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Q8K2B3

- SDHA_MOUSE

UniProt

Q8K2B3 - SDHA_MOUSE

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Protein

Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial

Gene

Sdha

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

Functioni

Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). Can act as a tumor suppressor.By similarity

Catalytic activityi

Succinate + a quinone = fumarate + a quinol.

Cofactori

FAD.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei275 – 2751FADBy similarity
Binding sitei296 – 2961SubstrateBy similarity
Binding sitei308 – 3081SubstrateBy similarity
Active sitei340 – 3401Proton acceptorBy similarity
Binding sitei407 – 4071SubstrateBy similarity
Binding sitei440 – 4401FADBy similarity
Binding sitei451 – 4511SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi68 – 736FADBy similarity
Nucleotide bindingi91 – 10616FADBy similarityAdd
BLAST
Nucleotide bindingi456 – 4572FADBy similarity

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: InterPro
  2. succinate dehydrogenase (ubiquinone) activity Source: UniProtKB-EC

GO - Biological processi

  1. nervous system development Source: Ensembl
  2. respiratory electron transport chain Source: UniProtKB
  3. succinate metabolic process Source: UniProtKB
  4. tricarboxylic acid cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport, Tricarboxylic acid cycle

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

UniPathwayiUPA00223; UER01006.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (EC:1.3.5.1)
Alternative name(s):
Flavoprotein subunit of complex II
Short name:
Fp
Gene namesi
Name:Sdha
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:1914195. Sdha.

Subcellular locationi

Mitochondrion inner membrane By similarity; Peripheral membrane protein By similarity; Matrix side By similarity

GO - Cellular componenti

  1. mitochondrial inner membrane Source: UniProtKB
  2. mitochondrial respiratory chain complex II Source: UniProtKB
  3. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4343MitochondrionBy similarityAdd
BLAST
Chaini44 – 664621Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrialPRO_0000010337Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei99 – 991Tele-8alpha-FAD histidineBy similarity
Modified residuei167 – 1671N6-acetyllysine1 Publication
Modified residuei179 – 1791N6-acetyllysine; alternate3 Publications
Modified residuei179 – 1791N6-succinyllysine; alternate1 Publication
Modified residuei182 – 1821N6-acetyllysine2 Publications
Modified residuei215 – 2151Phosphotyrosine; by SRCBy similarity
Modified residuei250 – 2501N6-acetyllysine; alternate1 Publication
Modified residuei250 – 2501N6-succinyllysine; alternate1 Publication
Modified residuei335 – 3351N6-acetyllysine; alternate2 Publications
Modified residuei335 – 3351N6-succinyllysine; alternate1 Publication
Modified residuei423 – 4231N6-acetyllysine1 Publication
Modified residuei480 – 4801N6-acetyllysine1 Publication
Modified residuei485 – 4851N6-acetyllysine; alternate1 Publication
Modified residuei485 – 4851N6-succinyllysine; alternate1 Publication
Modified residuei498 – 4981N6-acetyllysine; alternate2 Publications
Modified residuei498 – 4981N6-succinyllysine; alternate1 Publication
Modified residuei517 – 5171N6-acetyllysine1 Publication
Modified residuei538 – 5381N6-acetyllysine; alternate1 Publication
Modified residuei538 – 5381N6-succinyllysine; alternate1 Publication
Modified residuei547 – 5471N6-acetyllysine; alternate3 Publications
Modified residuei547 – 5471N6-succinyllysine; alternate1 Publication
Modified residuei550 – 5501N6-acetyllysine1 Publication
Modified residuei598 – 5981N6-acetyllysine1 Publication
Modified residuei608 – 6081N6-acetyllysine2 Publications
Modified residuei615 – 6151N6-succinyllysine1 Publication
Modified residuei624 – 6241N6-acetyllysine1 Publication
Modified residuei633 – 6331N6-acetyllysine1 Publication
Modified residuei636 – 6361N6-acetyllysine1 Publication
Modified residuei647 – 6471N6-acetyllysine1 Publication

Post-translational modificationi

Acetylation of Lys-498 and Lys-538 is observed in liver mitochondria from fasted mice but not from fed mice. Deacetylated by SIRT3.3 Publications
Phosphorylation at Tyr-215 is important for efficient electron transfer in complex II and the prevention of ROS generation.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8K2B3.
PaxDbiQ8K2B3.
PRIDEiQ8K2B3.

2D gel databases

REPRODUCTION-2DPAGEQ8K2B3.

PTM databases

PhosphoSiteiQ8K2B3.

Expressioni

Gene expression databases

BgeeiQ8K2B3.
ExpressionAtlasiQ8K2B3. baseline and differential.
GenevestigatoriQ8K2B3.

Interactioni

Subunit structurei

Component of complex II composed of four subunits: the flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a cytochrome b560 composed of SDHC and SDHD. Interacts with SDHAF2/SDH5; interaction is required for FAD attachment By similarity. Interacts with TRAP1 By similarity.By similarity

Protein-protein interaction databases

IntActiQ8K2B3. 7 interactions.
MINTiMINT-4122544.

