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Protein

Hexokinase-2

Gene

HK2

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

Functioni

Catalytic activityi

ATP + D-hexose = ADP + D-hexose 6-phosphate.

Enzyme regulationi

Hexokinase is an allosteric enzyme inhibited by its product Glc-6-P.

Pathwayi: hexose metabolism

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei30ATP 1By similarity1
Binding sitei209Glucose-6-phosphate 11 Publication1
Binding sitei232Glucose-6-phosphate 11 Publication1
Binding sitei235Substrate 11
Binding sitei260Substrate 11
Binding sitei449Glucose-6-phosphate 11 Publication1
Binding sitei558ATPSequence analysis1
Binding sitei657Glucose-6-phosphate 21 Publication1
Binding sitei680ATP 2By similarity1
Binding sitei680Glucose-6-phosphate 21 Publication1
Binding sitei708Substrate 21
Binding sitei897Glucose-6-phosphate 21 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi84 – 89ATP 1Sequence analysis6
Nucleotide bindingi425 – 426ATP 1By similarity2
Nucleotide bindingi532 – 537ATP 2By similarity6
Nucleotide bindingi747 – 748ATP 2By similarity2
Nucleotide bindingi784 – 788ATP 2By similarity5
Nucleotide bindingi863 – 867ATP 2By similarity5

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • fructokinase activity Source: GO_Central
  • glucokinase activity Source: GO_Central
  • glucose binding Source: Ensembl
  • hexokinase activity Source: ProtInc
  • mannokinase activity Source: GO_Central

GO - Biological processi

  • apoptotic mitochondrial changes Source: MGI
  • canonical glycolysis Source: Reactome
  • cellular glucose homeostasis Source: GO_Central
  • establishment of protein localization to mitochondrion Source: ParkinsonsUK-UCL
  • glucose transport Source: Reactome
  • glycolytic process Source: ParkinsonsUK-UCL
  • lactation Source: Ensembl
  • maintenance of protein location in mitochondrion Source: ParkinsonsUK-UCL
  • negative regulation of mitochondrial membrane permeability Source: Ensembl
  • negative regulation of reactive oxygen species metabolic process Source: Ensembl
  • positive regulation of mitophagy in response to mitochondrial depolarization Source: ParkinsonsUK-UCL
  • regulation of glucose import Source: Ensembl
  • response to ischemia Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS08399-MONOMER.
ZFISH:HS08399-MONOMER.
BRENDAi2.7.1.1. 2681.
ReactomeiR-HSA-70153. Glucose transport.
R-HSA-70171. Glycolysis.
SABIO-RKP52789.
UniPathwayiUPA00242.

Names & Taxonomyi

Protein namesi
Recommended name:
Hexokinase-2 (EC:2.7.1.1)
Alternative name(s):
Hexokinase type II
Short name:
HK II
Muscle form hexokinase
Gene namesi
Name:HK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:4923. HK2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: GO_Central
  • membrane Source: UniProtKB
  • mitochondrial outer membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi3099.
OpenTargetsiENSG00000159399.
PharmGKBiPA29301.

Chemistry databases

ChEMBLiCHEMBL2640.

Polymorphism and mutation databases

BioMutaiHK2.
DMDMi56405344.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001975871 – 917Hexokinase-2Add BLAST917

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP52789.
MaxQBiP52789.
PaxDbiP52789.
PeptideAtlasiP52789.
PRIDEiP52789.

PTM databases

iPTMnetiP52789.
PhosphoSitePlusiP52789.
SwissPalmiP52789.

Expressioni

Tissue specificityi

Predominant hexokinase isozyme expressed in insulin-responsive tissues such as skeletal muscle.

Gene expression databases

BgeeiENSG00000159399.
CleanExiHS_HK2.
ExpressionAtlasiP52789. baseline and differential.
GenevisibleiP52789. HS.

Organism-specific databases

HPAiHPA028587.

