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UniProtKB - P11498 (PYC_HUMAN)

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Protein

Pyruvate carboxylase, mitochondrial

Gene

PC

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

Functioni

Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. Catalyzes in a tissue specific manner, the initial reactions of glucose (liver, kidney) and lipid (adipose tissue, liver, brain) synthesis from pyruvate.

Catalytic activityi

ATP + pyruvate + HCO3- = ADP + phosphate + oxaloacetate.

Cofactori

Protein has several cofactor binding sites:

Pathwayi: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei152ATPBy similarity1
Binding sitei236ATPBy similarity1
Binding sitei271ATPBy similarity1
Active sitei328By similarity1
Metal bindingi572Manganese1 Publication1
Binding sitei644Substrate1
Metal bindingi741Manganese; via carbamate group1 Publication1
Metal bindingi771Manganese; via tele nitrogen1 Publication1
Metal bindingi773Manganese; via tele nitrogen1 Publication1
Binding sitei908Substrate1

GO - Molecular functioni

  • ATP binding Source: ProtInc
  • biotin binding Source: ProtInc
  • identical protein binding Source: IntAct
  • metal ion binding Source: UniProtKB-KW
  • pyruvate carboxylase activity Source: Reactome
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • biotin metabolic process Source: Reactome
  • gluconeogenesis Source: Reactome
  • lipid metabolic process Source: UniProtKB-KW
  • negative regulation of gene expression Source: AgBase
  • positive regulation by host of viral process Source: AgBase
  • positive regulation by host of viral release from host cell Source: AgBase
  • pyruvate metabolic process Source: InterPro
  • viral RNA genome packaging Source: AgBase
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionLigase, Multifunctional enzyme
Biological processGluconeogenesis, Lipid biosynthesis, Lipid metabolism
LigandATP-binding, Biotin, Manganese, Metal-binding, Nucleotide-binding, Pyruvate

Enzyme and pathway databases

BioCyciMetaCyc:HS10697-MONOMER
BRENDAi6.4.1.1 2681
ReactomeiR-HSA-196780 Biotin transport and metabolism
R-HSA-3371599 Defective HLCS causes multiple carboxylase deficiency
R-HSA-70263 Gluconeogenesis
SABIO-RKiP11498
SIGNORiP11498
UniPathwayiUPA00138

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate carboxylase, mitochondrial (EC:6.4.1.1)
Alternative name(s):
Pyruvic carboxylase
Short name:
PCB
Gene namesi
Name:PC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000173599.13
HGNCiHGNC:8636 PC
MIMi608786 gene
neXtProtiNX_P11498

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Pyruvate carboxylase deficiency (PC deficiency)
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionLeads to lactic acidosis, mental retardation and death. It occurs in three forms: mild or type A, severe neonatal or type B, and a very mild lacticacidemia.
See also OMIM:266150
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_015199145V → A in PC deficiency; mild. 2 PublicationsCorresponds to variant dbSNP:rs28940591EnsemblClinVar.1
Natural variantiVAR_058957156R → Q in PC deficiency. 1 PublicationCorresponds to variant dbSNP:rs119103241EnsemblClinVar.1
Natural variantiVAR_058958270R → W in PC deficiency. 1 Publication1
Natural variantiVAR_058959304Y → C in PC deficiency. 1 Publication1
Natural variantiVAR_015200451R → C in PC deficiency; mild. 2 PublicationsCorresponds to variant dbSNP:rs113994143EnsemblClinVar.1
Natural variantiVAR_058960583R → L in PC deficiency. 1 PublicationCorresponds to variant dbSNP:rs119103242EnsemblClinVar.1
Natural variantiVAR_008095610A → T in PC deficiency; mild. 2 PublicationsCorresponds to variant dbSNP:rs28940589EnsemblClinVar.1
Natural variantiVAR_058961631R → Q in PC deficiency. 1 PublicationCorresponds to variant dbSNP:rs113994145EnsemblClinVar.1
Natural variantiVAR_008096743M → I in PC deficiency; mild. 2 PublicationsCorresponds to variant dbSNP:rs28940590EnsemblClinVar.1
Natural variantiVAR_0589621131 – 1133Missing in PC deficiency. 1 Publication3

