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Q9BXM7

- PINK1_HUMAN

UniProt

Q9BXM7 - PINK1_HUMAN

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Protein

Serine/threonine-protein kinase PINK1, mitochondrial

Gene

PINK1

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

Functioni

Protects against mitochondrial dysfunction during cellular stress by phosphorylating mitochondrial proteins. Involved in the clearance of damaged mitochondria via selective autophagy (mitophagy) by mediating activation and translocation of PARK2. Targets PARK2 to dysfunctional depolarized mitochondria through the phosphorylation of MFN2. Activates PARK2 in 2 steps: (1) by mediating phosphorylation at 'Ser-65' of PARK2 and (2) mediating phosphorylation of ubiquitin, converting PARK2 to its fully-active form (PubMed:24660806, PubMed:24751536, PubMed:24784582).12 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.3 Publications

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei186 – 1861ATPPROSITE-ProRule annotation
Active sitei362 – 3621Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi162 – 1709ATPBy similarityPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. C3HC4-type RING finger domain binding Source: BHF-UCL
  3. calcium-dependent protein kinase activity Source: BHF-UCL
  4. kinase activity Source: ParkinsonsUK-UCL
  5. magnesium ion binding Source: UniProtKB
  6. peptidase activator activity Source: ParkinsonsUK-UCL
  7. protease binding Source: ParkinsonsUK-UCL
  8. protein kinase B binding Source: ParkinsonsUK-UCL
  9. protein serine/threonine kinase activity Source: UniProtKB
  10. ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  1. activation of protein kinase B activity Source: ParkinsonsUK-UCL
  2. cell death Source: UniProtKB-KW
  3. cellular response to hypoxia Source: ParkinsonsUK-UCL
  4. cellular response to toxic substance Source: ParkinsonsUK-UCL
  5. intracellular signal transduction Source: UniProtKB
  6. mitochondrion degradation Source: UniProtKB
  7. mitochondrion organization Source: ParkinsonsUK-UCL
  8. negative regulation of gene expression Source: ParkinsonsUK-UCL
  9. negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
  10. negative regulation of JNK cascade Source: ParkinsonsUK-UCL
  11. negative regulation of neuron apoptotic process Source: ParkinsonsUK-UCL
  12. negative regulation of oxidative stress-induced cell death Source: ParkinsonsUK-UCL
  13. negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
  14. negative regulation of oxidative stress-induced neuron death Source: ParkinsonsUK-UCL
  15. negative regulation of reactive oxygen species metabolic process Source: ParkinsonsUK-UCL
  16. peptidyl-serine autophosphorylation Source: ParkinsonsUK-UCL
  17. peptidyl-serine phosphorylation Source: BHF-UCL
  18. phosphorylation Source: ParkinsonsUK-UCL
  19. positive regulation of dopamine secretion Source: Ensembl
  20. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: BHF-UCL
  21. positive regulation of mitochondrial electron transport, NADH to ubiquinone Source: ParkinsonsUK-UCL
  22. positive regulation of peptidase activity Source: ParkinsonsUK-UCL
  23. positive regulation of peptidyl-serine phosphorylation Source: ParkinsonsUK-UCL
  24. positive regulation of protein kinase B signaling Source: ParkinsonsUK-UCL
  25. positive regulation of release of cytochrome c from mitochondria Source: BHF-UCL
  26. positive regulation of synaptic transmission, dopaminergic Source: Ensembl
  27. positive regulation of ubiquitin-protein transferase activity Source: ParkinsonsUK-UCL
  28. protein phosphorylation Source: UniProtKB
  29. protein ubiquitination Source: UniProtKB
  30. regulation of mitochondrial membrane potential Source: ParkinsonsUK-UCL
  31. regulation of mitochondrion degradation Source: ParkinsonsUK-UCL
  32. regulation of protein complex assembly Source: BHF-UCL
  33. regulation of protein ubiquitination Source: BHF-UCL
  34. regulation of reactive oxygen species metabolic process Source: ParkinsonsUK-UCL
  35. regulation of synaptic vesicle transport Source: ParkinsonsUK-UCL
  36. response to oxidative stress Source: ParkinsonsUK-UCL
  37. response to stress Source: UniProtKB
  38. TORC2 signaling Source: ParkinsonsUK-UCL
  39. ubiquitin-dependent protein catabolic process Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Autophagy

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ9BXM7.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase PINK1, mitochondrial (EC:2.7.11.13 Publications)
Alternative name(s):
BRPK
PTEN-induced putative kinase protein 1
Gene namesi
Name:PINK1
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:14581. PINK1.

