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Protein

Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial

Gene

Sucla2

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

Functioni

Catalyzes the ATP-dependent ligation of succinate and CoA to form succinyl-CoA.By similarity

Catalytic activityi

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

Pathwayi: tricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes succinate from succinyl-CoA (ligase route).
Proteins known to be involved in this subpathway in this organism are:
  1. Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial (Sucla2)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes succinate from succinyl-CoA (ligase route), the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: InterPro
  • succinate-CoA ligase (ADP-forming) activity Source: UniProtKB-EC
  • succinate-CoA ligase activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-71403. Citric acid cycle (TCA cycle).
UniPathwayiUPA00223; UER00999.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial (EC:6.2.1.5)
Alternative name(s):
ATP-specific succinyl-CoA synthetase subunit beta
Succinyl-CoA synthetase beta-A chain
Short name:
SCS-betaA
Gene namesi
Name:Sucla2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1306775. Sucla2.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
  • myelin sheath Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5252MitochondrionBy similarityAdd
BLAST
Chaini53 – 463411Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrialPRO_0000033353Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei78 – 781N6-acetyllysineCombined sources
Modified residuei84 – 841PhosphotyrosineBy similarity
Modified residuei88 – 881N6-acetyllysine; alternateCombined sources
Modified residuei88 – 881N6-succinyllysine; alternateCombined sources
Modified residuei129 – 1291N6-acetyllysineCombined sources
Modified residuei139 – 1391N6-acetyllysineCombined sources
Modified residuei143 – 1431N6-acetyllysineBy similarity
Modified residuei216 – 2161N6-acetyllysineCombined sources
Modified residuei279 – 2791PhosphoserineCombined sources
Modified residuei341 – 3411PhosphothreonineCombined sources
Modified residuei368 – 3681N6-acetyllysineCombined sources
Modified residuei438 – 4381N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9Z2I9.
MaxQBiQ9Z2I9.
PaxDbiQ9Z2I9.
PRIDEiQ9Z2I9.

2D gel databases

REPRODUCTION-2DPAGEIPI00261627.
Q9Z2I9.
UCD-2DPAGEQ9Z2I9.

PTM databases

iPTMnetiQ9Z2I9.
PhosphoSiteiQ9Z2I9.
SwissPalmiQ9Z2I9.

Expressioni

Gene expression databases

BgeeiQ9Z2I9.
GenevisibleiQ9Z2I9. MM.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. Interacts with ALAS2 (By similarity).By similarity

Protein-protein interaction databases

BioGridi203570. 1 interaction.
IntActiQ9Z2I9. 9 interactions.
MINTiMINT-1843246.
STRINGi10090.ENSMUSP00000022706.

Structurei

3D structure databases

ProteinModelPortaliQ9Z2I9.
SMRiQ9Z2I9. Positions 53-441.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 288228ATP-graspAdd
BLAST

Sequence similaritiesi

Contains 1 ATP-grasp domain.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2799. Eukaryota.
COG0045. LUCA.
GeneTreeiENSGT00390000010170.
HOVERGENiHBG055555.
InParanoidiQ9Z2I9.
KOiK01900.
OMAiYIESGCD.
PhylomeDBiQ9Z2I9.
TreeFamiTF300624.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.261. 1 hit.
HAMAPiMF_00558. Succ_CoA_beta.
InterProiIPR011761. ATP-grasp.
IPR013650. ATP-grasp_succ-CoA_synth-type.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR005811. CoA_ligase.
IPR017866. Succ-CoA_synthase_bsu_CS.
IPR005809. Succ_CoA_synthase_bsu.
IPR016102. Succinyl-CoA_synth-like.
[Graphical view]
PANTHERiPTHR11815. PTHR11815. 1 hit.
PfamiPF08442. ATP-grasp_2. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view]
PIRSFiPIRSF001554. SucCS_beta. 1 hit.
SUPFAMiSSF52210. SSF52210. 1 hit.
TIGRFAMsiTIGR01016. sucCoAbeta. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS01217. SUCCINYL_COA_LIG_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9Z2I9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASMFYGRQ LAAAALRSHR PQTTLRAAAQ VLGNSGLFNK HGLQVQQQQQ
60 70 80 90 100
RTLSLHEYLS MELLQEAGVS VPKGFVAKSS DEAYAIAKKL GSKDVVIKAQ
110 120 130 140 150
VLAGGRGKGT FTSGLKGGVK IVFSPEEAKA VSSQMIGQKL ITKQTGEKGR
160 170 180 190 200
ICNQVLVCER KYPRREYYFA ITMERSFQGP VLIGSAQGGV NIEDVAAENP
210 220 230 240 250
EAIVKEPIDI VEGIKKEQAV TLAQKMGFPS NIVDSAAENM IKLYNLFLKY
260 270 280 290 300
DATMVEINPM VEDSDGKVLC MDAKINFDSN SAYRQKKIFD LQDWSQEDER
310 320 330 340 350
DKEAANADIN YIGLDGSIGC LVNGAGLAMA TMDIIKLHGG TPANFLDVGG
360 370 380 390 400
GATVQQVTEA FKLITSDKKV QAILVNIFGG IMRCDVIAQG IVMAVKDLEI
410 420 430 440 450
RIPVVVRLQG TRVDDAKALI ADSGLKILAC DDLDEAAKMV VKLSEIVTLA
460
KEAHVDVKFQ LPI
Length:463
Mass (Da):50,114
Last modified:September 27, 2004 - v2
Checksum:i74CE8E962BC0BB27
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK081965 mRNA. Translation: BAC38380.1.
AK088801 mRNA. Translation: BAC40580.1.
AK132762 mRNA. Translation: BAE21343.1.
AK160130 mRNA. Translation: BAE35647.1.
AK160652 mRNA. Translation: BAE35942.1.
BC056353 mRNA. Translation: AAH56353.1.
BC057605 mRNA. Translation: AAH57605.1.
AF058955 mRNA. Translation: AAC64398.1.
CCDSiCCDS27271.1.
RefSeqiNP_035636.1. NM_011506.3.
UniGeneiMm.38951.