Interactioni

Subunit structurei

Monomer (By similarity). Interacts with TIGAR; the interaction increases hexokinase HK2 activity in a hypoxia- and HIF1A-dependent manner (PubMed:23185017).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MAGEA12Q6FHH83EBI-741469,EBI-10178394
UBQLN1Q9UMX04EBI-741469,EBI-741480
UBQLN1Q9UMX0-23EBI-741469,EBI-10173939

Protein-protein interaction databases

BioGridi109346. 46 interactors.
DIPiDIP-50110N.
IntActiP52789. 14 interactors.
MINTiMINT-1461614.
STRINGi9606.ENSP00000290573.

Structurei

Secondary structure

1917
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi19 – 25Combined sources7
Helixi27 – 29Combined sources3
Helixi33 – 51Combined sources19
Turni53 – 55Combined sources3
Helixi56 – 58Combined sources3
Beta strandi78 – 97Combined sources20
Beta strandi100 – 102Combined sources3
Beta strandi106 – 112Combined sources7
Helixi116 – 119Combined sources4
Helixi123 – 141Combined sources19
Helixi143 – 145Combined sources3
Beta strandi148 – 154Combined sources7
Beta strandi161 – 164Combined sources4
Beta strandi165 – 168Combined sources4
Helixi185 – 194Combined sources10
Beta strandi201 – 207Combined sources7
Helixi209 – 218Combined sources10
Beta strandi224 – 241Combined sources18
Helixi242 – 244Combined sources3
Beta strandi252 – 258Combined sources7
Helixi261 – 263Combined sources3
Turni264 – 267Combined sources4
Turni269 – 273Combined sources5
Helixi276 – 283Combined sources8
Beta strandi285 – 287Combined sources3
Helixi292 – 295Combined sources4
Turni299 – 301Combined sources3
Helixi302 – 315Combined sources14
Helixi320 – 322Combined sources3
Helixi326 – 329Combined sources4
Helixi336 – 344Combined sources9
Beta strandi345 – 347Combined sources3
Helixi348 – 358Combined sources11
Helixi365 – 401Combined sources37
Beta strandi404 – 413Combined sources10
Helixi415 – 419Combined sources5
Beta strandi420 – 422Combined sources3
Helixi423 – 434Combined sources12
Beta strandi438 – 444Combined sources7
Helixi449 – 474Combined sources26
Helixi475 – 477Combined sources3
Helixi481 – 499Combined sources19
Helixi501 – 504Combined sources4
Beta strandi527 – 536Combined sources10
Beta strandi539 – 545Combined sources7
Beta strandi548 – 550Combined sources3
Beta strandi553 – 559Combined sources7
Helixi564 – 568Combined sources5
Helixi571 – 588Combined sources18
Beta strandi597 – 602Combined sources6
Beta strandi606 – 610Combined sources5
Beta strandi613 – 616Combined sources4
Helixi633 – 642Combined sources10
Beta strandi650 – 655Combined sources6
Helixi657 – 666Combined sources10
Beta strandi672 – 689Combined sources18
Turni690 – 692Combined sources3
Beta strandi699 – 706Combined sources8
Helixi709 – 711Combined sources3
Turni712 – 715Combined sources4
Turni717 – 721Combined sources5
Helixi724 – 731Combined sources8
Beta strandi733 – 735Combined sources3
Helixi742 – 744Combined sources3
Turni747 – 749Combined sources3
Helixi750 – 763Combined sources14
Helixi768 – 770Combined sources3
Turni774 – 776Combined sources3
Helixi785 – 788Combined sources4
Turni789 – 791Combined sources3
Helixi797 – 806Combined sources10
Helixi813 – 848Combined sources36
Beta strandi852 – 861Combined sources10
Helixi863 – 867Combined sources5
Beta strandi868 – 870Combined sources3
Helixi871 – 882Combined sources12
Beta strandi886 – 892Combined sources7
Helixi897 – 911Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2NZTX-ray2.45A/B17-916[»]
5HEXX-ray2.73A/B17-917[»]
5HFUX-ray2.92A/B17-917[»]
5HG1X-ray2.76A17-916[»]
ProteinModelPortaliP52789.
SMRiP52789.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52789.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 458Hexokinase 1PROSITE-ProRule annotationAdd BLAST443
Domaini464 – 906Hexokinase 2PROSITE-ProRule annotationAdd BLAST443

