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Q9P2R7 (SUCB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial

EC=6.2.1.5
Alternative name(s):
ATP-specific succinyl-CoA synthetase subunit beta
Renal carcinoma antigen NY-REN-39
Succinyl-CoA synthetase beta-A chain
Short name=SCS-betaA
Gene names
Name:SUCLA2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length463 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the ATP-dependent ligation of succinate and CoA to form succinyl-CoA By similarity. HAMAP-Rule MF_00558

Catalytic activity

ATP + succinate + CoA = ADP + phosphate + succinyl-CoA. HAMAP-Rule MF_00558

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1. HAMAP-Rule MF_00558

Subunit structure

Heterodimer of an alpha and a beta subunit. Interacts with ALAS2. Ref.8

Subcellular location

Mitochondrion HAMAP-Rule MF_00558.

Tissue specificity

Widely expressed. Not expressed in liver and lung. Ref.6

Involvement in disease

Mitochondrial DNA depletion syndrome 5 (MTDPS5) [MIM:612073]: A disorder due to mitochondrial dysfunction. It is characterized by infantile onset of hypotonia, neurologic deterioration, a hyperkinetic-dystonic movement disorder, external ophthalmoplegia, deafness, variable renal tubular dysfunction, and mild methylmalonic aciduria in some patients.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.11 Ref.14 Ref.15

Sequence similarities

Belongs to the succinate/malate CoA ligase beta subunit family.

Contains 1 ATP-grasp domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9P2R7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9P2R7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     26-47: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5252Mitochondrion By similarity
Chain53 – 463411Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial HAMAP-Rule MF_00558
PRO_0000033352

Regions

Domain61 – 288228ATP-grasp

Amino acid modifications

Modified residue781N6-acetyllysine Ref.12
Modified residue841Phosphotyrosine Ref.10
Modified residue881N6-acetyllysine; alternate By similarity
Modified residue881N6-succinyllysine; alternate By similarity
Modified residue1291N6-acetyllysine By similarity
Modified residue1391N6-acetyllysine By similarity
Modified residue1431N6-acetyllysine Ref.12
Modified residue2161N6-acetyllysine By similarity
Modified residue3681N6-acetyllysine By similarity

Natural variations

Alternative sequence26 – 4722Missing in isoform 2.
VSP_006292
Natural variant131V → M.
Corresponds to variant rs35201084 [ dbSNP | Ensembl ].
VAR_046214
Natural variant1181G → R in MTDPS5. Ref.14
VAR_046215
Natural variant1991S → T. Ref.2 Ref.4 Ref.6
Corresponds to variant rs7320366 [ dbSNP | Ensembl ].
VAR_013459
Natural variant2511D → N in MTDPS5. Ref.15
VAR_070123
Natural variant2841R → C in MTDPS5. Ref.14
VAR_046216

Experimental info

Sequence conflict401N → D in BAA91939. Ref.2
Sequence conflict2031I → V in BAA91939. Ref.2
Sequence conflict3231N → S in BAA91703. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 2, 2006. Version 3.
Checksum: 1E1651728AF3B5CD

FASTA46350,317
        10         20         30         40         50         60 
MAASMFYGRL VAVATLRNHR PRTAQRAAAQ VLGSSGLFNN HGLQVQQQQQ RNLSLHEYMS 

        70         80         90        100        110        120 
MELLQEAGVS VPKGYVAKSP DEAYAIAKKL GSKDVVIKAQ VLAGGRGKGT FESGLKGGVK 

       130        140        150        160        170        180 
IVFSPEEAKA VSSQMIGKKL FTKQTGEKGR ICNQVLVCER KYPRREYYFA ITMERSFQGP 

       190        200        210        220        230        240 
VLIGSSHGGV NIEDVAAESP EAIIKEPIDI EEGIKKEQAL QLAQKMGFPP NIVESAAENM 

       250        260        270        280        290        300 
VKLYSLFLKY DATMIEINPM VEDSDGAVLC MDAKINFDSN SAYRQKKIFD LQDWTQEDER 

       310        320        330        340        350        360 
DKDAAKANLN YIGLDGNIGC LVNGAGLAMA TMDIIKLHGG TPANFLDVGG GATVHQVTEA 

       370        380        390        400        410        420 
FKLITSDKKV LAILVNIFGG IMRCDVIAQG IVMAVKDLEI KIPVVVRLQG TRVDDAKALI 

       430        440        450        460 
ADSGLKILAC DDLDEAARMV VKLSEIVTLA KQAHVDVKFQ LPI 

« Hide

Isoform 2 [UniParc].