Genome annotation databases

EnsembliENSMUST00000022706; ENSMUSP00000022706; ENSMUSG00000022110.
ENSMUST00000160507; ENSMUSP00000123765; ENSMUSG00000022110.
GeneIDi20916.
KEGGimmu:20916.
UCSCiuc007upx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK081965 mRNA. Translation: BAC38380.1.
AK088801 mRNA. Translation: BAC40580.1.
AK132762 mRNA. Translation: BAE21343.1.
AK160130 mRNA. Translation: BAE35647.1.
AK160652 mRNA. Translation: BAE35942.1.
BC056353 mRNA. Translation: AAH56353.1.
BC057605 mRNA. Translation: AAH57605.1.
AF058955 mRNA. Translation: AAC64398.1.
CCDSiCCDS27271.1.
RefSeqiNP_035636.1. NM_011506.3.
UniGeneiMm.38951.

3D structure databases

ProteinModelPortaliQ9Z2I9.
SMRiQ9Z2I9. Positions 53-441.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203570. 1 interaction.
IntActiQ9Z2I9. 9 interactions.
MINTiMINT-1843246.
STRINGi10090.ENSMUSP00000022706.

PTM databases

iPTMnetiQ9Z2I9.
PhosphoSiteiQ9Z2I9.
SwissPalmiQ9Z2I9.

2D gel databases

REPRODUCTION-2DPAGEIPI00261627.
Q9Z2I9.
UCD-2DPAGEQ9Z2I9.

Proteomic databases

EPDiQ9Z2I9.
MaxQBiQ9Z2I9.
PaxDbiQ9Z2I9.
PRIDEiQ9Z2I9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022706; ENSMUSP00000022706; ENSMUSG00000022110.
ENSMUST00000160507; ENSMUSP00000123765; ENSMUSG00000022110.
GeneIDi20916.
KEGGimmu:20916.
UCSCiuc007upx.1. mouse.

Organism-specific databases

CTDi8803.
MGIiMGI:1306775. Sucla2.

Phylogenomic databases

eggNOGiKOG2799. Eukaryota.
COG0045. LUCA.
GeneTreeiENSGT00390000010170.
HOVERGENiHBG055555.
InParanoidiQ9Z2I9.
KOiK01900.
OMAiYIESGCD.
PhylomeDBiQ9Z2I9.
TreeFamiTF300624.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00999.
ReactomeiR-MMU-71403. Citric acid cycle (TCA cycle).

Miscellaneous databases

ChiTaRSiSucla2. mouse.
PROiQ9Z2I9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z2I9.
GenevisibleiQ9Z2I9. MM.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.261. 1 hit.
HAMAPiMF_00558. Succ_CoA_beta.
InterProiIPR011761. ATP-grasp.
IPR013650. ATP-grasp_succ-CoA_synth-type.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR005811. CoA_ligase.
IPR017866. Succ-CoA_synthase_bsu_CS.
IPR005809. Succ_CoA_synthase_bsu.
IPR016102. Succinyl-CoA_synth-like.
[Graphical view]
PANTHERiPTHR11815. PTHR11815. 1 hit.
PfamiPF08442. ATP-grasp_2. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view]
PIRSFiPIRSF001554. SucCS_beta. 1 hit.
SUPFAMiSSF52210. SSF52210. 1 hit.
TIGRFAMsiTIGR01016. sucCoAbeta. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS01217. SUCCINYL_COA_LIG_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

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, Head, Testis and Thymus.
  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: C57BL/6J.
    Tissue: Brain.
  3. "Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA synthetases in multicellular eucaryotes."
    Johnson J.D., Mehus J.G., Tews K., Milavetz B.I., Lambeth D.O.
    J. Biol. Chem. 273:27580-27586(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 38-463.
    Tissue: Heart.
  4. Lubec G., Kang S.U., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 121-129; 206-215; 337-362 AND 443-451, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J and OF1.
    Tissue: Brain and Hippocampus.
  5. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
    Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
    Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279 AND THR-341, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "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-88, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  9. "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-78; LYS-88; LYS-129; LYS-139; LYS-216; LYS-368 AND LYS-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSUCB1_MOUSE
AccessioniPrimary (citable) accession number: Q9Z2I9
Secondary accession number(s): Q3TVH1, Q8BGS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: September 27, 2004
Last modified: June 8, 2016
This is version 146 of the entry and version 2 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

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 one 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.