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CDK16 (human)

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; Kinase, protein; Protein kinase, CMGC; Protein kinase, Ser/Thr (non-receptor); Motility/polarity/chemotaxis; CMGC group; CDK family; CDK/TAIRE subfamily; TAIRE subfamily Cellular Component: synaptic vesicle; extrinsic to internal side of plasma membrane; neuron projection; transport vesicle; cytoplasm; cell junction Molecular Function: protein serine/threonine kinase activity; protein binding; cyclin-dependent protein kinase activity; ATP binding Biological Process: growth hormone secretion; exocytosis; 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®

Select Structure to View Below CDK16 3MTL - A=163-478 (human)

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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

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	13		S12-p	KKIKRQLsMtLRGGR
0	1		T14-p	IKRQLsMtLRGGRGI
0	1		S36-p	EQIGLDEsGGGGGsD
0	2		S42-p	EsGGGGGsDPGEAPT
0	2		S64-p	RSARGPLssAPEIVH
0	3		S65-p	SARGPLssAPEIVHE
1	5		S78-p	HEDLKMGsDGEsDQA
0	3		S82-p	KMGsDGEsDQAsAts
0	1		S86-p	DGEsDQAsAtsSDEV
0	1		T88-p	EsDQAsAtsSDEVQs
0	1		S89-p	sDQAsAtsSDEVQsP
2	5		S95-p	tsSDEVQsPVRVRMR
0	1		K108-a	MRNHPPRkIstEDIN
1	37		S110-p	NHPPRkIstEDINkR
0	1		T111-p	HPPRkIstEDINkRL
0	1		K116-a	IstEDINkRLsLPAD
3	20		S119-p	EDINkRLsLPADIRL
0	1		K133-u	LPEGYLEkLtLNsPI
0	2		T135-p	EGYLEkLtLNsPIFD
1	31		S138-p	LEkLtLNsPIFDkPL
0	1		K143-u	LNsPIFDkPLSRRLR
2	149		S153-p	SRRLRRVsLsEIGFG
0	5		S155-p	RLRRVsLsEIGFGKL
0	1		K167-u	GKLETYIkLDKLGEG
0	17		T175-p	LDKLGEGtyAtVyKG
0	333		Y176-p	DKLGEGtyAtVyKGK
0	9		T178-p	LGEGtyAtVyKGKSK
0	24		Y180-p	EGtyAtVyKGKSKLT
0	1		K194-u	TDNLVALkEIRLEHE
0	5		K288	KVLHRDLKPQNLLIN
0	2		K301-u	INERGELkLADFGLA
0	1		K425	DGADLLTKLLQFEGR
0	1		K455-u	SLGERIHkLPDTTSI
0	1		K466-u	TTSIFALkEIQLQKE
0	1		S479-p	KEASLRSssMPDSGR
0	2		S480-p	EASLRSssMPDSGRP

	CDK16 iso3
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	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-u	KVLHRDLkPQNLLIN
K301-u	INERGELkLADFGLA
K425-u	DGADLLTkLLQFEGR
K455	SLGERIHKLPDTTSI
K466	TTSIFALKEVQLQKE
T479	KEANIRSTSMPDSGR
S480	EANIRSTSMPDSGRP

	rat
-	gap
S12	KKIKRQLSMTLRGGR
T14	IKRQLSMTLRGGRGI
S36	EQIGLDESGGGGGMT
M42	ESGGGGGMTLGEAPT
S64	RSIRGPLSSAPEIVH
S65	SIRGPLSSAPEIVHE
S78	HEDMKMGSDGESDQA
S82	KMGSDGESDQASATS
S86	DGESDQASATSSDEV
T88	ESDQASATSSDEVQS
S89	SDQASATSSDEVQSP
S95	TSSDEVQSPVRVRMR
K108	MRNHPPRKIsTEDIN
S110-p	NHPPRKIsTEDINKC
T111	HPPRKIsTEDINKCL
K116	IsTEDINKCLSLPAD
S119	EDINKCLSLPADIRL
K133	LPEGYLEKLTLNSPI
T135	EGYLEKLTLNSPIGD
S138	LEKLTLNSPIGDKPL
K143	LNSPIGDKPLSRRLR
S153	SRRLRPVSLSEIGFG
S155	RLRPVSLSEIGFGKL
K167	GKLETYIKLDKLGEG
T175	LDKLGEGTyATVyKG
Y176-p	DKLGEGTyATVyKGK
T178	LGEGTyATVyKGKSK
Y180-p	EGTyATVyKGKSKLT
K194	TDNLVALKEIRLEHE
K288-u	KVLHRDLkPQNLLIN
K301	INERGELKLADFGLA
K425	DGADLLTKLLQFEGR
K455	SLGERIHKLPDTTSI
K466	TTSIFALKEVQLQKE
T479	KEANIRSTSMPDSGR
S480	EANIRSTSMPDSGRP

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