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Q9UK58

- CCNL1_HUMAN

UniProt

Q9UK58 - CCNL1_HUMAN

Protein

Cyclin-L1

Gene

CCNL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Transcriptional regulator which participates in regulating the pre-mRNA splicing process. Seems to be involved in the regulation of RNA polymerase II (pol II). Functions in association with cyclin-dependent kinases (CDKs) and has a role in the second step of splicing. May be a candidate proto-oncogene in head and neck squamous cell carcinomas (HNSCC). Inhibited by the CDK-specific inhibitor p21.3 Publications

    GO - Biological processi

    1. regulation of cyclin-dependent protein serine/threonine kinase activity Source: InterPro
    2. regulation of transcription, DNA-templated Source: UniProtKB-KW
    3. RNA processing Source: InterPro
    4. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Cyclin

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    SignaLinkiQ9UK58.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclin-L1
    Short name:
    Cyclin-L
    Gene namesi
    Name:CCNL1
    ORF Names:BM-001, UNQ530/PRO1073
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:20569. CCNL1.

    Subcellular locationi

    Nucleus speckle By similarity
    Note: More specifically found in nuclear intrachromatin granules clusters (IGC), also called nuclear speckles, which are storage compartments for nuclear proteins involved in mRNA processing.By similarity

    GO - Cellular componenti

    1. nuclear speck Source: UniProtKB-SubCell
    2. nucleus Source: MGI

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA134980948.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 526526Cyclin-L1PRO_0000080480Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei325 – 3251Phosphothreonine1 Publication
    Modified residuei335 – 3351Phosphoserine3 Publications
    Modified residuei338 – 3381Phosphoserine2 Publications
    Modified residuei352 – 3521Phosphoserine3 Publications
    Modified residuei355 – 3551PhosphoserineBy similarity
    Modified residuei445 – 4451Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UK58.
    PaxDbiQ9UK58.
    PRIDEiQ9UK58.

    PTM databases

    PhosphoSiteiQ9UK58.

    Expressioni

    Tissue specificityi

    Ubiquitous with higher level in thymus. Overexpression in primary tumors of head and neck squamous cell carcinomas (HNSCC).3 Publications

    Gene expression databases

    ArrayExpressiQ9UK58.
    BgeeiQ9UK58.
    CleanExiHS_CCNL1.
    GenevestigatoriQ9UK58.

    Organism-specific databases

    HPAiHPA034752.

    Interactioni

    Subunit structurei

    Interacts with POLR2A via its hyperphosphorylated C-terminal domain (CTD) By similarity. Interacts with CDK11A, CDK11B, CDK12, CDK13 and SFRS2.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi121327. 8 interactions.
    IntActiQ9UK58. 8 interactions.
    MINTiMINT-4541433.
    STRINGi9606.ENSP00000295926.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UK58.
    SMRiQ9UK58. Positions 64-293.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni88 – 190103Cyclin-like 1Add
    BLAST
    Regioni203 – 28785Cyclin-like 2Add
    BLAST
    Regioni390 – 43243RSAdd
    BLAST

    Domaini

    Contains a RS region (arginine-serine dipeptide repeat) within the C-terminal domain which is the hallmark of the SR family of splicing factors. This region probably plays a role in protein-protein interactions.1 Publication

    Sequence similaritiesi

    Belongs to the cyclin family. Cyclin L subfamily.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5333.
    HOVERGENiHBG056044.
    InParanoidiQ9UK58.
    OMAiFERSHKG.
    PhylomeDBiQ9UK58.
    TreeFamiTF101011.

    Family and domain databases

    Gene3Di1.10.472.10. 2 hits.
    InterProiIPR013763. Cyclin-like.
    IPR015429. Cyclin_C/H/T/L.
    IPR017060. Cyclin_L.
    IPR015431. Cyclin_L1_chr.
    IPR006671. Cyclin_N.
    [Graphical view]
    PANTHERiPTHR10026. PTHR10026. 1 hit.
    PTHR10026:SF64. PTHR10026:SF64. 1 hit.
    PfamiPF00134. Cyclin_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036580. Cyclin_L. 1 hit.
    SMARTiSM00385. CYCLIN. 2 hits.
    [Graphical view]
    SUPFAMiSSF47954. SSF47954. 2 hits.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Ccnl1 is an immediate-early gene with independently regulated isoforms.

