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Q13085

- ACACA_HUMAN

UniProt

Q13085 - ACACA_HUMAN

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Protein

Acetyl-CoA carboxylase 1

Gene

ACACA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.1 Publication

Catalytic activityi

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.1 Publication
ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].1 Publication

Cofactori

Biotin.
Binds 2 manganese ions per subunit.

Enzyme regulationi

By phosphorylation (By similarity). Activity is increased by oligomerization. Citrate and MID1IP1 promote oligomerization.By similarity1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi424 – 4241Manganese 1By similarity
Metal bindingi437 – 4371Manganese 1By similarity
Metal bindingi437 – 4371Manganese 2By similarity
Metal bindingi439 – 4391Manganese 2By similarity
Active sitei441 – 4411By similarity
Binding sitei1823 – 18231Coenzyme ABy similarity
Binding sitei2127 – 21271Coenzyme ABy similarity
Binding sitei2129 – 21291Coenzyme ABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi315 – 3206ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. acetyl-CoA metabolic process Source: UniProtKB
  2. biotin metabolic process Source: Reactome
  3. carnitine shuttle Source: Reactome
  4. cellular lipid metabolic process Source: Reactome
  5. energy reserve metabolic process Source: Reactome
  6. fatty acid biosynthetic process Source: UniProtKB
  7. lipid homeostasis Source: Ensembl
  8. long-chain fatty-acyl-CoA biosynthetic process Source: Reactome
  9. malonyl-CoA biosynthetic process Source: UniProtKB-UniPathway
  10. multicellular organismal protein metabolic process Source: Ensembl
  11. positive regulation of cellular metabolic process Source: Reactome
  12. protein homotetramerization Source: UniProtKB
  13. small molecule metabolic process Source: Reactome
  14. tissue homeostasis Source: Ensembl
  15. triglyceride biosynthetic process Source: Reactome
  16. vitamin metabolic process Source: Reactome
  17. water-soluble vitamin metabolic process Source: Reactome
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

BRENDAi6.4.1.2. 2681.
ReactomeiREACT_11082. Import of palmitoyl-CoA into the mitochondrial matrix.
REACT_11153. Biotin transport and metabolism.
REACT_1319. Fatty Acyl-CoA Biosynthesis.
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_169312. Defective HLCS causes multiple carboxylase deficiency.
REACT_2122. ChREBP activates metabolic gene expression.
SABIO-RKQ13085.
UniPathwayiUPA00655; UER00711.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA carboxylase 1 (EC:6.4.1.2)
Short name:
ACC1
Alternative name(s):
ACC-alpha
Including the following 1 domains:
Biotin carboxylase (EC:6.3.4.14)
Gene namesi
Name:ACACA
Synonyms:ACAC, ACC1, ACCA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:84. ACACA.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
  3. mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Acetyl-CoA carboxylase 1 deficiency (ACACAD) [MIM:613933]: An inborn error of de novo fatty acid synthesis associated with severe brain damage, persistent myopathy and poor growth.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi78 – 781S → A: No effect on interaction with BRCA1. 1 Publication
Mutagenesisi344 – 3441S → A: No effect on interaction with BRCA1. 1 Publication
Mutagenesisi432 – 4321S → A: No effect on interaction with BRCA1. 1 Publication
Mutagenesisi1201 – 12011S → A: No effect on interaction with BRCA1. 1 Publication
Mutagenesisi1263 – 12631S → A: Abolishes interaction with BRCA1. 1 Publication
Mutagenesisi1585 – 15851S → A: No effect on interaction with BRCA1. 1 Publication
Mutagenesisi1952 – 19521S → A: No effect on interaction with BRCA1. 1 Publication
Mutagenesisi2211 – 22111S → A: No effect on interaction with BRCA1. 1 Publication

