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Q8CHT0

- AL4A1_MOUSE

UniProt

Q8CHT0 - AL4A1_MOUSE

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Protein
Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
Gene
Aldh4a1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Irreversible conversion of delta-1-pyrroline-5-carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes By similarity.

Catalytic activityi

L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei207 – 2071NAD
Sitei210 – 2101Transition state stabilizer By similarity
Binding sitei232 – 2321NAD
Active sitei313 – 3131Proton acceptor1 Publication
Active sitei347 – 3471Nucleophile1 Publication
Binding sitei446 – 4461NAD
Binding sitei512 – 5121Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi285 – 2895NAD

GO - Molecular functioni

  1. 1-pyrroline-5-carboxylate dehydrogenase activity Source: Ensembl
  2. oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor Source: InterPro

GO - Biological processi

  1. proline biosynthetic process Source: InterPro
  2. proline catabolic process to glutamate Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Proline metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00261; UER00374.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial (EC:1.2.1.88)
Short name:
P5C dehydrogenase
Alternative name(s):
Aldehyde dehydrogenase family 4 member A1
L-glutamate gamma-semialdehyde dehydrogenase
Gene namesi
Name:Aldh4a1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:2443883. Aldh4a1.

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
  2. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2323Mitochondrion By similarity
Add
BLAST
Chaini24 – 562539Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
PRO_0000007174Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei30 – 301N6-succinyllysine1 Publication
Modified residuei51 – 511N6-acetyllysine1 Publication
Modified residuei92 – 921N6-acetyllysine; alternate1 Publication
Modified residuei92 – 921N6-succinyllysine; alternate1 Publication
Modified residuei98 – 981N6-acetyllysine; alternate1 Publication
Modified residuei98 – 981N6-succinyllysine; alternate1 Publication
Modified residuei113 – 1131N6-acetyllysine; alternate1 Publication
Modified residuei113 – 1131N6-succinyllysine; alternate1 Publication
Modified residuei129 – 1291N6-acetyllysine; alternate1 Publication
Modified residuei129 – 1291N6-succinyllysine; alternate1 Publication
Modified residuei174 – 1741N6-acetyllysine; alternate1 Publication
Modified residuei174 – 1741N6-succinyllysine; alternate1 Publication
Modified residuei317 – 3171N6-acetyllysine1 Publication
Modified residuei346 – 3461N6-succinyllysine1 Publication
Modified residuei357 – 3571N6-acetyllysine; alternate1 Publication
Modified residuei357 – 3571N6-succinyllysine; alternate1 Publication
Modified residuei364 – 3641N6-acetyllysine1 Publication
Modified residuei375 – 3751N6-acetyllysine1 Publication
Modified residuei394 – 3941N6-succinyllysine1 Publication
Modified residuei461 – 4611N6-acetyllysine1 Publication
Modified residuei508 – 5081N6-acetyllysine; alternate1 Publication
Modified residuei508 – 5081N6-succinyllysine; alternate1 Publication
Modified residuei530 – 5301N6-acetyllysine1 Publication
Modified residuei551 – 5511N6-acetyllysine1 Publication

Post-translational modificationi

Acetylation of Lys-98, Lys-113 and Lys-401 is observed in liver mitochondria from fasted mice but not from fed mice.

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8CHT0.
PaxDbiQ8CHT0.
PRIDEiQ8CHT0.

PTM databases

PhosphoSiteiQ8CHT0.

Expressioni

Gene expression databases

ArrayExpressiQ8CHT0.
BgeeiQ8CHT0.
CleanExiMM_ALDH4A1.
GenevestigatoriQ8CHT0.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

IntActiQ8CHT0. 3 interactions.
MINTiMINT-1859863.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi44 – 5411
Turni55 – 584
Beta strandi65 – 673
Beta strandi70 – 723
Beta strandi77 – 826
Beta strandi85 – 9410
Helixi98 – 11720
Helixi120 – 13516
Turni136 – 1383
Helixi139 – 15012
Helixi154 – 1607
Helixi163 – 17917
Beta strandi190 – 1956
Beta strandi200 – 2067
Helixi212 – 22413
Beta strandi229 – 2324
Helixi235 – 2373
Helixi238 – 25013
Beta strandi257 – 2604
Helixi265 – 2728
Beta strandi278 – 2858
Helixi287 – 29913
Turni300 – 3034
Beta strandi309 – 3135
Beta strandi318 – 3225
Helixi328 – 34013
Helixi341 – 3444
Beta strandi350 – 3567
Helixi357 – 3593
Helixi360 – 37213
Turni379 – 3813
Helixi393 – 40816
Beta strandi412 – 4165
Beta strandi423 – 4253
Beta strandi431 – 4366
Helixi441 – 4433
Beta strandi449 – 4579
Helixi459 – 4613
Helixi462 – 47110
Beta strandi472 – 48211
Helixi486 – 49510
Turni496 – 4994
Beta strandi501 – 5077
Turni514 – 5163
Helixi536 – 5405
Beta strandi544 – 5496
Helixi559 – 5613

