSP00000133135; ENSMUSG00000024975.
GeneIDi18569.
KEGGimmu:18569.
UCSCiuc008hxb.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D50465 mRNA. Translation: BAA09056.1 .
D86344 mRNA. Translation: BAA13072.1 .
AB010139 Genomic DNA. Translation: BAA32356.1 .
DQ479921 Genomic DNA. Translation: ABF51670.1 .
CT010188 mRNA. Translation: CAJ18396.1 .
AK134366 mRNA. Translation: BAE22118.1 .
AK172654 mRNA. Translation: BAE43115.1 .
BC055739 mRNA. Translation: AAH55739.1 .
CCDSi CCDS29903.1.
PIRi JC4523.
RefSeqi NP_001161963.1. NM_001168491.1.
NP_001161964.1. NM_001168492.1.
NP_035180.2. NM_011050.4.
XP_006526825.1. XM_006526762.1.
UniGenei Mm.1605.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2HM8 NMR - A 319-449 [» ]
2IOL X-ray 2.00 A/B 320-469 [» ]
2ION X-ray 1.57 A 320-467 [» ]
2IOS X-ray 1.76 A 320-469 [» ]
2KZT NMR - B 319-449 [» ]
2NSZ X-ray 1.15 A 322-450 [» ]
3EIQ X-ray 3.50 C 120-469 [» ]
ProteinModelPortali Q61823.
SMRi Q61823. Positions 157-450.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202070. 1 interaction.
IntActi Q61823. 4 interactions.
MINTi MINT-7012023.

PTM databases

PhosphoSitei Q61823.

Proteomic databases

MaxQBi Q61823.
PaxDbi Q61823.
PRIDEi Q61823.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000025931 ; ENSMUSP00000025931 ; ENSMUSG00000024975 .
ENSMUST00000074371 ; ENSMUSP00000073975 ; ENSMUSG00000024975 .
ENSMUST00000165617 ; ENSMUSP00000133135 ; ENSMUSG00000024975 .
GeneIDi 18569.
KEGGi mmu:18569.
UCSCi uc008hxb.2. mouse.

Organism-specific databases

CTDi 27250.
MGIi MGI:107490. Pdcd4.

Phylogenomic databases

eggNOGi NOG249108.
GeneTreei ENSGT00390000015948.
HOGENOMi HOG000261612.
HOVERGENi HBG052841.
InParanoidi Q61823.
KOi K16865.
OMAi LSMSKGG.
OrthoDBi EOG7X9G6X.
PhylomeDBi Q61823.
TreeFami TF323207.

Miscellaneous databases

ChiTaRSi PDCD4. mouse.
EvolutionaryTracei Q61823.
NextBioi 294400.
PROi Q61823.
SOURCEi Search...

Gene expression databases

Bgeei Q61823.
CleanExi MM_PDCD4.
Genevestigatori Q61823.

Family and domain databases

Gene3Di 1.25.40.180. 2 hits.
InterProi IPR016024. ARM-type_fold.
IPR003891. Initiation_fac_eIF4g_MI.
IPR016021. MIF4-like_typ_1/2/3.
[Graphical view ]
Pfami PF02847. MA3. 2 hits.
[Graphical view ]
SMARTi SM00544. MA3. 2 hits.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 2 hits.
PROSITEi PS51366. MI. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of a novel mouse gene MA-3 that is induced upon programmed cell death."
    Shibahara K., Asano M., Ishida Y., Aoki T., Koike T., Honjo T.
    Gene 166:297-301(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: ICR.
    Tissue: Thymus.
  2. "Molecular cloning of the genes suppressed in RVC lymphoma cells by topoisomerase inhibitors."
    Onishi Y., Kizaki H.
    Biochem. Biophys. Res. Commun. 228:7-13(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lymphoma.
  3. "Cloning of the TIS gene suppressed by topoisomerase inhibitors."
    Onishi Y., Hashimoto S., Kizaki H.
    Gene 215:453-459(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: BTBR T+ tf/J.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Spleen and Testis.
  6. "Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
    Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  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].
    Strain: C57BL/6.
    Tissue: Brain.
  8. "The transformation suppressor Pdcd4 is a novel eukaryotic translation initiation factor 4A binding protein that inhibits translation."
    Yang H.-S., Jansen A.P., Komar A.A., Zheng X., Merrick W.C., Costes S., Lockett S.J., Sonenberg N., Colburn N.H.
    Mol. Cell. Biol. 23:26-37(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EIF4A1 AND EIF4A2.
  9. "The transformation suppressor protein Pdcd4 shuttles between nucleus and cytoplasm and binds RNA."
    Boehm M., Sawicka K., Siebrasse J.P., Brehmer-Fastnacht A., Peters R., Klempnauer K.-H.
    Oncogene 22:4905-4910(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. "Epidermal expression of the translation inhibitor programmed cell death 4 suppresses tumorigenesis."
    Jansen A.P., Camalier C.E., Colburn N.H.
    Cancer Res. 65:6034-6041(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Structural basis for inhibition of translation by the tumor suppressor pdcd4."
    Laronde-Leblanc N., Santhanam A.N., Baker A.R., Wlodawer A., Colburn N.H.
    Mol. Cell. Biol. 27:147-156(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 320-469, FUNCTION, INTERACTION WITH EIF4A AND EIF4G, SUBUNIT, MUTAGENESIS OF ASP-414; ASP-418 AND SER-457.
  12. "Structure of the C-terminal MA-3 domain of the tumour suppressor protein Pdcd4 and characterization of its interaction with eIF4A."
    Waters L.C., Veverka V., Bohm M., Schmedt T., Choong P.T., Muskett F.W., Klempnauer K.H., Carr M.D.
    Oncogene 26:4941-4950(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 319-449, INTERACTION WITH EIF4A1.
  13. "Structural basis for translational inhibition by the tumour suppressor Pdcd4."
    Loh P.G., Yang H.S., Walsh M.A., Wang Q., Wang X., Cheng Z., Liu D., Song H.
    EMBO J. 28:274-285(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 120-469 IN COMPLEX WITH EIF4A1, SUBUNIT, DOMAIN.

Entry informationi

Entry nameiPDCD4_MOUSE
AccessioniPrimary (citable) accession number: Q61823
Secondary accession number(s): P97296, Q3T9A9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: November 1, 1996
Last modified: October 29, 2014
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

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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