Organism-specific databases

MIMi613933. phenotype.
PharmGKBiPA24421.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 23462346Acetyl-CoA carboxylase 1PRO_0000146764Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications
Modified residuei5 – 51Phosphoserine2 Publications
Modified residuei23 – 231Phosphoserine3 Publications
Modified residuei25 – 251Phosphoserine2 Publications
Modified residuei29 – 291Phosphoserine7 Publications
Modified residuei53 – 531Phosphoserine1 Publication
Modified residuei78 – 781PhosphoserineBy similarity
Modified residuei80 – 801Phosphoserine4 Publications
Modified residuei488 – 4881Phosphoserine1 Publication
Modified residuei786 – 7861N6-biotinyllysineBy similarity
Modified residuei1201 – 12011PhosphoserineBy similarity
Modified residuei1216 – 12161PhosphoserineBy similarity
Modified residuei1263 – 12631Phosphoserine1 Publication
Modified residuei1334 – 13341N6-acetyllysine1 Publication

Post-translational modificationi

Phosphorylation on Ser-1263 is required for interaction with BRCA1.10 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ13085.
PaxDbiQ13085.
PRIDEiQ13085.

PTM databases

PhosphoSiteiQ13085.

Expressioni

Tissue specificityi

Expressed in brain, placental, skeletal muscle, renal, pancreatic and adipose tissues; expressed at low level in pulmonary tissue; not detected in the liver.

Gene expression databases

BgeeiQ13085.
ExpressionAtlasiQ13085. differential.
GenevestigatoriQ13085.

Organism-specific databases

HPAiCAB013715.

Interactioni

Subunit structurei

Monomer, homodimer, and homotetramer. Can form filamentous polymers. Interacts in its inactive phosphorylated form with the BRCT domains of BRCA1 which prevents ACACA dephosphorylation and inhibits lipid synthesis. Interacts with MID1IP1; interaction with MID1IP1 promotes oligomerization and increases its activity.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AKR1B10O602184EBI-717681,EBI-1572139
BRCA1P383982EBI-717681,EBI-349905
SIRT1Q96EB63EBI-717681,EBI-1802965

Protein-protein interaction databases

BioGridi106549. 55 interactions.
DIPiDIP-36122N.
IntActiQ13085. 26 interactions.
MINTiMINT-1415014.

Structurei

Secondary structure

1
2346
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi105 – 1117
Beta strandi120 – 1234
Helixi127 – 14519
Beta strandi150 – 1578
Helixi159 – 1635
Helixi168 – 1714
Beta strandi172 – 1776
Helixi183 – 1853
Turni186 – 1883
Helixi190 – 19910
Beta strandi203 – 2064
Turni211 – 2144
Helixi217 – 2248
Beta strandi228 – 2314
Helixi234 – 2418
Helixi243 – 25210
Turni261 – 2644
Helixi283 – 2897
Helixi294 – 30411
Beta strandi306 – 3127
Beta strandi320 – 3245
Turni327 – 3293
Helixi330 – 34011
Beta strandi346 – 3505
Beta strandi356 – 3649
Beta strandi370 – 38213
Beta strandi385 – 3928
Helixi398 – 41518
Beta strandi419 – 4279
Beta strandi433 – 4397
Turni444 – 4463
Helixi447 – 4537
Helixi457 – 4659
Helixi470 – 4723
Helixi474 – 4796
Turni492 – 4954
Beta strandi496 – 4983
Beta strandi503 – 5108
Beta strandi526 – 5305
Beta strandi537 – 5426
Beta strandi557 – 56610
Helixi567 – 58216
Helixi589 – 59911
Helixi601 – 6044
Helixi612 – 6165
Helixi1582 – 159211
Helixi1598 – 16003
Helixi1601 – 161919
Helixi1628 – 16314
Beta strandi1632 – 16398
Beta strandi1645 – 16484
Beta strandi1656 – 166611
Beta strandi1675 – 16828
Helixi1687 – 16893
Helixi1693 – 170917
Beta strandi1713 – 17175
Helixi1728 – 17314
Beta strandi1735 – 17395
Helixi1744 – 17463
Beta strandi1748 – 17536
Helixi1755 – 17617
Helixi1762 – 17643
Beta strandi1767 – 17748
Beta strandi1777 – 17859
Helixi1795 – 181319
Beta strandi1816 – 18205
Beta strandi1822 – 18254
Helixi1827 – 18348
Beta strandi1837 – 18415
Beta strandi1845 – 18495
Helixi1851 – 18588
Helixi1866 – 18705
Helixi1872 – 18754
Turni1876 – 18794
Beta strandi1882 – 18876
Helixi1888 – 189912
Beta strandi1914 – 19174
Helixi1934 – 19396
Beta strandi1944 – 19463
Beta strandi1961 – 19644
Beta strandi1971 – 19788
Beta strandi1981 – 19888
Beta strandi1993 – 19964
Beta strandi2010 – 20134
Helixi2020 – 203617
Beta strandi2040 – 20434
Helixi2053 – 20575
Helixi2060 – 207213
Beta strandi2078 – 20825
Beta strandi2087 – 20893
Helixi2090 – 20945
Helixi2098 – 21003
Turni2102 – 21043
Beta strandi2105 – 21106
Beta strandi2114 – 21185
Helixi2120 – 21278
Helixi2130 – 214011
Helixi2142 – 21509
Helixi2158 – 218831
Helixi2193 – 21986
Beta strandi2201 – 22066
Helixi2208 – 22103
Helixi2211 – 223525
Helixi2241 – 225616
Helixi2258 – 22658
Helixi2267 – 227812
Helixi2289 – 231022
Helixi2312 – 23143
Helixi2315 – 23228
Helixi2323 – 23253
Helixi2328 – 233710

