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P04406

- G3P_HUMAN

UniProt

P04406 - G3P_HUMAN

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Protein

Glyceraldehyde-3-phosphate dehydrogenase

Gene

GAPDH

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

Functioni

Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC. Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules By similarity. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation.By similarity3 Publications

Catalytic activityi

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH.1 PublicationPROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei35 – 351NAD2 Publications
Binding sitei80 – 801NAD; via carbonyl oxygen2 Publications
Binding sitei122 – 1221NAD2 Publications
Active sitei152 – 1521Nucleophile
Sitei179 – 1791Activates thiol group during catalysis
Binding sitei182 – 1821Glyceraldehyde 3-phosphateBy similarity
Binding sitei234 – 2341Glyceraldehyde 3-phosphateBy similarity
Binding sitei316 – 3161NAD2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 142NAD2 Publications

GO - Molecular functioni

  1. glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity Source: UniProtKB
  2. identical protein binding Source: IntAct
  3. microtubule binding Source: UniProtKB
  4. NAD binding Source: InterPro
  5. NADP binding Source: InterPro
  6. peptidyl-cysteine S-nitrosylase activity Source: UniProtKB

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. cellular response to interferon-gamma Source: UniProtKB
  3. gluconeogenesis Source: Reactome
  4. glucose metabolic process Source: Reactome
  5. glycolytic process Source: Reactome
  6. microtubule cytoskeleton organization Source: UniProtKB
  7. negative regulation of translation Source: UniProtKB
  8. neuron apoptotic process Source: UniProtKB
  9. peptidyl-cysteine S-trans-nitrosylation Source: UniProtKB
  10. protein stabilization Source: UniProtKB
  11. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Transferase

Keywords - Biological processi

Apoptosis, Glycolysis, Translation regulation

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:HS03433-MONOMER.
BRENDAi1.2.1.12. 2681.
ReactomeiREACT_1383. Glycolysis.
REACT_1520. Gluconeogenesis.
SABIO-RKP04406.
UniPathwayiUPA00109; UER00184.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyceraldehyde-3-phosphate dehydrogenase (EC:1.2.1.12)
Short name:
GAPDH
Alternative name(s):
Peptidyl-cysteine S-nitrosylase GAPDH (EC:2.6.99.-)
Gene namesi
Name:GAPDH
Synonyms:GAPD
ORF Names:CDABP0047, OK/SW-cl.12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:4141. GAPDH.

