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)

Q5TKA1

- LIN9_HUMAN

UniProt

Q5TKA1 - LIN9_HUMAN

Protein

Protein lin-9 homolog

Gene

LIN9

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 86 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Acts as a tumor suppressor. Inhibits DNA synthesis. Its ability to inhibit oncogenic transformation is mediated through its association with RB1. Plays a role in the expression of genes required for the G1/S transition.2 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. DNA replication Source: UniProtKB-KW
    2. G2/M transition of mitotic cell cycle Source: Reactome
    3. mitotic cell cycle Source: Reactome
    4. regulation of cell cycle Source: Reactome
    5. transcription, DNA-templated Source: InterPro

    Keywords - Biological processi

    Cell cycle, DNA synthesis

    Enzyme and pathway databases

    ReactomeiREACT_1006. Polo-like kinase mediated events.
    REACT_111214. G0 and Early G1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein lin-9 homolog
    Short name:
    HuLin-9
    Short name:
    hLin-9
    Alternative name(s):
    Beta subunit-associated regulator of apoptosis
    TUDOR gene similar protein
    Type I interferon receptor beta chain-associated protein
    pRB-associated protein
    Gene namesi
    Name:LIN9
    Synonyms:BARA, TGS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:30830. LIN9.

    Subcellular locationi

    Nucleusnucleoplasm 2 Publications
    Note: Found in perinucleolar structures. Associated with chromatin.

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. transcriptional repressor complex Source: InterPro

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA134970771.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 542541Protein lin-9 homologPRO_0000249546Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei65 – 651Phosphoserine1 Publication
    Modified residuei304 – 3041Phosphothreonine1 Publication
    Modified residuei309 – 3091Phosphoserine5 Publications
    Modified residuei321 – 3211Phosphoserine5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ5TKA1.
    PaxDbiQ5TKA1.
    PRIDEiQ5TKA1.

    PTM databases

    PhosphoSiteiQ5TKA1.

    Expressioni

    Tissue specificityi

    Expressed in thymus and testis.1 Publication

    Gene expression databases

    ArrayExpressiQ5TKA1.
    BgeeiQ5TKA1.
    CleanExiHS_LIN9.
    GenevestigatoriQ5TKA1.

    Organism-specific databases

    HPAiHPA030241.

    Interactioni

    Subunit structurei

    Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2. Interacts with RB1.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    E2F4Q162543EBI-1389424,EBI-448943
    MYBL2P102447EBI-1389424,EBI-1389468

    Protein-protein interaction databases

    BioGridi130420. 15 interactions.
    IntActiQ5TKA1. 14 interactions.
    MINTiMINT-4054198.
    STRINGi9606.ENSP00000329102.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 296295Sufficient for interaction with RB1Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili354 – 41360Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the lin-9 family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG148048.
    HOGENOMiHOG000007517.
    HOVERGENiHBG057743.
    InParanoidiQ5TKA1.
    OrthoDBiEOG71ZP10.
    PhylomeDBiQ5TKA1.
    TreeFamiTF314315.

    Family and domain databases

    InterProiIPR010561. LIN-9/ALY1.
    [Graphical view]
    PANTHERiPTHR21689. PTHR21689. 1 hit.
    PfamiPF06584. DIRP. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q5TKA1-1) [UniParc]FASTAAdd to Basket