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YL2X-ray2.30A/B78-617[»]
3COJX-ray3.21H/I/J/K/L/M/N/O1258-1270[»]
4ASIX-ray2.80A/B/C/D/E/F1571-2338[»]
ProteinModelPortaliQ13085.
SMRiQ13085. Positions 102-817, 1581-2338.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13085.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini117 – 618502Biotin carboxylationAdd
BLAST
Domaini275 – 466192ATP-graspPROSITE-ProRule annotationAdd
BLAST
Domaini752 – 81867Biotinyl-bindingAdd
BLAST
Domaini1698 – 2194497CarboxyltransferaseAdd
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.
GeneTreeiENSGT00550000074703.
HOVERGENiHBG005371.
InParanoidiQ13085.
KOiK11262.
OMAiHVFSGQC.
OrthoDBiEOG7HXCPW.
PhylomeDBiQ13085.
TreeFamiTF300061.

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]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative promoter usage. Align

Isoform 1 (identifier: Q13085-1) [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
MDEPSPLAQP LELNQHSRFI IGSVSEDNSE DEISNLVKLD LLEEKEGSLS
60 70 80 90 100
PASVGSDTLS DLGISSLQDG LALHIRSSMS GLHLVKQGRD RKKIDSQRDF
110 120 130 140 150
TVASPAEFVT RFGGNKVIEK VLIANNGIAA VKCMRSIRRW SYEMFRNERA
160 170 180 190 200
IRFVVMVTPE DLKANAEYIK MADHYVPVPG GPNNNNYANV ELILDIAKRI
210 220 230 240 250
PVQAVWAGWG HASENPKLPE LLLKNGIAFM GPPSQAMWAL GDKIASSIVA
260 270 280 290 300
QTAGIPTLPW SGSGLRVDWQ ENDFSKRILN VPQELYEKGY VKDVDDGLQA
310 320 330 340 350
AEEVGYPVMI KASEGGGGKG IRKVNNADDF PNLFRQVQAE VPGSPIFVMR
360 370 380 390 400
LAKQSRHLEV QILADQYGNA ISLFGRDCSV QRRHQKIIEE APATIATPAV
410 420 430 440 450
FEHMEQCAVK LAKMVGYVSA GTVEYLYSQD GSFYFLELNP RLQVEHPCTE
460 470 480 490 500
MVADVNLPAA QLQIAMGIPL YRIKDIRMMY GVSPWGDSPI DFEDSAHVPC
510 520 530 540 550
PRGHVIAARI TSENPDEGFK PSSGTVQELN FRSNKNVWGY FSVAAAGGLH
560 570 580 590 600
EFADSQFGHC FSWGENREEA ISNMVVALKE LSIRGDFRTT VEYLIKLLET
610 620 630 640 650
ESFQMNRIDT GWLDRLIAEK VQAERPDTML GVVCGALHVA DVSLRNSVSN
660 670 680 690 700
FLHSLERGQV LPAHTLLNTV DVELIYEGVK YVLKVTRQSP NSYVVIMNGS
710 720 730 740 750
CVEVDVHRLS DGGLLLSYDG SSYTTYMKEE VDRYRITIGN KTCVFEKEND
760 770 780 790 800
PSVMRSPSAG KLIQYIVEDG GHVFAGQCYA EIEVMKMVMT LTAVESGCIH
810 820 830 840 850
YVKRPGAALD PGCVLAKMQL DNPSKVQQAE LHTGSLPRIQ STALRGEKLH
860 870 880 890 900
RVFHYVLDNL VNVMNGYCLP DPFFSSKVKD WVERLMKTLR DPSLPLLELQ
910 920 930 940 950
DIMTSVSGRI PPNVEKSIKK EMAQYASNIT SVLCQFPSQQ IANILDSHAA
960 970 980 990 1000
