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Q9UK58

- CCNL1_HUMAN

UniProt

Q9UK58 - CCNL1_HUMAN

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Protein

Cyclin-L1

Gene
CCNL1, BM-001, UNQ530/PRO1073
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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 – 3551Phosphoserine By 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 SFRS2.1 Publication

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ9UK58.
SMRiQ9UK58. Positions 64-293.

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

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei163 – 17210RTPSPLILDQ → SDQLHLPKPG in isoform 3. VSP_016120
Alternative sequencei173 – 526354Missing in isoform 3. VSP_016121Add
BLAST
Alternative sequencei226 – 2327NYMNDSL → VVHDGKS in isoform 2. VSP_016122
Alternative sequencei233 – 526294Missing in isoform 2. VSP_016123Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti149 – 1491V → L in AAH67812. 1 Publication
Sequence conflicti507 – 5082RS → SP in AAF64257. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 120 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

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