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 12HydrophobicAdd BLAST12
Regioni13 – 475RegulatoryAdd BLAST463
Regioni73 – 207Hexokinase small subdomain 1PROSITE-ProRule annotationAdd BLAST135
Regioni84 – 88Glucose-6-phosphate 1 binding5
Regioni155 – 156Substrate 1 binding2
Regioni172 – 173Substrate 1 binding2
Regioni208 – 447Hexokinase large subdomain 1PROSITE-ProRule annotationAdd BLAST240
Regioni208 – 209Substrate 1 binding2
Regioni291 – 294Substrate 1 binding4
Regioni413 – 415Glucose-6-phosphate 1 binding3
Regioni476 – 917CatalyticAdd BLAST442
Regioni521 – 655Hexokinase small subdomain 2PROSITE-ProRule annotationAdd BLAST135
Regioni532 – 536Glucose-6-phosphate 2 binding5
Regioni603 – 604Substrate 2 binding2
Regioni620 – 621Substrate 2 binding2
Regioni656 – 895Hexokinase large subdomain 2PROSITE-ProRule annotationAdd BLAST240
Regioni656 – 657Substrate 2 binding2
Regioni682 – 683Substrate 2 binding2
Regioni739 – 742Substrate 2 binding4
Regioni861 – 863Glucose-6-phosphate 2 binding3

Domaini

The N- and C-terminal halves of this hexokinase show extensive sequence similarity to each other. The catalytic activity is associated with the C-terminus while regulatory function is associated with the N-terminus. Each domain can bind a single glucose and Gluc-6-P molecule.

Sequence similaritiesi

Belongs to the hexokinase family.PROSITE-ProRule annotationCurated
Contains 2 hexokinase domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1369. Eukaryota.
COG5026. LUCA.
GeneTreeiENSGT00390000017159.
HOGENOMiHOG000162671.
HOVERGENiHBG005020.
InParanoidiP52789.
KOiK00844.
OMAiHHLGLES.
OrthoDBiEOG091G08MD.
PhylomeDBiP52789.
TreeFamiTF314238.

Family and domain databases

InterProiIPR001312. Hexokinase.
IPR019807. Hexokinase_BS.
IPR022673. Hexokinase_C.
IPR022672. Hexokinase_N.
[Graphical view]
PANTHERiPTHR19443. PTHR19443. 1 hit.
PfamiPF00349. Hexokinase_1. 2 hits.
PF03727. Hexokinase_2. 2 hits.
[Graphical view]
PROSITEiPS00378. HEXOKINASE_1. 2 hits.
PS51748. HEXOKINASE_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P52789-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIASHLLAYF FTELNHDQVQ KVDQYLYHMR LSDETLLEIS KRFRKEMEKG
60 70 80 90 100
LGATTHPTAA VKMLPTFVRS TPDGTEHGEF LALDLGGTNF RVLWVKVTDN
110 120 130 140 150
GLQKVEMENQ IYAIPEDIMR GSGTQLFDHI AECLANFMDK LQIKDKKLPL
160 170 180 190 200
GFTFSFPCHQ TKLDESFLVS WTKGFKSSGV EGRDVVALIR KAIQRRGDFD
210 220 230 240 250
IDIVAVVNDT VGTMMTCGYD DHNCEIGLIV GTGSNACYME EMRHIDMVEG
260 270 280 290 300
DEGRMCINME WGAFGDDGSL NDIRTEFDQE IDMGSLNPGK QLFEKMISGM
310 320 330 340 350
YMGELVRLIL VKMAKEELLF GGKLSPELLN TGRFETKDIS DIEGEKDGIR
360 370 380 390 400
KAREVLMRLG LDPTQEDCVA THRICQIVST RSASLCAATL AAVLQRIKEN
410 420 430 440 450
KGEERLRSTI GVDGSVYKKH PHFAKRLHKT VRRLVPGCDV RFLRSEDGSG
460 470 480 490 500
KGAAMVTAVA YRLADQHRAR QKTLEHLQLS HDQLLEVKRR MKVEMERGLS
510 520 530 540 550
KETHASAPVK MLPTYVCATP DGTEKGDFLA LDLGGTNFRV LLVRVRNGKW
560 570 580 590 600
GGVEMHNKIY AIPQEVMHGT GDELFDHIVQ CIADFLEYMG MKGVSLPLGF
610 620 630 640 650
TFSFPCQQNS LDESILLKWT KGFKASGCEG EDVVTLLKEA IHRREEFDLD
660 670 680 690 700
VVAVVNDTVG TMMTCGFEDP HCEVGLIVGT GSNACYMEEM RNVELVEGEE
710 720 730 740 750
GRMCVNMEWG AFGDNGCLDD FRTEFDVAVD ELSLNPGKQR FEKMISGMYL
760 770 780 790 800
GEIVRNILID FTKRGLLFRG RISERLKTRG IFETKFLSQI ESDCLALLQV
810 820 830 840 850
RAILQHLGLE STCDDSIIVK EVCTVVARRA AQLCGAGMAA VVDRIRENRG
860 870 880 890 900
LDALKVTVGV DGTLYKLHPH FAKVMHETVK DLAPKCDVSF LQSEDGSGKG
910
AALITAVACR IREAGQR
Length:917
Mass (Da):102,380
Last modified:December 7, 2004 - v2
Checksum:iF17CE1938CF13880
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti803I → T in CAA86511 (PubMed:8250948).Curated1
Sequence conflicti870Missing in CAA86476 (PubMed:8786021).Curated1