TLNRKSEREV FFMNTQSIVQ LVQRYRSGIR GHMKAVVMDL LRQYLRVETQ
1010 1020 1030 1040 1050
FQNGHYDKCV FALREENKSD MNTVLNYIFS HAQVTKKNLL VTMLIDQLCG
1060 1070 1080 1090 1100
RDPTLTDELL NILTELTQLS KTTNAKVALR ARQVLIASHL PSYELRHNQV
1110 1120 1130 1140 1150
ESIFLSAIDM YGHQFCIENL QKLILSETSI FDVLPNFFYH SNQVVRMAAL
1160 1170 1180 1190 1200
EVYVRRAYIA YELNSVQHRQ LKDNTCVVEF QFMLPTSHPN RGNIPTLNRM
1210 1220 1230 1240 1250
SFSSNLNHYG MTHVASVSDV LLDNSFTPPC QRMGGMVSFR TFEDFVRIFD
1260 1270 1280 1290 1300
EVMGCFSDSP PQSPTFPEAG HTSLYDEDKV PRDEPIHILN VAIKTDCDIE
1310 1320 1330 1340 1350
DDRLAAMFRE FTQQNKATLV DHGIRRLTFL VAQKDFRKQV NYEVDRRFHR
1360 1370 1380 1390 1400
EFPKFFTFRA RDKFEEDRIY RHLEPALAFQ LELNRMRNFD LTAIPCANHK
1410 1420 1430 1440 1450
MHLYLGAAKV EVGTEVTDYR FFVRAIIRHS DLVTKEASFE YLQNEGERLL
1460 1470 1480 1490 1500
LEAMDELEVA FNNTNVRTDC NHIFLNFVPT VIMDPSKIEE SVRSMVMRYG
1510 1520 1530 1540 1550
SRLWKLRVLQ AELKINIRLT PTGKAIPIRL FLTNESGYYL DISLYKEVTD
1560 1570 1580 1590 1600
SRTAQIMFQA YGDKQGPLHG MLINTPYVTK DLLQSKRFQA QSLGTTYIYD
1610 1620 1630 1640 1650
IPEMFRQSLI KLWESMSTQA FLPSPPLPSD MLTYTELVLD DQGQLVHMNR
1660 1670 1680 1690 1700
LPGGNEIGMV AWKMTFKSPE YPEGRDIIVI GNDITYRIGS FGPQEDLLFL
1710 1720 1730 1740 1750
RASELARAEG IPRIYVSANS GARIGLAEEI RHMFHVAWVD PEDPYKGYRY
1760 1770 1780 1790 1800
LYLTPQDYKR VSALNSVHCE HVEDEGESRY KITDIIGKEE GIGPENLRGS
1810 1820 1830 1840 1850
GMIAGESSLA YNEIITISLV TCRAIGIGAY LVRLGQRTIQ VENSHLILTG
1860 1870 1880 1890 1900
AGALNKVLGR EVYTSNNQLG GIQIMHNNGV THCTVCDDFE GVFTVLHWLS
1910 1920 1930 1940 1950
YMPKSVHSSV PLLNSKDPID RIIEFVPTKT PYDPRWMLAG RPHPTQKGQW
1960 1970 1980 1990 2000
LSGFFDYGSF SEIMQPWAQT VVVGRARLGG IPVGVVAVET RTVELSIPAD
2010 2020 2030 2040 2050
PANLDSEAKI IQQAGQVWFP DSAFKTYQAI KDFNREGLPL MVFANWRGFS
2060 2070 2080 2090 2100
GGMKDMYDQV LKFGAYIVDG LRECCQPVLV YIPPQAELRG GSWVVIDSSI
2110 2120 2130 2140 2150
NPRHMEMYAD RESRGSVLEP EGTVEIKFRR KDLVKTMRRV DPVYIHLAER
2160 2170 2180 2190 2200
LGTPELSTAE RKELENKLKE REEFLIPIYH QVAVQFADLH DTPGRMQEKG
2210 2220 2230 2240 2250
VISDILDWKT SRTFFYWRLR RLLLEDLVKK KIHNANPELT DGQIQAMLRR
2260 2270 2280 2290 2300
WFVEVEGTVK AYVWDNNKDL AEWLEKQLTE EDGVHSVIEE NIKCISRDYV
2310 2320 2330 2340
LKQIRSLVQA NPEVAMDSII HMTQHISPTQ RAEVIRILST MDSPST
Length:2,346
Mass (Da):265,554
Last modified:October 31, 2006 - v2
Checksum:iF1F0A518F8824FFC
GO
Isoform 2 (identifier: Q13085-2) [UniParc]FASTAAdd to Basket

