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Protein Page:
PBK (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PBK Phosphorylates MAP kinase p38. Seems to be active only in mitosis. May also play a role in the activation of lymphoid cells. When phosphorylated, forms a complex with TP53, leading to TP53 destabilization and attenuation of G2/M checkpoint during doxorubicin-induced DNA damage. Interacts with DLG1 and TP53. Expressed in the testis and placenta. In the testis, restrictedly expressed in outer cell layer of seminiferous tubules. Activated by phosphorylation. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. MAP kinase kinase subfamily. Note: This description may include information from UniProtKB.
Protein type: Protein kinase, Other; EC 2.7.12.2; Protein kinase, Ser/Thr (non-receptor); Cancer Testis Antigen (CTA); Kinase, protein; Other group; TOPK family
Chromosomal Location of Human Ortholog: 8p21.2
Cellular Component: nucleus
Molecular Function: protein binding; protein serine/threonine kinase activity
Reference #:  Q96KB5 (UniProtKB)
Alt. Names/Synonyms: Cancer/testis antigen 84; CT84; FLJ14385; Lymphokine-activated killer T-cell-originated protein kinase; MAPKK-like protein kinase; Nori-3; PBK; PDZ binding kinase; PDZ-binding kinase; Spermatogenesis-related protein kinase; SPK; T-LAK cell-originated protein kinase; TOPK
Gene Symbols: PBK
Molecular weight: 36,085 Da
Basal Isoelectric point: 4.98  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PBK

Protein Structure Not Found.


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Sites Implicated In
carcinogenesis, induced: Y74‑p, Y272‑p
cytoskeletal reorganization: T9‑p
enzymatic activity, induced: T9‑p, Y74‑p, Y272‑p
molecular association, regulation: T9‑p
protein stabilization: Y74‑p, Y272‑p

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



 LTP 

LTP: 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.


 HTP 

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


       human

 
0 1 K8‑sm MEGISNFktPskLsE
4 11 T9‑p EGISNFktPskLsEk
0 1 S11‑p ISNFktPskLsEkkK
0 6 K12‑ac SNFktPskLsEkkKs
0 1 K12‑sm SNFktPskLsEkkKs
0 4 S14‑p FktPskLsEkkKsVL
0 3 K16‑ac tPskLsEkkKsVLCs
0 1 K17‑ac PskLsEkkKsVLCst
0 9 S19‑p kLsEkkKsVLCstPt
0 4 S23‑p kkKsVLCstPtINIP
0 29 T24‑p kKsVLCstPtINIPA
0 3 T26‑p sVLCstPtINIPAsP
0 39 S32‑p PtINIPAsPFMQKLG
0 2 Y47‑p FGTGVNVyLMkRsPR
0 1 K50‑ub GVNVyLMkRsPRGLs
0 1 S52‑p NVyLMkRsPRGLsHs
0 3 S57‑p kRsPRGLsHsPWAVk
0 30 S59‑p sPRGLsHsPWAVkkI
0 1 K64‑ac sHsPWAVkkINPICN
0 1 K64‑sm sHsPWAVkkINPICN
0 1 K65‑ub HsPWAVkkINPICND
0 1 K65‑sm HsPWAVkkINPICND
1 166 Y74‑p NPICNDHyRsVyQKR
0 1 S76‑p ICNDHyRsVyQKRLM
0 1 Y78‑p NDHyRsVyQKRLMDE
0 2 K90‑ub MDEAKILksLHHPNI
0 2 S91‑p DEAKILksLHHPNIV
0 1 Y100‑p HHPNIVGyRAFTEAN
0 1 S122 MEYGGEKSLNDLIEE
0 3 K132‑ub DLIEERYkASQDPFP
0 1 K155‑sm LNMARGLkYLHQEKk
0 1 K162‑sm kYLHQEKkLLHGDIk
0 2 K169‑ub kLLHGDIkSSNVVIk
0 1 K169‑sm kLLHGDIkSSNVVIk
0 1 K176‑sm kSSNVVIkGDFETIK
1 0 T198 LPLDENMTVTDPEAC
0 1 T260‑p DDDDEDKtFDESDFD
1 0 Y272‑p DFDDEAYyAALGTRP
0 1 P280 AALGTRPPINMEELD
0 1 S310‑p EDPKDRPsAAHIVEA
4941 : Phospho-PBK/TOPK (Thr9) Antibody
  mouse

