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Q00536

- CDK16_HUMAN

UniProt

Q00536 - CDK16_HUMAN

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Protein
Cyclin-dependent kinase 16
Gene
CDK16, PCTAIRE1, PCTK1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Protein kinase that plays a role in vesicle-mediated transport processes and exocytosis. Regulates GH1 release by brain neurons. Phosphorylates NSF, and thereby regulates NSF oligomerization. Required for normal spermatogenesis. Regulates neuron differentiation and dendrite development By similarity. Plays a role in the regulation of insulin secretion in response to changes in blood glucose levels. Can phosphorylate CCNY at 'Ser-336' (in vitro).3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei194 – 1941ATP Inferred
Active sitei286 – 2861Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi171 – 1799ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB-EC
  3. protein binding Source: IntAct
  4. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. exocytosis Source: UniProtKB
  2. growth hormone secretion Source: UniProtKB
  3. neuron projection development Source: UniProtKB
  4. protein phosphorylation Source: ProtInc
  5. regulation of insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
  6. spermatogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Differentiation, Spermatogenesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.22. 2681.
SignaLinkiQ00536.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-dependent kinase 16 (EC:2.7.11.22)
Alternative name(s):
Cell division protein kinase 16
PCTAIRE-motif protein kinase 1
Serine/threonine-protein kinase PCTAIRE-1
Gene namesi
Name:CDK16
Synonyms:PCTAIRE1, PCTK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:8749. CDK16.

Subcellular locationi

Cytoplasm. Cytoplasmic vesiclesecretory vesicle. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junctionsynapsesynaptosome By similarity
Note: Colocalizes with insulin in pancreas islets. Recruited to the cell membrane by CCNY.2 Publications

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cytoplasm Source: UniProtKB
  3. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  4. microtubule cytoskeleton Source: HPA
  5. neuron projection Source: UniProtKB-SubCell
  6. plasma membrane Source: HPA
  7. synaptic vesicle Source: Ensembl
  8. transport vesicle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoplasmic vesicle, Membrane, Synapse, Synaptosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi12 – 121S → A: Abolishes phosphorylation by BRSK2. Abolishes effect on insulin secretion. 1 Publication
Mutagenesisi119 – 1191S → A: Strongly reduces interaction with CCNY. 1 Publication
Mutagenesisi153 – 1531S → A: Constitutively activated, due to loss of an inhibitory phosphorylation site. Increases interaction with CCNY. 2 Publications
Mutagenesisi153 – 1531S → D: Abolishes interaction with CCNY. 2 Publications
Mutagenesisi194 – 1941K → A: Loss of kinase activity. Abolishes effect on insulin secretion. 2 Publications
Mutagenesisi194 – 1941K → R: Loss of kinase activity. 2 Publications

Organism-specific databases

PharmGKBiPA33095.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 496496Cyclin-dependent kinase 16
PRO_0000086484Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121Phosphoserine; by BRSK21 Publication
Modified residuei42 – 421Phosphoserine1 Publication
Modified residuei78 – 781Phosphoserine2 Publications
Modified residuei82 – 821Phosphoserine2 Publications
Modified residuei95 – 951Phosphoserine; by CDK52 Publications
Modified residuei119 – 1191Phosphoserine3 Publications
Modified residuei138 – 1381Phosphoserine3 Publications
Modified residuei153 – 1531Phosphoserine3 Publications
Modified residuei155 – 1551Phosphoserine1 Publication

Post-translational modificationi

Phosphorylation at Ser-153 inhibits kinase activity.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ00536.
PaxDbiQ00536.
PRIDEiQ00536.

PTM databases

PhosphoSiteiQ00536.

Expressioni

Tissue specificityi

Detected in pancreas islets (at protein level). Detected in brain and pancreas.1 Publication

Gene expression databases

ArrayExpressiQ00536.
BgeeiQ00536.
CleanExiHS_PCTK1.
GenevestigatoriQ00536.

Organism-specific databases

HPAiCAB016535.
HPA000974.
HPA001366.