Also known as: E5A

The sequence of this isoform differs from the canonical sequence as follows:
     1-75: MDEPSPLAQP...SLQDGLALHI → MEGSPEENKEMRYYMLQ

Show »
Length:2,288
Mass (Da):259,686
Checksum:i4E2C75958216CC8B
GO
Isoform 3 (identifier: Q13085-3) [UniParc]FASTAAdd to Basket

Also known as: E5B

The sequence of this isoform differs from the canonical sequence as follows:
     1-78: Missing.

Show »
Length:2,268
Mass (Da):257,239
Checksum:iC78033F62C492D3E
GO
Isoform 4 (identifier: Q13085-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MWWSTLMSILRARSFWKWISTQTVRIIRAVRAHFGGIM

Show »
Length:2,383
Mass (Da):269,999
Checksum:i1F2B8F96208B9983
GO

Sequence cautioni

The sequence AAP94120.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 661S → A in AAC50139. (PubMed:7732023)Curated
Sequence conflicti79 – 791M → W in AAC50139. (PubMed:7732023)Curated
Sequence conflicti89 – 891R → G in AAC50139. (PubMed:7732023)Curated
Sequence conflicti182 – 1821P → A in AAC50139. (PubMed:7732023)Curated
Sequence conflicti234 – 2341S → N in AAC50139. (PubMed:7732023)Curated
Sequence conflicti299 – 2991Q → K in AAC50139. (PubMed:7732023)Curated
Sequence conflicti303 – 3031E → K in AAC50139. (PubMed:7732023)Curated
Sequence conflicti364 – 3641A → V in AAP94122. (PubMed:12810950)Curated
Sequence conflicti446 – 4461H → Q in AAC50139. (PubMed:7732023)Curated
Sequence conflicti494 – 4941D → N in AAC50139. (PubMed:7732023)Curated
Sequence conflicti554 – 5541D → G in AAC50139. (PubMed:7732023)Curated
Sequence conflicti622 – 6221Q → R in AAC50139. (PubMed:7732023)Curated
Sequence conflicti640 – 6401A → G in AAC50139. (PubMed:7732023)Curated
Sequence conflicti814 – 8141V → I in AAP94122. (PubMed:12810950)Curated
Sequence conflicti1061 – 10611N → S in AAC50139. (PubMed:7732023)Curated
Sequence conflicti1094 – 10952EL → DV in AAC50139. (PubMed:7732023)Curated
Sequence conflicti1225 – 12251S → A in AAC50139. (PubMed:7732023)Curated
Sequence conflicti1257 – 12571S → C in AAC50139. (PubMed:7732023)Curated
Sequence conflicti1297 – 12971C → G in AAC50139. (PubMed:7732023)Curated
Sequence conflicti1320 – 13201V → A in AAC50139. (PubMed:7732023)Curated
Sequence conflicti1444 – 14441N → S in AAC50139. (PubMed:7732023)Curated
Sequence conflicti1474 – 14741F → L in AAC50139. (PubMed:7732023)Curated
Sequence conflicti1665 – 16662TF → SL in AAC50139. (PubMed:7732023)Curated
Sequence conflicti1677 – 16771I → V in AAC50139. (PubMed:7732023)Curated
Sequence conflicti1741 – 17411P → S in AAC50139. (PubMed:7732023)Curated
Sequence conflicti1762 – 17621S → G in AAC50139. (PubMed:7732023)Curated
Sequence conflicti1822 – 18221C → S in AAC50139. (PubMed:7732023)Curated
Sequence conflicti1875 – 18751M → T in AAC50139. (PubMed:7732023)Curated
Sequence conflicti1888 – 18881D → G in AAC50139. (PubMed:7732023)Curated
Sequence conflicti1997 – 19971I → V in AAC50139. (PubMed:7732023)Curated
Sequence conflicti2013 – 20131Q → H in AAC50139. (PubMed:7732023)Curated
Sequence conflicti2058 – 20581D → H in AAC50139. (PubMed:7732023)Curated
Sequence conflicti2075 – 20751C → S in AAC50139. (PubMed:7732023)Curated
Sequence conflicti2098 – 20992SS → PT in AAC50139. (PubMed:7732023)Curated
Sequence conflicti2158 – 21592TA → PT in AAC50139. (PubMed:7732023)Curated
Sequence conflicti2166 – 21661N → S in AAC50139. (PubMed:7732023)Curated
Sequence conflicti2234 – 22341N → S in AAC50139. (PubMed:7732023)Curated
Sequence conflicti2321 – 23211H → R in AAP94122. (PubMed:12810950)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti838 – 8381R → W.
Corresponds to variant rs2287351 [ dbSNP | Ensembl ].
VAR_042941
Natural varianti1687 – 16871R → Q in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036514
Natural varianti2271 – 22711A → V Rare polymorphism; frequency <0.004; may play a role in breast cancer susceptibility. 1 Publication
VAR_028929

