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P78820

- ACAC_SCHPO

UniProt

P78820 - ACAC_SCHPO

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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

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

Protein has several cofactor binding sites:
  • biotinBy similarityNote: Biotin.By similarity
  • Mn2+By similarityNote: 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
Complete GO annotation...

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.
REACT_229743. ChREBP activates metabolic gene expression.
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
Complete GO annotation...

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 similarityPROSITE-ProRule annotation
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. 4 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
Domaini704 – 77875Biotinyl-bindingPROSITE-ProRule annotationAdd
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.CuratedPROSITE-ProRule annotation
Contains 1 carboxyltransferase domain.Curated

Phylogenomic databases

eggNOGiCOG0511.
HOGENOMiHOG000214115.
InParanoidiP78820.
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

        10         20         30         40         50
MRQSVTSSSS CSKLYAIKAT ISLPRLFYRR LRTMAPRVAS HFLGGNSLDK
60 70 80 90 100
APAGKVKDYI ASHGGHTVIT SILIANNGIA AVKEIRSIRK WAYETFNNER
110 120 130 140 150
AIKFTVMATP DDLKVNADYI RMADQYVEVP GGSNNNNYAN VELIVDIAER
160 170 180 190 200
MNVHAVWAGW GHASENPKLP EMLSASSKKI VFIGPPGSAM RSLGDKISST
210 220 230 240 250
IVAQSARVPC MSWSGNELDQ VRIDEETNIV TVDDDVYQKA CIRSAEEGIA
260 270 280 290 300
VAEKIGYPVM IKASEGGGGK GIRQVTSTEK FAQAFQQVLD ELPGSPVFVM
310 320 330 340 350
KLAGQARHLE VQILADQYGN NISLFGRDCS VQRRHQKIIE EAPVTIAPAA
360 370 380 390 400
TFHEMERAAV RLGELVGYAS AGTIEYLYEP ENDRFYFLEL NPRLQVEHPT
410 420 430 440 450
TEMVSGVNLP AAQLQVAMGL PLSRIPHIRE LYGLPRDGDS EIDFFFQNPE
460 470 480 490 500
SFKVQKVPTP KGHCVACRIT SEDPGEGFKP SSGMIKDLNF RSSSNVWGYF
510 520 530 540 550
SVGTAGGIHE FADSQFGHIF SFAESRESSR KSMVVALKEL SIRGDFRTTV
560 570 580 590 600
EYLVRLLETK EFSENEFTTG WLDRLIAQKV TSARPDKMLA VVCGALVRAH
610 620 630 640 650
ATADTQYRAF KSYLERGQVP SREFLKNVYD IEFIYDNTRY RFTASRSSPG
660 670 680 690 700
SYHLFLNGSR CTAGVRSLTD GGLLVLLNGH SYTVYYRDEV TGTRISIDNL
710 720 730 740 750
SCMLEQENDP TQLRTPSPGK LVRFLVETGE HIKAGEAYAE VEVMKMIMPL
760 770 780 790 800
VATEDGVVQL IKQPGASLDA GDILGILTLD DPSRVTHALP FDGQLPNWGE
810 820 830 840 850
PQIAGNKPCQ RYHALLCILL DILKGYDNQI ILNSTYNEFV EVLRNHELPY
860 870 880 890 900
SEWSAHYSAL VNRISPVLDK LFVSIIEKAR SRKAEFPAKQ LEVAIQTYCD
910 920 930 940 950
GQNLATTQQL KVQIAPLLKI ISDYKDGLKV HEYNVIKGLL EEYYNVEKLF
960 970 980 990 1000
