Skip Header

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

Q9WUM5

- SUCA_MOUSE

UniProt

Q9WUM5 - SUCA_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Succinyl-CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial

Gene

Suclg1

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

Functioni

Catalyzes the ATP- or GTP-dependent ligation of succinate and CoA to form succinyl-CoA. The nature of the beta subunit determines the nucleotide specificity (By similarity).By similarity

Catalytic activityi

GTP + succinate + CoA = GDP + phosphate + succinyl-CoA.
ATP + succinate + CoA = ADP + phosphate + succinyl-CoA.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei299 – 2991Tele-phosphohistidine intermediateBy similarity

GO - Molecular functioni

  1. ATP citrate synthase activity Source: InterPro
  2. cofactor binding Source: InterPro
  3. GDP binding Source: Ensembl
  4. GTP binding Source: UniProtKB-KW
  5. poly(A) RNA binding Source: Ensembl
  6. succinate-CoA ligase (ADP-forming) activity Source: UniProtKB-EC
  7. succinate-CoA ligase (GDP-forming) activity Source: UniProtKB-EC

GO - Biological processi

  1. succinate metabolic process Source: Ensembl
  2. succinyl-CoA metabolic process Source: Ensembl
  3. tricarboxylic acid cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_249033. Citric acid cycle (TCA cycle).
UniPathwayiUPA00223.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinyl-CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (EC:6.2.1.4, EC:6.2.1.5)
Alternative name(s):
Succinyl-CoA synthetase subunit alpha
Short name:
SCS-alpha
Gene namesi
Name:Suclg1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:1927234. Suclg1.

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. mitochondrial inner membrane Source: MGI
  3. mitochondrion Source: MGI
  4. succinate-CoA ligase complex (GDP-forming) Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4040MitochondrionBy similarityAdd
BLAST
Chaini41 – 346306Succinyl-CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrialPRO_0000033341Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 541N6-acetyllysine1 Publication
Modified residuei57 – 571N6-acetyllysine; alternate1 Publication
Modified residuei57 – 571N6-succinyllysine; alternate1 Publication
Modified residuei66 – 661N6-acetyllysine; alternate1 Publication
Modified residuei66 – 661N6-succinyllysine; alternate1 Publication
Modified residuei81 – 811N6-acetyllysine1 Publication
Modified residuei94 – 941N6-acetyllysine1 Publication
Modified residuei105 – 1051N6-acetyllysine1 Publication
Cross-linki280 – 280Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei338 – 3381N6-succinyllysine1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ9WUM5.
PaxDbiQ9WUM5.
PRIDEiQ9WUM5.

PTM databases

PhosphoSiteiQ9WUM5.

Expressioni

Gene expression databases

BgeeiQ9WUM5.
CleanExiMM_SUCLG1.
ExpressionAtlasiQ9WUM5. baseline and differential.
GenevestigatoriQ9WUM5.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit.By similarity

Protein-protein interaction databases

IntActiQ9WUM5. 4 interactions.
MINTiMINT-1841915.

Structurei

3D structure databases

ProteinModelPortaliQ9WUM5.
SMRiQ9WUM5. Positions 42-346.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0074.
GeneTreeiENSGT00530000063275.
HOGENOMiHOG000239685.
HOVERGENiHBG000957.
InParanoidiQ9WUM5.
KOiK01899.
OMAiFEQDPQT.
OrthoDBiEOG74BJSG.
PhylomeDBiQ9WUM5.
TreeFamiTF300666.

Family and domain databases

Gene3Di3.40.50.261. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR017440. Cit_synth/succinyl-CoA_lig_AS.
IPR003781. CoA-bd.
IPR005810. CoA_lig_alpha.
IPR005811. CoA_ligase.
IPR016040. NAD(P)-bd_dom.
IPR016102. Succinyl-CoA_synth-like.
[Graphical view]
PfamiPF02629. CoA_binding. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view]
PIRSFiPIRSF001553. SucCS_alpha. 1 hit.
PRINTSiPR01798. SCOASYNTHASE.
SMARTiSM00881. CoA_binding. 1 hit.
[Graphical view]
SUPFAMiSSF52210. SSF52210. 1 hit.
TIGRFAMsiTIGR01019. sucCoAalpha. 1 hit.
PROSITEiPS01216. SUCCINYL_COA_LIG_1. 1 hit.
PS00399. SUCCINYL_COA_LIG_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9WUM5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTATVVAAAA TATMVSSSSG LAAARLLSRT FLLQQNGIRH GSYTASRKHI
60 70 80 90 100
YIDKNTKIIC QGFTGKQGTF HSQQALEYGT KLVGGTTPGK GGQKHLGLPV
110 120 130 140 150
FNTVKEAKEK TGATASVIYV PPPFAAAAIN EAIDAEIPLV VCITEGIPQQ
160 170 180 190 200
DMVRVKHRLT RQGTTRLIGP NCPGVINPGE CKIGIMPGHI HKKGRIGIVS
210 220 230 240 250
RSGTLTYEAV HQTTQVGLGQ SLCIGIGGDP FNGTDFIDCL EVFLNDPATE
260 270 280 290 300
GIILIGEIGG HAEENAAAFL KEHNSGPKAK PVVSFIAGIT APPGRRMGHA
310 320 330 340
GAIIAGGKGG AKEKISALQS AGVVVSMSPA QLGTTIYKEF EKRKML
Length:346
Mass (Da):36,155
Last modified:February 10, 2009 - v4
Checksum:i1EB7A444DFCE32FA
GO

