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Protein

Serine/threonine-protein kinase Nek6

Gene

NEK6

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

Functioni

Protein kinase which plays an important role in mitotic cell cycle progression. Required for chromosome segregation at metaphase-anaphase transition, robust mitotic spindle formation and cytokinesis. Phosphorylates ATF4, CIR1, PTN, RAD26L, RBBP6, RPS7, RPS6KB1, TRIP4, STAT3 and histones H1 and H3. Phosphorylates KIF11 to promote mitotic spindle formation. Involved in G2/M phase cell cycle arrest induced by DNA damage. Inhibition of activity results in apoptosis. May contribute to tumorigenesis by suppressing p53/TP53-induced cancer cell senescence.8 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Enzyme regulationi

Binding to NEK9 stimulates its activity by releasing the autoinhibitory function of Tyr-108.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei74 – 741ATPPROSITE-ProRule annotation
Sitei108 – 1081Autoinhibitory
Active sitei172 – 1721Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi51 – 599ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • kinesin binding Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB
  • signal transducer activity Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • chromosome segregation Source: UniProtKB
  • cytokinesis Source: UniProtKB
  • G2 DNA damage checkpoint Source: UniProtKB
  • mitotic nuclear division Source: UniProtKB-KW
  • mitotic nuclear envelope disassembly Source: Reactome
  • peptidyl-serine phosphorylation Source: UniProtKB
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • protein autophosphorylation Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • regulation of cellular senescence Source: UniProtKB
  • regulation of mitotic cell cycle Source: UniProtKB
  • regulation of mitotic metaphase/anaphase transition Source: UniProtKB
  • spindle assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Cell cycle, Cell division, Chromosome partition, Mitosis

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiR-HSA-2980767. Activation of NIMA Kinases NEK9, NEK6, NEK7.
R-HSA-3301854. Nuclear Pore Complex (NPC) Disassembly.
SignaLinkiQ9HC98.
SIGNORiQ9HC98.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase Nek6 (EC:2.7.11.1)
Alternative name(s):
Never in mitosis A-related kinase 6
Short name:
NimA-related protein kinase 6
Protein kinase SID6-1512
Gene namesi
Name:NEK6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:7749. NEK6.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • intracellular membrane-bounded organelle Source: HPA
  • microtubule Source: UniProtKB-KW
  • microtubule organizing center Source: HPA
  • nuclear speck Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • spindle pole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi74 – 741K → M: Loss of autophosphorylation and of kinase activity and induction of apoptosis; when associated with M-75. 2 Publications
Mutagenesisi75 – 751K → M: Loss of autophosphorylation and of kinase activity and induction of apoptosis; when associated with M-74. 2 Publications
Mutagenesisi108 – 1081Y → A: Increase in catalytic activity. 1 Publication

Organism-specific databases

PharmGKBiPA31550.

Chemistry

ChEMBLiCHEMBL4309.
GuidetoPHARMACOLOGYi2121.

Polymorphism and mutation databases

BioMutaiNEK6.
DMDMi37537993.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 313313Serine/threonine-protein kinase Nek6PRO_0000086427Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei37 – 371Phosphoserine1 Publication
Modified residuei202 – 2021Phosphothreonine1 Publication
Modified residuei206 – 2061Phosphoserine; by NEK9Combined sources2 Publications
Modified residuei210 – 2101Phosphothreonine1 Publication

Post-translational modificationi

Autophosphorylated. Phosphorylation at Ser-206 is required for its activation. Phosphorylated upon IR or UV-induced DNA damage. Phosphorylated by CHEK1 and CHEK2. Interaction with APBB1 down-regulates phosphorylation at Thr-210.4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9HC98.
PaxDbiQ9HC98.
PeptideAtlasiQ9HC98.
PRIDEiQ9HC98.

PTM databases

iPTMnetiQ9HC98.
PhosphoSiteiQ9HC98.

Expressioni

Tissue specificityi

Ubiquitous, with highest expression in heart and skeletal muscle. Up-regulated in a variety of malignant cancers, such as breast, colon, lung, and gastric cancers.2 Publications

Inductioni

Up-regulated during the M phase of cell cycle progression. Down-regulated in both replicative and premature senescence of cancer cells.2 Publications

Gene expression databases

BgeeiENSG00000119408.
CleanExiHS_NEK6.
ExpressionAtlasiQ9HC98. baseline and differential.
GenevisibleiQ9HC98. HS.