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1077F → A or E: Loss of tetramerization and enzyme activity, resulting in an inactive homodimer. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi5091
GeneReviewsiPC
MalaCardsiPC
MIMi266150 phenotype
OpenTargetsiENSG00000173599
Orphaneti353320 Pyruvate carboxylase deficiency, benign type
353308 Pyruvate carboxylase deficiency, infantile form
353314 Pyruvate carboxylase deficiency, severe neonatal type
PharmGKBiPA32975

Chemistry databases

DrugBankiDB00121 Biotin
DB00119 Pyruvic acid

Polymorphism and mutation databases

BioMutaiPC
DMDMi1709947

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 20MitochondrionSequence analysisAdd BLAST20
ChainiPRO_000000284021 – 1178Pyruvate carboxylase, mitochondrialAdd BLAST1158

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei35N6-acetyllysineBy similarity1
Modified residuei39N6-acetyllysineBy similarity1
Modified residuei79N6-acetyllysine; alternateBy similarity1
Modified residuei79N6-succinyllysine; alternateBy similarity1
Modified residuei148N6-acetyllysineBy similarity1
Modified residuei152N6-acetyllysineBy similarity1
Modified residuei241N6-acetyllysineBy similarity1
Modified residuei297N6-acetyllysineBy similarity1
Modified residuei319N6-acetyllysineBy similarity1
Modified residuei434N6-acetyllysineBy similarity1
Modified residuei442N6-succinyllysineBy similarity1
Modified residuei589N6-acetyllysineBy similarity1
Modified residuei661N6-acetyllysineBy similarity1
Modified residuei717N6-acetyllysineBy similarity1
Modified residuei741N6-carboxylysine1 Publication1
Modified residuei748N6-acetyllysineBy similarity1
Modified residuei892N6-acetyllysineBy similarity1
Modified residuei969N6-acetyllysineBy similarity1
Modified residuei992N6-acetyllysineBy similarity1
Modified residuei1003PhosphothreonineBy similarity1
Modified residuei1061N6-acetyllysineBy similarity1
Modified residuei1090N6-acetyllysineCombined sources1
Modified residuei1124N6-acetyllysineBy similarity1
Modified residuei1144N6-biotinyllysinePROSITE-ProRule annotation2 Publications1

Post-translational modificationi

Acetylation of Lys-748 might play a role in catalytic activity regulation.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP11498
MaxQBiP11498
PaxDbiP11498
PeptideAtlasiP11498
PRIDEiP11498
ProteomicsDBi52785

PTM databases

iPTMnetiP11498
PhosphoSitePlusiP11498
SwissPalmiP11498

Expressioni

Gene expression databases

BgeeiENSG00000173599
CleanExiHS_PC
ExpressionAtlasiP11498 baseline and differential
GenevisibleiP11498 HS

Organism-specific databases

HPAiCAB033742
HPA043922
HPA058765

Interactioni

Subunit structurei

Homotetramer (PubMed:18297087). Interacts (via the biotin carboxylation domain) with SIRT4 (PubMed:23438705).2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi111124, 73 interactors
DIPiDIP-46372N
IntActiP11498, 16 interactors
MINTiP11498
STRINGi9606.ENSP00000377527