Subcellular locationi

Mitochondrion outer membrane; Single-pass membrane protein 4 Publications. Cytoplasmcytosol 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini78 – 9316Mitochondrial intermembraneSequence AnalysisAdd
BLAST
Transmembranei94 – 11017HelicalSequence AnalysisAdd
BLAST
Topological domaini111 – 581471CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. astrocyte projection Source: ParkinsonsUK-UCL
  2. axon Source: ParkinsonsUK-UCL
  3. cell body Source: ParkinsonsUK-UCL
  4. chromatin Source: ParkinsonsUK-UCL
  5. cytoplasm Source: ParkinsonsUK-UCL
  6. cytoskeleton Source: ParkinsonsUK-UCL
  7. cytosol Source: UniProtKB
  8. integral component of mitochondrial outer membrane Source: ParkinsonsUK-UCL
  9. Lewy body Source: ParkinsonsUK-UCL
  10. membrane Source: ParkinsonsUK-UCL
  11. mitochondrial inner membrane Source: ParkinsonsUK-UCL
  12. mitochondrial intermembrane space Source: ParkinsonsUK-UCL
  13. mitochondrial outer membrane Source: ParkinsonsUK-UCL
  14. mitochondrion Source: UniProtKB
  15. nucleus Source: ParkinsonsUK-UCL
  16. perinuclear region of cytoplasm Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Involvement in diseasei

Parkinson disease 6 (PARK6) [MIM:605909]: A neurodegenerative disorder characterized by parkinsonian signs such as rigidity, resting tremor and bradykinesia. A subset of patients manifest additional symptoms including hyperreflexia, autonomic instability, dementia and psychiatric disturbances. Symptoms show diurnal fluctuation and can improve after sleep.17 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti92 – 921C → F in PARK6. 1 Publication
VAR_046568
Natural varianti125 – 1251C → G in PARK6. 1 Publication
VAR_062773
Natural varianti126 – 1261Q → P in PARK6; strongly reduces interaction with PARK2. 1 Publication
VAR_064344
Natural varianti147 – 1471R → H in PARK6; unknown pathological significance. 1 Publication
VAR_046574
Natural varianti168 – 1681A → P in PARK6; has reduced autophosphorylation activity compared to wild-type; localizes to the mitochondria and immunogold experiments reveal that both wild-type and mutant proteins face the mitochondrial intermembrane space. 2 Publications
VAR_046575
Natural varianti196 – 1961P → L in PARK6. 1 Publication
VAR_046577
Natural varianti217 – 2171A → D in PARK6. 1 Publication
VAR_046578
Natural varianti240 – 2401E → K in PARK6. 2 Publications
VAR_046581
Natural varianti268 – 2681L → V in PARK6. 2 Publications
VAR_046584
Natural varianti271 – 2711H → Q in PARK6. 1 Publication
VAR_046585
Natural varianti279 – 2791R → H in PARK6. 1 Publication
VAR_046587
Natural varianti280 – 2801A → T in PARK6; early-onset. 1 Publication
VAR_062774
Natural varianti309 – 3091G → D in PARK6; fails to maintain mitochondrial membrane potential; has reduced autophosphorylation activity compared to wild-type; strongly reduces interaction with PARK2. 1 Publication
VAR_018994
Natural varianti313 – 3131T → M in PARK6. 1 Publication
VAR_046589
Natural varianti347 – 3471L → P in PARK6; strongly reduces interaction with PARK2. 3 Publications
VAR_046593
Natural varianti369 – 3691L → P in PARK6. 1 Publication
VAR_062775
Natural varianti386 – 3861G → A in PARK6; abolishes kinase activity. 1 Publication
VAR_062776
Natural varianti388 – 3881C → R in PARK6. 1 Publication
VAR_046596
Natural varianti399 – 3991P → L in PARK6; digenic inheritance; associated with Ser-39 mutation in PARK7 gene. 1 Publication
VAR_062777
Natural varianti407 – 4071R → Q in PARK6; early-onset. 1 Publication
VAR_062778
Natural varianti409 – 4091G → V in PARK6. 1 Publication
VAR_062779
Natural varianti417 – 4171E → G in PARK6. 1 Publication
VAR_046599
Natural varianti464 – 4641R → H in PARK6. 1 Publication
VAR_046605
Natural varianti489 – 4891L → P in PARK6. 1 Publication
VAR_046607
Natural varianti534 – 5341Q → QQ in PARK6. 1 Publication
VAR_046610

