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Q9P2R7

- SUCB1_HUMAN

UniProt

Q9P2R7 - SUCB1_HUMAN

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
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 3 (02 May 2006)
      Previous versions | rss
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    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. 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

    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

    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.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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 – 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

    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.
    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.
    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

    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:
    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

    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: October 1, 2014
    This is version 149 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