Structurei

3D structure databases

ProteinModelPortaliQ8K2B3.
SMRiQ8K2B3. Positions 52-664.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1053.
GeneTreeiENSGT00390000010046.
HOVERGENiHBG001461.
InParanoidiQ8K2B3.
KOiK00234.
OMAiRTEQGRI.
OrthoDBiEOG7MH0XJ.
PhylomeDBiQ8K2B3.
TreeFamiTF300763.

Family and domain databases

Gene3Di1.20.58.100. 1 hit.
3.90.700.10. 1 hit.
InterProiIPR003953. FAD_bind_dom.
IPR003952. FRD_SDH_FAD_BS.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR027477. Succ_DH/fumarate_Rdtase_cat.
IPR011281. Succ_DH_flav_su_fwd.
IPR014006. Succ_Dhase_FrdA_Gneg.
[Graphical view]
PfamiPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF46977. SSF46977. 1 hit.
SSF56425. SSF56425. 1 hit.
TIGRFAMsiTIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEiPS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8K2B3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGVGAVSRL LRGRRLALTG AWPGTLQKQT CGFHFSVGEN KKASAKVSDA
60 70 80 90 100
ISTQYPVVDH EFDAVVVGAG GAGLRAAFGL SEAGFNTACL TKLFPTRSHT
110 120 130 140 150
VAAQGGINAA LGNMEEDNWR WHFYDTVKGS DWLGDQDAIH YMTEQAPASV
160 170 180 190 200
VELENYGMPF SRTEDGKIYQ RAFGGQSLKF GKGGQAHRCC CVADRTGHSL
210 220 230 240 250
LHTLYGRSLR YDTSYFVEYF ALDLLMENGE CRGVIALCIE DGSIHRIRAK
260 270 280 290 300
NTVIATGGYG RTYFSCTSAH TSTGDGTAMV TRAGLPCQDL EFVQFHPTGI
310 320 330 340 350
YGAGCLITEG CRGEGGILIN SQGERFMERY APVAKDLASR DVVSRSMTLE
360 370 380 390 400
IREGRGCGPE KDHVYLQLHH LPPEQLATRL PGISETAMIF AGVDVTKEPI
410 420 430 440 450
PVLPTVHYNM GGIPTNYKGQ VLKHVNGQDQ IVPGLYACGE AACASVHGAN
460 470 480 490 500
RLGANSLLDL VVFGRACALS IAESCRPGDK VPSIKANAGE ESVMNLDKLR
510 520 530 540 550
FADGSIRTSE LRLNMQKSMQ NHAAVFRVGS VLQEGCEKIS QLYGDLKHLK
560 570 580 590 600
TFDRGMVWNT DLVETLELQN LMLCALQTIY GAEARKESRG AHAREDYKVR
610 620 630 640 650
VDEYDYSKPI QGQQKKPFGE HWRKHTLSYV DIKTGKVTLE YRPVIDKTLN
660
EADCATVPPA IRSY
Length:664
Mass (Da):72,585
Last modified:October 1, 2002 - v1
Checksum:iDDCE1535163C9449
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691A → V in BAE26754. (PubMed:16141072)Curated
Sequence conflicti246 – 2461R → Q in BAE26754. (PubMed:16141072)Curated
Sequence conflicti428 – 4281Q → R in BAE26754. (PubMed:16141072)Curated
Sequence conflicti501 – 5011F → L in ABD77308. (PubMed:16751257)Curated
Sequence conflicti517 – 5171K → M in ABD77308. (PubMed:16751257)Curated
Sequence conflicti571 – 5711L → M in ABD77308. (PubMed:16751257)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK029520 mRNA. Translation: BAC26491.1.
AK034928 mRNA. Translation: BAC28884.1.
AK049590 mRNA. Translation: BAC33831.1.
AK050475 mRNA. Translation: BAC34276.1.
AK075990 mRNA. Translation: BAC36101.1.
AK145923 mRNA. Translation: BAE26754.1.
AK147286 mRNA. Translation: BAE27822.1.
AK147624 mRNA. Translation: BAE28032.1.
AK153085 mRNA. Translation: BAE31710.1.
AK162148 mRNA. Translation: BAE36754.1.
AK169254 mRNA. Translation: BAE41018.1.
AK004362 mRNA. Translation: BAE43173.1.
BC011301 mRNA. Translation: AAH11301.1.
BC031849 mRNA. Translation: AAH31849.1.
DQ402975 mRNA. Translation: ABD77308.1.
AF095938 mRNA. Translation: AAC72373.1.
CCDSiCCDS26643.1.
RefSeqiNP_075770.1. NM_023281.1.
UniGeneiMm.158231.