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi219 – 2191K → A: Abolishes MFN2 phosphorylation and interaction with PARK2; when associated with ALA-362 and ALA-384. 1 Publication
Mutagenesisi362 – 3621D → A: Abolishes MFN2 phosphorylation and interaction with PARK2; when associated with ALA-219 and ALA-384. 1 Publication
Mutagenesisi384 – 3841D → A: Abolishes MFN2 phosphorylation and interaction with PARK2; when associated with ALA-219 and ALA-362. 1 Publication

Keywords - Diseasei

Disease mutation, Neurodegeneration, Parkinson disease, Parkinsonism

Organism-specific databases

MIMi168600. phenotype.
605909. phenotype.
Orphaneti2828. Young adult-onset Parkinsonism.
PharmGKBiPA33325.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 7777MitochondrionSequence AnalysisAdd
BLAST
Chaini78 – 581504Serine/threonine-protein kinase PINK1, mitochondrialPRO_0000024369Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei228 – 2281Phosphoserine; by autocatalysis1 Publication
Modified residuei402 – 4021Phosphoserine; by autocatalysis1 Publication

Post-translational modificationi

Autophosphorylation at Ser-228 and Ser-402 is essential for Parkin/PARK2 recruitment to depolarized mitochondria.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9BXM7.
PRIDEiQ9BXM7.

PTM databases

PhosphoSiteiQ9BXM7.

Expressioni

Tissue specificityi

Highly expressed in heart, skeletal muscle and testis, and at lower levels in brain, placenta, liver, kidney, pancreas, prostate, ovary and small intestine. Present in the embryonic testis from an early stage of development.1 Publication

Gene expression databases

BgeeiQ9BXM7.
CleanExiHS_PINK1.
GenevestigatoriQ9BXM7.

Organism-specific databases

HPAiCAB026191.
HPA001931.

Interactioni

Subunit structurei

Interacts with PARK2. Interacts with FBXO7.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EEDO755306EBI-2846068,EBI-923794
FBXO7Q9Y3I18EBI-2846068,EBI-1161222
FBXO7Q9Y3I1-12EBI-2846068,EBI-9102965
MAP1LC3BQ9GZQ83EBI-2846068,EBI-373144
PARK2O602607EBI-2846068,EBI-716346
RHOT1Q8IXI23EBI-2846068,EBI-1396430

Protein-protein interaction databases

BioGridi122376. 54 interactions.
DIPiDIP-29427N.
IntActiQ9BXM7. 11 interactions.
MINTiMINT-6781189.
STRINGi9606.ENSP00000364204.