Interactioni

Subunit structurei

Found in a complex containing CABLES1, CDK17 and TDRD7. Interacts with YWHAH, YWHAQ and YWHAZ. Interacts with NSF. Identified in a complex with NSF, syntaxin-1, synaptotagmin, SYN1, SYP and CDK5R1 By similarity. Interacts with BRSK2. Interacts with CCNY; this increases the CDK16 kinase activity.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SEC23AQ154363EBI-726261,EBI-81088

Protein-protein interaction databases

BioGridi111154. 20 interactions.
IntActiQ00536. 9 interactions.
STRINGi9606.ENSP00000405798.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi164 – 17310
Beta strandi175 – 18410
Turni185 – 1873
Beta strandi190 – 1967
Helixi212 – 2154
Beta strandi226 – 2316
Beta strandi236 – 2416
Beta strandi244 – 2463
Helixi247 – 2537
Turni254 – 2563
Helixi260 – 27920
Beta strandi282 – 2865
Helixi289 – 2913
Beta strandi292 – 2943
Beta strandi300 – 3023
Beta strandi304 – 3096
Helixi325 – 3273
Helixi330 – 3334
Helixi342 – 35716
Helixi367 – 37812
Turni383 – 3853
Helixi389 – 3913
Helixi393 – 3975
Helixi408 – 4114
Helixi417 – 42610
Helixi431 – 4333
Helixi437 – 4404
Helixi444 – 4496
Beta strandi454 – 4563
Helixi462 – 4643

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MTLX-ray2.40A163-478[»]
ProteinModelPortaliQ00536.
SMRiQ00536. Positions 71-472.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini165 – 446282Protein kinase
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiQ00536.
KOiK08820.
OMAiVAMDRMK.
OrthoDBiEOG7966H8.
PhylomeDBiQ00536.
TreeFamiTF106508.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q00536-1) [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

MDRMKKIKRQ LSMTLRGGRG IDKTNGAPEQ IGLDESGGGG GSDPGEAPTR    50
AAPGELRSAR GPLSSAPEIV HEDLKMGSDG ESDQASATSS DEVQSPVRVR 100
MRNHPPRKIS TEDINKRLSL PADIRLPEGY LEKLTLNSPI FDKPLSRRLR 150
RVSLSEIGFG KLETYIKLDK LGEGTYATVY KGKSKLTDNL VALKEIRLEH 200
EEGAPCTAIR EVSLLKDLKH ANIVTLHDII HTEKSLTLVF EYLDKDLKQY 250
LDDCGNIINM HNVKLFLFQL LRGLAYCHRQ KVLHRDLKPQ NLLINERGEL 300
KLADFGLARA KSIPTKTYSN EVVTLWYRPP DILLGSTDYS TQIDMWGVGC 350
IFYEMATGRP LFPGSTVEEQ LHFIFRILGT PTEETWPGIL SNEEFKTYNY 400
PKYRAEALLS HAPRLDSDGA DLLTKLLQFE GRNRISAEDA MKHPFFLSLG 450
ERIHKLPDTT SIFALKEIQL QKEASLRSSS MPDSGRPAFR VVDTEF 496
Length:496
Mass (Da):55,716
Last modified:April 1, 1993 - v1
Checksum:i9A5DDD34A5E5CBBB
GO
Isoform 2 (identifier: Q00536-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:570
Mass (Da):63,458
Checksum:i9D3020F5CADD1899
GO
Isoform 3 (identifier: Q00536-3) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:502
Mass (Da):56,375
Checksum:iAC4B7353DFF4D005
GO

Sequence cautioni

The sequence AAH01048.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAH15607.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MPLYGRARDHVTHPSILGTR PGRPMAGPITAAVPEKICNG AFCSCSGAFPLDPNNPSLGP LPSISHLNLRTQIAM in isoform 2.
VSP_046134
Alternative sequencei1 – 11M → MQSEIAM in isoform 3.
VSP_046342

