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)

Q9Y2H1

- ST38L_HUMAN

UniProt

Q9Y2H1 - ST38L_HUMAN

Protein

Serine/threonine-protein kinase 38-like

Gene

STK38L

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 128 (01 Oct 2014)
      Sequence version 3 (21 Dec 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved in the regulation of structural processes in differentiating and mature neuronal cells.By similarity

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.

    Enzyme regulationi

    Activated by binding of S100B which releases autoinhibitory N-lobe interactions, enabling ATP to bind and the autophosphorylation of Ser-282. Thr-442 then undergoes calcium-dependent phosphorylation by STK24/MST3. Interactions between phosphorylated Thr-442 and the N-lobe promote additional structural changes that complete the activation of the kinase. Autoinhibition is also released by the binding of MOB1/MOBKL1A and MOB2/HCCA2 to the N-terminal of STK38L.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei119 – 1191ATP1 PublicationPROSITE-ProRule annotation
    Active sitei213 – 2131Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi96 – 1049ATPBy similarityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. magnesium ion binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. intracellular signal transduction Source: UniProtKB
    2. protein phosphorylation Source: UniProtKB
    3. regulation of cellular component organization Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    Actin-binding, ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiQ9Y2H1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase 38-like (EC:2.7.11.1)
    Alternative name(s):
    NDR2 protein kinase
    Nuclear Dbf2-related kinase 2
    Gene namesi
    Name:STK38LImported
    Synonyms:KIAA0965Imported, NDR21 Publication
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:17848. STK38L.

    Subcellular locationi

    Cytoplasm. Cytoplasmcytoskeleton. Membrane
    Note: Associated with the actin cytoskeleton. Co-localizes with STK24/MST3 in the membrane.

    GO - Cellular componenti

    1. actin cytoskeleton Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi75 – 751T → A: Decreased kinase activity. Reduced binding of S100B. 1 Publication
    Mutagenesisi119 – 1191K → A: Loss of autophosphorylation and kinase activity. 1 Publication
    Mutagenesisi282 – 2821S → A: Loss of autophosphorylation and kinase activity. 1 Publication
    Mutagenesisi442 – 4421T → A: Decreased kinase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA38252.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 464463Serine/threonine-protein kinase 38-likePRO_0000086720Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei75 – 751Phosphothreonine1 Publication
    Modified residuei282 – 2821Phosphoserine; by autocatalysis1 Publication
    Modified residuei442 – 4421Phosphothreonine; by STK24/MST32 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y2H1.
    PaxDbiQ9Y2H1.
    PeptideAtlasiQ9Y2H1.
    PRIDEiQ9Y2H1.

    PTM databases

    PhosphoSiteiQ9Y2H1.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed with highest levels observed in the thymus.1 Publication

    Gene expression databases

    ArrayExpressiQ9Y2H1.
    BgeeiQ9Y2H1.
    CleanExiHS_STK38L.
    GenevestigatoriQ9Y2H1.

    Organism-specific databases

    HPAiHPA038623.

    Interactioni

    Subunit structurei

    Homodimeric S100B binds two molecules of STK38L. Interacts with MICAL1; leading to inhibit the protein kinase activity by antagonizing activation by MST1/STK4 By similarity. Interacts with MOB1 and MOB2.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDC37Q165432EBI-991501,EBI-295634
    MOB1AQ9H8S93EBI-991501,EBI-748229

    Protein-protein interaction databases

    BioGridi116654. 13 interactions.
    IntActiQ9Y2H1. 7 interactions.
    MINTiMINT-1631355.
    STRINGi9606.ENSP00000373684.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y2H1.
    SMRiQ9Y2H1. Positions 71-443.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini90 – 383294Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini384 – 45370AGC-kinase C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni63 – 8826S100B bindingBy similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233033.
    HOVERGENiHBG104247.
    InParanoidiQ9Y2H1.
    KOiK08790.
    OMAiYMKAGKA.
    PhylomeDBiQ9Y2H1.
    TreeFamiTF105337.

    Family and domain databases

    InterProiIPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR017892. Pkinase_C.
    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.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view]
    SMARTiSM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 2 hits.
    PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y2H1-1) [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

    MAMTAGTTTT FPMSNHTRER VTVAKLTLEN FYSNLILQHE ERETRQKKLE    50
    VAMEEEGLAD EEKKLRRSQH ARKETEFLRL KRTRLGLDDF ESLKVIGRGA 100
    FGEVRLVQKK DTGHIYAMKI LRKSDMLEKE QVAHIRAERD ILVEADGAWV 150
    VKMFYSFQDK RNLYLIMEFL PGGDMMTLLM KKDTLTEEET QFYISETVLA 200
    IDAIHQLGFI HRDIKPDNLL LDAKGHVKLS DFGLCTGLKK AHRTEFYRNL 250
    THNPPSDFSF QNMNSKRKAE TWKKNRRQLA YSTVGTPDYI APEVFMQTGY 300
    NKLCDWWSLG VIMYEMLIGY PPFCSETPQE TYRKVMNWKE TLVFPPEVPI 350
    SEKAKDLILR FCIDSENRIG NSGVEEIKGH PFFEGVDWEH IRERPAAIPI 400
    EIKSIDDTSN FDDFPESDIL QPVPNTTEPD YKSKDWVFLN YTYKRFEGLT 450
    QRGSIPTYMK AGKL 464
    Length:464
    Mass (Da):54,003
    Last modified:December 21, 2004 - v3
    Checksum:i71347E80BC3ADCB3
    GO
    Isoform 2 (identifier: Q9Y2H1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-52: Missing.
         62-102: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:371
    Mass (Da):43,170
    Checksum:iA8E29D3ED6CE7959
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti99 – 991G → A in a aLL TEL/AML1+ sample; somatic mutation. 1 Publication
    VAR_041199

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5252Missing in isoform 2. 1 PublicationVSP_056233Add
    BLAST
    Alternative sequencei62 – 10241Missing in isoform 2. 1 PublicationVSP_056234Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB023182 mRNA. Translation: BAA76809.2.
    AK291055 mRNA. Translation: BAF83744.1.
    AK304755 mRNA. Translation: BAG65510.1.
    AC092827 Genomic DNA. No translation available.
    AC092829 Genomic DNA. No translation available.
    CH471094 Genomic DNA. Translation: EAW96549.1.
    BC028603 mRNA. Translation: AAH28603.1.
    CCDSiCCDS31761.1.
    RefSeqiNP_055815.1. NM_015000.3.
    XP_006719121.1. XM_006719058.1.
    UniGeneiHs.184523.

