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P78820

- ACAC_SCHPO

UniProt

P78820 - ACAC_SCHPO

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Protein

Acetyl-CoA carboxylase

Gene
cut6, SPAC56E4.04c
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

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 1 By similarity
Metal bindingi389 – 3891Manganese 1 By similarity
Metal bindingi389 – 3891Manganese 2 By similarity
Metal bindingi391 – 3911Manganese 2 By similarity
Active sitei393 – 3931 By similarity
Binding sitei1772 – 17721Coenzyme A By similarity
Binding sitei2074 – 20741Coenzyme A By similarity
Binding sitei2076 – 20761Coenzyme A By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi266 – 2716ATP By similarity

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
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.
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-biotinyllysine By 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.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 1 ATP-grasp domain.

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.

Sequence conflict

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

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

« 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: September 3, 2014
This is version 134 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

Similar proteinsi