Organism-specific databases

HPAiCAB045993.
HPA056828.

Interactioni

Subunit structurei

Interacts with STAT3 and RPS6KB1 (By similarity). Interacts with NEK9, predominantly in mitosis. Interacts with KIF11 (via C-terminus). Interacts with APBB1 (via WW domain). Interacts with ANKRA2, ATF4, ARHGAP33, CDC42, CIR1, PRAM1, PTN, PRDX3, PIN1, RAD26L, RBBP6, RPS7 and TRIP4.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AESQ081173EBI-740364,EBI-717810
CCDC36Q8IYA83EBI-740364,EBI-8638439
FAM208BQ5VWN6-23EBI-740364,EBI-10172380
HSD17B14Q9BPX13EBI-740364,EBI-742664
IKZF1Q134223EBI-740364,EBI-745305
IKZF3Q9UKT93EBI-740364,EBI-747204
INCA1Q0VD863EBI-740364,EBI-6509505
KRT31Q153233EBI-740364,EBI-948001
KRT40Q6A1623EBI-740364,EBI-10171697
LNX1Q8TBB13EBI-740364,EBI-739832
LZTS2Q9BRK43EBI-740364,EBI-741037
NECAB2H3BTW23EBI-740364,EBI-10172876
PIN1Q135263EBI-740364,EBI-714158
TCF4P158843EBI-740364,EBI-533224
TNK2Q079123EBI-740364,EBI-603457
TRIM23P364063EBI-740364,EBI-740098
TRIM27P143733EBI-740364,EBI-719493
XIAPP981703EBI-740364,EBI-517127

GO - Molecular functioni

  • kinesin binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116000. 64 interactions.
IntActiQ9HC98. 24 interactions.
STRINGi9606.ENSP00000362702.

Chemistry

BindingDBiQ9HC98.

Structurei

3D structure databases

ProteinModelPortaliQ9HC98.
SMRiQ9HC98. Positions 41-307.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 310266Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 4444Interaction with ARHGAP33, ANKRA2, CDC42, PRDX3, RAD26L, RBBP6, RPS7 and TRIP4Add
BLAST
Regioni267 – 2704Interaction with APBB1

Domaini

Displays an autoinhibited conformation: Tyr-108 side chain points into the active site, interacts with the activation loop, and blocks the alphaC helix. The autoinhibitory conformation is released upon binding with NEK9.1 Publication

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0591. Eukaryota.
ENOG410XNQP. LUCA.
GeneTreeiENSGT00760000118997.
HOVERGENiHBG105886.
InParanoidiQ9HC98.
KOiK08857.
OMAiTLADFQI.
OrthoDBiEOG091G0AER.
PhylomeDBiQ9HC98.
TreeFamiTF101021.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9HC98-1) [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
MAGQPGHMPH GGSSNNLCHT LGPVHPPDPQ RHPNTLSFRC SLADFQIEKK
60 70 80 90 100
IGRGQFSEVY KATCLLDRKT VALKKVQIFE MMDAKARQDC VKEIGLLKQL
110 120 130 140 150
NHPNIIKYLD SFIEDNELNI VLELADAGDL SQMIKYFKKQ KRLIPERTVW
160 170 180 190 200
KYFVQLCSAV EHMHSRRVMH RDIKPANVFI TATGVVKLGD LGLGRFFSSE
210 220 230 240 250
TTAAHSLVGT PYYMSPERIH ENGYNFKSDI WSLGCLLYEM AALQSPFYGD
260 270 280 290 300
KMNLFSLCQK IEQCDYPPLP GEHYSEKLRE LVSMCICPDP HQRPDIGYVH
310
QVAKQMHIWM SST
Length:313
Mass (Da):35,714
Last modified:October 3, 2003 - v2
Checksum:iB898DC57407A8C16
GO
Isoform 2 (identifier: Q9HC98-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPRREVCWEAAHFRQEEQSLPRPRVRALVRLACRM

Show »
Length:347
Mass (Da):39,844
Checksum:i2CA3B83E91024B8A
GO
Isoform 3 (identifier: Q9HC98-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGRRRPAPFRALVRLACRM

Show »
Length:331
Mass (Da):37,823
Checksum:iDF83ECFFE6F5B2F6
GO
Isoform 4 (identifier: Q9HC98-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEATGWDSRCSPGTQVRALVRLACRM

