Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phosphoglycerate kinase 1

Gene

Pgk1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391SubstrateBy similarity
Binding sitei123 – 1231SubstrateBy similarity
Binding sitei171 – 1711SubstrateBy similarity
Binding sitei220 – 2201ATPBy similarity
Binding sitei313 – 3131ATP; via carbonyl oxygenBy similarity
Binding sitei344 – 3441ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi373 – 3764ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. phosphoglycerate kinase activity Source: UniProtKB

GO - Biological processi

  1. glycolytic process Source: UniProtKB-UniPathway
  2. phosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_232322. Glycolysis.
REACT_263230. Gluconeogenesis.
SABIO-RKP09411.
UniPathwayiUPA00109; UER00185.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglycerate kinase 1 (EC:2.7.2.3)
Gene namesi
Name:Pgk1
Synonyms:Pgk-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12, UP000000589: Chromosome X

Organism-specific databases

MGIiMGI:97555. Pgk1.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 417416Phosphoglycerate kinase 1PRO_0000145835Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei6 – 61N6-succinyllysine1 Publication
Modified residuei11 – 111N6-acetyllysine1 Publication
Modified residuei48 – 481N6-acetyllysine; alternateBy similarity
Modified residuei48 – 481N6-succinyllysine; alternate1 Publication
Modified residuei75 – 751N6-acetyllysineBy similarity
Modified residuei76 – 761Phosphotyrosine1 Publication
Modified residuei86 – 861N6-acetyllysineBy similarity
Modified residuei91 – 911N6-acetyllysine1 Publication
Modified residuei97 – 971N6-acetyllysineBy similarity
Modified residuei131 – 1311N6-acetyllysine; alternateBy similarity
Modified residuei131 – 1311N6-malonyllysine; alternateBy similarity
Modified residuei146 – 1461N6-acetyllysineBy similarity
Modified residuei191 – 1911N6-succinyllysine1 Publication
Modified residuei196 – 1961PhosphotyrosineBy similarity
Modified residuei199 – 1991N6-acetyllysineBy similarity
Modified residuei203 – 2031Phosphoserine2 Publications
Modified residuei267 – 2671N6-acetyllysineBy similarity
Modified residuei291 – 2911N6-acetyllysine1 Publication
Modified residuei361 – 3611N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP09411.
PaxDbiP09411.
PRIDEiP09411.

2D gel databases

COMPLUYEAST-2DPAGEP09411.
REPRODUCTION-2DPAGEIPI00555069.
P09411.
SWISS-2DPAGEP09411.

PTM databases

PhosphoSiteiP09411.

Expressioni

Gene expression databases

BgeeiP09411.
CleanExiMM_PGK1.
ExpressionAtlasiP09411. baseline and differential.
GenevestigatoriP09411.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi202133. 4 interactions.
IntActiP09411. 7 interactions.
MINTiMINT-1854650.

Structurei

Secondary structure

1
417
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 113Combined sources
Beta strandi18 – 225Combined sources
Beta strandi33 – 353Combined sources
Helixi38 – 5215Combined sources
Beta strandi56 – 616Combined sources
Turni73 – 753Combined sources
Helixi79 – 8911Combined sources
Beta strandi93 – 953Combined sources
Beta strandi99 – 1013Combined sources
Helixi102 – 1098Combined sources
Beta strandi115 – 1184Combined sources
Helixi122 – 1243Combined sources
Turni126 – 1294Combined sources
Beta strandi130 – 1334Combined sources
Beta strandi139 – 1413Combined sources
Helixi144 – 15512Combined sources
Beta strandi159 – 1635Combined sources
Helixi166 – 1683Combined sources
Helixi174 – 1774Combined sources
Beta strandi184 – 1863Combined sources
Helixi188 – 20215Combined sources
Beta strandi206 – 2127Combined sources
Helixi218 – 2203Combined sources
Helixi221 – 2288Combined sources
Beta strandi232 – 2365Combined sources
Helixi238 – 2403Combined sources
Helixi241 – 2499Combined sources
Helixi260 – 2634Combined sources
Helixi266 – 27611Combined sources
Beta strandi279 – 2813Combined sources
Beta strandi284 – 29310Combined sources
Beta strandi298 – 3025Combined sources
Turni303 – 3053Combined sources
Beta strandi312 – 3165Combined sources
Helixi318 – 33013Combined sources
Beta strandi332 – 3387Combined sources
Helixi346 – 3483Combined sources
Helixi350 – 36415Combined sources
Beta strandi368 – 3769Combined sources
Beta strandi389 – 3946Combined sources
Helixi396 – 4038Combined sources
Helixi409 – 4124Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4O3FX-ray2.11A1-417[»]
ProteinModelPortaliP09411.
SMRiP09411. Positions 5-417.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni24 – 263Substrate bindingBy similarity
Regioni63 – 664Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the phosphoglycerate kinase family.Curated