Structurei

Secondary structure

11178
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi495 – 510Combined sources16
Helixi541 – 559Combined sources19
Beta strandi564 – 567Combined sources4
Turni569 – 571Combined sources3
Helixi572 – 577Combined sources6
Helixi584 – 597Combined sources14
Beta strandi602 – 608Combined sources7
Helixi611 – 617Combined sources7
Helixi623 – 633Combined sources11
Beta strandi635 – 637Combined sources3
Beta strandi639 – 643Combined sources5
Helixi645 – 647Combined sources3
Beta strandi650 – 652Combined sources3
Helixi656 – 669Combined sources14
Beta strandi673 – 677Combined sources5
Helixi683 – 694Combined sources12
Turni695 – 697Combined sources3
Beta strandi698 – 705Combined sources8
Helixi720 – 733Combined sources14
Beta strandi736 – 741Combined sources6
Helixi749 – 762Combined sources14
Beta strandi768 – 771Combined sources4
Helixi779 – 788Combined sources10
Beta strandi792 – 797Combined sources6
Helixi799 – 801Combined sources3
Helixi810 – 817Combined sources8
Helixi828 – 844Combined sources17
Helixi845 – 848Combined sources4
Helixi850 – 852Combined sources3
Helixi861 – 864Combined sources4
Helixi868 – 875Combined sources8
Helixi876 – 878Combined sources3
Turni879 – 881Combined sources3
Helixi886 – 900Combined sources15
Helixi910 – 923Combined sources14
Helixi928 – 934Combined sources7
Turni935 – 937Combined sources3
Helixi942 – 947Combined sources6
Turni948 – 950Combined sources3
Helixi961 – 968Combined sources8
Beta strandi969 – 971Combined sources3
Helixi978 – 981Combined sources4
Helixi989 – 997Combined sources9
Helixi1004 – 1012Combined sources9
Helixi1014 – 1026Combined sources13
Helixi1035 – 1040Combined sources6
Beta strandi1047 – 1051Combined sources5
Turni1053 – 1055Combined sources3
Beta strandi1057 – 1068Combined sources12
Beta strandi1072 – 1090Combined sources19
Helixi1092 – 1094Combined sources3
Beta strandi1108 – 1110Combined sources3
Beta strandi1118 – 1123Combined sources6
Beta strandi1138 – 1144Combined sources7
Beta strandi1146 – 1149Combined sources4
Beta strandi1164 – 1168Combined sources5
Beta strandi1173 – 1175Combined sources3

3D structure databases

ProteinModelPortaliP11498
SMRiP11498
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11498

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini36 – 486Biotin carboxylationAdd BLAST451
Domaini156 – 353ATP-graspPROSITE-ProRule annotationAdd BLAST198
Domaini563 – 832Pyruvate carboxyltransferasePROSITE-ProRule annotationAdd BLAST270
Domaini1109 – 1178Biotinyl-bindingPROSITE-ProRule annotationAdd BLAST70

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni571 – 575Substrate binding5

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IU5D Eukaryota
COG1038 LUCA
GeneTreeiENSGT00900000141164
HOGENOMiHOG000282801
HOVERGENiHBG008340
InParanoidiP11498
KOiK01958
OrthoDBiEOG091G00X2
PhylomeDBiP11498
TreeFamiTF300535

Family and domain databases

Gene3Di3.20.20.70, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR011761 ATP-grasp
IPR005481 BC-like_N
IPR001882 Biotin_BS
IPR011764 Biotin_carboxylation_dom
IPR005482 Biotin_COase_C
IPR000089 Biotin_lipoyl
IPR003379 Carboxylase_cons_dom
IPR005479 CbamoylP_synth_lsu-like_ATP-bd
IPR016185 PreATP-grasp_dom_sf
IPR000891 PYR_CT
IPR005930 Pyruv_COase
IPR011054 Rudment_hybrid_motif
IPR011053 Single_hybrid_motif
PfamiView protein in Pfam
PF02785 Biotin_carb_C, 1 hit
PF00289 Biotin_carb_N, 1 hit
PF00364 Biotin_lipoyl, 1 hit
PF02786 CPSase_L_D2, 1 hit
PF00682 HMGL-like, 1 hit
PF02436 PYC_OADA, 1 hit
PIRSFiPIRSF001594 Pyruv_carbox, 1 hit
SMARTiView protein in SMART
SM00878 Biotin_carb_C, 1 hit
SUPFAMiSSF51230 SSF51230, 1 hit
SSF51246 SSF51246, 1 hit
SSF52440 SSF52440, 1 hit
TIGRFAMsiTIGR01235 pyruv_carbox, 1 hit
PROSITEiView protein in PROSITE
PS50975 ATP_GRASP, 1 hit
PS50979 BC, 1 hit
PS00188 BIOTIN, 1 hit
PS50968 BIOTINYL_LIPOYL, 1 hit
PS50991 PYR_CT, 1 hit