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7878Missing in isoform 3. 2 PublicationsVSP_026098Add
BLAST
Alternative sequencei1 – 7575MDEPS…LALHI → MEGSPEENKEMRYYMLQ in isoform 2. 2 PublicationsVSP_026099Add
BLAST
Alternative sequencei1 – 11M → MWWSTLMSILRARSFWKWIS TQTVRIIRAVRAHFGGIM in isoform 4. 2 PublicationsVSP_026100

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U19822 mRNA. Translation: AAC50139.1.
AY315619 mRNA. Translation: AAP94114.1.
AY315620 mRNA. Translation: AAP94115.1.
AY315621 mRNA. Translation: AAP94116.1.
AY315623 mRNA. Translation: AAP94118.1.
AY315625 mRNA. Translation: AAP94120.1. Different initiation.
AY315627 mRNA. Translation: AAP94122.1.
AY237919 mRNA. Translation: AAP69841.1.
BC137287 mRNA. Translation: AAI37288.1.
AJ534888 mRNA. Translation: CAD59556.1.
AJ534889 mRNA. Translation: CAD59557.1.
AJ564444 mRNA. Translation: CAD92089.1.
CCDSiCCDS11317.1. [Q13085-1]
CCDS11318.1. [Q13085-2]
CCDS42302.1. [Q13085-4]
CCDS42303.1. [Q13085-3]
PIRiI38928.
RefSeqiNP_942131.1. NM_198834.2. [Q13085-4]
NP_942133.1. NM_198836.2. [Q13085-1]
NP_942134.1. NM_198837.1. [Q13085-2]
NP_942135.1. NM_198838.1. [Q13085-3]
NP_942136.1. NM_198839.2. [Q13085-1]
UniGeneiHs.160556.

Genome annotation databases

EnsembliENST00000612895; ENSP00000482269; ENSG00000278540. [Q13085-2]
ENST00000614428; ENSP00000478547; ENSG00000278540. [Q13085-1]
ENST00000616317; ENSP00000483300; ENSG00000278540. [Q13085-4]
ENST00000616352; ENSP00000477912; ENSG00000278540.
ENST00000617649; ENSP00000482368; ENSG00000278540. [Q13085-3]
GeneIDi31.
KEGGihsa:31.
UCSCiuc002hnk.3. human. [Q13085-1]
uc002hnl.3. human. [Q13085-2]
uc002hno.3. human. [Q13085-4]

Polymorphism databases

DMDMi118601083.