Phylogenomic databases

eggNOGiCOG0126.
GeneTreeiENSGT00390000008820.
HOGENOMiHOG000227107.
HOVERGENiHBG008177.
InParanoidiP09411.
KOiK00927.
OMAiIKHCLDH.
OrthoDBiEOG74R1QN.
PhylomeDBiP09411.
TreeFamiTF300489.

Family and domain databases

Gene3Di3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPiMF_00145. Phosphoglyc_kinase.
InterProiIPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view]
PANTHERiPTHR11406. PTHR11406. 1 hit.
PfamiPF00162. PGK. 1 hit.
[Graphical view]
PIRSFiPIRSF000724. Pgk. 1 hit.
PRINTSiPR00477. PHGLYCKINASE.
SUPFAMiSSF53748. SSF53748. 1 hit.
PROSITEiPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P09411-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLSNKLTLD KLDVKGKRVV MRVDFNVPMK NNQITNNQRI KAAVPSIKFC
60 70 80 90 100
LDNGAKSVVL MSHLGRPDGV PMPDKYSLEP VAAELKSLLG KDVLFLKDCV
110 120 130 140 150
GPEVENACAN PAAGTVILLE NLRFHVEEEG KGKDASGNKV KAEPAKIDAF
160 170 180 190 200
RASLSKLGDV YVNDAFGTAH RAHSSMVGVN LPQKAGGFLM KKELNYFAKA
210 220 230 240 250
LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM AFTFLKVLNN
260 270 280 290 300
MEIGTSLYDE EGAKIVKDLM SKAEKNGVKI TLPVDFVTAD KFDENAKTGQ
310 320 330 340 350
ATVASGIPAG WMGLDCGTES SKKYAEAVGR AKQIVWNGPV GVFEWEAFAR
360 370 380 390 400
GTKSLMDEVV KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL
410
ELLEGKVLPG VDALSNV
Length:417
Mass (Da):44,550
Last modified:May 1, 2007 - v4
Checksum:i5E2EE194FF9D8CEE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 561K → N in AAA70267 (PubMed:3542714).Curated
Sequence conflicti184 – 1841K → R in BAE26693 (PubMed:16141072).Curated
Sequence conflicti265 – 2651I → V in BAE37790 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15668 mRNA. Translation: AAA70267.1.
AK145846 mRNA. Translation: BAE26693.1.
AK167710 mRNA. Translation: BAE39754.1.
AK167459 mRNA. Translation: BAE39544.1.
AK167441 mRNA. Translation: BAE39527.1.
AK133877 mRNA. Translation: BAE21906.1.
AK164440 mRNA. Translation: BAE37790.1.
BX469914 Genomic DNA. Translation: CAM17784.1.
BC083355 mRNA. Translation: AAH83355.1.
BC108372 mRNA. Translation: AAI08373.1.
M18735 Genomic DNA. Translation: AAA39919.1.
X55309 Genomic DNA. Translation: CAA39013.1.
X15339 Genomic DNA. Translation: CAA33391.1.
CCDSiCCDS30339.1.
PIRiA25567.
RefSeqiNP_032854.2. NM_008828.3.
UniGeneiMm.316355.
Mm.336204.
Mm.336205.

Genome annotation databases

EnsembliENSMUST00000081593; ENSMUSP00000080302; ENSMUSG00000062070.
ENSMUST00000085735; ENSMUSP00000136544; ENSMUSG00000066632.
GeneIDi18655.
KEGGimmu:18655.
UCSCiuc009ubo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15668 mRNA. Translation: AAA70267.1.
AK145846 mRNA. Translation: BAE26693.1.
AK167710 mRNA. Translation: BAE39754.1.
AK167459 mRNA. Translation: BAE39544.1.
AK167441 mRNA. Translation: BAE39527.1.
AK133877 mRNA. Translation: BAE21906.1.
AK164440 mRNA. Translation: BAE37790.1.
BX469914 Genomic DNA. Translation: CAM17784.1.
BC083355 mRNA. Translation: AAH83355.1.
BC108372 mRNA. Translation: AAI08373.1.
M18735 Genomic DNA. Translation: AAA39919.1.
X55309 Genomic DNA. Translation: CAA39013.1.
X15339 Genomic DNA. Translation: CAA33391.1.
CCDSiCCDS30339.1.
PIRiA25567.
RefSeqiNP_032854.2. NM_008828.3.
UniGeneiMm.316355.
Mm.336204.
Mm.336205.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4O3FX-ray2.11A1-417[»]
ProteinModelPortaliP09411.
SMRiP09411. Positions 5-417.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202133. 4 interactions.
IntActiP09411. 7 interactions.
MINTiMINT-1854650.

