Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P78820

- ACAC_SCHPO

UniProt

P78820 - ACAC_SCHPO

Protein

Acetyl-CoA carboxylase

Gene

cut6

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 2 (11 Jan 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.

    Catalytic activityi

    ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.
    ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].

    Cofactori

    Biotin.By similarity
    Binds 2 manganese ions per subunit.By similarity

    Enzyme regulationi

    By phosphorylation.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi375 – 3751Manganese 1By similarity
    Metal bindingi389 – 3891Manganese 1By similarity
    Metal bindingi389 – 3891Manganese 2By similarity
    Metal bindingi391 – 3911Manganese 2By similarity
    Active sitei393 – 3931By similarity
    Binding sitei1772 – 17721Coenzyme ABy similarity
    Binding sitei2074 – 20741Coenzyme ABy similarity
    Binding sitei2076 – 20761Coenzyme ABy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi266 – 2716ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. acetyl-CoA carboxylase activity Source: PomBase
    2. ATP binding Source: PomBase
    3. biotin carboxylase activity Source: PomBase
    4. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. long-chain fatty acid biosynthetic process Source: PomBase
    2. malonyl-CoA biosynthetic process Source: UniProtKB-UniPathway
    3. regulation of mitosis Source: PomBase

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Keywords - Ligandi

    ATP-binding, Biotin, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_188246. Biotin transport and metabolism.
    REACT_193506. Defective HLCS causes multiple carboxylase deficiency.
    REACT_210492. Import of palmitoyl-CoA into the mitochondrial matrix.
    REACT_218197. Fatty Acyl-CoA Biosynthesis.
    UniPathwayiUPA00655; UER00711.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyl-CoA carboxylase (EC:6.4.1.2)
    Short name:
    ACC
    Alternative name(s):
    Cell untimely torn protein 6
    Including the following 1 domains:
    Biotin carboxylase (EC:6.3.4.14)
    Gene namesi
    Name:cut6
    ORF Names:SPAC56E4.04c
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome I

    Organism-specific databases

    PomBaseiSPAC56E4.04c.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: PomBase
    2. cytosol Source: PomBase
    3. fungal-type vacuole membrane Source: PomBase

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 22802280Acetyl-CoA carboxylasePRO_0000146769Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei745 – 7451N6-biotinyllysineBy similarity
    Modified residuei1179 – 11791Phosphoserine1 Publication
    Modified residuei1181 – 11811Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP78820.
    PaxDbiP78820.

    Interactioni

    Subunit structurei

    Interacts with sad1.1 Publication

    Protein-protein interaction databases

    BioGridi279766. 6 interactions.
    IntActiP78820. 1 interaction.
    MINTiMINT-4691347.
    STRINGi4896.SPAC56E4.04c-1.

    Structurei

    3D structure databases

    ProteinModelPortaliP78820.
    SMRiP78820. Positions 41-559, 699-793, 1520-2261.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini68 – 577510Biotin carboxylationAdd
    BLAST
    Domaini226 – 418193ATP-graspPROSITE-ProRule annotationAdd
    BLAST
    Domaini711 – 77767Biotinyl-bindingAdd
    BLAST
    Domaini1644 – 2141498CarboxyltransferaseAdd
    BLAST

    Sequence similaritiesi

    Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
    Contains 1 biotin carboxylation domain.Curated
    Contains 1 biotinyl-binding domain.Curated
    Contains 1 carboxyltransferase domain.Curated

    Phylogenomic databases

    eggNOGiCOG0511.
    HOGENOMiHOG000214115.
    KOiK11262.
    OMAiVEEPRYR.
    OrthoDBiEOG74J9H5.
    PhylomeDBiP78820.

