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Q9P2R7

- SUCB1_HUMAN

UniProt

Q9P2R7 - SUCB1_HUMAN

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Protein
Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial
Gene
SUCLA2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Pathwayi

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: InterPro
  3. protein binding Source: UniProtKB
  4. succinate-CoA ligase (ADP-forming) activity Source: UniProtKB

GO - Biological processi

  1. cellular metabolic process Source: Reactome
  2. small molecule metabolic process Source: Reactome
  3. succinate metabolic process Source: Ensembl
  4. succinyl-CoA metabolic process Source: ProtInc
  5. succinyl-CoA pathway Source: UniProtKB
  6. tricarboxylic acid cycle Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000136143-MONOMER.
ReactomeiREACT_1785. 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
Renal carcinoma antigen NY-REN-39
Succinyl-CoA synthetase beta-A chain
Short name:
SCS-betaA
Gene namesi
Name:SUCLA2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:11448. SUCLA2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. mitochondrial matrix Source: Reactome
  3. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

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.4 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti118 – 1181G → R in MTDPS5. 1 Publication
VAR_046215
Natural varianti251 – 2511D → N in MTDPS5. 1 Publication
VAR_070123
Natural varianti284 – 2841R → C in MTDPS5. 1 Publication
VAR_046216

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi612073. phenotype.
Orphaneti1933. Mitochondrial DNA depletion syndrome, encephalomyopathic form with methylmalonic aciduria.
PharmGKBiPA36245.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5252Mitochondrion By similarity
Add
BLAST
Chaini53 – 463411Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrialUniRule annotation
PRO_0000033352Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei78 – 781N6-acetyllysine1 Publication
Modified residuei84 – 841Phosphotyrosine1 Publication
Modified residuei88 – 881N6-acetyllysine; alternate By similarity
Modified residuei88 – 881N6-succinyllysine; alternate By similarity
Modified residuei129 – 1291N6-acetyllysine By similarity
Modified residuei139 – 1391N6-acetyllysine By similarity
Modified residuei143 – 1431N6-acetyllysine1 Publication
Modified residuei216 – 2161N6-acetyllysine By similarity
Modified residuei368 – 3681N6-acetyllysine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9P2R7.
PaxDbiQ9P2R7.
PRIDEiQ9P2R7.

PTM databases

PhosphoSiteiQ9P2R7.

Expressioni

Tissue specificityi

Widely expressed. Not expressed in liver and lung.1 Publication

Gene expression databases

ArrayExpressiQ9P2R7.
BgeeiQ9P2R7.
CleanExiHS_SUCLA2.
GenevestigatoriQ9P2R7.

Organism-specific databases

HPAiHPA039435.
HPA039536.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. Interacts with ALAS2.1 Publication

Protein-protein interaction databases

BioGridi114331. 21 interactions.
IntActiQ9P2R7. 6 interactions.
MINTiMINT-3078782.
STRINGi9606.ENSP00000367923.

Structurei

3D structure databases

ProteinModelPortaliQ9P2R7.
SMRiQ9P2R7. Positions 53-441.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 1 ATP-grasp domain.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0045.
HOVERGENiHBG055555.
InParanoidiQ9P2R7.
KOiK01900.
OMAiKVVFMAS.
OrthoDBiEOG7CZK66.
PhylomeDBiQ9P2R7.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9P2R7-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAASMFYGRL VAVATLRNHR PRTAQRAAAQ VLGSSGLFNN HGLQVQQQQQ    50
RNLSLHEYMS MELLQEAGVS VPKGYVAKSP DEAYAIAKKL GSKDVVIKAQ 100
VLAGGRGKGT FESGLKGGVK IVFSPEEAKA VSSQMIGKKL FTKQTGEKGR 150
ICNQVLVCER KYPRREYYFA ITMERSFQGP VLIGSSHGGV NIEDVAAESP 200
EAIIKEPIDI EEGIKKEQAL QLAQKMGFPP NIVESAAENM VKLYSLFLKY 250
DATMIEINPM VEDSDGAVLC MDAKINFDSN SAYRQKKIFD LQDWTQEDER 300
DKDAAKANLN YIGLDGNIGC LVNGAGLAMA TMDIIKLHGG TPANFLDVGG 350
GATVHQVTEA FKLITSDKKV LAILVNIFGG IMRCDVIAQG IVMAVKDLEI 400
KIPVVVRLQG TRVDDAKALI ADSGLKILAC DDLDEAARMV VKLSEIVTLA 450
KQAHVDVKFQ LPI 463
Length:463
Mass (Da):50,317
Last modified:May 2, 2006 - v3
Checksum:i1E1651728AF3B5CD
GO
Isoform 2 (identifier: Q9P2R7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     26-47: Missing.

