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Protein Page:
CDK16 (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
CDK16 May play a role in signal transduction cascades in terminally differentiated cells. Found in a complex containing CABLES1, CDK17 and TDRD7. Interacts with YWHAH, YWHAQ and YWHAZ. Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. Note: This description may include information from UniProtKB.
Protein type: EC 2.7.11.22; Protein kinase, CMGC; Kinase, protein; Motility/polarity/chemotaxis; Protein kinase, Ser/Thr (non-receptor); CMGC group; CDK family; TAIRE subfamily; CDK/TAIRE subfamily
Chromosomal Location of Human Ortholog: Xp11
Cellular Component: microtubule cytoskeleton; synaptic vesicle; extrinsic to internal side of plasma membrane; neuron projection; transport vesicle; cytoplasm; plasma membrane; cell junction
Molecular Function: protein serine/threonine kinase activity; protein binding; cyclin-dependent protein kinase activity; ATP binding
Biological Process: growth hormone secretion; exocytosis; regulation of cell cycle; spermatogenesis; protein amino acid phosphorylation; neurite development
Reference #:  Q00536 (UniProtKB)
Alt. Names/Synonyms: CDK16; Cell division protein kinase 16; cyclin-dependent kinase 16; FLJ16665; PCTAIRE; PCTAIRE-motif protein kinase 1; PCTAIRE1; PCTGAIRE; PCTK1; Serine/threonine-protein kinase PCTAIRE-1
Gene Symbols: CDK16
Molecular weight: 55,716 Da
Basal Isoelectric point: 7.23  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

CDK16

Protein Structure Not Found.


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Sites Implicated In
cytoskeletal reorganization: S119‑p, S153‑p
enzymatic activity, inhibited: S153‑p
intracellular localization: S153‑p
molecular association, regulation: S119‑p, S153‑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


 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

► Hide Isoforms
 
0 1 - gap
2 19 S12-p KKIKRQLsMtLRGGR
0 2 T14-p IKRQLsMtLRGGRGI
0 2 S36-p EQIGLDEsGGGGGsD
0 3 S42-p EsGGGGGsDPGEAPT
0 2 S64-p RSARGPLssAPEIVH
0 8 S65-p SARGPLssAPEIVHE
1 6 S78-p HEDLKMGsDGEsDQA
0 3 S82-p KMGsDGEsDQAsAts
0 1 S86-p DGEsDQAsAtsSDEV
0 1 T88-p EsDQAsAtsSDEVQs
0 1 S89-p sDQAsAtsSDEVQsP
2 10 S95-p tsSDEVQsPVRVRMR
0 1 K108-ac MRNHPPRkIstEDIN
1 43 S110-p NHPPRkIstEDINkR
0 3 T111-p HPPRkIstEDINkRL
0 1 K116-ac IstEDINkRLsLPAD
3 33 S119-p EDINkRLsLPADIRL
0 1 K133-ub LPEGYLEkLtLNsPI
0 4 T135-p EGYLEkLtLNsPIFD
1 43 S138-p LEkLtLNsPIFDkPL
0 1 K143-ub LNsPIFDkPLSRRLR
2 194 S153-p SRRLRRVsLsEIGFG
0 7 S155-p RLRRVsLsEIGFGKL
0 1 K167-ub GKLETYIkLDKLGEG
0 25 T175-p LDKLGEGtyAtVyKG
0 327 Y176-p DKLGEGtyAtVyKGK
0 10 T178-p LGEGtyAtVyKGKSK
0 24 Y180-p EGtyAtVyKGKSKLT
0 1 K194-ub TDNLVALkEIRLEHE
0 5 K288 KVLHRDLKPQNLLIN
0 2 K301-ub INERGELkLADFGLA
0 1 K425 DGADLLTKLLQFEGR
0 1 K455-ub SLGERIHkLPDTTSI
0 1 K466-ub TTSIFALkEIQLQKE
0 1 S479-p KEASLRSssMPDSGR
0 3 S480-p EASLRSssMPDSGRP
  CDK16 iso2  
T30-p RPMAGPItAAVPEKI
S86 KKIKRQLSMTLRGGR
T88 IKRQLSMTLRGGRGI
S110 EQIGLDESGGGGGSD
S116 ESGGGGGSDPGEAPT
S138 RSARGPLSSAPEIVH
S139 SARGPLSSAPEIVHE
S152 HEDLKMGSDGESDQA
S156 KMGSDGESDQASATS
S160 DGESDQASATSSDEV
T162 ESDQASATSSDEVQS
S163 SDQASATSSDEVQSP
S169 TSSDEVQSPVRVRMR
K182 MRNHPPRKISTEDIN
S184 NHPPRKISTEDINKR
T185 HPPRKISTEDINKRL
K190 ISTEDINKRLSLPAD
S193 EDINKRLSLPADIRL
K207 LPEGYLEKLTLNSPI
T209 EGYLEKLTLNSPIFD
S212 LEKLTLNSPIFDKPL
K217 LNSPIFDKPLSRRLR
S227 SRRLRRVSLSEIGFG
S229 RLRRVSLSEIGFGKL
K241 GKLETYIKLDKLGEG
T249 LDKLGEGTYATVYKG
Y250 DKLGEGTYATVYKGK
T252 LGEGTYATVYKGKSK
Y254 EGTYATVYKGKSKLT
K268 TDNLVALKEIRLEHE
K362 KVLHRDLKPQNLLIN
K375 INERGELKLADFGLA
K499 DGADLLTKLLQFEGR
K529 SLGERIHKLPDTTSI
K540 TTSIFALKEIQLQKE
S553 KEASLRSSSMPDSGR
S554 EASLRSSSMPDSGRP
  mouse