Keywords - Coding sequence diversityi

Alternative promoter usage, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Acetyl-CoA carboxylase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U19822 mRNA. Translation: AAC50139.1 .
AY315619 mRNA. Translation: AAP94114.1 .
AY315620 mRNA. Translation: AAP94115.1 .
AY315621 mRNA. Translation: AAP94116.1 .
AY315623 mRNA. Translation: AAP94118.1 .
AY315625 mRNA. Translation: AAP94120.1 . Different initiation.
AY315627 mRNA. Translation: AAP94122.1 .
AY237919 mRNA. Translation: AAP69841.1 .
BC137287 mRNA. Translation: AAI37288.1 .
AJ534888 mRNA. Translation: CAD59556.1 .
AJ534889 mRNA. Translation: CAD59557.1 .
AJ564444 mRNA. Translation: CAD92089.1 .
CCDSi CCDS11317.1. [Q13085-1 ]
CCDS11318.1. [Q13085-2 ]
CCDS42302.1. [Q13085-4 ]
CCDS42303.1. [Q13085-3 ]
PIRi I38928.
RefSeqi NP_942131.1. NM_198834.2. [Q13085-4 ]
NP_942133.1. NM_198836.2. [Q13085-1 ]
NP_942134.1. NM_198837.1. [Q13085-2 ]
NP_942135.1. NM_198838.1. [Q13085-3 ]
NP_942136.1. NM_198839.2. [Q13085-1 ]
UniGenei Hs.160556.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YL2 X-ray 2.30 A/B 78-617 [» ]
3COJ X-ray 3.21 H/I/J/K/L/M/N/O 1258-1270 [» ]
4ASI X-ray 2.80 A/B/C/D/E/F 1571-2338 [» ]
ProteinModelPortali Q13085.
SMRi Q13085. Positions 102-817, 1581-2338.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106549. 55 interactions.
DIPi DIP-36122N.
IntActi Q13085. 26 interactions.
MINTi MINT-1415014.

Chemistry

BindingDBi Q13085.
ChEMBLi CHEMBL3351.
DrugBanki DB00121. Biotin.
GuidetoPHARMACOLOGYi 1263.

PTM databases

PhosphoSitei Q13085.

Polymorphism databases

DMDMi 118601083.

Proteomic databases

MaxQBi Q13085.
PaxDbi Q13085.
PRIDEi Q13085.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000612895 ; ENSP00000482269 ; ENSG00000278540 . [Q13085-2 ]
ENST00000614428 ; ENSP00000478547 ; ENSG00000278540 . [Q13085-1 ]
ENST00000616317 ; ENSP00000483300 ; ENSG00000278540 . [Q13085-4 ]
ENST00000616352 ; ENSP00000477912 ; ENSG00000278540 .
ENST00000617649 ; ENSP00000482368 ; ENSG00000278540 . [Q13085-3 ]
GeneIDi 31.
KEGGi hsa:31.
UCSCi uc002hnk.3. human. [Q13085-1 ]
uc002hnl.3. human. [Q13085-2 ]
uc002hno.3. human. [Q13085-4 ]

Organism-specific databases

CTDi 31.
GeneCardsi GC17M035441.
HGNCi HGNC:84. ACACA.
HPAi CAB013715.
MIMi 200350. gene.
613933. phenotype.
neXtProti NX_Q13085.
PharmGKBi PA24421.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0511.
GeneTreei ENSGT00550000074703.
HOVERGENi HBG005371.
InParanoidi Q13085.
KOi K11262.
OMAi HVFSGQC.
OrthoDBi EOG7HXCPW.
PhylomeDBi Q13085.
TreeFami TF300061.

Enzyme and pathway databases

UniPathwayi UPA00655 ; UER00711 .
BRENDAi 6.4.1.2. 2681.
Reactomei REACT_11082. Import of palmitoyl-CoA into the mitochondrial matrix.
REACT_11153. Biotin transport and metabolism.
REACT_1319. Fatty Acyl-CoA Biosynthesis.
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_169312. Defective HLCS causes multiple carboxylase deficiency.
REACT_2122. ChREBP activates metabolic gene expression.
SABIO-RK Q13085.