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251N → D in BAH13564. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66363 mRNA. Translation: CAA47006.1.
BT006827 mRNA. Translation: AAP35473.1.
AK290145 mRNA. Translation: BAF82834.1.
AK301832 mRNA. Translation: BAH13564.1.
AL096791 Genomic DNA. Translation: CAD20055.1.
AL513366 Genomic DNA. No translation available.
CH471164 Genomic DNA. Translation: EAW59295.1.
CH471164 Genomic DNA. Translation: EAW59297.1.
BC001048 mRNA. Translation: AAH01048.1. Different initiation.
BC015607 mRNA. Translation: AAH15607.1. Different initiation.
CCDSiCCDS14276.1. [Q00536-1]
CCDS48101.1. [Q00536-3]
CCDS55408.1. [Q00536-2]
PIRiS23385.
RefSeqiNP_001163931.1. NM_001170460.1. [Q00536-2]
NP_006192.1. NM_006201.4. [Q00536-1]
NP_148978.2. NM_033018.3. [Q00536-3]
XP_005272672.1. XM_005272615.1. [Q00536-1]
XP_006724597.1. XM_006724534.1. [Q00536-1]
XP_006724598.1. XM_006724535.1. [Q00536-1]
UniGeneiHs.496068.

Genome annotation databases

EnsembliENST00000276052; ENSP00000276052; ENSG00000102225. [Q00536-2]
ENST00000357227; ENSP00000349762; ENSG00000102225. [Q00536-1]
ENST00000457458; ENSP00000405798; ENSG00000102225. [Q00536-3]
ENST00000518022; ENSP00000429751; ENSG00000102225. [Q00536-1]
ENST00000603165; ENSP00000474587; ENSG00000270633. [Q00536-2]
ENST00000604531; ENSP00000474779; ENSG00000270633. [Q00536-3]
ENST00000605184; ENSP00000474747; ENSG00000270633. [Q00536-1]
ENST00000605853; ENSP00000475112; ENSG00000270633. [Q00536-1]
GeneIDi5127.
KEGGihsa:5127.
UCSCiuc004dho.3. human. [Q00536-1]
uc011mli.2. human.

Polymorphism databases

DMDMi266425.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66363 mRNA. Translation: CAA47006.1 .
BT006827 mRNA. Translation: AAP35473.1 .
AK290145 mRNA. Translation: BAF82834.1 .
AK301832 mRNA. Translation: BAH13564.1 .
AL096791 Genomic DNA. Translation: CAD20055.1 .
AL513366 Genomic DNA. No translation available.
CH471164 Genomic DNA. Translation: EAW59295.1 .
CH471164 Genomic DNA. Translation: EAW59297.1 .
BC001048 mRNA. Translation: AAH01048.1 . Different initiation.
BC015607 mRNA. Translation: AAH15607.1 . Different initiation.
CCDSi CCDS14276.1. [Q00536-1 ]
CCDS48101.1. [Q00536-3 ]
CCDS55408.1. [Q00536-2 ]
PIRi S23385.
RefSeqi NP_001163931.1. NM_001170460.1. [Q00536-2 ]
NP_006192.1. NM_006201.4. [Q00536-1 ]
NP_148978.2. NM_033018.3. [Q00536-3 ]
XP_005272672.1. XM_005272615.1. [Q00536-1 ]
XP_006724597.1. XM_006724534.1. [Q00536-1 ]
XP_006724598.1. XM_006724535.1. [Q00536-1 ]
UniGenei Hs.496068.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3MTL X-ray 2.40 A 163-478 [» ]
ProteinModelPortali Q00536.
SMRi Q00536. Positions 71-472.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111154. 20 interactions.
IntActi Q00536. 9 interactions.
STRINGi 9606.ENSP00000405798.

Chemistry

BindingDBi Q00536.
ChEMBLi CHEMBL4597.
GuidetoPHARMACOLOGYi 1969.

PTM databases

PhosphoSitei Q00536.

Polymorphism databases

DMDMi 266425.

Proteomic databases

MaxQBi Q00536.
PaxDbi Q00536.
PRIDEi Q00536.