Checksum: B0B5E3CA063BEAD1
Show »

FASTA44148,040

References

« Hide 'large scale' references
[1]"Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is disrupted in sideroblastic anemia."
Furuyama K., Shigeru S.
J. Clin. Invest. 105:757-764(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT THR-199.
Tissue: Placenta and Tongue.
[3]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT THR-199.
[5]"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] (ISOFORM 1).
Tissue: Testis.
[6]"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 (ISOFORM 1), TISSUE SPECIFICITY, VARIANT THR-199.
Tissue: Liver.
[7]"Antigens recognized by autologous antibody in patients with renal-cell carcinoma."
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J.
Int. J. Cancer 83:456-464(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
Tissue: Renal cell carcinoma.
[8]"The major splice variant of human 5-aminolevulinate synthase-2 contributes significantly to erythroid heme biosynthesis."
Cox T.C., Sadlon T.J., Schwarz Q.P., Matthews C.S., Wise P.D., Cox L.L., Bottomley S.S., May B.K.
Int. J. Biochem. Cell Biol. 36:281-295(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ALAS2.
[9]"Deficiency of the ADP-forming succinyl-CoA synthase activity is associated with encephalomyopathy and mitochondrial DNA depletion."
Elpeleg O., Miller C., Hershkovitz E., Bitner-Glindzicz M., Bondi-Rubinstein G., Rahman S., Pagnamenta A., Eshhar S., Saada A.
Am. J. Hum. Genet. 76:1081-1086(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MTDPS5.
[10]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-84, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Mitochondrial encephalomyopathy with elevated methylmalonic acid is caused by SUCLA2 mutations."
Ostergaard E., Hansen F.J., Sorensen N., Duno M., Vissing J., Larsen P.L., Faeroe O., Thorgrimsson S., Wibrand F., Christensen E., Schwartz M.
Brain 130:853-861(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MTDPS5.
[12]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-78 AND LYS-143, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"SUCLA2 mutations are associated with mild methylmalonic aciduria, Leigh-like encephalomyopathy, dystonia and deafness."
Carrozzo R., Dionisi-Vici C., Steuerwald U., Lucioli S., Deodato F., Di Giandomenico S., Bertini E., Franke B., Kluijtmans L.A., Meschini M.C., Rizzo C., Piemonte F., Rodenburg R., Santer R., Santorelli F.M., van Rooij A., Vermunt-de Koning D., Morava E., Wevers R.A.
Brain 130:862-874(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MTDPS5 ARG-118 AND CYS-284.
[15]"The novel mutation p.Asp251Asn in the beta-subunit of succinate-CoA ligase causes encephalomyopathy and elevated succinylcarnitine."
Jaberi E., Chitsazian F., Ali Shahidi G., Rohani M., Sina F., Safari I., Malakouti Nejad M., Houshmand M., Klotzle B., Elahi E.
J. Hum. Genet. 58:526-530(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MTDPS5 ASN-251.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB035863 mRNA. Translation: BAA92873.1.
AK001458 mRNA. Translation: BAA91703.1.
AK001847 mRNA. Translation: BAA91939.1.
AK315513 mRNA. Translation: BAG37894.1.
AL157369 Genomic DNA. Translation: CAI15149.1.
AL157369 Genomic DNA. Translation: CAI15153.1.
CH471075 Genomic DNA. Translation: EAX08777.1.
BC027587 mRNA. Translation: AAH27587.1.
AF058953 mRNA. Translation: AAC64396.1.
RefSeqNP_003841.1. NM_003850.2.
UniGeneHs.743361.

3D structure databases

ProteinModelPortalQ9P2R7.
SMRQ9P2R7. Positions 53-441.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114331. 21 interactions.
IntActQ9P2R7. 6 interactions.
MINTMINT-3078782.
STRING9606.ENSP00000367923.

Chemistry

DrugBankDB00139. Succinic acid.

PTM databases

PhosphoSiteQ9P2R7.

Polymorphism databases

DMDM94730427.

Proteomic databases

PaxDbQ9P2R7.
PRIDEQ9P2R7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378654; ENSP00000367923; ENSG00000136143. [Q9P2R7-1]
GeneID8803.
KEGGhsa:8803.
UCSCuc001vbs.3. human. [Q9P2R7-1]

Organism-specific databases

CTD8803.
GeneCardsGC13M048510.
HGNCHGNC:11448. SUCLA2.
HPAHPA039435.
HPA039536.
MIM603921. gene.
612073. phenotype.
neXtProtNX_Q9P2R7.
Orphanet1933. Mitochondrial DNA depletion syndrome, encephalomyopathic form with methylmalonic aciduria.
PharmGKBPA36245.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0045.
HOVERGENHBG055555.
InParanoidQ9P2R7.
KOK01900.
OMALCMDAKF.
OrthoDBEOG7CZK66.
PhylomeDBQ9P2R7.
TreeFamTF300624.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000136143-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00223; UER00999.

Gene expression databases

ArrayExpressQ9P2R7.
BgeeQ9P2R7.
CleanExHS_SUCLA2.
GenevestigatorQ9P2R7.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.261. 1 hit.
HAMAPMF_00558. Succ_CoA_beta.
InterProIPR011761. 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]
PANTHERPTHR11815. PTHR11815. 1 hit.
PfamPF08442. ATP-grasp_2. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view]
PIRSFPIRSF001554. SucCS_beta. 1 hit.
SUPFAMSSF52210. SSF52210. 1 hit.
TIGRFAMsTIGR01016. sucCoAbeta. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
PS01217. SUCCINYL_COA_LIG_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSUCLA2. human.
GeneWikiSUCLA2.
GenomeRNAi8803.
NextBio33020.
PROQ9P2R7.
SOURCESearch...

Entry information

Entry nameSUCB1_HUMAN
AccessionPrimary (citable) accession number: Q9P2R7
Secondary accession number(s): B2RDE7 expand/collapse secondary AC list , O95194, Q5T9Q4, Q5T9Q6, Q9NV21, Q9NVP7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: May 2, 2006
Last modified: April 16, 2014
This is version 144 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM