Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q00536

- CDK16_HUMAN

UniProt

Q00536 - CDK16_HUMAN

Protein

Cyclin-dependent kinase 16

Gene

CDK16

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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).By similarity3 Publications

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei194 – 1941ATPCurated
    Active sitei286 – 2861Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi171 – 1799ATPPROSITE-ProRule annotation

    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

    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.

    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

    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 16PRO_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.6 Publications

    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.By similarity3 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

    1
    496
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini165 – 446282Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251N → D in BAH13564. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MPLYGRARDHVTHPSILGTR PGRPMAGPITAAVPEKICNG AFCSCSGAFPLDPNNPSLGP LPSISHLNLRTQIAM in isoform 2. 1 PublicationVSP_046134
    Alternative sequencei1 – 11M → MQSEIAM in isoform 3. 1 PublicationVSP_046342

    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]
    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 ]
    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

    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: October 1, 2014
    This is version 151 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