Subcellular locationi

Cytoplasmcytosol 1 Publication. Nucleus By similarity. Cytoplasmperinuclear region 1 Publication. Membrane 1 Publication. Cytoplasmcytoskeleton By similarity
Note: Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal By similarity. Postnuclear and Perinuclear regions.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
  4. GAIT complex Source: UniProtKB
  5. lipid particle Source: UniProtKB
  6. membrane Source: UniProtKB
  7. microtubule cytoskeleton Source: UniProtKB
  8. nucleus Source: UniProtKB
  9. plasma membrane Source: HPA
  10. ribonucleoprotein complex Source: UniProtKB
  11. vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28554.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 335334Glyceraldehyde-3-phosphate dehydrogenasePRO_0000145486Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51N6,N6-dimethyllysine1 Publication
Modified residuei9 – 91Deamidated asparagine1 Publication
Modified residuei42 – 421Phosphotyrosine1 Publication
Modified residuei61 – 611N6-acetyllysine1 Publication
Modified residuei64 – 641Deamidated asparagine1 Publication
Modified residuei66 – 661N6,N6-dimethyllysine1 Publication
Modified residuei70 – 701Deamidated asparagine1 Publication
Modified residuei75 – 751Phosphothreonine2 Publications
Modified residuei83 – 831Phosphoserine4 Publications
Modified residuei122 – 1221Phosphoserine1 Publication
Modified residuei148 – 1481Phosphoserine1 Publication
Modified residuei149 – 1491Deamidated asparagine1 Publication
Modified residuei151 – 1511Phosphoserine1 Publication
Modified residuei152 – 1521ADP-ribosylcysteine; by autocatalysis; in irreversibly inhibited formBy similarity
Modified residuei152 – 1521Cysteine persulfideBy similarity
Modified residuei152 – 1521S-nitrosocysteine; in reversibly inhibited formBy similarity
Modified residuei155 – 1551Deamidated asparagine1 Publication
Modified residuei184 – 1841Phosphothreonine3 Publications
Modified residuei194 – 1941N6,N6-dimethyllysine; alternate1 Publication
Modified residuei194 – 1941N6-acetyllysine; alternate1 Publication
Modified residuei194 – 1941N6-malonyllysine; alternate1 Publication
Modified residuei211 – 2111Phosphothreonine1 Publication
Modified residuei215 – 2151N6,N6-dimethyllysine; alternate1 Publication
Modified residuei215 – 2151N6-malonyllysine; alternate1 Publication
Modified residuei219 – 2191N6-acetyllysine1 Publication
Modified residuei225 – 2251Deamidated asparagine1 Publication
Modified residuei227 – 2271N6,N6-dimethyllysine; alternate1 Publication
Modified residuei227 – 2271N6-acetyllysine; alternate1 Publication
Modified residuei229 – 2291Phosphothreonine1 Publication
Modified residuei237 – 2371Phosphothreonine1 Publication
Modified residuei254 – 2541N6-acetyllysine1 Publication
Modified residuei260 – 2601N6,N6-dimethyllysine1 Publication
Modified residuei263 – 2631N6,N6-dimethyllysine1 Publication
Modified residuei312 – 3121Phosphoserine2 Publications
Modified residuei316 – 3161Deamidated asparagine1 Publication
Modified residuei334 – 3341N6,N6-dimethyllysine1 Publication

Post-translational modificationi

S-nitrosylation of Cys-152 leads to interaction with SIAH1, followed by translocation to the nucleus.By similarity
ISGylated.1 Publication
Sulfhydration at Cys-152 increases catalytic activity.By similarity

Keywords - PTMi

Acetylation, ADP-ribosylation, Methylation, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

MaxQBiP04406.
PaxDbiP04406.
PRIDEiP04406.

2D gel databases

DOSAC-COBS-2DPAGEP04406.
OGPiP04406.
REPRODUCTION-2DPAGEIPI00219018.
P04406.
SWISS-2DPAGEP04406.
UCD-2DPAGEP04406.

PTM databases

PhosphoSiteiP04406.

Expressioni

Gene expression databases

BgeeiP04406.
CleanExiHS_GAPDH.
ExpressionAtlasiP04406. baseline and differential.
GenevestigatoriP04406.

Organism-specific databases

HPAiCAB005197.
CAB016392.
HPA040067.

Interactioni

Subunit structurei

Homotetramer. Interacts with TPPP; the interaction is direct. Interacts (when S-nitrosylated) with SIAH1; leading to nuclear translocation. Interacts with RILPL1/GOSPEL, leading to prevent the interaction between GAPDH and SIAH1 and prevent nuclear translocation. Interacts with CHP1; the interaction increases the binding of CHP1 with microtubules. Associates with microtubules By similarity. Interacts with EIF1AD, USP25, PRKCI and WARS. Component of the GAIT complex. Interacts with FKBP6; leading to inhibit GAPDH catalytic activity.By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-354056,EBI-354056
EGFRP005336EBI-354056,EBI-297353
PCNAP120043EBI-354056,EBI-358311
PGK1P005582EBI-354056,EBI-709599
PREPP481475EBI-354056,EBI-1049962
RPA2P159272EBI-354056,EBI-621404

Protein-protein interaction databases

BioGridi108868. 158 interactions.
DIPiDIP-32521N.
IntActiP04406. 71 interactions.
MINTiMINT-1150338.
STRINGi9606.ENSP00000229239.

Structurei

Secondary structure

1
335
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95
Helixi13 – 2513
Beta strandi27 – 348
Beta strandi36 – 383
Helixi40 – 489
Turni51 – 533
Beta strandi60 – 634
Beta strandi66 – 694
Beta strandi72 – 776
Helixi82 – 843
Turni87 – 915
Beta strandi94 – 974
Beta strandi99 – 1013
Helixi105 – 1084
Helixi109 – 1146
Beta strandi117 – 1237
Beta strandi126 – 1283
Turni133 – 1353
Helixi137 – 1393
Beta strandi145 – 1484
Helixi152 – 16817
Beta strandi170 – 18011
Beta strandi185 – 1895
Helixi196 – 1994
Turni202 – 2043
Beta strandi207 – 2104
Turni213 – 2164
Helixi217 – 2204
Helixi222 – 2243
Beta strandi227 – 23610
Beta strandi241 – 25111
Helixi255 – 26713
Turni268 – 2736
Beta strandi274 – 2774
Helixi283 – 2864
Beta strandi292 – 2965
Turni297 – 2993
Beta strandi301 – 3044
Beta strandi307 – 3148
Helixi318 – 33316

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U8FX-ray1.75O/P/Q/R1-335[»]
1ZNQX-ray2.50O/P/Q/R1-335[»]
2FEHmodel-O/P/Q/R1-335[»]
3GPDX-ray3.50G/R2-335[»]
ProteinModelPortaliP04406.
SMRiP04406. Positions 3-335.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04406.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 148147Interaction with WARSAdd
BLAST
Regioni151 – 1533Glyceraldehyde 3-phosphate bindingBy similarity
Regioni211 – 2122Glyceraldehyde 3-phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0057.
GeneTreeiENSGT00760000119172.
HOGENOMiHOG000071678.
HOVERGENiHBG000227.
InParanoidiP04406.
KOiK00134.
OMAiKFASEGP.
OrthoDBiEOG7Q5HDF.
PhylomeDBiP04406.
TreeFamiTF300533.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR020831. GlycerAld/Erythrose_P_DH.
IPR020830. GlycerAld_3-P_DH_AS.
IPR020829. GlycerAld_3-P_DH_cat.
IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
IPR006424. Glyceraldehyde-3-P_DH_1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10836. PTHR10836. 1 hit.
PfamiPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000149. GAP_DH. 1 hit.
PRINTSiPR00078. G3PDHDRGNASE.
SMARTiSM00846. Gp_dh_N. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
PROSITEiPS00071. GAPDH. 1 hit.
[Graphical view]

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. Align

Isoform 1 (identifier: P04406-1) [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
MGKVKVGVNG FGRIGRLVTR AAFNSGKVDI VAINDPFIDL NYMVYMFQYD
60 70 80 90 100
STHGKFHGTV KAENGKLVIN GNPITIFQER DPSKIKWGDA GAEYVVESTG
110 120 130 140 150
VFTTMEKAGA HLQGGAKRVI ISAPSADAPM FVMGVNHEKY DNSLKIISNA
160 170 180 190 200
SCTTNCLAPL AKVIHDNFGI VEGLMTTVHA ITATQKTVDG PSGKLWRDGR
210 220 230 240 250
GALQNIIPAS TGAAKAVGKV IPELNGKLTG MAFRVPTANV SVVDLTCRLE
260 270 280 290 300
KPAKYDDIKK VVKQASEGPL KGILGYTEHQ VVSSDFNSDT HSSTFDAGAG
310 320 330
IALNDHFVKL ISWYDNEFGY SNRVVDLMAH MASKE
Length:335
Mass (Da):36,053
Last modified:January 23, 2007 - v3
Checksum:iC9C135E8AE3E8744
GO
Isoform 2 (identifier: P04406-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-42: Missing.

Note: No experimental confirmation available. Gene prediction based on EST data.

Show »
Length:293
Mass (Da):31,548
Checksum:i6705C1F127BB6C09
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti225 – 2251N → D in CAA25833. (PubMed:6096821)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti22 – 221A → G.1 Publication
Corresponds to variant rs45541435 [ dbSNP | Ensembl ].
VAR_018889
Natural varianti251 – 2511K → N.
Corresponds to variant rs1062429 [ dbSNP | Ensembl ].
VAR_049218

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4242Missing in isoform 2. CuratedVSP_047289Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X01677 mRNA. Translation: CAA25833.1.
M17851 mRNA. Translation: AAA86283.1.
M33197 mRNA. Translation: AAA52518.1.
J02642 mRNA. Translation: AAA52496.1.
J04038 Genomic DNA. Translation: AAA53191.1.
X53778 mRNA. Translation: CAA37794.1.
AF261085 mRNA. Translation: AAF99678.1.
AY007133 mRNA. Translation: AAG01996.1.
AB062273 mRNA. Translation: BAB93466.1.
BT006893 mRNA. Translation: AAP35539.1.
AY340484 Genomic DNA. Translation: AAP88932.1.
CR407671 mRNA. Translation: CAG28599.1.
AC006064 Genomic DNA. No translation available.
CH471116 Genomic DNA. Translation: EAW88787.1.
BC001601 mRNA. Translation: AAH01601.1.
BC004109 mRNA. Translation: AAH04109.1.
BC009081 mRNA. Translation: AAH09081.1.
BC013310 mRNA. Translation: AAH13310.1.
BC023632 mRNA. Translation: AAH23632.1.
BC025925 mRNA. Translation: AAH25925.1.
BC026907 mRNA. Translation: AAH26907.1.
BC029618 mRNA. Translation: AAH29618.1.
BC083511 mRNA. Translation: AAH83511.1.
CCDSiCCDS58201.1. [P04406-2]
CCDS8549.1. [P04406-1]
PIRiA31988. DEHUG3.
RefSeqiNP_001243728.1. NM_001256799.2. [P04406-2]
NP_001276674.1. NM_001289745.1. [P04406-1]
NP_001276675.1. NM_001289746.1. [P04406-1]
NP_002037.2. NM_002046.5. [P04406-1]
UniGeneiHs.544577.
Hs.592355.
Hs.598320.

Genome annotation databases

EnsembliENST00000229239; ENSP00000229239; ENSG00000111640. [P04406-1]
ENST00000396858; ENSP00000380067; ENSG00000111640. [P04406-2]
ENST00000396859; ENSP00000380068; ENSG00000111640. [P04406-1]
ENST00000396861; ENSP00000380070; ENSG00000111640. [P04406-1]
ENST00000619601; ENSP00000478864; ENSG00000111640. [P04406-2]
GeneIDi2597.
KEGGihsa:2597.
UCSCiuc001qop.2. human. [P04406-1]

Polymorphism databases

DMDMi120649.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Glyceraldehyde 3-phosphate dehydrogenase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X01677 mRNA. Translation: CAA25833.1 .
M17851 mRNA. Translation: AAA86283.1 .
M33197 mRNA. Translation: AAA52518.1 .
J02642 mRNA. Translation: AAA52496.1 .
J04038 Genomic DNA. Translation: AAA53191.1 .
X53778 mRNA. Translation: CAA37794.1 .
AF261085 mRNA. Translation: AAF99678.1 .
AY007133 mRNA. Translation: AAG01996.1 .
AB062273 mRNA. Translation: BAB93466.1 .
BT006893 mRNA. Translation: AAP35539.1 .
AY340484 Genomic DNA. Translation: AAP88932.1 .
CR407671 mRNA. Translation: CAG28599.1 .
AC006064 Genomic DNA. No translation available.
CH471116 Genomic DNA. Translation: EAW88787.1 .
BC001601 mRNA. Translation: AAH01601.1 .
BC004109 mRNA. Translation: AAH04109.1 .
BC009081 mRNA. Translation: AAH09081.1 .
BC013310 mRNA. Translation: AAH13310.1 .
BC023632 mRNA. Translation: AAH23632.1 .
BC025925 mRNA. Translation: AAH25925.1 .
BC026907 mRNA. Translation: AAH26907.1 .
BC029618 mRNA. Translation: AAH29618.1 .
BC083511 mRNA. Translation: AAH83511.1 .
CCDSi CCDS58201.1. [P04406-2 ]
CCDS8549.1. [P04406-1 ]
PIRi A31988. DEHUG3.
RefSeqi NP_001243728.1. NM_001256799.2. [P04406-2 ]
NP_001276674.1. NM_001289745.1. [P04406-1 ]
NP_001276675.1. NM_001289746.1. [P04406-1 ]
NP_002037.2. NM_002046.5. [P04406-1 ]
UniGenei Hs.544577.
Hs.592355.
Hs.598320.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1U8F X-ray 1.75 O/P/Q/R 1-335 [» ]
1ZNQ X-ray 2.50 O/P/Q/R 1-335 [» ]
2FEH model - O/P/Q/R 1-335 [» ]
3GPD X-ray 3.50 G/R 2-335 [» ]
ProteinModelPortali P04406.
SMRi P04406. Positions 3-335.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108868. 158 interactions.
DIPi DIP-32521N.
IntActi P04406. 71 interactions.
MINTi MINT-1150338.
STRINGi 9606.ENSP00000229239.

Chemistry

BindingDBi P04406.
ChEMBLi CHEMBL2284.

PTM databases

PhosphoSitei P04406.

Polymorphism databases

DMDMi 120649.

2D gel databases

DOSAC-COBS-2DPAGE P04406.
OGPi P04406.
REPRODUCTION-2DPAGE IPI00219018.
P04406.
SWISS-2DPAGE P04406.
UCD-2DPAGE P04406.

Proteomic databases

MaxQBi P04406.
PaxDbi P04406.
PRIDEi P04406.

Protocols and materials databases

DNASUi 2597.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000229239 ; ENSP00000229239 ; ENSG00000111640 . [P04406-1 ]
ENST00000396858 ; ENSP00000380067 ; ENSG00000111640 . [P04406-2 ]
ENST00000396859 ; ENSP00000380068 ; ENSG00000111640 . [P04406-1 ]
ENST00000396861 ; ENSP00000380070 ; ENSG00000111640 . [P04406-1 ]
ENST00000619601 ; ENSP00000478864 ; ENSG00000111640 . [P04406-2 ]
GeneIDi 2597.
KEGGi hsa:2597.
UCSCi uc001qop.2. human. [P04406-1 ]

Organism-specific databases

CTDi 2597.
GeneCardsi GC12P006643.
H-InvDB HIX0000949.
HIX0024996.
HGNCi HGNC:4141. GAPDH.
HPAi CAB005197.
CAB016392.
HPA040067.
MIMi 138400. gene.
neXtProti NX_P04406.
PharmGKBi PA28554.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0057.
GeneTreei ENSGT00760000119172.
HOGENOMi HOG000071678.
HOVERGENi HBG000227.
InParanoidi P04406.
KOi K00134.
OMAi KFASEGP.
OrthoDBi EOG7Q5HDF.
PhylomeDBi P04406.
TreeFami TF300533.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00184 .
BioCyci MetaCyc:HS03433-MONOMER.
BRENDAi 1.2.1.12. 2681.
Reactomei REACT_1383. Glycolysis.
REACT_1520. Gluconeogenesis.
SABIO-RK P04406.

Miscellaneous databases

ChiTaRSi GAPDH. human.
EvolutionaryTracei P04406.
GeneWikii Glyceraldehyde_3-phosphate_dehydrogenase.
GenomeRNAii 2597.
NextBioi 10271.
PROi P04406.
SOURCEi Search...