    Also known as: Lin9-L, Long form

    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

    MAELDQLPDE SSSAKALVSL KEGSLSNTWN EKYSSLQKTP VWKGRNTSSA    50
    VEMPFRNSKR SRLFSDEDDR QINTRSPKRN QRVAMVPQKF TATMSTPDKK 100
    ASQKIGFRLR NLLKLPKAHK WCIYEWFYSN IDKPLFEGDN DFCVCLKESF 150
    PNLKTRKLTR VEWGKIRRLM GKPRRCSSAF FEEERSALKQ KRQKIRLLQQ 200
    RKVADVSQFK DLPDEIPLPL VIGTKVTARL RGVHDGLFTG QIDAVDTLNA 250
    TYRVTFDRTG LGTHTIPDYE VLSNEPHETM PIAAFGQKQR PSRFFMTPPR 300
    LHYTPPLQSP IIDNDPLLGQ SPWRSKISGS DTETLGGFPV EFLIQVTRLS 350
    KILMIKKEHI KKLREMNTEA EKLKSYSMPI SIEFQRRYAT IVLELEQLNK 400
    DLNKVLHKVQ QYCYELAPDQ GLQPADQPTD MRRRCEEEAQ EIVRHANSST 450
    GQPCVENENL TDLISRLTAI LLQIKCLAEG GDLNSFEFKS LTDSLNDIKS 500
    TIDASNISCF QNNVEIHVAH IQSGLSQMGN LHAFAANNTN RD 542
    Length:542
    Mass (Da):61,946
    Last modified:December 21, 2004 - v1
    Checksum:i1107865E6FF33037
    GO
    Isoform 2 (identifier: Q5TKA1-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:558
    Mass (Da):63,811
    Checksum:i90ECE86266AF02CE
    GO
    Isoform 3 (identifier: Q5TKA1-3) [UniParc]FASTAAdd to Basket

    Also known as: Lin9-S, Short form

    The sequence of this isoform differs from the canonical sequence as follows:
         54-88: Missing.

    Show »
    Length:507
    Mass (Da):57,733
    Checksum:iB657E9DD7A2882F0
    GO

    Sequence cautioni

    The sequence AAH43444.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAD97871.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti436 – 4361E → V in AAH43444. (PubMed:15489334)Curated
    Sequence conflicti508 – 5081S → R in AAV41873. (PubMed:15538385)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MHRGGQPLKKRRGSFKM in isoform 2. 1 PublicationVSP_020509
    Alternative sequencei54 – 8835Missing in isoform 3. 2 PublicationsVSP_020510Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY786184 mRNA. Translation: AAV41873.1.
    AF190323 mRNA. Translation: AAQ13710.1.
    AF190324 mRNA. Translation: AAQ13711.1.
    AK126177 mRNA. Translation: BAC86475.1.
    BX537869 mRNA. Translation: CAD97871.1. Different initiation.
    BC043444 mRNA. Translation: AAH43444.1. Different initiation.
    BC045625 mRNA. Translation: AAH45625.1.
    CCDSiCCDS1553.1. [Q5TKA1-2]
    RefSeqiNP_001257338.1. NM_001270409.1.
    NP_001257339.1. NM_001270410.1.
    NP_775106.2. NM_173083.3. [Q5TKA1-2]
    UniGeneiHs.120817.

    Genome annotation databases

    EnsembliENST00000328205; ENSP00000329102; ENSG00000183814. [Q5TKA1-2]
    GeneIDi286826.
    KEGGihsa:286826.
    UCSCiuc001hqa.3. human. [Q5TKA1-2]
    uc001hqc.4. human. [Q5TKA1-1]

    Polymorphism databases

    DMDMi74708186.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY786184 mRNA. Translation: AAV41873.1 .
    AF190323 mRNA. Translation: AAQ13710.1 .
    AF190324 mRNA. Translation: AAQ13711.1 .
    AK126177 mRNA. Translation: BAC86475.1 .
    BX537869 mRNA. Translation: CAD97871.1 . Different initiation.
    BC043444 mRNA. Translation: AAH43444.1 . Different initiation.
    BC045625 mRNA. Translation: AAH45625.1 .
    CCDSi CCDS1553.1. [Q5TKA1-2 ]
    RefSeqi NP_001257338.1. NM_001270409.1.
    NP_001257339.1. NM_001270410.1.
    NP_775106.2. NM_173083.3. [Q5TKA1-2 ]
    UniGenei Hs.120817.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 130420. 15 interactions.
    IntActi Q5TKA1. 14 interactions.
    MINTi MINT-4054198.
    STRINGi 9606.ENSP00000329102.