Polymorphismi

Although found in NIDDM patients, genetic variations of HK2 do not contribute to the disease (PubMed:7883122, PubMed:7883123).2 Publications

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_003691142Q → H Does not affect activity. 4 PublicationsCorresponds to variant rs2229621dbSNPEnsembl.1
Natural variantiVAR_010577148L → F.1 Publication1
Natural variantiVAR_020504274R → C.1 PublicationCorresponds to variant rs28363006dbSNPEnsembl.1
Natural variantiVAR_020505314A → P.1 PublicationCorresponds to variant rs28363015dbSNPEnsembl.1
Natural variantiVAR_010578314A → V.1 Publication1
Natural variantiVAR_020506331T → I.1 PublicationCorresponds to variant rs28363016dbSNPEnsembl.1
Natural variantiVAR_010579353R → C.1 PublicationCorresponds to variant rs61748096dbSNPEnsembl.1
Natural variantiVAR_020507387A → S.1 PublicationCorresponds to variant rs28363029dbSNPEnsembl.1
Natural variantiVAR_010580497R → Q.1 PublicationCorresponds to variant rs145124653dbSNPEnsembl.1
Natural variantiVAR_010581775R → Q.1 PublicationCorresponds to variant rs185927605dbSNPEnsembl.1
Natural variantiVAR_020508801R → Q.1 PublicationCorresponds to variant rs28363057dbSNPEnsembl.1
Natural variantiVAR_010582844R → K.2 PublicationsCorresponds to variant rs2229629dbSNPEnsembl.1
Natural variantiVAR_020509881D → N.1 PublicationCorresponds to variant rs28363065dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46376 mRNA. Translation: CAA86511.1.
Z46354
, Z46355, Z46604, Z46356, Z46357, Z46358, Z46359, Z46360, Z46361, Z46362, Z46363, Z46364, Z46365, Z46366, Z46367, Z46368, Z46369 Genomic DNA. Translation: CAA86476.2.
AF148513 mRNA. Translation: AAD30174.1.
AY623118 Genomic DNA. Translation: AAT38114.1.
CH471053 Genomic DNA. Translation: EAW99601.1.
CH471053 Genomic DNA. Translation: EAW99602.1.
BC021116 mRNA. Translation: AAH21116.1.
BC064369 mRNA. Translation: AAH64369.1.
D25412 Genomic DNA. Translation: BAA04999.1.
CCDSiCCDS1956.1.
PIRiS48809. JC2025.
RefSeqiNP_000180.2. NM_000189.4.
UniGeneiHs.406266.
Hs.591588.