Structurei

3D structure databases

ProteinModelPortaliQ9BXM7.
SMRiQ9BXM7. Positions 246-545.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini156 – 511356Protein kinaseCuratedPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00390000001206.
HOGENOMiHOG000231649.
HOVERGENiHBG053601.
InParanoidiQ9BXM7.
KOiK05688.
OMAiGPKQLAP.
OrthoDBiEOG7TBC1R.
PhylomeDBiQ9BXM7.
TreeFamiTF313183.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 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 11 Publication (identifier: Q9BXM7-1) [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
MAVRQALGRG LQLGRALLLR FTGKPGRAYG LGRPGPAAGC VRGERPGWAA
60 70 80 90 100
GPGAEPRRVG LGLPNRLRFF RQSVAGLAAR LQRQFVVRAW GCAGPCGRAV
110 120 130 140 150
FLAFGLGLGL IEEKQAESRR AVSACQEIQA IFTQKSKPGP DPLDTRRLQG
160 170 180 190 200
FRLEEYLIGQ SIGKGCSAAV YEATMPTLPQ NLEVTKSTGL LPGRGPGTSA
210 220 230 240 250
PGEGQERAPG APAFPLAIKM MWNISAGSSS EAILNTMSQE LVPASRVALA
260 270 280 290 300
GEYGAVTYRK SKRGPKQLAP HPNIIRVLRA FTSSVPLLPG ALVDYPDVLP
310 320 330 340 350
SRLHPEGLGH GRTLFLVMKN YPCTLRQYLC VNTPSPRLAA MMLLQLLEGV
360 370 380 390 400
DHLVQQGIAH RDLKSDNILV ELDPDGCPWL VIADFGCCLA DESIGLQLPF
410 420 430 440 450
SSWYVDRGGN GCLMAPEVST ARPGPRAVID YSKADAWAVG AIAYEIFGLV
460 470 480 490 500
NPFYGQGKAH LESRSYQEAQ LPALPESVPP DVRQLVRALL QREASKRPSA
510 520 530 540 550
RVAANVLHLS LWGEHILALK NLKLDKMVGW LLQQSAATLL ANRLTEKCCV
560 570 580
ETKMKMLFLA NLECETLCQA ALLLCSWRAA L
Length:581
Mass (Da):62,769
Last modified:June 1, 2001 - v1
Checksum:i721FE01F63263A64
GO
Isoform 2Curated (identifier: Q9BXM7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-307: Missing.
     308-320: LGHGRTLFLVMKN → MCGSQRPSPLSTS