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P11498-1) [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
MLKFRTVHGG LRLLGIRRTS TAPAASPNVR RLEYKPIKKV MVANRGEIAI 
        60         70         80         90        100
RVFRACTELG IRTVAIYSEQ DTGQMHRQKA DEAYLIGRGL APVQAYLHIP 
       110        120        130        140        150
DIIKVAKENN VDAVHPGYGF LSERADFAQA CQDAGVRFIG PSPEVVRKMG 
       160        170        180        190        200
DKVEARAIAI AAGVPVVPGT DAPITSLHEA HEFSNTYGFP IIFKAAYGGG 
       210        220        230        240        250
GRGMRVVHSY EELEENYTRA YSEALAAFGN GALFVEKFIE KPRHIEVQIL 
       260        270        280        290        300
GDQYGNILHL YERDCSIQRR HQKVVEIAPA AHLDPQLRTR LTSDSVKLAK 
       310        320        330        340        350
QVGYENAGTV EFLVDRHGKH YFIEVNSRLQ VEHTVTEEIT DVDLVHAQIH 
       360        370        380        390        400
VAEGRSLPDL GLRQENIRIN GCAIQCRVTT EDPARSFQPD TGRIEVFRSG 
       410        420        430        440        450
EGMGIRLDNA SAFQGAVISP HYDSLLVKVI AHGKDHPTAA TKMSRALAEF 
       460        470        480        490        500
RVRGVKTNIA FLQNVLNNQQ FLAGTVDTQF IDENPELFQL RPAQNRAQKL 
       510        520        530        540        550
LHYLGHVMVN GPTTPIPVKA SPSPTDPVVP AVPIGPPPAG FRDILLREGP 
       560        570        580        590        600
EGFARAVRNH PGLLLMDTTF RDAHQSLLAT RVRTHDLKKI APYVAHNFSK 
       610        620        630        640        650
LFSMENWGGA TFDVAMRFLY ECPWRRLQEL RELIPNIPFQ MLLRGANAVG 
       660        670        680        690        700
YTNYPDNVVF KFCEVAKENG MDVFRVFDSL NYLPNMLLGM EAAGSAGGVV 
       710        720        730        740        750
EAAISYTGDV ADPSRTKYSL QYYMGLAEEL VRAGTHILCI KDMAGLLKPT 
       760        770        780        790        800
ACTMLVSSLR DRFPDLPLHI HTHDTSGAGV AAMLACAQAG ADVVDVAADS 
       810        820        830        840        850
MSGMTSQPSM GALVACTRGT PLDTEVPMER VFDYSEYWEG ARGLYAAFDC 
       860        870        880        890        900
TATMKSGNSD VYENEIPGGQ YTNLHFQAHS MGLGSKFKEV KKAYVEANQM 
       910        920        930        940        950
LGDLIKVTPS SKIVGDLAQF MVQNGLSRAE AEAQAEELSF PRSVVEFLQG 
       960        970        980        990       1000
YIGVPHGGFP EPFRSKVLKD LPRVEGRPGA SLPPLDLQAL EKELVDRHGE 
      1010       1020       1030       1040       1050
EVTPEDVLSA AMYPDVFAHF KDFTATFGPL DSLNTRLFLQ GPKIAEEFEV 
      1060       1070       1080       1090       1100
ELERGKTLHI KALAVSDLNR AGQRQVFFEL NGQLRSILVK DTQAMKEMHF 
      1110       1120       1130       1140       1150
HPKALKDVKG QIGAPMPGKV IDIKVVAGAK VAKGQPLCVL SAMKMETVVT 
      1160       1170 
SPMEGTVRKV HVTKDMTLEG DDLILEIE
Length:1,178
Mass (Da):129,634
Last modified:October 1, 1996 - v2
Checksum:i381F527553A20095
GO
Isoform 2 (identifier: P11498-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     457-529: TNIAFLQNVL...ASPSPTDPVV → VRRHQAQPLA...STEVSPTILL
     530-1178: Missing.