Gene expression databases

Bgeei P04406.
CleanExi HS_GAPDH.
ExpressionAtlasi P04406. baseline and differential.
Genevestigatori P04406.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR020831. GlycerAld/Erythrose_P_DH.
IPR020830. GlycerAld_3-P_DH_AS.
IPR020829. GlycerAld_3-P_DH_cat.
IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
IPR006424. Glyceraldehyde-3-P_DH_1.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PANTHERi PTHR10836. PTHR10836. 1 hit.
Pfami PF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000149. GAP_DH. 1 hit.
PRINTSi PR00078. G3PDHDRGNASE.
SMARTi SM00846. Gp_dh_N. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01534. GAPDH-I. 1 hit.
PROSITEi PS00071. GAPDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The glyceraldehyde 3 phosphate dehydrogenase gene family: structure of a human cDNA and of an X chromosome linked pseudogene; amazing complexity of the gene family in mouse."
    Hanauer A., Mandel J.-L.
    EMBO J. 3:2627-2633(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The complete sequence of a full length cDNA for human liver glyceraldehyde-3-phosphate dehydrogenase: evidence for multiple mRNA species."
    Arcari P., Martinelli R., Salvatore F.
    Nucleic Acids Res. 12:9179-9189(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Isolation and characterization of rat and human glyceraldehyde-3-phosphate dehydrogenase cDNAs: genomic complexity and molecular evolution of the gene."
    Tso J.Y., Sun X.-H., Kao T.-H., Reece K.S., Wu R.
    Nucleic Acids Res. 13:2485-2502(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  4. "Enhanced expression of a glyceraldehyde-3-phosphate dehydrogenase gene in human lung cancers."
    Tokunaga K., Nakamura Y., Sakata K., Fujimori K., Ohkubo M., Sawada K., Sakiyama S.
    Cancer Res. 47:5616-5619(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung.
  5. "Identification of the 37-kDa protein displaying a variable interaction with the erythroid cell membrane as glyceraldehyde-3-phosphate dehydrogenase."
    Allen R.W., Trach K.A., Hoch J.A.
    J. Biol. Chem. 262:649-653(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  6. "Isolation and complete sequence of a functional human glyceraldehyde-3-phosphate dehydrogenase gene."
    Ercolani L., Florence B., Denaro M., Alexander M.
    J. Biol. Chem. 263:15335-15341(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY.
  7. "A human nuclear uracil DNA glycosylase is the 37-kDa subunit of glyceraldehyde-3-phosphate dehydrogenase."
    Meyer-Siegler K., Mauro D.J., Seal G., Wurzer J., Deriel J.K., Sirover M.A.
    Proc. Natl. Acad. Sci. U.S.A. 88:8460-8464(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  8. "cDNA cloning by amplification of circularized first strand cDNAs reveals non-IRE-regulated iron-responsive mRNAs."
    Ye Z., Connor J.R.
    Biochem. Biophys. Res. Commun. 275:223-227(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Astrocytoma.
  9. "Pediatric leukemia cDNA sequencing project."
    Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A., Margolin J.F.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Leukemia.
  10. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
    Shichijo S., Itoh K.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon adenocarcinoma.
  11. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  12. NIEHS SNPs program
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-22.
  13. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  14. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  15. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  16. "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].
    Tissue: Eye, Kidney, Lung, Lymph and Placenta.
  17. "The complete amino acid sequence of human muscle glyceraldehyde 3-phosphate dehydrogenase."
    Nowak K., Wolny M., Banas T.
    FEBS Lett. 134:143-146(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-335.
    Tissue: Muscle.
  18. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Tissue: Platelet.
  19. Bienvenut W.V., Gao M., Leug H.
    Submitted (JUL-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13; 62-84; 118-139; 198-215; 220-227; 235-248 AND 310-335, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Prostatic carcinoma.
  20. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 67-80; 87-107; 119-139; 146-186; 201-215; 235-248 AND 310-334, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  21. "The major protein expression profile and two-dimensional protein database of human heart."
    Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A., Ershova E.S., Egorov T.A., Musalyamov A.K.
    Electrophoresis 16:1160-1169(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 220-226 AND 242-246.
    Tissue: Heart.
  22. "The covalent structure of glyceraldehyde-phosphate dehydrogenase from human muscles. Isolation and amino acid sequences of peptides from tryptic digest."
    Nowak K., Kuczek M., Ostropolska L., Malarska A., Wolny M., Branowski T.
    Hoppe-Seyler's Z. Physiol. Chem. 356:1181-1183(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Tissue: Muscle.