    Family and domain databases

    Gene3Di3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    3.90.226.10. 3 hits.
    InterProiIPR013537. AcCoA_COase_cen.
    IPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR001882. Biotin_BS.
    IPR011764. Biotin_carboxylation_dom.
    IPR005482. Biotin_COase_C.
    IPR000089. Biotin_lipoyl.
    IPR005481. CarbamoylP_synth_lsu_N.
    IPR000022. Carboxyl_trans.
    IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
    IPR029045. ClpP/crotonase-like_dom.
    IPR011763. COA_CT_C.
    IPR011762. COA_CT_N.
    IPR016185. PreATP-grasp_dom.
    IPR011054. Rudment_hybrid_motif.
    IPR011053. Single_hybrid_motif.
    [Graphical view]
    PfamiPF08326. ACC_central. 1 hit.
    PF02785. Biotin_carb_C. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF01039. Carboxyl_trans. 1 hit.
    PF00289. CPSase_L_chain. 1 hit.
    PF02786. CPSase_L_D2. 1 hit.
    [Graphical view]
    SMARTiSM00878. Biotin_carb_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF51230. SSF51230. 1 hit.
    SSF51246. SSF51246. 1 hit.
    SSF52096. SSF52096. 2 hits.
    SSF52440. SSF52440. 1 hit.
    PROSITEiPS50975. ATP_GRASP. 1 hit.
    PS50979. BC. 1 hit.
    PS00188. BIOTIN. 1 hit.
    PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS50989. COA_CT_CTER. 1 hit.
    PS50980. COA_CT_NTER. 1 hit.
    PS00866. CPSASE_1. 1 hit.
    PS00867. CPSASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P78820-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRQSVTSSSS CSKLYAIKAT ISLPRLFYRR LRTMAPRVAS HFLGGNSLDK     50
    APAGKVKDYI ASHGGHTVIT SILIANNGIA AVKEIRSIRK WAYETFNNER 100
    AIKFTVMATP DDLKVNADYI RMADQYVEVP GGSNNNNYAN VELIVDIAER 150
    MNVHAVWAGW GHASENPKLP EMLSASSKKI VFIGPPGSAM RSLGDKISST 200
    IVAQSARVPC MSWSGNELDQ VRIDEETNIV TVDDDVYQKA CIRSAEEGIA 250
    VAEKIGYPVM IKASEGGGGK GIRQVTSTEK FAQAFQQVLD ELPGSPVFVM 300
    KLAGQARHLE VQILADQYGN NISLFGRDCS VQRRHQKIIE EAPVTIAPAA 350
    TFHEMERAAV RLGELVGYAS AGTIEYLYEP ENDRFYFLEL NPRLQVEHPT 400
    TEMVSGVNLP AAQLQVAMGL PLSRIPHIRE LYGLPRDGDS EIDFFFQNPE 450
    SFKVQKVPTP KGHCVACRIT SEDPGEGFKP SSGMIKDLNF RSSSNVWGYF 500
    SVGTAGGIHE FADSQFGHIF SFAESRESSR KSMVVALKEL SIRGDFRTTV 550
    EYLVRLLETK EFSENEFTTG WLDRLIAQKV TSARPDKMLA VVCGALVRAH 600
    ATADTQYRAF KSYLERGQVP SREFLKNVYD IEFIYDNTRY RFTASRSSPG 650
    SYHLFLNGSR CTAGVRSLTD GGLLVLLNGH SYTVYYRDEV TGTRISIDNL 700
    SCMLEQENDP TQLRTPSPGK LVRFLVETGE HIKAGEAYAE VEVMKMIMPL 750
    VATEDGVVQL IKQPGASLDA GDILGILTLD DPSRVTHALP FDGQLPNWGE 800
    PQIAGNKPCQ RYHALLCILL DILKGYDNQI ILNSTYNEFV EVLRNHELPY 850
    SEWSAHYSAL VNRISPVLDK LFVSIIEKAR SRKAEFPAKQ LEVAIQTYCD 900
    GQNLATTQQL KVQIAPLLKI ISDYKDGLKV HEYNVIKGLL EEYYNVEKLF 950
    SGINKREEDV ILRLRDENKD DVDKVIALAL SHSRIGSKNN LLITILDLMK 1000
    SEPSTFVSLY FNDILRKLTD LDSRVTSKVS LKARELLITC AMPSLNERFS 1050
    QMEHILKSSV VESHYGDAKF SHRTPSLDIL KELIDSKYTV FDVLPAFFCH 1100
    TDPWVSLAAL EVYVRRAYRA YSVLEINYHT EAGTPYVLTW RFQLHSSGAP 1150
    GLGANSTNGS NFPASTTPSY ENSNRRLQSV SDLSWYVNKT DSEPFRFGTM 1200
    IAAETFDELE NNLALAIDRL PLSRNYFNAG LTLDGNSSSA NDNTQELTNV 1250
    VNVALTSTGD LDDSAIVSKL NQILSDFRDD LLEHNVRRVT IVGGRINKSA 1300
    YPSYYTYRVS AEQKDGNLVH YNEDERIRHI EPALAFQLEL GRLSNFNIEP 1350
    VFTDNHNIHV YRATAKNMDT DKRFFTRALV RPGRLRDEIP TAEYLISETH 1400
    RLINDILDAL EVIGHEQTDL NHIFINFTPA FGLAPKQVEA ALGGFLERFG 1450
    RRLWRLRVTA AEIRIICTDP STNTLFPLRV IISNVSGFVV NVEIYAEVKT 1500
    ENNSWIFKSI GQPGSMHLRP ISTPYPTKEW LQPRRYKAQL MGTTFVYDFP 1550
    ELFRRAFTDS WKKVPNGRSK VTIPQNMFEC KELVADEHGV LQEVNREPGT 1600
    NSCGMVAWCI TVKTPEYPNG RKIIVVANDI TFQIGSFGPQ EDEYFYKVTQ 1650
    LARQRGIPRI YLAANSGARI GVADEIVPLF NIAWVDPDSP EKGFDYIYLT 1700
    PEAYERLQKE NPNILTTEEV VTETGELRHK ITTIIGSSEG LGVECLRGSG 1750
    LIAGVTSRAY NDIFTCTLVT CRAVGIGAYL VRLGQRAVQI EGQPIILTGA 1800
    PALNKVLGRE VYTSNLQLGG TQVMHRNGIS HLTSQDDFDG ISKIVNWISY 1850
    IPDKRNNPVP ISPSSDTWDR DVEFYPSQNG YDPRWLIAGK EDEDSFLYGL 1900
    FDKGSFQETL NGWAKTVVVG RARMGGIPTG VIAVETRTIE NTVPADPANP 1950
    DSTEQVLMEA GQVWYPNSAF KTAQAINDFN HGEQLPLFIL ANWRGFSGGQ 2000
    RDMFNEVLKY GSYIVDALAS YKQPVFVYIP PFSELRGGSW VVVDPTINED 2050
    QMEMYADEES RAGVLEPEGM VSIKFRREKL LSLMRRCDHK YASLCNELKR 2100
    DDLSADDLST IKVKLMEREQ KLMPIYQQIS IHFADLHDRV GRMVAKKVVR 2150
    KPLKWTEARR FFYWRLRRRL NEHYALQKIT QLIPSLTIRE SREYLQKWYE 2200
    EWCGKQDWDE SDKSVVCWIE EHNDDLSKRT QELKSTYYSE RLSKLLRSDR 2250
    KGMIDSLAQV LTELDENEKK ELAGKLASVN 2280
    Length:2,280
    Mass (Da):256,843
    Last modified:January 11, 2001 - v2
    Checksum:i8262C9A1A5C8E891
    GO