Miscellaneous databases

ChiTaRSi ACACA. human.
EvolutionaryTracei Q13085.
GeneWikii ACACA.
GenomeRNAii 31.
NextBioi 111.
PROi Q13085.
SOURCEi Search...

Gene expression databases

Bgeei Q13085.
ExpressionAtlasi Q13085. differential.
Genevestigatori Q13085.

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. "Human acetyl-CoA carboxylase: characterization, molecular cloning, and evidence for two isoforms."
    Abu-Elheiga L., Jayakumar A., Baldini A., Chirala S.S., Wakil S.J.
    Proc. Natl. Acad. Sci. U.S.A. 92:4011-4015(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  2. "Human acetyl-CoA carboxylase 1 gene: presence of three promoters and heterogeneity at the 5'-untranslated mRNA region."
    Mao J., Chirala S.S., Wakil S.J.
    Proc. Natl. Acad. Sci. U.S.A. 100:7515-7520(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 1-366 (ISOFORMS 2 AND 3), NUCLEOTIDE SEQUENCE [MRNA] OF 1-120 (ISOFORM 4).
    Tissue: Adipocyte.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-2271.
  4. "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 4).
    Tissue: Brain.
  5. "Characterisation of an N-terminal variant of acetyl-CoA carboxylase-alpha: expression in human tissues and evolutionary aspects."
    Travers M.T., Vallance A.J., Clegg R.A., Thomson R., Price N.T., Barber M.C.
    Biochim. Biophys. Acta 1634:97-106(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-113 (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 1-93 (ISOFORM 3).
    Tissue: Mammary gland and Testis.
  6. "Asymmetric expression of transcripts derived from the shared promoter between the divergently oriented ACACA and TADA2L genes."
    Travers M.T., Cambot M., Kennedy H.T., Lenoir G.M., Barber M.C., Joulin V.
    Genomics 85:71-84(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-47 (ISOFORM 1).
    Tissue: Testis.
  7. Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.
    Submitted (JUL-2007) to UniProtKB
    Tissue: Hepatoma.
  8. "BRCA1 interacts with acetyl-CoA carboxylase through its tandem of BRCT domains."
    Magnard C., Bachelier R., Vincent A., Jaquinod M., Kieffer S., Lenoir G.M., Venezia N.D.
    Oncogene 21:6729-6739(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BRCA1.
  9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "BRCA1 affects lipid synthesis through its interaction with acetyl-CoA carboxylase."
    Moreau K., Dizin E., Ray H., Luquain C., Lefai E., Foufelle F., Billaud M., Lenoir G.M., Venezia N.D.
    J. Biol. Chem. 281:3172-3181(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BRCA1.
  11. "ACCA phosphopeptide recognition by the BRCT repeats of BRCA1."
    Ray H., Moreau K., Dizin E., Callebaut I., Venezia N.D.
    J. Mol. Biol. 359:973-982(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-1263, MUTAGENESIS OF SER-78; SER-344; SER-432; SER-1201; SER-1263; SER-1585; SER-1952 AND SER-2211.
  12. "Acetyl-CoA carboxylase deficiency: an inborn error of de novo fatty acid synthesis."
    Blom W., de Muinck Keizer S.M.P.F., Scholte H.R.
    N. Engl. J. Med. 305:465-466(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN ACACAD.
  13. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25; SER-29 AND SER-80, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5 AND SER-29, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25 AND SER-29, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  19. "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-1334, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ENZYME REGULATION, INTERACTION WITH MID1IP1.
  21. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-23; SER-29 AND SER-80, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-80, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-1687.

Entry informationi

Entry nameiACACA_HUMAN
AccessioniPrimary (citable) accession number: Q13085
Secondary accession number(s): B2RP68
, Q6KEV6, Q6XDA8, Q7Z2G8, Q7Z561, Q7Z563, Q7Z564, Q86WB2, Q86WB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 31, 2006
Last modified: October 29, 2014
This is version 149 of the entry and version 2 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

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3