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3V9JX-ray1.30A/B21-562[»]
3V9KX-ray1.50A/B21-562[»]
3V9LX-ray1.50A/B21-562[»]
4E3XX-ray1.24A/B21-562[»]
4LGZX-ray1.68A/B21-562[»]
4LH0X-ray1.67A/B21-562[»]
4LH1X-ray1.67A/B21-562[»]
4LH2X-ray1.67A/B21-562[»]
4LH3X-ray1.81A/B21-562[»]
ProteinModelPortaliQ8CHT0.
SMRiQ8CHT0. Positions 21-562.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1012.
GeneTreeiENSGT00560000077335.
HOGENOMiHOG000271511.
HOVERGENiHBG050484.
InParanoidiB1AXW8.
KOiK00294.
OMAiLRWKHTS.
OrthoDBiEOG7T1R9D.
TreeFamiTF300481.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR005931. P5CDH/ALDH4A1.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR01236. D1pyr5carbox1. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8CHT0-1 [UniParc]FASTAAdd to Basket

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MLPLPSLRRS LLSHAWRGAG LRWKHTSSLK VTNEPILAFS QGSPERDALQ    50
KALKDLKGQM EAIPCVVGDE EVWTSDIQYQ LSPFNHAHKV AKFCYADKAL 100
LNRAIDAALA ARKEWDLKPM ADRAQVFLKA ADMLSGPRRA EVLAKTMVGQ 150
GKTVIQAEID AAAELIDFFR FNAKFAVELE GEQPISVPPS TNHTVYRGLE 200
GFVAAISPFN FTAIGGNLAG APALMGNVVL WKPSDTAMLA SYAVYRILRE 250
AGLPPNIIQF VPADGPTFGD TVTSSEHLCG INFTGSVPTF KHLWRQVAQN 300
LDRFRTFPRL AGECGGKNFH FVHSSADVDS VVSGTLRSAF EYGGQKCSAC 350
SRLYVPKSLW PQIKGRLLEE HSRIKVGDPA EDFGTFFSAV IDAKAFARIK 400
KWLEHARSSP SLSILAGGQC NESVGYYVEP CIIESKDPQE PIMKEEIFGP 450
VLTVYVYPDD KYRETLQLVD STTSYGLTGA VFAQDKAIVQ EATRMLRNAA 500
GNFYINDKST GSVVGQQPFG GARASGTNDK PGGPHYILRW TSPQVIKETH 550
KPLGDWRYSY MQ 562
Length:562
Mass (Da):61,841
Last modified:July 27, 2011 - v3
Checksum:i4D8A0C9C68A99478
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181G → S in BAC32045. 1 Publication
Sequence conflicti18 – 181G → S in AAH56226. 1 Publication
Sequence conflicti18 – 181G → S in AAH39281. 1 Publication
Sequence conflicti18 – 181G → S in AAH24133. 1 Publication
Sequence conflicti32 – 321T → A in BAC32045. 1 Publication
Sequence conflicti32 – 321T → A in AAH56226. 1 Publication
Sequence conflicti32 – 321T → A in AAH39281. 1 Publication
Sequence conflicti32 – 321T → A in AAH24133. 1 Publication
Sequence conflicti47 – 471D → G in BAC32045. 1 Publication
Sequence conflicti60 – 601M → T in BAC32045. 1 Publication
Sequence conflicti60 – 601M → T in AAH56226. 1 Publication
Sequence conflicti60 – 601M → T in AAH39281. 1 Publication
Sequence conflicti60 – 601M → T in AAH24133. 1 Publication
Sequence conflicti467 – 4671Q → K in BAC32045. 1 Publication
Sequence conflicti467 – 4671Q → K in AAH56226. 1 Publication
Sequence conflicti467 – 4671Q → K in AAH39281. 1 Publication
Sequence conflicti467 – 4671Q → K in AAH24133. 1 Publication
Sequence conflicti467 – 4671Q → K in AAH26589. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK044712 mRNA. Translation: BAC32045.1.
AL831790 Genomic DNA. Translation: CAM21310.1.
CH466615 Genomic DNA. Translation: EDL13315.1.
BC024133 mRNA. Translation: AAH24133.1.
BC026589 mRNA. Translation: AAH26589.1.
BC039281 mRNA. Translation: AAH39281.2.
BC056226 mRNA. Translation: AAH56226.1.
CCDSiCCDS18848.1.
RefSeqiNP_780647.3. NM_175438.4.
UniGeneiMm.273571.