Genome annotation databases

EnsembliENSMUST00000022062; ENSMUSP00000022062; ENSMUSG00000021577.
GeneIDi66945.
KEGGimmu:66945.
UCSCiuc007rfa.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK029520 mRNA. Translation: BAC26491.1 .
AK034928 mRNA. Translation: BAC28884.1 .
AK049590 mRNA. Translation: BAC33831.1 .
AK050475 mRNA. Translation: BAC34276.1 .
AK075990 mRNA. Translation: BAC36101.1 .
AK145923 mRNA. Translation: BAE26754.1 .
AK147286 mRNA. Translation: BAE27822.1 .
AK147624 mRNA. Translation: BAE28032.1 .
AK153085 mRNA. Translation: BAE31710.1 .
AK162148 mRNA. Translation: BAE36754.1 .
AK169254 mRNA. Translation: BAE41018.1 .
AK004362 mRNA. Translation: BAE43173.1 .
BC011301 mRNA. Translation: AAH11301.1 .
BC031849 mRNA. Translation: AAH31849.1 .
DQ402975 mRNA. Translation: ABD77308.1 .
AF095938 mRNA. Translation: AAC72373.1 .
CCDSi CCDS26643.1.
RefSeqi NP_075770.1. NM_023281.1.
UniGenei Mm.158231.

3D structure databases

ProteinModelPortali Q8K2B3.
SMRi Q8K2B3. Positions 52-664.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8K2B3. 7 interactions.
MINTi MINT-4122544.

PTM databases

PhosphoSitei Q8K2B3.

2D gel databases

REPRODUCTION-2DPAGE Q8K2B3.

Proteomic databases

MaxQBi Q8K2B3.
PaxDbi Q8K2B3.
PRIDEi Q8K2B3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000022062 ; ENSMUSP00000022062 ; ENSMUSG00000021577 .
GeneIDi 66945.
KEGGi mmu:66945.
UCSCi uc007rfa.1. mouse.

Organism-specific databases

CTDi 6389.
MGIi MGI:1914195. Sdha.

Phylogenomic databases

eggNOGi COG1053.
GeneTreei ENSGT00390000010046.
HOVERGENi HBG001461.
InParanoidi Q8K2B3.
KOi K00234.
OMAi RTEQGRI.
OrthoDBi EOG7MH0XJ.
PhylomeDBi Q8K2B3.
TreeFami TF300763.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01006 .

Miscellaneous databases

ChiTaRSi SdhA. mouse.
NextBioi 323092.
PROi Q8K2B3.
SOURCEi Search...

Gene expression databases

Bgeei Q8K2B3.
ExpressionAtlasi Q8K2B3. baseline and differential.
Genevestigatori Q8K2B3.

Family and domain databases

Gene3Di 1.20.58.100. 1 hit.
3.90.700.10. 1 hit.
InterProi IPR003953. FAD_bind_dom.
IPR003952. FRD_SDH_FAD_BS.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR027477. Succ_DH/fumarate_Rdtase_cat.
IPR011281. Succ_DH_flav_su_fwd.
IPR014006. Succ_Dhase_FrdA_Gneg.
[Graphical view ]
Pfami PF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view ]
SUPFAMi SSF46977. SSF46977. 1 hit.
SSF56425. SSF56425. 1 hit.
TIGRFAMsi TIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEi PS00504. FRD_SDH_FAD_BINDING. 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: Bone marrow, Egg, Heart, Pancreas and Testis.
  2. "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: Czech II and FVB/N.
    Tissue: Mammary gland and Mammary tumor.
  3. Lubec G., Klug S., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-14; 47-92; 121-128; 196-207; 233-246; 251-282; 313-325; 362-418; 452-480; 486-498; 528-547; 601-615; 624-633 AND 637-647.
    Strain: C57BL/6.
    Tissue: Brain and Hippocampus.
  4. "Housekeeping genes for phylogenetic analysis of eutherian relationships."
    Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.
    Mol. Biol. Evol. 23:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 59-609.
    Tissue: Liver.
  5. "OXPHOS genes in mammals and the molecular clock."
    Weinreich D.M.
    Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 74-605.
    Tissue: Heart.
  6. "Succinate dehydrogenase is a direct target of sirtuin 3 deacetylase activity."
    Finley L.W., Haas W., Desquiret-Dumas V., Wallace D.C., Procaccio V., Gygi S.P., Haigis M.C.
    PLoS ONE 6:E23295-E23295(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-179; LYS-182; LYS-250; LYS-335; LYS-480; LYS-485; LYS-498; LYS-547; LYS-550; LYS-598; LYS-608; LYS-624 AND LYS-633, DEACETYLATION BY SIRT3, MUTAGENESIS OF LYS-.
  7. "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 LYS-179 AND LYS-547, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-179; LYS-250; LYS-335; LYS-485; LYS-498; LYS-538; LYS-547 AND LYS-615, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.
  8. "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-167; LYS-179; LYS-182; LYS-335; LYS-423; LYS-498; LYS-517; LYS-538; LYS-547; LYS-608; LYS-636 AND LYS-647, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSDHA_MOUSE
AccessioniPrimary (citable) accession number: Q8K2B3
Secondary accession number(s): Q0QF19
, Q3UH25, Q3UKP7, Q3V4B1, Q921P5, Q9Z1Z4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: October 1, 2002
Last modified: October 29, 2014
This is version 112 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

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3