Genome annotation databases

EnsembliENST00000290573; ENSP00000290573; ENSG00000159399.
GeneIDi3099.
KEGGihsa:3099.
UCSCiuc002snd.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Hexokinase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46376 mRNA. Translation: CAA86511.1.
Z46354
, Z46355, Z46604, Z46356, Z46357, Z46358, Z46359, Z46360, Z46361, Z46362, Z46363, Z46364, Z46365, Z46366, Z46367, Z46368, Z46369 Genomic DNA. Translation: CAA86476.2.
AF148513 mRNA. Translation: AAD30174.1.
AY623118 Genomic DNA. Translation: AAT38114.1.
CH471053 Genomic DNA. Translation: EAW99601.1.
CH471053 Genomic DNA. Translation: EAW99602.1.
BC021116 mRNA. Translation: AAH21116.1.
BC064369 mRNA. Translation: AAH64369.1.
D25412 Genomic DNA. Translation: BAA04999.1.
CCDSiCCDS1956.1.
PIRiS48809. JC2025.
RefSeqiNP_000180.2. NM_000189.4.
UniGeneiHs.406266.
Hs.591588.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2NZTX-ray2.45A/B17-916[»]
5HEXX-ray2.73A/B17-917[»]
5HFUX-ray2.92A/B17-917[»]
5HG1X-ray2.76A17-916[»]
ProteinModelPortaliP52789.
SMRiP52789.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109346. 46 interactors.
DIPiDIP-50110N.
IntActiP52789. 14 interactors.
MINTiMINT-1461614.
STRINGi9606.ENSP00000290573.

Chemistry databases

ChEMBLiCHEMBL2640.

PTM databases

iPTMnetiP52789.
PhosphoSitePlusiP52789.
SwissPalmiP52789.

Polymorphism and mutation databases

BioMutaiHK2.
DMDMi56405344.

Proteomic databases

EPDiP52789.
MaxQBiP52789.
PaxDbiP52789.
PeptideAtlasiP52789.
PRIDEiP52789.

Protocols and materials databases

DNASUi3099.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000290573; ENSP00000290573; ENSG00000159399.
GeneIDi3099.
KEGGihsa:3099.
UCSCiuc002snd.4. human.

Organism-specific databases

CTDi3099.
DisGeNETi3099.
GeneCardsiHK2.
H-InvDBHIX0030207.
HGNCiHGNC:4923. HK2.
HPAiHPA028587.
MIMi601125. gene.
neXtProtiNX_P52789.
OpenTargetsiENSG00000159399.
PharmGKBiPA29301.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1369. Eukaryota.
COG5026. LUCA.
GeneTreeiENSGT00390000017159.
HOGENOMiHOG000162671.
HOVERGENiHBG005020.
InParanoidiP52789.
KOiK00844.
OMAiHHLGLES.
OrthoDBiEOG091G08MD.
PhylomeDBiP52789.
TreeFamiTF314238.

Enzyme and pathway databases

UniPathwayiUPA00242.
BioCyciMetaCyc:HS08399-MONOMER.
ZFISH:HS08399-MONOMER.
BRENDAi2.7.1.1. 2681.
ReactomeiR-HSA-70153. Glucose transport.
R-HSA-70171. Glycolysis.
SABIO-RKP52789.

Miscellaneous databases

ChiTaRSiHK2. human.
EvolutionaryTraceiP52789.
GeneWikiiHK2.
GenomeRNAii3099.
PROiP52789.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000159399.
CleanExiHS_HK2.
ExpressionAtlasiP52789. baseline and differential.
GenevisibleiP52789. HS.

Family and domain databases

InterProiIPR001312. Hexokinase.
IPR019807. Hexokinase_BS.
IPR022673. Hexokinase_C.
IPR022672. Hexokinase_N.
[Graphical view]
PANTHERiPTHR19443. PTHR19443. 1 hit.
PfamiPF00349. Hexokinase_1. 2 hits.
PF03727. Hexokinase_2. 2 hits.
[Graphical view]
PROSITEiPS00378. HEXOKINASE_1. 2 hits.
PS51748. HEXOKINASE_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHXK2_HUMAN
AccessioniPrimary (citable) accession number: P52789
Secondary accession number(s): D6W5J2, Q8WU87, Q9UN82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 7, 2004
Last modified: November 2, 2016
This is version 172 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

Miscellaneous

In vertebrates there are four major glucose-phosphorylating isoenzymes, designated hexokinase I, II, III and IV (glucokinase).

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.