    Genome annotation databases

    EnsembliENST00000389032; ENSP00000373684; ENSG00000211455.
    ENST00000539577; ENSP00000446386; ENSG00000211455.
    GeneIDi23012.
    KEGGihsa:23012.
    UCSCiuc001rhr.3. human.

    Polymorphism databases

    DMDMi56749668.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB023182 mRNA. Translation: BAA76809.2 .
    AK291055 mRNA. Translation: BAF83744.1 .
    AK304755 mRNA. Translation: BAG65510.1 .
    AC092827 Genomic DNA. No translation available.
    AC092829 Genomic DNA. No translation available.
    CH471094 Genomic DNA. Translation: EAW96549.1 .
    BC028603 mRNA. Translation: AAH28603.1 .
    CCDSi CCDS31761.1.
    RefSeqi NP_055815.1. NM_015000.3.
    XP_006719121.1. XM_006719058.1.
    UniGenei Hs.184523.

    3D structure databases

    ProteinModelPortali Q9Y2H1.
    SMRi Q9Y2H1. Positions 71-443.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116654. 13 interactions.
    IntActi Q9Y2H1. 7 interactions.
    MINTi MINT-1631355.
    STRINGi 9606.ENSP00000373684.

    Chemistry

    BindingDBi Q9Y2H1.
    ChEMBLi CHEMBL4851.
    GuidetoPHARMACOLOGYi 1518.

    PTM databases

    PhosphoSitei Q9Y2H1.

    Polymorphism databases

    DMDMi 56749668.

    Proteomic databases

    MaxQBi Q9Y2H1.
    PaxDbi Q9Y2H1.
    PeptideAtlasi Q9Y2H1.
    PRIDEi Q9Y2H1.

    Protocols and materials databases

    DNASUi 23012.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000389032 ; ENSP00000373684 ; ENSG00000211455 .
    ENST00000539577 ; ENSP00000446386 ; ENSG00000211455 .
    GeneIDi 23012.
    KEGGi hsa:23012.
    UCSCi uc001rhr.3. human.

    Organism-specific databases

    CTDi 23012.
    GeneCardsi GC12P027396.
    HGNCi HGNC:17848. STK38L.
    HPAi HPA038623.
    MIMi 615836. gene.
    neXtProti NX_Q9Y2H1.
    PharmGKBi PA38252.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233033.
    HOVERGENi HBG104247.
    InParanoidi Q9Y2H1.
    KOi K08790.
    OMAi YMKAGKA.
    PhylomeDBi Q9Y2H1.
    TreeFami TF105337.

    Enzyme and pathway databases

    SignaLinki Q9Y2H1.

    Miscellaneous databases

    ChiTaRSi STK38L. human.
    GeneWikii STK38L.
    GenomeRNAii 23012.
    NextBioi 43932.
    PROi Q9Y2H1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y2H1.
    Bgeei Q9Y2H1.
    CleanExi HS_STK38L.
    Genevestigatori Q9Y2H1.

    Family and domain databases

    InterProi IPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR017892. Pkinase_C.
    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.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view ]
    SMARTi SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 2 hits.
    PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Regulation of NDR2 protein kinase by multi-site phosphorylation and the S100B calcium-binding protein."
      Stegert M.R., Tamaskovic R., Bichsel S.J., Hergovich A., Hemmings B.A.
      J. Biol. Chem. 279:23806-23812(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, INTERACTION WITH S100, PHOSPHORYLATION AT THR-75; SER-282 AND THR-442, MUTAGENESIS OF THR-75; LYS-119; SER-282 AND THR-442.
      Tissue: Brain1 Publication.
    2. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: BrainImported.
    3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    4. "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: Uterus.
    5. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 1).
      Tissue: TestisImported.
    8. Bienvenut W.V., Vousden K.H., Lukashchuk N., Calvo F., Kolch W.
      Submitted (MAR-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-18; 26-42; 48-64; 73-79; 83-98; 123-161; 213-224; 229-240; 249-266; 340-392 AND 433-460, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma and Lung carcinoma.
    9. "Human Mob proteins regulate the NDR1 and NDR2 serine-threonine kinases."
      Devroe E., Erdjument-Bromage H., Tempst P., Silver P.A.
      J. Biol. Chem. 279:24444-24451(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ENZYME REGULATION, INTERACTION WITH MOB1 AND MOB2.
    10. "Regulation of NDR protein kinase by hydrophobic motif phosphorylation mediated by the mammalian Ste20-like kinase MST3."
      Stegert M.R., Hergovich A., Tamaskovic R., Bichsel S.J., Hemmings B.A.
      Mol. Cell. Biol. 25:11019-11029(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-442, ENZYME REGULATION, SUBCELLULAR LOCATION.
    11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-99.

    Entry informationi

    Entry nameiST38L_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y2H1
    Secondary accession number(s): A8K4U0, B4E3J8, Q8TBX7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 21, 2004
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 128 of the entry and version 3 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3