Note: No experimental confirmation available.

Show »
Length:441
Mass (Da):48,040
Checksum:iB0B5E3CA063BEAD1
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti13 – 131V → M.
Corresponds to variant rs35201084 [ dbSNP | Ensembl ].
VAR_046214
Natural varianti118 – 1181G → R in MTDPS5. 1 Publication
VAR_046215
Natural varianti199 – 1991S → T.3 Publications
Corresponds to variant rs7320366 [ dbSNP | Ensembl ].
VAR_013459
Natural varianti251 – 2511D → N in MTDPS5. 1 Publication
VAR_070123
Natural varianti284 – 2841R → C in MTDPS5. 1 Publication
VAR_046216

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei26 – 4722Missing in isoform 2.
VSP_006292Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401N → D in BAA91939. 1 Publication
Sequence conflicti203 – 2031I → V in BAA91939. 1 Publication
Sequence conflicti323 – 3231N → S in BAA91703. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS9406.1. [Q9P2R7-1]
RefSeqiNP_003841.1. NM_003850.2. [Q9P2R7-1]
UniGeneiHs.743361.

Genome annotation databases

EnsembliENST00000378654; ENSP00000367923; ENSG00000136143. [Q9P2R7-1]
GeneIDi8803.
KEGGihsa:8803.
UCSCiuc001vbs.3. human. [Q9P2R7-1]

Polymorphism databases

DMDMi94730427.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS9406.1. [Q9P2R7-1 ]
RefSeqi NP_003841.1. NM_003850.2. [Q9P2R7-1 ]
UniGenei Hs.743361.

3D structure databases

ProteinModelPortali Q9P2R7.
SMRi Q9P2R7. Positions 53-441.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114331. 21 interactions.
IntActi Q9P2R7. 6 interactions.
MINTi MINT-3078782.
STRINGi 9606.ENSP00000367923.

Chemistry

DrugBanki DB00139. Succinic acid.

PTM databases

PhosphoSitei Q9P2R7.

Polymorphism databases

DMDMi 94730427.

Proteomic databases

MaxQBi Q9P2R7.
PaxDbi Q9P2R7.
PRIDEi Q9P2R7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000378654 ; ENSP00000367923 ; ENSG00000136143 . [Q9P2R7-1 ]
GeneIDi 8803.
KEGGi hsa:8803.
UCSCi uc001vbs.3. human. [Q9P2R7-1 ]

Organism-specific databases

CTDi 8803.
GeneCardsi GC13M048510.
GeneReviewsi SUCLA2.
HGNCi HGNC:11448. SUCLA2.
HPAi HPA039435.
HPA039536.
MIMi 603921. gene.
612073. phenotype.
neXtProti NX_Q9P2R7.
Orphaneti 1933. Mitochondrial DNA depletion syndrome, encephalomyopathic form with methylmalonic aciduria.
PharmGKBi PA36245.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0045.
HOVERGENi HBG055555.
InParanoidi Q9P2R7.
KOi K01900.
OMAi KVVFMAS.
OrthoDBi EOG7CZK66.
PhylomeDBi Q9P2R7.
TreeFami TF300624.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER00999 .
BioCyci MetaCyc:ENSG00000136143-MONOMER.
Reactomei REACT_1785. Citric acid cycle (TCA cycle).

Miscellaneous databases

ChiTaRSi SUCLA2. human.
GeneWikii SUCLA2.
GenomeRNAii 8803.
NextBioi 33020.
PROi Q9P2R7.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9P2R7.
Bgeei Q9P2R7.
CleanExi HS_SUCLA2.
Genevestigatori Q9P2R7.

Family and domain databases

Gene3Di 3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.261. 1 hit.
HAMAPi MF_00558. Succ_CoA_beta.
InterProi IPR011761. 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 ]
PANTHERi PTHR11815. PTHR11815. 1 hit.
Pfami PF08442. ATP-grasp_2. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view ]
PIRSFi PIRSF001554. SucCS_beta. 1 hit.
SUPFAMi SSF52210. SSF52210. 1 hit.
TIGRFAMsi TIGR01016. sucCoAbeta. 1 hit.
PROSITEi PS50975. ATP_GRASP. 1 hit.
PS01217. SUCCINYL_COA_LIG_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. 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.

Entry informationi

Entry nameiSUCB1_HUMAN
AccessioniPrimary (citable) accession number: Q9P2R7
Secondary accession number(s): B2RDE7
, O95194, Q5T9Q4, Q5T9Q6, Q9NV21, Q9NVP7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: May 2, 2006
Last modified: September 3, 2014
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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