    Isoform 1 (identifier: Q9UK58-1) [UniParc]FASTAAdd to Basket

    Also known as: Cyclin L alpha

    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

    MASGPHSTAT AAAAASSAAP SAGGSSSGTT TTTTTTTGGI LIGDRLYSEV    50
    SLTIDHSLIP EERLSPTPSM QDGLDLPSET DLRILGCELI QAAGILLRLP 100
    QVAMATGQVL FHRFFYSKSF VKHSFEIVAM ACINLASKIE EAPRRIRDVI 150
    NVFHHLRQLR GKRTPSPLIL DQNYINTKNQ VIKAERRVLK ELGFCVHVKH 200
    PHKIIVMYLQ VLECERNQTL VQTAWNYMND SLRTNVFVRF QPETIACACI 250
    YLAARALQIP LPTRPHWFLL FGTTEEEIQE ICIETLRLYT RKKPNYELLE 300
    KEVEKRKVAL QEAKLKAKGL NPDGTPALST LGGFSPASKP SSPREVKAEE 350
    KSPISINVKT VKKEPEDRQQ ASKSPYNGVR KDSKRSRNSR SASRSRSRTR 400
    SRSRSHTPRR HYNNRRSRSG TYSSRSRSRS RSHSESPRRH HNHGSPHLKA 450
    KHTRDDLKSS NRHGHKRKKS RSRSQSKSRD HSDAAKKHRH ERGHHRDRRE 500
    RSRSFERSHK SKHHGGSRSG HGRHRR 526
    Length:526
    Mass (Da):59,634
    Last modified:May 1, 2000 - v1
    Checksum:i64C0CAEF54A3E9F9
    GO
    Isoform 2 (identifier: Q9UK58-4) [UniParc]FASTAAdd to Basket

    Also known as: Cyclin L beta

    The sequence of this isoform differs from the canonical sequence as follows:
         226-232: NYMNDSL → VVHDGKS
         233-526: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:232
    Mass (Da):25,408
    Checksum:iACD35FB41FF67306
    GO
    Isoform 3 (identifier: Q9UK58-5) [UniParc]FASTAAdd to Basket

    Also known as: Cyclin L gamma

    The sequence of this isoform differs from the canonical sequence as follows:
         163-172: RTPSPLILDQ → SDQLHLPKPG
         173-526: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:172
    Mass (Da):18,322
    Checksum:i972B0E52D25720E1
    GO

    Sequence cautioni

    The sequence AAF64257.1 differs from that shown. Reason: Probable cloning artifact.
    The sequence AAQ89026.1 differs from that shown. Reason: Probable cloning artifact.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti149 – 1491V → L in AAH67812. (PubMed:15489334)Curated
    Sequence conflicti507 – 5082RS → SP in AAF64257. (PubMed:11042152)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei163 – 17210RTPSPLILDQ → SDQLHLPKPG in isoform 3. 1 PublicationVSP_016120
    Alternative sequencei173 – 526354Missing in isoform 3. 1 PublicationVSP_016121Add
    BLAST
    Alternative sequencei226 – 2327NYMNDSL → VVHDGKS in isoform 2. 1 PublicationVSP_016122
    Alternative sequencei233 – 526294Missing in isoform 2. 1 PublicationVSP_016123Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF180920 mRNA. Translation: AAD53184.1.
    AK022974 mRNA. Translation: BAG51145.1.
    AF367476 mRNA. Translation: AAM21204.1.
    AF367477 mRNA. Translation: AAM21205.1.
    AY034790 mRNA. Translation: AAK61551.1.
    CH471052 Genomic DNA. Translation: EAW78712.1.
    BC007081 mRNA. Translation: AAH07081.1.
    BC038394 mRNA. Translation: AAH38394.1.
    BC067812 mRNA. Translation: AAH67812.1.
    AF208843 mRNA. Translation: AAF64257.1. Sequence problems.
    AY358663 mRNA. Translation: AAQ89026.1. Sequence problems.
    CCDSiCCDS3178.1. [Q9UK58-1]
    RefSeqiNP_064703.1. NM_020307.2. [Q9UK58-1]
    XP_005247707.1. XM_005247650.1.
    XP_005247708.1. XM_005247651.1. [Q9UK58-4]
    UniGeneiHs.4859.

    Genome annotation databases

    EnsembliENST00000295925; ENSP00000295925; ENSG00000163660. [Q9UK58-5]
    ENST00000295926; ENSP00000295926; ENSG00000163660. [Q9UK58-1]
    ENST00000465947; ENSP00000418094; ENSG00000163660. [Q9UK58-5]
    ENST00000470121; ENSP00000417237; ENSG00000163660. [Q9UK58-4]
    ENST00000475298; ENSP00000417343; ENSG00000163660. [Q9UK58-5]
    ENST00000477127; ENSP00000418449; ENSG00000163660. [Q9UK58-5]
    GeneIDi57018.
    KEGGihsa:57018.
    UCSCiuc003fbe.3. human. [Q9UK58-1]

    Polymorphism databases

    DMDMi74753368.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF180920 mRNA. Translation: AAD53184.1 .
    AK022974 mRNA. Translation: BAG51145.1 .
    AF367476 mRNA. Translation: AAM21204.1 .
    AF367477 mRNA. Translation: AAM21205.1 .
    AY034790 mRNA. Translation: AAK61551.1 .
    CH471052 Genomic DNA. Translation: EAW78712.1 .
    BC007081 mRNA. Translation: AAH07081.1 .
    BC038394 mRNA. Translation: AAH38394.1 .
    BC067812 mRNA. Translation: AAH67812.1 .
    AF208843 mRNA. Translation: AAF64257.1 . Sequence problems.
    AY358663 mRNA. Translation: AAQ89026.1 . Sequence problems.
    CCDSi CCDS3178.1. [Q9UK58-1 ]
    RefSeqi NP_064703.1. NM_020307.2. [Q9UK58-1 ]
    XP_005247707.1. XM_005247650.1.
    XP_005247708.1. XM_005247651.1. [Q9UK58-4 ]
    UniGenei Hs.4859.