SGINKREEDV ILRLRDENKD DVDKVIALAL SHSRIGSKNN LLITILDLMK
1010 1020 1030 1040 1050
SEPSTFVSLY FNDILRKLTD LDSRVTSKVS LKARELLITC AMPSLNERFS
1060 1070 1080 1090 1100
QMEHILKSSV VESHYGDAKF SHRTPSLDIL KELIDSKYTV FDVLPAFFCH
1110 1120 1130 1140 1150
TDPWVSLAAL EVYVRRAYRA YSVLEINYHT EAGTPYVLTW RFQLHSSGAP
1160 1170 1180 1190 1200
GLGANSTNGS NFPASTTPSY ENSNRRLQSV SDLSWYVNKT DSEPFRFGTM
1210 1220 1230 1240 1250
IAAETFDELE NNLALAIDRL PLSRNYFNAG LTLDGNSSSA NDNTQELTNV
1260 1270 1280 1290 1300
VNVALTSTGD LDDSAIVSKL NQILSDFRDD LLEHNVRRVT IVGGRINKSA
1310 1320 1330 1340 1350
YPSYYTYRVS AEQKDGNLVH YNEDERIRHI EPALAFQLEL GRLSNFNIEP
1360 1370 1380 1390 1400
VFTDNHNIHV YRATAKNMDT DKRFFTRALV RPGRLRDEIP TAEYLISETH
1410 1420 1430 1440 1450
RLINDILDAL EVIGHEQTDL NHIFINFTPA FGLAPKQVEA ALGGFLERFG
1460 1470 1480 1490 1500
RRLWRLRVTA AEIRIICTDP STNTLFPLRV IISNVSGFVV NVEIYAEVKT
1510 1520 1530 1540 1550
ENNSWIFKSI GQPGSMHLRP ISTPYPTKEW LQPRRYKAQL MGTTFVYDFP
1560 1570 1580 1590 1600
ELFRRAFTDS WKKVPNGRSK VTIPQNMFEC KELVADEHGV LQEVNREPGT
1610 1620 1630 1640 1650
NSCGMVAWCI TVKTPEYPNG RKIIVVANDI TFQIGSFGPQ EDEYFYKVTQ
1660 1670 1680 1690 1700
LARQRGIPRI YLAANSGARI GVADEIVPLF NIAWVDPDSP EKGFDYIYLT
1710 1720 1730 1740 1750
PEAYERLQKE NPNILTTEEV VTETGELRHK ITTIIGSSEG LGVECLRGSG
1760 1770 1780 1790 1800
LIAGVTSRAY NDIFTCTLVT CRAVGIGAYL VRLGQRAVQI EGQPIILTGA
1810 1820 1830 1840 1850
PALNKVLGRE VYTSNLQLGG TQVMHRNGIS HLTSQDDFDG ISKIVNWISY
1860 1870 1880 1890 1900
IPDKRNNPVP ISPSSDTWDR DVEFYPSQNG YDPRWLIAGK EDEDSFLYGL
1910 1920 1930 1940 1950
FDKGSFQETL NGWAKTVVVG RARMGGIPTG VIAVETRTIE NTVPADPANP
1960 1970 1980 1990 2000
DSTEQVLMEA GQVWYPNSAF KTAQAINDFN HGEQLPLFIL ANWRGFSGGQ
2010 2020 2030 2040 2050
RDMFNEVLKY GSYIVDALAS YKQPVFVYIP PFSELRGGSW VVVDPTINED
2060 2070 2080 2090 2100
QMEMYADEES RAGVLEPEGM VSIKFRREKL LSLMRRCDHK YASLCNELKR
2110 2120 2130 2140 2150
DDLSADDLST IKVKLMEREQ KLMPIYQQIS IHFADLHDRV GRMVAKKVVR
2160 2170 2180 2190 2200
KPLKWTEARR FFYWRLRRRL NEHYALQKIT QLIPSLTIRE SREYLQKWYE
2210 2220 2230 2240 2250
EWCGKQDWDE SDKSVVCWIE EHNDDLSKRT QELKSTYYSE RLSKLLRSDR
2260 2270 2280
KGMIDSLAQV LTELDENEKK ELAGKLASVN
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. Curated
The sequence BAA11917.1 differs from that shown. Reason: Frameshift at position 1005. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 4 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.
InParanoidi P78820.
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.
REACT_229743. ChREBP activates metabolic gene expression.

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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 137 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