Protocols and materials databases

DNASUi 5127.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000276052 ; ENSP00000276052 ; ENSG00000102225 . [Q00536-2 ]
ENST00000357227 ; ENSP00000349762 ; ENSG00000102225 . [Q00536-1 ]
ENST00000457458 ; ENSP00000405798 ; ENSG00000102225 . [Q00536-3 ]
ENST00000518022 ; ENSP00000429751 ; ENSG00000102225 . [Q00536-1 ]
ENST00000603165 ; ENSP00000474587 ; ENSG00000270633 . [Q00536-2 ]
ENST00000604531 ; ENSP00000474779 ; ENSG00000270633 . [Q00536-3 ]
ENST00000605184 ; ENSP00000474747 ; ENSG00000270633 . [Q00536-1 ]
ENST00000605853 ; ENSP00000475112 ; ENSG00000270633 . [Q00536-1 ]
GeneIDi 5127.
KEGGi hsa:5127.
UCSCi uc004dho.3. human. [Q00536-1 ]
uc011mli.2. human.

Organism-specific databases

CTDi 5127.
GeneCardsi GC0XP047078.
HGNCi HGNC:8749. CDK16.
HPAi CAB016535.
HPA000974.
HPA001366.
MIMi 311550. gene.
neXtProti NX_Q00536.
PharmGKBi PA33095.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233024.
HOVERGENi HBG014652.
InParanoidi Q00536.
KOi K08820.
OMAi VAMDRMK.
OrthoDBi EOG7966H8.
PhylomeDBi Q00536.
TreeFami TF106508.

Enzyme and pathway databases

BRENDAi 2.7.11.22. 2681.
SignaLinki Q00536.

Miscellaneous databases

ChiTaRSi CDK16. human.
GeneWikii PCTK1.
GenomeRNAii 5127.
NextBioi 19762.
PROi Q00536.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q00536.
Bgeei Q00536.
CleanExi HS_PCTK1.
Genevestigatori Q00536.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A family of human cdc2-related protein kinases."
    Meyerson M., Enders G.H., Wu C.-L., Su L.-K., Gorka C., Nelson C., Harlow E., Tsai L.-H.
    EMBO J. 11:2909-2917(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Fetal brain.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Testis and Thalamus.
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Brain and Placenta.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-82; SER-95; SER-119 AND SER-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138; SER-153 AND SER-155, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-78; SER-82; SER-95; SER-119 AND SER-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND SER-153, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Analysis of substrate specificity and cyclin Y binding of PCTAIRE-1 kinase."
    Shehata S.N., Hunter R.W., Ohta E., Peggie M.W., Lou H.J., Sicheri F., Zeqiraj E., Turk B.E., Sakamoto K.
    Cell. Signal. 24:2085-2094(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CCNY.
  15. "Brain-selective kinase 2 (BRSK2) phosphorylation on PCTAIRE1 negatively regulates glucose-stimulated insulin secretion in pancreatic beta-cells."
    Chen X.Y., Gu X.T., Saiyin H., Wan B., Zhang Y.J., Li J., Wang Y.L., Gao R., Wang Y.F., Dong W.P., Najjar S.M., Zhang C.Y., Ding H.F., Liu J.O., Yu L.
    J. Biol. Chem. 287:30368-30375(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH BRSK2, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-12; SER-153 AND LYS-194, PHOSPHORYLATION AT SER-12, TISSUE SPECIFICITY.
  16. "Cyclin-dependent kinase 16/PCTAIRE kinase 1 is activated by cyclin Y and is essential for spermatogenesis."
    Mikolcevic P., Sigl R., Rauch V., Hess M.W., Pfaller K., Barisic M., Pelliniemi L.J., Boesl M., Geley S.
    Mol. Cell. Biol. 32:868-879(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH CCNY, MUTAGENESIS OF SER-119; SER-153 AND LYS-194.
  17. "Crystal structure of the PCTAIRE1 kinase in complex with indirubin e804."
    Structural genomics consortium (SGC)
    Submitted (JUN-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 163-478.

Entry informationi

Entry nameiCDK16_HUMAN
AccessioniPrimary (citable) accession number: Q00536
Secondary accession number(s): A8K280
, B7Z7C8, J3KN74, J3KQP7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: July 9, 2014
This is version 150 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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