    Sequence cautioni

    The sequence BAA11916.1 differs from that shown. Reason: Frameshift at position 1511.
    The sequence BAA11917.1 differs from that shown. Reason: Frameshift at position 1005.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 4229LYAIK…VASHF → RFIFIDVLLISQLSISSFSF FILYFINHI in BAA11914. (PubMed:8769419)CuratedAdd
    BLAST
    Sequence conflicti258 – 2581P → S in BAA11238. 1 PublicationCurated
    Sequence conflicti339 – 3402IE → L in BAA11238. 1 PublicationCurated
    Sequence conflicti512 – 5121A → S in BAA11238. 1 PublicationCurated
    Sequence conflicti523 – 5231A → T in BAA11238. 1 PublicationCurated
    Sequence conflicti636 – 6394DNTR → YRIP in BAA11915. (PubMed:8769419)Curated
    Sequence conflicti1017 – 10171K → N in BAA11917. (PubMed:8769419)Curated
    Sequence conflicti1073 – 10731R → H in BAA11917. (PubMed:8769419)Curated
    Sequence conflicti1098 – 10981F → L in BAA11917. (PubMed:8769419)Curated
    Sequence conflicti1105 – 11051V → Y in BAA11238. 1 PublicationCurated
    Sequence conflicti1362 – 13621R → S in BAA11238. 1 PublicationCurated
    Sequence conflicti1427 – 14271F → Y in BAA11916. (PubMed:8769419)Curated
    Sequence conflicti1444 – 14441G → E in BAA11238. 1 PublicationCurated
    Sequence conflicti1445 – 14451F → C in BAA11916. (PubMed:8769419)Curated
    Sequence conflicti1449 – 14491F → L in BAA11916. (PubMed:8769419)Curated
    Sequence conflicti1451 – 14511R → S in BAA11238. 1 PublicationCurated
    Sequence conflicti1465 – 14651I → F in BAA11916. (PubMed:8769419)Curated
    Sequence conflicti1480 – 14801V → L in BAA11916. (PubMed:8769419)Curated
    Sequence conflicti1485 – 14851V → L in BAA11916. (PubMed:8769419)Curated
    Sequence conflicti1496 – 14961A → S in BAA11238. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D78169 Genomic DNA. Translation: BAA11238.1.
    CU329670 Genomic DNA. Translation: CAB16395.1.
    D83413 Genomic DNA. Translation: BAA11914.1.
    D83414 Genomic DNA. Translation: BAA11915.1.
    D83416 Genomic DNA. Translation: BAA11917.1. Frameshift.
    D83415 Genomic DNA. Translation: BAA11916.1. Frameshift.
    PIRiT38906.
    T42531.
    RefSeqiNP_593271.1. NM_001018668.2.

