Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
Pnk1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
Pnk1 polynucleotide kinase 3'-phosphatase. May be involved in double-strand break repair by non-homologous end joining. Required for normal response to DNA damage by gamma-radiation or camptothecin in S. pombe. Note: This description may include information from UniProtKB.
Protein type: Phosphatase (non-protein); EC 2.7.1.78; EC 3.1.3.32; DNA binding protein; Kinase, other
Cellular Component: nucleolus; nucleus
Molecular Function: protein binding; ATP-dependent polydeoxyribonucleotide 5'-hydroxyl-kinase activity; purine nucleotide binding; polynucleotide 3'-phosphatase activity; endonuclease activity; double-stranded DNA binding; damaged DNA binding; nucleotide kinase activity; ATP binding
Biological Process: response to radiation; dephosphorylation; nucleotide-excision repair, DNA damage removal; DNA damage response, detection of DNA damage; response to oxidative stress; DNA-dependent DNA replication; DNA repair; nucleotide phosphorylation
Reference #:  Q96T60 (UniProtKB)
Alt. Names/Synonyms: 2'(3')-polynucleotidase; Bifunctional polynucleotide phosphatase/kinase; DNA 5'-kinase/3'-phosphatase; Homo sapiens polynucleotide kinase 3'-phosphatase (PNKP); PNK; PNKP; Polynucleotide 3'-phosphatase; Polynucleotide 5'-hydroxyl-kinase; polynucleotide kinase 3'-phosphatase; polynucleotide kinase 3-prime-phosphatase; Polynucleotide kinase-3'-phosphatase
Gene Symbols: PNKP
Molecular weight: 57,076 Da
Basal Isoelectric point: 8.73  Predict pI for various phosphorylation states
Select Structure to View Below

Pnk1

Protein Structure Not Found.


STRING  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 T109-p LTLRWEEtRtPEsQP
0 13 T111-p LRWEEtRtPEsQPDt
2 34 S114-p EEtRtPEsQPDtPPG
0 124 T118-p tPEsQPDtPPGtPLV
0 96 T122-p QPDtPPGtPLVsQDE
2 22 S126-p PPGtPLVsQDEKRDA
0 1 S143-p PKKRMRKsNPGWENL
0 6 N144 KKRMRKsNPGWENLE
0 1 E151 NPGWENLEKLLVFTA
0 2 K183-ac LITTRSGkVFPTGPS
0 1 G188 SGkVFPTGPSDWRIL
0 1 R224-m1 TNQMSIGrGKLPAEE
0 1 K233 KLPAEEFKAKVEAVV
0 1 K242 KVEAVVEKLGVPFQV
0 1 S364-p SRALLSAsPEVVVAV
0 1 S379-p GFPGAGKsTFLKKHL
0 1 K484-ub MVMYGYRkQFEAPTL
3522 : Phospho-PNK1 (Ser114/Thr118) Antibody
3522 : Phospho-PNK1 (Ser114/Thr118) Antibody
  mouse

 
L109 LTLRWEELSTSGsQP
T111 LRWEELSTSGsQPDA
S114-p EELSTSGsQPDAPPD
A118 TSGsQPDAPPDtPGD
T122-p QPDAPPDtPGDPEEG
P126 PPDtPGDPEEGEDTE
S142 QKKRVRKSsLGWESL
S143-p KKRVRKSsLGWESLk
K150-ub sLGWESLkKLLVFTA
K182 LITTRSGKVFPTsPS
S187-p SGKVFPTsPSDWRIL
R223 TNQMGIGRGKLPAEV
K232-ac KLPAEVFkGKVEAVL
K241-ac KVEAVLEkLGVPFQV
N363 SSSLLSPNPEVVVAV
S378 GFPGAGKSTFIQEHL
K483 MVMFSYRKQFEPPTL
  rat

 
I109 LTLRWEEISTPGsPP
T111 LRWEEISTPGsPPDt
S114-p EEISTPGsPPDtPPG
T118-p TPGsPPDtPPGNPVD
N122 PPDtPPGNPVDPEEG
P126 PPGNPVDPEEGKDTE
S142 QKKRMRKSSPGWESF
S143 KKRMRKSSPGWESFK
K150 SPGWESFKQLLVFTA
K182 LITTRSGKVFPTSPS
S187 SGKVFPTSPSDWRIL
R223 TNQMGIGRGKLPAEV
K232 KLPAEVFKAKVEAVL
K241 KVEAVLEKLGVPFQV
N363 SSFLLSPNPEVVVAV
S378 GFPGAGKSTFIQKHL
K483 MVMFSYRKQFEPPTL
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.