Show »
Length:338
Mass (Da):38,460
Checksum:i2B680899AE6D5765
GO

Sequence cautioni

The sequence AAG13417 differs from that shown.Contaminating sequence. Sequence of unknown origin in the N-terminal part.Curated
The sequence AAH00101 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH04174 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH04209 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA85045 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti88 – 881Q → W in CAG33372 (Ref. 7) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MPRREVCWEAAHFRQEEQSL PRPRVRALVRLACRM in isoform 2. 1 PublicationVSP_041798
Alternative sequencei1 – 11M → MGRRRPAPFRALVRLACRM in isoform 3. 1 PublicationVSP_041799
Alternative sequencei1 – 11M → MEATGWDSRCSPGTQVRALV RLACRM in isoform 4. 1 PublicationVSP_041800

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF087909 mRNA. Translation: AAG13417.1. Sequence problems.
AB026289 mRNA. Translation: BAA85045.1. Different initiation.
AK294614 mRNA. Translation: BAH11825.1.
AK313071 mRNA. Translation: BAG35899.1.
AL162724, AL137846 Genomic DNA. Translation: CAH70247.1.
AL162724, AL137846 Genomic DNA. Translation: CAH70254.1.
AL137846, AL162724 Genomic DNA. Translation: CAI10876.1.
AL137846, AL162724 Genomic DNA. Translation: CAI10883.1.
CH471090 Genomic DNA. Translation: EAW87579.1.
CH471090 Genomic DNA. Translation: EAW87581.1.
BC000101 mRNA. Translation: AAH00101.2. Different initiation.
BC004174 mRNA. Translation: AAH04174.2. Different initiation.
BC004209 mRNA. Translation: AAH04209.2. Different initiation.
BC012761 mRNA. Translation: AAH12761.1.
CR457091 mRNA. Translation: CAG33372.1.
CR542222 mRNA. Translation: CAG47018.1.
CCDSiCCDS48015.1. [Q9HC98-2]
CCDS55338.1. [Q9HC98-3]
CCDS55339.1. [Q9HC98-4]
CCDS6854.1. [Q9HC98-1]
PIRiJC7838.
RefSeqiNP_001138473.1. NM_001145001.2. [Q9HC98-2]
NP_001159639.1. NM_001166167.1. [Q9HC98-3]
NP_001159640.1. NM_001166168.1. [Q9HC98-1]
NP_001159641.1. NM_001166169.1. [Q9HC98-4]
NP_001159642.1. NM_001166170.1. [Q9HC98-1]
NP_001159643.1. NM_001166171.1. [Q9HC98-2]
NP_055212.2. NM_014397.5. [Q9HC98-1]
XP_005251721.1. XM_005251664.1. [Q9HC98-1]
XP_006716999.1. XM_006716936.2. [Q9HC98-1]
UniGeneiHs.197071.

Genome annotation databases

EnsembliENST00000320246; ENSP00000319734; ENSG00000119408. [Q9HC98-1]
ENST00000373600; ENSP00000362702; ENSG00000119408. [Q9HC98-2]
ENST00000373603; ENSP00000362705; ENSG00000119408. [Q9HC98-1]
ENST00000394199; ENSP00000377749; ENSG00000119408. [Q9HC98-2]
ENST00000539416; ENSP00000439651; ENSG00000119408. [Q9HC98-4]
ENST00000540326; ENSP00000441469; ENSG00000119408. [Q9HC98-3]
ENST00000545174; ENSP00000442636; ENSG00000119408. [Q9HC98-1]
ENST00000546191; ENSP00000441426; ENSG00000119408. [Q9HC98-1]
GeneIDi10783.
KEGGihsa:10783.
UCSCiuc004bof.4. human. [Q9HC98-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF087909 mRNA. Translation: AAG13417.1. Sequence problems.
AB026289 mRNA. Translation: BAA85045.1. Different initiation.
AK294614 mRNA. Translation: BAH11825.1.
AK313071 mRNA. Translation: BAG35899.1.
AL162724, AL137846 Genomic DNA. Translation: CAH70247.1.
AL162724, AL137846 Genomic DNA. Translation: CAH70254.1.
AL137846, AL162724 Genomic DNA. Translation: CAI10876.1.
AL137846, AL162724 Genomic DNA. Translation: CAI10883.1.
CH471090 Genomic DNA. Translation: EAW87579.1.
CH471090 Genomic DNA. Translation: EAW87581.1.
BC000101 mRNA. Translation: AAH00101.2. Different initiation.
BC004174 mRNA. Translation: AAH04174.2. Different initiation.
BC004209 mRNA. Translation: AAH04209.2. Different initiation.
BC012761 mRNA. Translation: AAH12761.1.
CR457091 mRNA. Translation: CAG33372.1.
CR542222 mRNA. Translation: CAG47018.1.
CCDSiCCDS48015.1. [Q9HC98-2]
CCDS55338.1. [Q9HC98-3]
CCDS55339.1. [Q9HC98-4]
CCDS6854.1. [Q9HC98-1]
PIRiJC7838.
RefSeqiNP_001138473.1. NM_001145001.2. [Q9HC98-2]
NP_001159639.1. NM_001166167.1. [Q9HC98-3]
NP_001159640.1. NM_001166168.1. [Q9HC98-1]
NP_001159641.1. NM_001166169.1. [Q9HC98-4]
NP_001159642.1. NM_001166170.1. [Q9HC98-1]
NP_001159643.1. NM_001166171.1. [Q9HC98-2]
NP_055212.2. NM_014397.5. [Q9HC98-1]
XP_005251721.1. XM_005251664.1. [Q9HC98-1]
XP_006716999.1. XM_006716936.2. [Q9HC98-1]
UniGeneiHs.197071.