Note: No experimental confirmation available.
Show »
Length:529
Mass (Da):57,925
Checksum:i35B87A653BF6F9C3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti225 – 226LA → WP in AAB31500 (PubMed:8048912).Curated2
Sequence conflicti352A → S in AAA82937 (Ref. 3) Curated1
Sequence conflicti385 – 386RS → PT in AAB31500 (PubMed:8048912).Curated2
Sequence conflicti486 – 487EL → DV in AAB31500 (PubMed:8048912).Curated2
Sequence conflicti638P → R in AAB31500 (PubMed:8048912).Curated1
Sequence conflicti729E → A in AAB31500 (PubMed:8048912).Curated1
Sequence conflicti774 – 775DT → AP in AAB31500 (PubMed:8048912).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04841676H → L. Corresponds to variant dbSNP:rs7104156EnsemblClinVar.1
Natural variantiVAR_015199145V → A in PC deficiency; mild. 2 PublicationsCorresponds to variant dbSNP:rs28940591EnsemblClinVar.1
Natural variantiVAR_058957156R → Q in PC deficiency. 1 PublicationCorresponds to variant dbSNP:rs119103241EnsemblClinVar.1
Natural variantiVAR_058958270R → W in PC deficiency. 1 Publication1
Natural variantiVAR_058959304Y → C in PC deficiency. 1 Publication1
Natural variantiVAR_015200451R → C in PC deficiency; mild. 2 PublicationsCorresponds to variant dbSNP:rs113994143EnsemblClinVar.1
Natural variantiVAR_058960583R → L in PC deficiency. 1 PublicationCorresponds to variant dbSNP:rs119103242EnsemblClinVar.1
Natural variantiVAR_008095610A → T in PC deficiency; mild. 2 PublicationsCorresponds to variant dbSNP:rs28940589EnsemblClinVar.1
Natural variantiVAR_058961631R → Q in PC deficiency. 1 PublicationCorresponds to variant dbSNP:rs113994145EnsemblClinVar.1
Natural variantiVAR_008096743M → I in PC deficiency; mild. 2 PublicationsCorresponds to variant dbSNP:rs28940590EnsemblClinVar.1
Natural variantiVAR_0589621131 – 1133Missing in PC deficiency. 1 Publication3

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_056358457 – 529TNIAF…TDPVV → VRRHQAQPLAAALGRPCGQE ARRPQAAVTAPTGPGSPTLV RVPPAARVLSSRLGGPSQTT PETSTEVSPTILL in isoform 2. 1 PublicationAdd BLAST73
Alternative sequenceiVSP_056359530 – 1178Missing in isoform 2. 1 PublicationAdd BLAST649

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04641 mRNA Translation: AAA99537.1
S72370 mRNA Translation: AAB31500.1
U30891 mRNA Translation: AAA82937.1
AK297705 mRNA Translation: BAG60062.1
AP000485 Genomic DNA No translation available.
AP003176 Genomic DNA No translation available.
BC011617 mRNA Translation: AAH11617.1
M26122 mRNA Translation: AAA36423.1
K02282 mRNA Translation: AAA60033.1
CCDSiCCDS8152.1 [P11498-1]
PIRiG01933 JC2460
RefSeqiNP_000911.2, NM_000920.3 [P11498-1]
NP_001035806.1, NM_001040716.1 [P11498-1]
NP_071504.2, NM_022172.2 [P11498-1]
XP_005274088.1, XM_005274031.4 [P11498-1]
XP_005274089.1, XM_005274032.4 [P11498-1]
XP_006718641.1, XM_006718578.3 [P11498-1]
XP_011543388.1, XM_011545086.2 [P11498-1]
XP_016873357.1, XM_017017868.1 [P11498-1]
XP_016873358.1, XM_017017869.1 [P11498-1]
XP_016873359.1, XM_017017870.1 [P11498-1]
XP_016873360.1, XM_017017871.1 [P11498-1]
XP_016873361.1, XM_017017872.1 [P11498-1]
UniGeneiHs.89890

Genome annotation databases

EnsembliENST00000393955; ENSP00000377527; ENSG00000173599 [P11498-1]
ENST00000393958; ENSP00000377530; ENSG00000173599 [P11498-1]
ENST00000393960; ENSP00000377532; ENSG00000173599 [P11498-1]
GeneIDi5091
KEGGihsa:5091
UCSCiuc001ojn.2 human [P11498-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPYC_HUMAN
AccessioniPrimary (citable) accession number: P11498
Secondary accession number(s): B4DN00, Q16705
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1996
Last modified: June 20, 2018
This is version 206 of the entry and version 2 of the sequence. See 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, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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

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