Note: No experimental confirmation available.Curated

Show »
Length:274
Mass (Da):30,104
Checksum:iC54C628F879B4BED
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti209 – 2091P → A in AAH28215. (PubMed:15489334)Curated
Sequence conflicti419 – 4191S → P in BAC11484. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671L → F.1 Publication
VAR_046566
Natural varianti68 – 681R → P.1 Publication
VAR_046567
Natural varianti92 – 921C → F in PARK6. 1 Publication
VAR_046568
Natural varianti98 – 981R → W.1 Publication
VAR_046569
Natural varianti111 – 1111I → S.1 Publication
VAR_046570
Natural varianti115 – 1151Q → L.2 Publications
Corresponds to variant rs148871409 [ dbSNP | Ensembl ].
VAR_046571
Natural varianti124 – 1241A → V.1 Publication
VAR_046572
Natural varianti125 – 1251C → G in PARK6. 1 Publication
VAR_062773
Natural varianti126 – 1261Q → P in PARK6; strongly reduces interaction with PARK2. 1 Publication
VAR_064344
Natural varianti145 – 1451T → M.1 Publication
Corresponds to variant rs45604240 [ dbSNP | Ensembl ].
VAR_046573
Natural varianti147 – 1471R → H in PARK6; unknown pathological significance. 1 Publication
VAR_046574
Natural varianti148 – 1481L → W.1 Publication
Corresponds to variant rs56297806 [ dbSNP | Ensembl ].
VAR_041010
Natural varianti168 – 1681A → P in PARK6; has reduced autophosphorylation activity compared to wild-type; localizes to the mitochondria and immunogold experiments reveal that both wild-type and mutant proteins face the mitochondrial intermembrane space. 2 Publications
VAR_046575
Natural varianti186 – 1861K → N.1 Publication
VAR_046576
Natural varianti196 – 1961P → L in PARK6. 1 Publication
VAR_046577
Natural varianti196 – 1961P → S.1 Publication
Corresponds to variant rs35802484 [ dbSNP | Ensembl ].
VAR_041011
Natural varianti209 – 2091P → L.1 Publication
Corresponds to variant rs34677717 [ dbSNP | Ensembl ].
VAR_041012
Natural varianti215 – 2151P → L in a glioblastoma multiforme sample; somatic mutation. 1 Publication
VAR_041013
Natural varianti217 – 2171A → D in PARK6. 1 Publication
VAR_046578
Natural varianti231 – 2311E → G.1 Publication
VAR_046579
Natural varianti235 – 2351N → I.1 Publication
VAR_046580
Natural varianti240 – 2401E → K in PARK6. 2 Publications
VAR_046581
Natural varianti257 – 2571T → I.
VAR_046582
Natural varianti263 – 2631R → G.1 Publication
VAR_046583
Natural varianti268 – 2681L → V in PARK6. 2 Publications
VAR_046584
Natural varianti271 – 2711H → Q in PARK6. 1 Publication
VAR_046585
Natural varianti276 – 2761R → Q.1 Publication
VAR_046586
Natural varianti279 – 2791R → H in PARK6. 1 Publication
VAR_046587
Natural varianti280 – 2801A → T in PARK6; early-onset. 1 Publication
VAR_062774
Natural varianti296 – 2961P → L.2 Publications
VAR_046588
Natural varianti305 – 3051P → L.
Corresponds to variant rs7349186 [ dbSNP | Ensembl ].
VAR_018993
Natural varianti309 – 3091G → D in PARK6; fails to maintain mitochondrial membrane potential; has reduced autophosphorylation activity compared to wild-type; strongly reduces interaction with PARK2. 1 Publication
VAR_018994
Natural varianti313 – 3131T → M in PARK6. 1 Publication
VAR_046589
Natural varianti317 – 3171V → I.2 Publications
Corresponds to variant rs200949139 [ dbSNP | Ensembl ].
VAR_046590
Natural varianti318 – 3181M → L.1 Publication
VAR_046591
Natural varianti322 – 3221P → L.1 Publication
VAR_046592
Natural varianti339 – 3391A → T.4 Publications
Corresponds to variant rs55831733 [ dbSNP | Ensembl ].
VAR_041014
Natural varianti340 – 3401A → T.7 Publications
Corresponds to variant rs3738136 [ dbSNP | Ensembl ].
VAR_018995
Natural varianti341 – 3411M → I.1 Publication
Corresponds to variant rs35813094 [ dbSNP | Ensembl ].
VAR_041015
Natural varianti347 – 3471L → P in PARK6; strongly reduces interaction with PARK2. 3 Publications
VAR_046593
Natural varianti362 – 3621D → H.1 Publication
VAR_046594
Natural varianti369 – 3691L → P in PARK6. 1 Publication
VAR_062775
Natural varianti377 – 3771C → F.1 Publication
Corresponds to variant rs34203620 [ dbSNP | Ensembl ].
VAR_041016
Natural varianti383 – 3831A → T.2 Publications
Corresponds to variant rs45515602 [ dbSNP | Ensembl ].
VAR_046595
Natural varianti386 – 3861G → A in PARK6; abolishes kinase activity. 1 Publication
VAR_062776
Natural varianti388 – 3881C → R in PARK6. 1 Publication
VAR_046596
Natural varianti395 – 3951G → V.1 Publication
VAR_046597
Natural varianti399 – 3991P → L in PARK6; digenic inheritance; associated with Ser-39 mutation in PARK7 gene. 1 Publication
VAR_062777
Natural varianti407 – 4071R → Q in PARK6; early-onset. 1 Publication
VAR_062778
Natural varianti409 – 4091G → V in PARK6. 1 Publication
VAR_062779
Natural varianti411 – 4111G → S.1 Publication
Corresponds to variant rs45478900 [ dbSNP | Ensembl ].
VAR_046598
Natural varianti417 – 4171E → G in PARK6. 1 Publication
VAR_046599
Natural varianti425 – 4251P → S.1 Publication
VAR_046600
Natural varianti431 – 4311Y → H May predispose to Parkinson disease development; shows decreased mitochondrial membrane potential under stress conditions. 1 Publication
VAR_046601
Natural varianti442 – 4421I → T.2 Publications
VAR_046602
Natural varianti451 – 4511N → S May predispose to Parkinson disease development; shows decreased mitochondrial membrane potential under stress conditions. 1 Publication
VAR_046603
Natural varianti461 – 4611L → S.1 Publication
VAR_046604
Natural varianti464 – 4641R → H in PARK6. 1 Publication
VAR_046605
Natural varianti476 – 4761E → K May predispose to Parkinson disease development; shows decreased mitochondrial membrane potential under stress conditions. 5 Publications
Corresponds to variant rs115477764 [ dbSNP | Ensembl ].
VAR_046606
Natural varianti477 – 4771S → T.1 Publication
Corresponds to variant rs34416410 [ dbSNP | Ensembl ].
VAR_041017
Natural varianti489 – 4891L → P in PARK6. 1 Publication
VAR_046607
Natural varianti501 – 5011R → P May predispose to Parkinson disease development; shows decreased mitochondrial membrane potential under stress conditions. 1 Publication
VAR_046608
Natural varianti521 – 5211N → T.7 Publications
Corresponds to variant rs1043424 [ dbSNP | Ensembl ].
VAR_018996
Natural varianti525 – 5251D → N.2 Publications
VAR_046609
Natural varianti534 – 5341Q → QQ in PARK6. 1 Publication
VAR_046610
Natural varianti537 – 5371A → T.1 Publication
VAR_046611
Natural varianti575 – 5751C → R May predispose to Parkinson disease development; shows decreased mitochondrial membrane potential under stress conditions. 1 Publication
VAR_046612