    Genome annotation databases

    EnsemblFungiiSPAC56E4.04c.1; SPAC56E4.04c.1:pep; SPAC56E4.04c.
    GeneIDi2543344.
    KEGGispo:SPAC56E4.04c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D78169 Genomic DNA. Translation: BAA11238.1 .
    CU329670 Genomic DNA. Translation: CAB16395.1 .
    D83413 Genomic DNA. Translation: BAA11914.1 .
    D83414 Genomic DNA. Translation: BAA11915.1 .
    D83416 Genomic DNA. Translation: BAA11917.1 . Frameshift.
    D83415 Genomic DNA. Translation: BAA11916.1 . Frameshift.
    PIRi T38906.
    T42531.
    RefSeqi NP_593271.1. NM_001018668.2.

    3D structure databases

    ProteinModelPortali P78820.
    SMRi P78820. Positions 41-559, 699-793, 1520-2261.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 279766. 6 interactions.
    IntActi P78820. 1 interaction.
    MINTi MINT-4691347.
    STRINGi 4896.SPAC56E4.04c-1.

    Proteomic databases

    MaxQBi P78820.
    PaxDbi P78820.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPAC56E4.04c.1 ; SPAC56E4.04c.1:pep ; SPAC56E4.04c .
    GeneIDi 2543344.
    KEGGi spo:SPAC56E4.04c.

    Organism-specific databases

    PomBasei SPAC56E4.04c.

    Phylogenomic databases

    eggNOGi COG0511.
    HOGENOMi HOG000214115.
    KOi K11262.
    OMAi VEEPRYR.
    OrthoDBi EOG74J9H5.
    PhylomeDBi P78820.

    Enzyme and pathway databases

    UniPathwayi UPA00655 ; UER00711 .
    Reactomei REACT_188246. Biotin transport and metabolism.
    REACT_193506. Defective HLCS causes multiple carboxylase deficiency.
    REACT_210492. Import of palmitoyl-CoA into the mitochondrial matrix.
    REACT_218197. Fatty Acyl-CoA Biosynthesis.

    Miscellaneous databases

    NextBioi 20804359.

    Family and domain databases

    Gene3Di 3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    3.90.226.10. 3 hits.
    InterProi IPR013537. AcCoA_COase_cen.
    IPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR001882. Biotin_BS.
    IPR011764. Biotin_carboxylation_dom.
    IPR005482. Biotin_COase_C.
    IPR000089. Biotin_lipoyl.
    IPR005481. CarbamoylP_synth_lsu_N.
    IPR000022. Carboxyl_trans.
    IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
    IPR029045. ClpP/crotonase-like_dom.
    IPR011763. COA_CT_C.
    IPR011762. COA_CT_N.
    IPR016185. PreATP-grasp_dom.
    IPR011054. Rudment_hybrid_motif.
    IPR011053. Single_hybrid_motif.
    [Graphical view ]
    Pfami PF08326. ACC_central. 1 hit.
    PF02785. Biotin_carb_C. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF01039. Carboxyl_trans. 1 hit.
    PF00289. CPSase_L_chain. 1 hit.
    PF02786. CPSase_L_D2. 1 hit.
    [Graphical view ]
    SMARTi SM00878. Biotin_carb_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51230. SSF51230. 1 hit.
    SSF51246. SSF51246. 1 hit.
    SSF52096. SSF52096. 2 hits.
    SSF52440. SSF52440. 1 hit.
    PROSITEi PS50975. ATP_GRASP. 1 hit.
    PS50979. BC. 1 hit.
    PS00188. BIOTIN. 1 hit.
    PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS50989. COA_CT_CTER. 1 hit.
    PS50980. COA_CT_NTER. 1 hit.
    PS00866. CPSASE_1. 1 hit.
    PS00867. CPSASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Biotin-dependent enzymes in Schizosaccharomyces pombe: cloning and nucleotide sequences of acetyl-CoA carboxylase and pyruvate carboxylase."
      Saito A., Kazuta Y., Toh H., Kondo H., Tanabe T.
      Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 972 / HM123.
    2. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    3. "Aberrant mitosis in fission yeast mutants defective in fatty acid synthetase and acetyl CoA carboxylase."
      Saitoh S., Takahashi K., Nabeshima K., Yamashita Y., Nakaseko Y., Hirata A., Yanagida M.
      J. Cell Biol. 134:949-961(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-161; 636-871; 998-1098 AND 1380-1547.
    4. "Two-hybrid search for proteins that interact with Sad1 and Kms1, two membrane-bound components of the spindle pole body in fission yeast."
      Miki F., Kurabayashi A., Tange Y., Okazaki K., Shimanuki M., Niwa O.
      Mol. Genet. Genomics 270:449-461(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SAD1.
    5. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
      Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
      Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1179 AND SER-1181, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiACAC_SCHPO
    AccessioniPrimary (citable) accession number: P78820
    Secondary accession number(s): O94557
    , Q09447, Q09576, Q09616, Q09667
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 11, 2001
    Last modified: October 1, 2014
    This is version 135 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3