Skip Header

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

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

Gene

SUCLA2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Catalytic activityi

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

Pathwayi

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: InterPro
  3. 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.
BRENDAi6.2.1.5. 2681.
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 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:11448. SUCLA2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  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)4 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:612073
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.

Chemistry

DrugBankiDB00139. Succinic acid.

Polymorphism and mutation databases

BioMutaiSUCLA2.
DMDMi94730427.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5252MitochondrionBy similarityAdd
BLAST
Chaini53 – 463411Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrialPRO_0000033352Add
BLAST

Amino acid modifications

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

BgeeiQ9P2R7.
CleanExiHS_SUCLA2.
ExpressionAtlasiQ9P2R7. baseline and differential.
GenevestigatoriQ9P2R7.

Organism-specific databases

HPAiHPA039435.
HPA039536.
HPA061528.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi114331. 26 interactions.
IntActiQ9P2R7. 6 interactions.
MINTiMINT-3078782.
STRINGi9606.ENSP00000367923.

Structurei

3D structure databases

ProteinModelPortaliQ9P2R7.
SMRiQ9P2R7. 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

eggNOGiCOG0045.
GeneTreeiENSGT00390000010170.
HOVERGENiHBG055555.
InParanoidiQ9P2R7.
KOiK01900.
OMAiLCMDAKF.
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. AlignAdd to basket

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

        10         20         30         40         50
MAASMFYGRL VAVATLRNHR PRTAQRAAAQ VLGSSGLFNN HGLQVQQQQQ
60 70 80 90 100
RNLSLHEYMS MELLQEAGVS VPKGYVAKSP DEAYAIAKKL GSKDVVIKAQ
110 120 130 140 150
VLAGGRGKGT FESGLKGGVK IVFSPEEAKA VSSQMIGKKL FTKQTGEKGR
160 170 180 190 200
ICNQVLVCER KYPRREYYFA ITMERSFQGP VLIGSSHGGV NIEDVAAESP
210 220 230 240 250
EAIIKEPIDI EEGIKKEQAL QLAQKMGFPP NIVESAAENM VKLYSLFLKY
260 270 280 290 300
DATMIEINPM VEDSDGAVLC MDAKINFDSN SAYRQKKIFD LQDWTQEDER
310 320 330 340 350
DKDAAKANLN YIGLDGNIGC LVNGAGLAMA TMDIIKLHGG TPANFLDVGG
360 370 380 390 400
GATVHQVTEA FKLITSDKKV LAILVNIFGG IMRCDVIAQG IVMAVKDLEI
410 420 430 440 450
KIPVVVRLQG TRVDDAKALI ADSGLKILAC DDLDEAARMV VKLSEIVTLA
460
KQAHVDVKFQ LPI
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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401N → D in BAA91939 (PubMed:14702039).Curated
Sequence conflicti203 – 2031I → V in BAA91939 (PubMed:14702039).Curated
Sequence conflicti323 – 3231N → S in BAA91703 (PubMed:14702039).Curated

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. 1 PublicationVSP_006292Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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 and mutation databases

BioMutaiSUCLA2.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9P2R7.
SMRiQ9P2R7. Positions 53-441.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114331. 26 interactions.
IntActiQ9P2R7. 6 interactions.
MINTiMINT-3078782.
STRINGi9606.ENSP00000367923.

Chemistry

DrugBankiDB00139. Succinic acid.

PTM databases

PhosphoSiteiQ9P2R7.

Polymorphism and mutation databases

BioMutaiSUCLA2.
DMDMi94730427.

Proteomic databases

MaxQBiQ9P2R7.
PaxDbiQ9P2R7.
PRIDEiQ9P2R7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi8803.
GeneCardsiGC13M048510.
GeneReviewsiSUCLA2.
HGNCiHGNC:11448. SUCLA2.
HPAiHPA039435.
HPA039536.
HPA061528.
MIMi603921. gene.
612073. phenotype.
neXtProtiNX_Q9P2R7.
Orphaneti1933. Mitochondrial DNA depletion syndrome, encephalomyopathic form with methylmalonic aciduria.
PharmGKBiPA36245.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0045.
GeneTreeiENSGT00390000010170.
HOVERGENiHBG055555.
InParanoidiQ9P2R7.
KOiK01900.
OMAiLCMDAKF.
OrthoDBiEOG7CZK66.
PhylomeDBiQ9P2R7.
TreeFamiTF300624.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00999.
BioCyciMetaCyc:ENSG00000136143-MONOMER.
BRENDAi6.2.1.5. 2681.
ReactomeiREACT_1785. Citric acid cycle (TCA cycle).

Miscellaneous databases

ChiTaRSiSUCLA2. human.
GeneWikiiSUCLA2.
GenomeRNAii8803.
NextBioi33020.
PROiQ9P2R7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9P2R7.
CleanExiHS_SUCLA2.
ExpressionAtlasiQ9P2R7. baseline and differential.
GenevestigatoriQ9P2R7.

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. "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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. Cited for: VARIANTS MTDPS5 ARG-118 AND CYS-284.
  16. "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: April 29, 2015
This is version 155 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

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 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.