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 307307Missing in isoform 2. 1 PublicationVSP_050754Add
BLAST
Alternative sequencei308 – 32013LGHGR…LVMKN → MCGSQRPSPLSTS in isoform 2. 1 PublicationVSP_050755Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB053323 mRNA. Translation: BAB55647.1.
AF316873 mRNA. Translation: AAK28062.1.
AK075225 mRNA. Translation: BAC11484.1.
AL391357 Genomic DNA. Translation: CAH73475.1.
BC009534 mRNA. Translation: AAH09534.1.
BC028215 mRNA. Translation: AAH28215.1.
CCDSiCCDS211.1. [Q9BXM7-1]
RefSeqiNP_115785.1. NM_032409.2. [Q9BXM7-1]
UniGeneiHs.389171.

Genome annotation databases

GeneIDi65018.
KEGGihsa:65018.
UCSCiuc001bdm.3. human. [Q9BXM7-1]
uc001bdn.3. human. [Q9BXM7-2]

Polymorphism databases

DMDMi48428484.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB053323 mRNA. Translation: BAB55647.1 .
AF316873 mRNA. Translation: AAK28062.1 .
AK075225 mRNA. Translation: BAC11484.1 .
AL391357 Genomic DNA. Translation: CAH73475.1 .
BC009534 mRNA. Translation: AAH09534.1 .
BC028215 mRNA. Translation: AAH28215.1 .
CCDSi CCDS211.1. [Q9BXM7-1 ]
RefSeqi NP_115785.1. NM_032409.2. [Q9BXM7-1 ]
UniGenei Hs.389171.

3D structure databases

ProteinModelPortali Q9BXM7.
SMRi Q9BXM7. Positions 246-545.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122376. 54 interactions.
DIPi DIP-29427N.
IntActi Q9BXM7. 11 interactions.
MINTi MINT-6781189.
STRINGi 9606.ENSP00000364204.

PTM databases

PhosphoSitei Q9BXM7.

Polymorphism databases

DMDMi 48428484.

Proteomic databases

PaxDbi Q9BXM7.
PRIDEi Q9BXM7.

Protocols and materials databases

DNASUi 65018.
Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 65018.
KEGGi hsa:65018.
UCSCi uc001bdm.3. human. [Q9BXM7-1 ]
uc001bdn.3. human. [Q9BXM7-2 ]

Organism-specific databases

CTDi 65018.
GeneCardsi GC01P020959.
GeneReviewsi PINK1.
HGNCi HGNC:14581. PINK1.
HPAi CAB026191.
HPA001931.
MIMi 168600. phenotype.
605909. phenotype.
608309. gene.
neXtProti NX_Q9BXM7.
Orphaneti 2828. Young adult-onset Parkinsonism.
PharmGKBi PA33325.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00390000001206.
HOGENOMi HOG000231649.
HOVERGENi HBG053601.
InParanoidi Q9BXM7.
KOi K05688.
OMAi GPKQLAP.
OrthoDBi EOG7TBC1R.
PhylomeDBi Q9BXM7.
TreeFami TF313183.

Enzyme and pathway databases

SignaLinki Q9BXM7.

Miscellaneous databases

ChiTaRSi PINK1. human.
GeneWikii PINK1.
GenomeRNAii 65018.
NextBioi 67218.
PROi Q9BXM7.
SOURCEi Search...