 
K8 MEGINNFKtPNKSEK
T9‑p EGINNFKtPNKSEKR
N11 INNFKtPNKSEKRKs
K12 NNFKtPNKSEKRKsV
K12 NNFKtPNKSEKRKsV
S13 NFKtPNKSEKRKsVL
K15 KtPNKSEKRKsVLCs
R16 tPNKSEKRKsVLCst
S18‑p NKSEKRKsVLCstPC
S22‑p KRKsVLCstPCVNIP
T23‑p RKsVLCstPCVNIPA
C25 sVLCstPCVNIPAsP
S31‑p PCVNIPAsPFMQKLG
Y46 FGTGVSVYLMKRSPR
K49 GVSVYLMKRSPRGLS
S51 SVYLMKRSPRGLSHs
S56 KRSPRGLSHsPWAVK
S58‑p SPRGLSHsPWAVKKI
K63 SHsPWAVKKISLLCD
K63 SHsPWAVKKISLLCD
K64 HsPWAVKKISLLCDD
K64 HsPWAVKKISLLCDD
Y73 SLLCDDHYRTVYQKR
T75 LCDDHYRTVYQKRLT
Y77 DDHYRTVYQKRLTDE
K89 TDEAKILKNLNHPNI
N90 DEAKILKNLNHPNII
Y99 NHPNIIGYRAFTEAS
S121‑p MEYGGEKsLNDLIEE
K131 DLIEERNKDSGSPFP
K154 LHMARGLKYLHQEKK
K161 KYLHQEKKLLHGDIK
K168 KLLHGDIKSSNVVIK
K168 KLLHGDIKSSNVVIK
K175 KSSNVVIKGDFETIK
T197‑p LPLDENMtVTDPEAC
T259 DDVDEDATFDESDFD
Y271 DFDDEAYYAALGTRP
S279‑p AALGTRPsINMEELD
S309 EDPKDRPSAAHIVEA
  rat

 
K8 MEGISNFKTPNKLSE
T9 EGISNFKTPNKLSEK
N11 ISNFKTPNKLSEKRK
K12 SNFKTPNKLSEKRKS
K12 SNFKTPNKLSEKRKS
S14 FKTPNKLSEKRKSVL
K16 TPNKLSEKRKSVLCS
R17 PNKLSEKRKSVLCST
S19 KLSEKRKSVLCSTPC
S23 KRKSVLCSTPCVNIP
T24 RKSVLCSTPCVNIPA
C26 SVLCSTPCVNIPASP
S32 PCVNIPASPFMQKLG
Y47 FGTGVSVYLMKRSPR
K50 GVSVYLMKRSPRGLS
S52 SVYLMKRSPRGLSHs
S57 KRSPRGLSHsPWAVK
S59‑p SPRGLSHsPWAVKKI
K64 SHsPWAVKKINPLCD
K64 SHsPWAVKKINPLCD
K65 HsPWAVKKINPLCDD
K65 HsPWAVKKINPLCDD
Y74 NPLCDDHYRTVYQKR
T76 LCDDHYRTVYQKRLT
Y78 DDHYRTVYQKRLTDE
K90 TDEAKILKNLNHPNI
N91 DEAKILKNLNHPNIV
Y100 NHPNIVGYRAFTEAS
S122 MEYGGEKSLNDLIEE
K132 DLIEERNKDSGSPFP
K155 LHMARGLKYLHQEKK
K162 KYLHQEKKLLHGDIK
K169 KLLHGDIKSSNVVIK
K169 KLLHGDIKSSNVVIK
K176 KSSNVVIKGDFETIK
T198 LPLDENMTVTDPEAC
T260 DDDDEDATFDESDFD
Y272 DFDDEAYYAALGTRP
S280 AALGTRPSINMEELD
S310 EDPKDRPSAAHIVEA
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