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)

Q13085

- ACACA_HUMAN

UniProt

Q13085 - ACACA_HUMAN

Protein

Acetyl-CoA carboxylase 1

Gene

ACACA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (31 Oct 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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
    5. protein binding Source: UniProtKB

    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

    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

    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

    ArrayExpressiQ13085.
    BgeeiQ13085.
    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. 49 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.
    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

    MDEPSPLAQP LELNQHSRFI IGSVSEDNSE DEISNLVKLD LLEEKEGSLS     50
    PASVGSDTLS DLGISSLQDG LALHIRSSMS GLHLVKQGRD RKKIDSQRDF 100
    TVASPAEFVT RFGGNKVIEK VLIANNGIAA VKCMRSIRRW SYEMFRNERA 150
    IRFVVMVTPE DLKANAEYIK MADHYVPVPG GPNNNNYANV ELILDIAKRI 200
    PVQAVWAGWG HASENPKLPE LLLKNGIAFM GPPSQAMWAL GDKIASSIVA 250
    QTAGIPTLPW SGSGLRVDWQ ENDFSKRILN VPQELYEKGY VKDVDDGLQA 300
    AEEVGYPVMI KASEGGGGKG IRKVNNADDF PNLFRQVQAE VPGSPIFVMR 350
    LAKQSRHLEV QILADQYGNA ISLFGRDCSV QRRHQKIIEE APATIATPAV 400
    FEHMEQCAVK LAKMVGYVSA GTVEYLYSQD GSFYFLELNP RLQVEHPCTE 450
    MVADVNLPAA QLQIAMGIPL YRIKDIRMMY GVSPWGDSPI DFEDSAHVPC 500
    PRGHVIAARI TSENPDEGFK PSSGTVQELN FRSNKNVWGY FSVAAAGGLH 550
    EFADSQFGHC FSWGENREEA ISNMVVALKE LSIRGDFRTT VEYLIKLLET 600
    ESFQMNRIDT GWLDRLIAEK VQAERPDTML GVVCGALHVA DVSLRNSVSN 650
    FLHSLERGQV LPAHTLLNTV DVELIYEGVK YVLKVTRQSP NSYVVIMNGS 700
    CVEVDVHRLS DGGLLLSYDG SSYTTYMKEE VDRYRITIGN KTCVFEKEND 750
    PSVMRSPSAG KLIQYIVEDG GHVFAGQCYA EIEVMKMVMT LTAVESGCIH 800
    YVKRPGAALD PGCVLAKMQL DNPSKVQQAE LHTGSLPRIQ STALRGEKLH 850
    RVFHYVLDNL VNVMNGYCLP DPFFSSKVKD WVERLMKTLR DPSLPLLELQ 900
    DIMTSVSGRI PPNVEKSIKK EMAQYASNIT SVLCQFPSQQ IANILDSHAA 950
    TLNRKSEREV FFMNTQSIVQ LVQRYRSGIR GHMKAVVMDL LRQYLRVETQ 1000
    FQNGHYDKCV FALREENKSD MNTVLNYIFS HAQVTKKNLL VTMLIDQLCG 1050
    RDPTLTDELL NILTELTQLS KTTNAKVALR ARQVLIASHL PSYELRHNQV 1100
    ESIFLSAIDM YGHQFCIENL QKLILSETSI FDVLPNFFYH SNQVVRMAAL 1150
    EVYVRRAYIA YELNSVQHRQ LKDNTCVVEF QFMLPTSHPN RGNIPTLNRM 1200
    SFSSNLNHYG MTHVASVSDV LLDNSFTPPC QRMGGMVSFR TFEDFVRIFD 1250
    EVMGCFSDSP PQSPTFPEAG HTSLYDEDKV PRDEPIHILN VAIKTDCDIE 1300
    DDRLAAMFRE FTQQNKATLV DHGIRRLTFL VAQKDFRKQV NYEVDRRFHR 1350
    EFPKFFTFRA RDKFEEDRIY RHLEPALAFQ LELNRMRNFD LTAIPCANHK 1400
    MHLYLGAAKV EVGTEVTDYR FFVRAIIRHS DLVTKEASFE YLQNEGERLL 1450
    LEAMDELEVA FNNTNVRTDC NHIFLNFVPT VIMDPSKIEE SVRSMVMRYG 1500
    SRLWKLRVLQ AELKINIRLT PTGKAIPIRL FLTNESGYYL DISLYKEVTD 1550
    SRTAQIMFQA YGDKQGPLHG MLINTPYVTK DLLQSKRFQA QSLGTTYIYD 1600
    IPEMFRQSLI KLWESMSTQA FLPSPPLPSD MLTYTELVLD DQGQLVHMNR 1650
    LPGGNEIGMV AWKMTFKSPE YPEGRDIIVI GNDITYRIGS FGPQEDLLFL 1700
    RASELARAEG IPRIYVSANS GARIGLAEEI RHMFHVAWVD PEDPYKGYRY 1750
    LYLTPQDYKR VSALNSVHCE HVEDEGESRY KITDIIGKEE GIGPENLRGS 1800
    GMIAGESSLA YNEIITISLV TCRAIGIGAY LVRLGQRTIQ VENSHLILTG 1850
    AGALNKVLGR EVYTSNNQLG GIQIMHNNGV THCTVCDDFE GVFTVLHWLS 1900
    YMPKSVHSSV PLLNSKDPID RIIEFVPTKT PYDPRWMLAG RPHPTQKGQW 1950
    LSGFFDYGSF SEIMQPWAQT VVVGRARLGG IPVGVVAVET RTVELSIPAD 2000
    PANLDSEAKI IQQAGQVWFP DSAFKTYQAI KDFNREGLPL MVFANWRGFS 2050
    GGMKDMYDQV LKFGAYIVDG LRECCQPVLV YIPPQAELRG GSWVVIDSSI 2100
    NPRHMEMYAD RESRGSVLEP EGTVEIKFRR KDLVKTMRRV DPVYIHLAER 2150
    LGTPELSTAE RKELENKLKE REEFLIPIYH QVAVQFADLH DTPGRMQEKG 2200
    VISDILDWKT SRTFFYWRLR RLLLEDLVKK KIHNANPELT DGQIQAMLRR 2250
    WFVEVEGTVK AYVWDNNKDL AEWLEKQLTE EDGVHSVIEE NIKCISRDYV 2300
    LKQIRSLVQA NPEVAMDSII HMTQHISPTQ RAEVIRILST MDSPST 2346
    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

    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. 49 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

    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.
    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

    ArrayExpressi Q13085.
    Bgeei Q13085.
    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

    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 1, 2014
    This is version 148 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