Gene expression databases

Bgeei Q9BXM7.
CleanExi HS_PINK1.
Genevestigatori Q9BXM7.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 2 hits.
PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Growth-suppressive effects of BPOZ and EGR2, two genes involved in the PTEN signaling pathway."
    Unoki M., Nakamura Y.
    Oncogene 20:4457-4465(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Endometrium1 Publication.
  2. "BRPK, a novel protein kinase showing increased expression in mouse cancer cell lines with higher metastatic potential."
    Nakajima A., Kataoka K., Hong M., Sakaguchi M., Huh N.-H.
    Cancer Lett. 201:195-201(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AUTOPHOSPHORYLATION.
    Tissue: PlacentaImported.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS THR-340 AND THR-521.
    Tissue: PlacentaImported.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 1).
    Tissue: LeukocyteImported and LungImported.
  6. Cited for: SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY.
  7. "The PINK1/Parkin-mediated mitophagy is compromised by PD-associated mutations."
    Geisler S., Holmstrom K.M., Treis A., Skujat D., Weber S.S., Fiesel F.C., Kahle P.J., Springer W.
    Autophagy 6:871-878(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MITOCHONDRIAL AUTOPHAGY, SUBCELLULAR LOCATION, INTERACTION WITH PARK2, CHARACTERIZATION OF VARIANTS PARK6 PRO-126; ASP-309 AND PRO-347.
  8. "PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy."
    Matsuda N., Sato S., Shiba K., Okatsu K., Saisho K., Gautier C.A., Sou Y.S., Saiki S., Kawajiri S., Sato F., Kimura M., Komatsu M., Hattori N., Tanaka K.
    J. Cell Biol. 189:211-221(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MITOCHONDRIAL AUTOPHAGY.
  9. Cited for: FUNCTION IN MITOCHONDRIAL AUTOPHAGY, INTERACTION WITH PARK2.
  10. "PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria."
    Okatsu K., Oka T., Iguchi M., Imamura K., Kosako H., Tani N., Kimura M., Go E., Koyano F., Funayama M., Shiba-Fukushima K., Sato S., Shimizu H., Fukunaga Y., Taniguchi H., Komatsu M., Hattori N., Mihara K., Tanaka K., Matsuda N.
    Nat. Commun. 3:1016-1016(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-228 AND SER-402.
  11. "Parkin-catalyzed ubiquitin-ester transfer is triggered by PINK1-dependent phosphorylation."
    Iguchi M., Kujuro Y., Okatsu K., Koyano F., Kosako H., Kimura M., Suzuki N., Uchiyama S., Tanaka K., Matsuda N.
    J. Biol. Chem. 288:22019-22032(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FBXO7.
  13. "PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria."
    Chen Y., Dorn G.W. II
    Science 340:471-475(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MITOPHAGY, MUTAGENESIS OF LYS-219; ASP-362 AND ASP-384.
  14. Cited for: FUNCTION, CATALYTIC ACTIVITY.
  15. "PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity."
    Kane L.A., Lazarou M., Fogel A.I., Li Y., Yamano K., Sarraf S.A., Banerjee S., Youle R.J.
    J. Cell Biol. 205:143-153(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  16. Cited for: FUNCTION, CATALYTIC ACTIVITY, CHARACTERIZATION OF VARIANTS PARK6 PRO-168 AND ALA-386.
  17. "The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy."
    Bingol B., Tea J.S., Phu L., Reichelt M., Bakalarski C.E., Song Q., Foreman O., Kirkpatrick D.S., Sheng M.
    Nature 510:370-375(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. Cited for: VARIANTS PARK6 PHE-92; PRO-168 AND HIS-464, VARIANTS LEU-296; THR-340; THR-442; LYS-476; THR-521 AND ASN-525.
  19. Cited for: VARIANTS PARK6 GLN-271; PRO-347 AND GLY-417.
  20. Cited for: VARIANTS PARK6 LYS-240; PRO-347 AND PRO-489, VARIANTS GLY-231; ILE-235; GLY-263; LEU-318; THR-339; THR-340; HIS-362; SER-425; LYS-476 AND THR-521.
  21. Cited for: VARIANT PARK6 HIS-147.
  22. Cited for: VARIANT PARK6 ASP-309, CHARACTERIZATION OF VARIANT PARK6 ASP-309, FUNCTION, SUBCELLULAR LOCATION.