    3D structure databases

    ProteinModelPortali Q9UK58.
    SMRi Q9UK58. Positions 64-293.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121327. 8 interactions.
    IntActi Q9UK58. 8 interactions.
    MINTi MINT-4541433.
    STRINGi 9606.ENSP00000295926.

    PTM databases

    PhosphoSitei Q9UK58.

    Polymorphism databases

    DMDMi 74753368.

    Proteomic databases

    MaxQBi Q9UK58.
    PaxDbi Q9UK58.
    PRIDEi Q9UK58.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295925 ; ENSP00000295925 ; ENSG00000163660 . [Q9UK58-5 ]
    ENST00000295926 ; ENSP00000295926 ; ENSG00000163660 . [Q9UK58-1 ]
    ENST00000465947 ; ENSP00000418094 ; ENSG00000163660 . [Q9UK58-5 ]
    ENST00000470121 ; ENSP00000417237 ; ENSG00000163660 . [Q9UK58-4 ]
    ENST00000475298 ; ENSP00000417343 ; ENSG00000163660 . [Q9UK58-5 ]
    ENST00000477127 ; ENSP00000418449 ; ENSG00000163660 . [Q9UK58-5 ]
    GeneIDi 57018.
    KEGGi hsa:57018.
    UCSCi uc003fbe.3. human. [Q9UK58-1 ]

    Organism-specific databases

    CTDi 57018.
    GeneCardsi GC03M156864.
    HGNCi HGNC:20569. CCNL1.
    HPAi HPA034752.
    MIMi 613384. gene.
    neXtProti NX_Q9UK58.
    PharmGKBi PA134980948.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5333.
    HOVERGENi HBG056044.
    InParanoidi Q9UK58.
    OMAi FERSHKG.
    PhylomeDBi Q9UK58.
    TreeFami TF101011.

    Enzyme and pathway databases

    SignaLinki Q9UK58.

    Miscellaneous databases

    GeneWikii CCNL1.
    GenomeRNAii 57018.
    NextBioi 62766.
    PROi Q9UK58.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UK58.
    Bgeei Q9UK58.
    CleanExi HS_CCNL1.
    Genevestigatori Q9UK58.

    Family and domain databases

    Gene3Di 1.10.472.10. 2 hits.
    InterProi IPR013763. Cyclin-like.
    IPR015429. Cyclin_C/H/T/L.
    IPR017060. Cyclin_L.
    IPR015431. Cyclin_L1_chr.
    IPR006671. Cyclin_N.
    [Graphical view ]
    PANTHERi PTHR10026. PTHR10026. 1 hit.
    PTHR10026:SF64. PTHR10026:SF64. 1 hit.
    Pfami PF00134. Cyclin_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036580. Cyclin_L. 1 hit.
    SMARTi SM00385. CYCLIN. 2 hits.
    [Graphical view ]
    SUPFAMi SSF47954. SSF47954. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Cyclin L is an RS domain protein involved in pre-mRNA splicing."
      Dickinson L.A., Edgar A.J., Ehley J., Gottesfeld J.M.
      J. Biol. Chem. 277:25465-25473(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, TISSUE SPECIFICITY, DOMAIN, INTERACTION WITH CDC2L AND SFRS2.
      Tissue: Lung.
    2. "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 1).
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Brain and Testis.
    5. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 204-526 (ISOFORM 1).
      Tissue: Bone marrow.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 226-526 (ISOFORM 1).
    7. "Amplicon mapping and transcriptional analysis pinpoint cyclin L as a candidate oncogene in head and neck cancer."
      Redon R., Hussenet T., Bour G., Caulee K., Jost B., Muller D., Abecassis J., du Manoir S.
      Cancer Res. 62:6211-6217(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    8. "Amplification of Cyclin L1 is associated with lymph node metastases in head and neck squamous cell carcinoma (HNSCC)."
      Sticht C., Hofele C., Flechtenmacher C., Bosch F.X., Freier K., Lichter P., Joos S.
      Br. J. Cancer 92:770-774(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-325; SER-335 AND SER-338, 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: IDENTIFICATION BY MASS SPECTROMETRY [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-335; SER-338 AND SER-352, 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-335; SER-352 AND SER-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCCNL1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UK58
    Secondary accession number(s): B3KMY3
    , Q6NVY9, Q6UWS7, Q8NI48, Q96QT0, Q9NZF3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 121 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

    Miscellaneous

    CCNL1 is amplified in several HNSCC. May play a critical role in the formation of loco-regional metastases and an unfavorable clinical outcome of HNSCC.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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