3D structure databases

ProteinModelPortaliQ9HC98.
SMRiQ9HC98. Positions 41-307.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116000. 64 interactions.
IntActiQ9HC98. 24 interactions.
STRINGi9606.ENSP00000362702.

Chemistry

BindingDBiQ9HC98.
ChEMBLiCHEMBL4309.
GuidetoPHARMACOLOGYi2121.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

PTM databases

iPTMnetiQ9HC98.
PhosphoSiteiQ9HC98.

Polymorphism and mutation databases

BioMutaiNEK6.
DMDMi37537993.

Proteomic databases

MaxQBiQ9HC98.
PaxDbiQ9HC98.
PeptideAtlasiQ9HC98.
PRIDEiQ9HC98.

Protocols and materials databases

DNASUi10783.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000320246; ENSP00000319734; ENSG00000119408. [Q9HC98-1]
ENST00000373600; ENSP00000362702; ENSG00000119408. [Q9HC98-2]
ENST00000373603; ENSP00000362705; ENSG00000119408. [Q9HC98-1]
ENST00000394199; ENSP00000377749; ENSG00000119408. [Q9HC98-2]
ENST00000539416; ENSP00000439651; ENSG00000119408. [Q9HC98-4]
ENST00000540326; ENSP00000441469; ENSG00000119408. [Q9HC98-3]
ENST00000545174; ENSP00000442636; ENSG00000119408. [Q9HC98-1]
ENST00000546191; ENSP00000441426; ENSG00000119408. [Q9HC98-1]
GeneIDi10783.
KEGGihsa:10783.
UCSCiuc004bof.4. human. [Q9HC98-1]

Organism-specific databases

CTDi10783.
GeneCardsiNEK6.
HGNCiHGNC:7749. NEK6.
HPAiCAB045993.
HPA056828.
MIMi604884. gene.
neXtProtiNX_Q9HC98.
PharmGKBiPA31550.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0591. Eukaryota.
ENOG410XNQP. LUCA.
GeneTreeiENSGT00760000118997.
HOVERGENiHBG105886.
InParanoidiQ9HC98.
KOiK08857.
OMAiTLADFQI.
OrthoDBiEOG091G0AER.
PhylomeDBiQ9HC98.
TreeFamiTF101021.

Enzyme and pathway databases

ReactomeiR-HSA-2980767. Activation of NIMA Kinases NEK9, NEK6, NEK7.
R-HSA-3301854. Nuclear Pore Complex (NPC) Disassembly.
SignaLinkiQ9HC98.
SIGNORiQ9HC98.

Miscellaneous databases

ChiTaRSiNEK6. human.
GeneWikiiNEK6.
GenomeRNAii10783.
PROiQ9HC98.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000119408.
CleanExiHS_NEK6.
ExpressionAtlasiQ9HC98. baseline and differential.
GenevisibleiQ9HC98. HS.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNEK6_HUMAN
AccessioniPrimary (citable) accession number: Q9HC98
Secondary accession number(s): B7Z2D9
, Q5TBG3, Q5TBG9, Q6FG86, Q6IAR3, Q96E83, Q9ULX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 3, 2003
Last modified: September 7, 2016
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. 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.