  23. Cited for: VARIANT PARK6 VAL-268.
  24. Cited for: VARIANTS PARK6 HIS-279 AND GLN-534 INS, VARIANT LEU-115.
  25. "Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive parkinsonism."
    Silvestri L., Caputo V., Bellacchio E., Atorino L., Dallapiccola B., Valente E.M., Casari G.
    Hum. Mol. Genet. 14:3477-3492(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS PARK6 PRO-168 AND ASP-309.
  26. "Clinicogenetic study of PINK1 mutations in autosomal recessive early-onset parkinsonism."
    Li Y., Tomiyama H., Sato K., Hatano Y., Yoshino H., Atsumi M., Kitaguchi M., Sasaki S., Kawaguchi S., Miyajima H., Toda T., Mizuno Y., Hattori N.
    Neurology 64:1955-1957(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PARK6 ARG-388.
  27. Cited for: VARIANTS PARK6 PRO-168 AND LEU-196, VARIANTS LEU-115; THR-340; LYS-476 AND THR-521.
  28. Cited for: VARIANTS ILE-317; THR-339; THR-383; SER-411; HIS-431; SER-451; SER-461; LYS-476; PRO-501 AND ARG-575, CHARACTERIZATION OF VARIANTS HIS-431; SER-451; LYS-476; PRO-501 AND ARG-575.
  29. "Juvenile-onset Parkinsonism as a result of the first mutation in the adenosine triphosphate orientation domain of PINK1."
    Leutenegger A.-L., Salih M.A.M., Ibanez P., Mukhtar M.M., Lesage S., Arabi A., Lohmann E., Duerr A., Ahmed A.E.M., Brice A.
    Arch. Neurol. 63:1257-1261(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PARK6 ASP-217.
  30. "T313M PINK1 mutation in an extended highly consanguineous Saudi family with early-onset Parkinson disease."
    Chishti M.A., Bohlega S., Ahmed M., Loualich A., Carroll P., Sato C., St George-Hyslop P., Westaway D., Rogaeva E.
    Arch. Neurol. 63:1483-1485(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PARK6 MET-313.
  31. "Mutational analysis of the PINK1 gene in early-onset parkinsonism in Europe and North Africa."
    The French Parkinson's disease genetics study group
    Ibanez P., Lesage S., Lohmann E., Thobois S., De Michele G., Borg M., Agid Y., Durr A., Brice A.
    Brain 129:686-694(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PARK6 GLY-125; LYS-240; PRO-369; ALA-386 AND VAL-409.
  32. "Association of PINK1 and DJ-1 confers digenic inheritance of early-onset Parkinson's disease."
    Tang B., Xiong H., Sun P., Zhang Y., Wang D., Hu Z., Zhu Z., Ma H., Pan Q., Xia J.-H., Xia K., Zhang Z.
    Hum. Mol. Genet. 15:1816-1825(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PARK6 LEU-399.
  33. Cited for: VARIANT PARK6 THR-280, VARIANTS THR-340 AND THR-521.
  34. "Analysis of the PINK1 gene in a cohort of patients with sporadic early-onset parkinsonism in Taiwan."
    Fung H.-C., Chen C.-M., Hardy J., Singleton A.B., Lee-Chen G.-J., Wu Y.-R.
    Neurosci. Lett. 394:33-36(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PARK6 GLN-407, VARIANTS THR-340 AND THR-521.
  35. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] TRP-148; SER-196; LEU-209; LEU-215; THR-339; THR-340; ILE-341; PHE-377; THR-477 AND THR-521.
  36. Cited for: VARIANTS PHE-67; PRO-68; TRP-98; SER-111; VAL-124; MET-145; ASN-186; ILE-257 VAL-268; GLN-276; LEU-296; ILE-317; LEU-322; THR-339; THR-383; VAL-395; THR-442; LYS-476; ASN-525 AND THR-537.
  37. "Clinical and molecular characterisation of a Parkinson family with a novel PINK1 mutation."
    Prestel J., Gempel K., Hauser T.K., Schweitzer K., Prokisch H., Ahting U., Freudenstein D., Bueltmann E., Naegele T., Berg D., Klopstock T., Gasser T.
    J. Neurol. 255:643-648(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PARK6 PRO-126.
  38. Cited for: VARIANT PARK6 PRO-347.

Entry informationi

Entry nameiPINK1_HUMAN
AccessioniPrimary (citable) accession number: Q9BXM7
Secondary accession number(s): Q8N6T9, Q8NBU3, Q96DE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 1, 2001
Last modified: November 26, 2014
This is version 133 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3