 
- gap
S12-p KKIKRQLsMTLRGGR
T14 IKRQLsMTLRGGRGI
S36 EQIGLDESGGGGGSD
S42 ESGGGGGSDLGEAPT
S64 RSVRGPLSsAPEIVH
S65-p SVRGPLSsAPEIVHE
S78-p HEDMKMGsDGEsDQA
S82-p KMGsDGEsDQASATS
S86 DGEsDQASATSSDEV
T88 EsDQASATSSDEVQs
S89 sDQASATSSDEVQsP
S95-p TSSDEVQsPVRVRMR
K108 MRNHPPRKIstEDIN
S110-p NHPPRKIstEDINKR
T111-p HPPRKIstEDINKRL
K116 IstEDINKRLsLPAD
S119-p EDINKRLsLPADIRL
K133 LPEGYLEKLTLNsPI
T135 EGYLEKLTLNsPIFD
S138-p LEKLTLNsPIFDKPL
K143 LNsPIFDKPLSRRLR
S153-p SRRLRRVsLSEIGFG
S155 RLRRVsLSEIGFGKL
K167 GKLETYIKLDKLGEG
T175-p LDKLGEGtyAtVyKG
Y176-p DKLGEGtyAtVyKGK
T178-p LGEGtyAtVyKGKSK
Y180-p EGtyAtVyKGKSKLT
K194 TDNLVALKEIRLEHE
K288-ub KVLHRDLkPQNLLIN
K301-ub INERGELkLADFGLA
K425-ub DGADLLTkLLQFEGR
K455 SLGERIHKLPDTTSI
K466 TTSIFALKEVQLQKE
T479 KEANIRSTSMPDSGR
S480 EANIRSTSMPDSGRP
  rat

 
- gap
S12 KKIKRQLSMTLRGGR
T14 IKRQLSMTLRGGRGI
S36 EQIGLDESGGGGGMT
M42 ESGGGGGMTLGEAPT
S64 RSIRGPLSSAPEIVH
S65 SIRGPLSSAPEIVHE
S78-p HEDMKMGsDGESDQA
S82 KMGsDGESDQASATS
S86 DGESDQASATSSDEV
T88 ESDQASATSSDEVQs
S89 SDQASATSSDEVQsP
S95-p TSSDEVQsPVRVRMR
K108 MRNHPPRKIsTEDIN
S110-p NHPPRKIsTEDINKC
T111 HPPRKIsTEDINKCL
K116 IsTEDINKCLSLPAD
S119 EDINKCLSLPADIRL
K133 LPEGYLEKLTLNSPI
T135 EGYLEKLTLNSPIGD
S138 LEKLTLNSPIGDKPL
K143 LNSPIGDKPLSRRLR
S153 SRRLRPVSLsEIGFG
S155-p RLRPVSLsEIGFGKL
K167 GKLETYIKLDKLGEG
T175 LDKLGEGTyATVYKG
Y176-p DKLGEGTyATVYKGK
T178 LGEGTyATVYKGKSK
Y180 EGTyATVYKGKSKLT
K194 TDNLVALKEIRLEHE
K288-ub KVLHRDLkPQNLLIN
K301 INERGELKLADFGLA
K425 DGADLLTKLLQFEGR
K455 SLGERIHKLPDTTSI
K466 TTSIFALKEVQLQKE
T479 KEANIRSTSMPDSGR
S480 EANIRSTSMPDSGRP
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