Sequence cautioni

The sequence AAD33927.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH11087.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB22331.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB23804.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC40634.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61V → L in AAD33927. 1 PublicationCurated
Sequence conflicti175 – 1751V → I in BAC40634. (PubMed:16141072)Curated
Sequence conflicti188 – 1881G → A in BAB22331. (PubMed:16141072)Curated
Sequence conflicti201 – 2011R → K in AAD33927. 1 PublicationCurated
Sequence conflicti220 – 2201Q → H in AAD33927. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002754 mRNA. Translation: BAB22331.1. Different initiation.
AK005080 mRNA. Translation: BAB23804.1. Different initiation.
AK088888 mRNA. Translation: BAC40634.1. Different initiation.
AF144101 mRNA. Translation: AAD33927.2. Different initiation.
BC011087 mRNA. Translation: AAH11087.1. Different initiation.
CCDSiCCDS20246.2.
RefSeqiNP_063932.2. NM_019879.3.
UniGeneiMm.29845.

Genome annotation databases

EnsembliENSMUST00000064740; ENSMUSP00000065113; ENSMUSG00000052738.
GeneIDi56451.
KEGGimmu:56451.
UCSCiuc009cjm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002754 mRNA. Translation: BAB22331.1 . Different initiation.
AK005080 mRNA. Translation: BAB23804.1 . Different initiation.
AK088888 mRNA. Translation: BAC40634.1 . Different initiation.
AF144101 mRNA. Translation: AAD33927.2 . Different initiation.
BC011087 mRNA. Translation: AAH11087.1 . Different initiation.
CCDSi CCDS20246.2.
RefSeqi NP_063932.2. NM_019879.3.
UniGenei Mm.29845.

3D structure databases

ProteinModelPortali Q9WUM5.
SMRi Q9WUM5. Positions 42-346.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9WUM5. 4 interactions.
MINTi MINT-1841915.

PTM databases

PhosphoSitei Q9WUM5.

Proteomic databases

MaxQBi Q9WUM5.
PaxDbi Q9WUM5.
PRIDEi Q9WUM5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000064740 ; ENSMUSP00000065113 ; ENSMUSG00000052738 .
GeneIDi 56451.
KEGGi mmu:56451.
UCSCi uc009cjm.2. mouse.

Organism-specific databases

CTDi 8802.
MGIi MGI:1927234. Suclg1.

Phylogenomic databases

eggNOGi COG0074.
GeneTreei ENSGT00530000063275.
HOGENOMi HOG000239685.
HOVERGENi HBG000957.
InParanoidi Q9WUM5.
KOi K01899.
OMAi FEQDPQT.
OrthoDBi EOG74BJSG.
PhylomeDBi Q9WUM5.
TreeFami TF300666.

Enzyme and pathway databases

UniPathwayi UPA00223 .
Reactomei REACT_249033. Citric acid cycle (TCA cycle).

Miscellaneous databases

ChiTaRSi Suclg1. mouse.
NextBioi 312668.
PROi Q9WUM5.
SOURCEi Search...

Gene expression databases

Bgeei Q9WUM5.
CleanExi MM_SUCLG1.
ExpressionAtlasi Q9WUM5. baseline and differential.
Genevestigatori Q9WUM5.

Family and domain databases

Gene3Di 3.40.50.261. 1 hit.
3.40.50.720. 1 hit.
InterProi IPR017440. Cit_synth/succinyl-CoA_lig_AS.
IPR003781. CoA-bd.
IPR005810. CoA_lig_alpha.
IPR005811. CoA_ligase.
IPR016040. NAD(P)-bd_dom.
IPR016102. Succinyl-CoA_synth-like.
[Graphical view ]
Pfami PF02629. CoA_binding. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view ]
PIRSFi PIRSF001553. SucCS_alpha. 1 hit.
PRINTSi PR01798. SCOASYNTHASE.
SMARTi SM00881. CoA_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF52210. SSF52210. 1 hit.
TIGRFAMsi TIGR01019. sucCoAalpha. 1 hit.
PROSITEi PS01216. SUCCINYL_COA_LIG_1. 1 hit.
PS00399. SUCCINYL_COA_LIG_2. 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 and NOD.
    Tissue: Cerebellum, Kidney and Thymus.
  2. "Sequence of the alpha subunit of succinyl-CoA synthetase in mouse."
    Tews K.N., Milavetz B.M., Lambeth D.O.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-346.
    Tissue: Heart.
  3. "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] OF 10-346.
  4. Lubec G., Kang S.U., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 45-53; 58-92; 154-169 AND 279-295, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  5. "A proteomics approach to identify the ubiquitinated proteins in mouse heart."
    Jeon H.B., Choi E.S., Yoon J.H., Hwang J.H., Chang J.W., Lee E.K., Choi H.W., Park Z.-Y., Yoo Y.J.
    Biochem. Biophys. Res. Commun. 357:731-736(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-280.
    Tissue: Heart.
  6. "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-57; LYS-66 AND LYS-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.
  7. "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-54; LYS-57; LYS-66; LYS-81; LYS-94 AND LYS-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSUCA_MOUSE
AccessioniPrimary (citable) accession number: Q9WUM5
Secondary accession number(s): Q8C2C3, Q9DBA3, Q9DCI8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: February 10, 2009
Last modified: November 26, 2014
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

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