PTM databases

PhosphoSiteiP09411.

2D gel databases

COMPLUYEAST-2DPAGEP09411.
REPRODUCTION-2DPAGEIPI00555069.
P09411.
SWISS-2DPAGEP09411.

Proteomic databases

MaxQBiP09411.
PaxDbiP09411.
PRIDEiP09411.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000081593; ENSMUSP00000080302; ENSMUSG00000062070.
ENSMUST00000085735; ENSMUSP00000136544; ENSMUSG00000066632.
GeneIDi18655.
KEGGimmu:18655.
UCSCiuc009ubo.1. mouse.

Organism-specific databases

CTDi5230.
MGIiMGI:97555. Pgk1.

Phylogenomic databases

eggNOGiCOG0126.
GeneTreeiENSGT00390000008820.
HOGENOMiHOG000227107.
HOVERGENiHBG008177.
InParanoidiP09411.
KOiK00927.
OMAiIKHCLDH.
OrthoDBiEOG74R1QN.
PhylomeDBiP09411.
TreeFamiTF300489.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00185.
ReactomeiREACT_232322. Glycolysis.
REACT_263230. Gluconeogenesis.
SABIO-RKP09411.

Miscellaneous databases

NextBioi294662.
PROiP09411.
SOURCEiSearch...

Gene expression databases

BgeeiP09411.
CleanExiMM_PGK1.
ExpressionAtlasiP09411. baseline and differential.
GenevestigatoriP09411.

Family and domain databases

Gene3Di3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPiMF_00145. Phosphoglyc_kinase.
InterProiIPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view]
PANTHERiPTHR11406. PTHR11406. 1 hit.
PfamiPF00162. PGK. 1 hit.
[Graphical view]
PIRSFiPIRSF000724. Pgk. 1 hit.
PRINTSiPR00477. PHGLYCKINASE.
SUPFAMiSSF53748. SSF53748. 1 hit.
PROSITEiPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of a cDNA clone containing the entire coding region for mouse X-chromosome-linked phosphoglycerate kinase."
    Mori N., Singer-Sam J., Lee C.-Y., Riggs A.D.
    Gene 45:275-280(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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.
    Tissue: Eye and Placenta.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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].
    Strain: 129 and C57BL/6.
    Tissue: Brain and Mammary tumor.
  5. "Cloning and expression of the mouse pgk-1 gene and the nucleotide sequence of its promoter."
    Adra C.N., Boer P.H., McBurney M.W.
    Gene 60:65-74(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
  6. "Selective activation of testis-specific genes in cultured rat spermatogenic cells."
    Tamaru M., Nagao Y., Taira M., Tatibana M., Masamune Y., Nakanishi Y.
    Biochim. Biophys. Acta 1049:331-338(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
  7. "Polymorphisms in the coding and noncoding regions of murine Pgk-1 alleles."
    Boer P.H., Potten H., Adra C.N., Jardine K., Mullhofer G., McBurney M.W.
    Biochem. Genet. 28:299-308(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
  8. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 23-30; 76-86; 98-123; 157-184; 193-216; 247-264; 280-297; 333-350 AND 389-417, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain and Hippocampus.
  9. "Evolutionary conservation of the substrate-binding cleft of phosphoglycerate kinases."
    Mori N., Singer-Sam J., Riggs A.D.
    FEBS Lett. 204:313-317(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISCUSSION OF SEQUENCE.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-76, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  12. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  13. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-11; LYS-91; LYS-291 AND LYS-361, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-48 AND LYS-191, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.

Entry informationi

Entry nameiPGK1_MOUSE
AccessioniPrimary (citable) accession number: P09411
Secondary accession number(s): Q3TPE6, Q3UKV8, Q5XJE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: May 1, 2007
Last modified: March 4, 2015
This is version 138 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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

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.