    PTM databases

    PhosphoSitei Q5TKA1.

    Polymorphism databases

    DMDMi 74708186.

    Proteomic databases

    MaxQBi Q5TKA1.
    PaxDbi Q5TKA1.
    PRIDEi Q5TKA1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000328205 ; ENSP00000329102 ; ENSG00000183814 . [Q5TKA1-2 ]
    GeneIDi 286826.
    KEGGi hsa:286826.
    UCSCi uc001hqa.3. human. [Q5TKA1-2 ]
    uc001hqc.4. human. [Q5TKA1-1 ]

    Organism-specific databases

    CTDi 286826.
    GeneCardsi GC01M226420.
    HGNCi HGNC:30830. LIN9.
    HPAi HPA030241.
    MIMi 609375. gene.
    neXtProti NX_Q5TKA1.
    PharmGKBi PA134970771.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG148048.
    HOGENOMi HOG000007517.
    HOVERGENi HBG057743.
    InParanoidi Q5TKA1.
    OrthoDBi EOG71ZP10.
    PhylomeDBi Q5TKA1.
    TreeFami TF314315.

    Enzyme and pathway databases

    Reactomei REACT_1006. Polo-like kinase mediated events.
    REACT_111214. G0 and Early G1.

    Miscellaneous databases

    GeneWikii LIN9.
    GenomeRNAii 286826.
    NextBioi 96300.
    PROi Q5TKA1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q5TKA1.
    Bgeei Q5TKA1.
    CleanExi HS_LIN9.
    Genevestigatori Q5TKA1.

    Family and domain databases

    InterProi IPR010561. LIN-9/ALY1.
    [Graphical view ]
    PANTHERi PTHR21689. PTHR21689. 1 hit.
    Pfami PF06584. DIRP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Inhibition of oncogenic transformation by mammalian Lin-9, a pRB-associated protein."
      Gagrica S., Hauser S., Kolfschoten I., Osterloh L., Agami R., Gaubatz S.
      EMBO J. 23:4627-4638(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH RB1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Cervix carcinoma.
    2. "A mutant allele of BARA/LIN-9 rescues the cdk4-/- phenotype by releasing the repression on E2F-regulated genes."
      Sandoval R., Xue J., Tian X., Barrett K., Pilkinton M., Ucker D.S., Raychaudhuri P., Kineman R.D., Luque R.M., Baida G., Zou X., Valli V.E., Cook J.L., Kiyokawa H., Colamonici O.R.
      Exp. Cell Res. 312:2465-2475(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, SUBCELLULAR LOCATION.
      Tissue: Myeloma.
    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] (ISOFORM 3).
      Tissue: Thymus.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Heart.
    5. "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] (ISOFORMS 1 AND 2).
      Tissue: Testis.
    6. "LINC, a human complex that is related to pRB-containing complexes in invertebrates regulates the expression of G2/M genes."
      Schmit F., Korenjak M., Mannefeld M., Schmitt K., Franke C., von Eyss B., Gagrica S., Haenel F., Brehm A., Gaubatz S.
      Cell Cycle 6:1903-1913(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE DREAM COMPLEX.
    7. "Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein complex represses human cell cycle-dependent genes in quiescence."
      Litovchick L., Sadasivam S., Florens L., Zhu X., Swanson S.K., Velmurugan S., Chen R., Washburn M.P., Liu X.S., DeCaprio J.A.
      Mol. Cell 26:539-551(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE DREAM COMPLEX.
    8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309 AND SER-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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-309 AND SER-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309 AND SER-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309 AND SER-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "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-65; THR-304; SER-309 AND SER-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.

    Entry informationi

    Entry nameiLIN9_HUMAN
    AccessioniPrimary (citable) accession number: Q5TKA1
    Secondary accession number(s): Q5U5L8
    , Q5U7E1, Q6PI55, Q6ZTV4, Q7Z3J1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2006
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 86 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3