  23. "Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Ciota /lambda and plays a role in microtubule dynamics in the early secretory pathway."
    Tisdale E.J.
    J. Biol. Chem. 277:3334-3341(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PRKCI.
  24. "Subcellular localization of human glyceraldehyde-3-phosphate dehydrogenase is independent of its glycolytic function."
    Mazzola J.L., Sirover M.A.
    Biochim. Biophys. Acta 1622:50-56(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  25. "Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-specific silencing of translation."
    Sampath P., Mazumder B., Seshadri V., Gerber C.A., Chavatte L., Kinter M., Ting S.M., Dignam J.D., Kim S., Driscoll D.M., Fox P.L.
    Cell 119:195-208(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE GAIT COMPLEX.
  26. "Oxidative stress-responsive intracellular regulation specific for the angiostatic form of human tryptophanyl-tRNA synthetase."
    Wakasugi K., Nakano T., Morishima I.
    Biochemistry 44:225-232(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WARS.
  27. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "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-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  29. "The ubiquitin-specific protease USP25 interacts with three sarcomeric proteins."
    Bosch-Comas A., Lindsten K., Gonzalez-Duarte R., Masucci M.G., Marfany G.
    Cell. Mol. Life Sci. 63:723-734(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH USP25.
  30. "HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I IFN-induced ISGylation of protein targets."
    Wong J.J., Pung Y.F., Sze N.S., Chin K.C.
    Proc. Natl. Acad. Sci. U.S.A. 103:10735-10740(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISGYLATION.
  31. "Strategy for comprehensive identification of post-translational modifications in cellular proteins, including low abundant modifications: application to glyceraldehyde-3-phosphate dehydrogenase."
    Seo J., Jeong J., Kim Y.M., Hwang N., Paek E., Lee K.-J.
    J. Proteome Res. 7:587-602(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-75; SER-122; SER-148; THR-229; THR-237 AND SER-312, DEAMIDATION AT ASN-9; ASN-64; ASN-70; ASN-149; ASN-155; ASN-225 AND ASN-316, METHYLATION AT LYS-5; LYS-66; LYS-194; LYS-215; LYS-227; LYS-260; LYS-263 AND LYS-334.
  32. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-151 AND THR-184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  33. "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].
  34. "FKBP36 is an inherent multifunctional glyceraldehyde-3-phosphate dehydrogenase inhibitor."
    Jarczowski F., Jahreis G., Erdmann F., Schierhorn A., Fischer G., Edlich F.
    J. Biol. Chem. 284:766-773(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FKBP6.
  35. "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 THR-184; THR-211 AND SER-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  36. "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-61; LYS-194; LYS-219; LYS-227 AND LYS-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  37. "Haponin (eIF1AD) interacts with glyceraldehyde 3-phosphate dehydrogenase in the CHO-K1 cell line."
    Rakitina T.V., Bogatova O.V., Smirnova E.V., Pozdeev V.I., Kostanian I.A., Lipkin V.M.
    Bioorg. Khim. 36:312-318(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EIF1AD.
  38. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-75; SER-83 AND THR-184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  39. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  40. Cited for: MALONYLATION AT LYS-194 AND LYS-215.
  41. "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-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  42. "Heterotrimeric GAIT complex drives transcript-selective translation inhibition in murine macrophages."
    Arif A., Chatterjee P., Moodt R.A., Fox P.L.
    Mol. Cell. Biol. 32:5046-5055(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RECONSTITUTION OF THE GAIT COMPLEX.
  43. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  44. "Twinning in crystals of human skeletal muscle D-glyceraldehyde-3-phosphate dehydrogenase."
    Mercer W.D., Winn S.I., Watson H.C.
    J. Mol. Biol. 104:277-283(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
  45. "Structural analysis of human liver glyceraldehyde-3-phosphate dehydrogenase."
    Ismail S.A., Park H.W.
    Acta Crystallogr. D 61:1508-1513(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD, SUBUNIT.
  46. "High-resolution structure of human D-glyceraldehyde-3-phosphate dehydrogenase."
    Jenkins J.L., Tanner J.J.
    Acta Crystallogr. D 62:290-301(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH NAD, SUBUNIT.

Entry informationi

Entry nameiG3P_HUMAN
AccessioniPrimary (citable) accession number: P04406
Secondary accession number(s): E7EUT4, P00354, Q53X65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 197 of the entry and version 3 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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

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