Genome annotation databases

EnsembliENSMUST00000039818; ENSMUSP00000043821; ENSMUSG00000028737.
GeneIDi212647.
KEGGimmu:212647.
UCSCiuc012dnu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK044712 mRNA. Translation: BAC32045.1 .
AL831790 Genomic DNA. Translation: CAM21310.1 .
CH466615 Genomic DNA. Translation: EDL13315.1 .
BC024133 mRNA. Translation: AAH24133.1 .
BC026589 mRNA. Translation: AAH26589.1 .
BC039281 mRNA. Translation: AAH39281.2 .
BC056226 mRNA. Translation: AAH56226.1 .
CCDSi CCDS18848.1.
RefSeqi NP_780647.3. NM_175438.4.
UniGenei Mm.273571.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3V9J X-ray 1.30 A/B 21-562 [» ]
3V9K X-ray 1.50 A/B 21-562 [» ]
3V9L X-ray 1.50 A/B 21-562 [» ]
4E3X X-ray 1.24 A/B 21-562 [» ]
4LGZ X-ray 1.68 A/B 21-562 [» ]
4LH0 X-ray 1.67 A/B 21-562 [» ]
4LH1 X-ray 1.67 A/B 21-562 [» ]
4LH2 X-ray 1.67 A/B 21-562 [» ]
4LH3 X-ray 1.81 A/B 21-562 [» ]
ProteinModelPortali Q8CHT0.
SMRi Q8CHT0. Positions 21-562.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8CHT0. 3 interactions.
MINTi MINT-1859863.

PTM databases

PhosphoSitei Q8CHT0.

Proteomic databases

MaxQBi Q8CHT0.
PaxDbi Q8CHT0.
PRIDEi Q8CHT0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000039818 ; ENSMUSP00000043821 ; ENSMUSG00000028737 .
GeneIDi 212647.
KEGGi mmu:212647.
UCSCi uc012dnu.1. mouse.

Organism-specific databases

CTDi 8659.
MGIi MGI:2443883. Aldh4a1.

Phylogenomic databases

eggNOGi COG1012.
GeneTreei ENSGT00560000077335.
HOGENOMi HOG000271511.
HOVERGENi HBG050484.
InParanoidi B1AXW8.
KOi K00294.
OMAi LRWKHTS.
OrthoDBi EOG7T1R9D.
TreeFami TF300481.

Enzyme and pathway databases

UniPathwayi UPA00261 ; UER00374 .

Miscellaneous databases

ChiTaRSi ALDH4A1. mouse.
NextBioi 373656.
PROi Q8CHT0.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8CHT0.
Bgeei Q8CHT0.
CleanExi MM_ALDH4A1.
Genevestigatori Q8CHT0.

Family and domain databases

Gene3Di 3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProi IPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR005931. P5CDH/ALDH4A1.
[Graphical view ]
Pfami PF00171. Aldedh. 1 hit.
[Graphical view ]
SUPFAMi SSF53720. SSF53720. 1 hit.
TIGRFAMsi TIGR01236. D1pyr5carbox1. 1 hit.
PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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: Retina.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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: FVB/N.
    Tissue: Kidney and Liver.
  5. "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: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-30; LYS-92; LYS-98; LYS-113; LYS-129; LYS-174; LYS-346; LYS-357; LYS-394 AND LYS-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51; LYS-92; LYS-98; LYS-113; LYS-129; LYS-174; LYS-317; LYS-357; LYS-364; LYS-375; LYS-461; LYS-508; LYS-530 AND LYS-551, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "Proline: Mother Nature's cryoprotectant applied to protein crystallography."
    Pemberton T.A., Still B.R., Christensen E.M., Singh H., Srivastava D., Tanner J.J.
    Acta Crystallogr. D 68:1010-1018(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) OF 21-562.
  8. "The three-dimensional structural basis of type II hyperprolinemia."
    Srivastava D., Singh R.K., Moxley M.A., Henzl M.T., Becker D.F., Tanner J.J.
    J. Mol. Biol. 420:176-189(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 21-562 IN COMPLEXES WITH GLUTAMATE AND NAD, SUBUNIT, ACTIVE SITE.

Entry informationi

Entry nameiAL4A1_MOUSE
AccessioniPrimary (citable) accession number: Q8CHT0
Secondary accession number(s): B1AXW8
, Q7TND0, Q8BXM3, Q8R0N1, Q8R1S2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 109 of the entry and version 3 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. 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

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