Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cyclin-L1

Gene

CCNL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

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 Componenti: 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

  • nuclear speck Source: UniProtKB-SubCell
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA134980948.

Polymorphism and mutation databases

BioMutaiCCNL1.
DMDMi74753368.

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 – 3521Phosphoserine4 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

BgeeiQ9UK58.
CleanExiHS_CCNL1.
ExpressionAtlasiQ9UK58. baseline and differential.
GenevisibleiQ9UK58. HS.

Organism-specific databases

HPAiHPA034752.
HPA057911.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
APPBP2Q926243EBI-2836773,EBI-743771
TFIP11Q9UBB93EBI-2836773,EBI-1105213

Protein-protein interaction databases

BioGridi121327. 11 interactions.
IntActiQ9UK58. 10 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.
GeneTreeiENSGT00760000119191.
HOVERGENiHBG056044.
InParanoidiQ9UK58.
OMAiCELIQSA.
PhylomeDBiQ9UK58.
TreeFamiTF101011.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR015429. Cyclin_C/H/T/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. AlignAdd to basket

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

        10         20         30         40         50
MASGPHSTAT AAAAASSAAP SAGGSSSGTT TTTTTTTGGI LIGDRLYSEV
60 70 80 90 100
SLTIDHSLIP EERLSPTPSM QDGLDLPSET DLRILGCELI QAAGILLRLP
110 120 130 140 150
QVAMATGQVL FHRFFYSKSF VKHSFEIVAM ACINLASKIE EAPRRIRDVI
160 170 180 190 200
NVFHHLRQLR GKRTPSPLIL DQNYINTKNQ VIKAERRVLK ELGFCVHVKH
210 220 230 240 250
PHKIIVMYLQ VLECERNQTL VQTAWNYMND SLRTNVFVRF QPETIACACI
260 270 280 290 300
YLAARALQIP LPTRPHWFLL FGTTEEEIQE ICIETLRLYT RKKPNYELLE
310 320 330 340 350
KEVEKRKVAL QEAKLKAKGL NPDGTPALST LGGFSPASKP SSPREVKAEE
360 370 380 390 400
KSPISINVKT VKKEPEDRQQ ASKSPYNGVR KDSKRSRNSR SASRSRSRTR
410 420 430 440 450
SRSRSHTPRR HYNNRRSRSG TYSSRSRSRS RSHSESPRRH HNHGSPHLKA
460 470 480 490 500
KHTRDDLKSS NRHGHKRKKS RSRSQSKSRD HSDAAKKHRH ERGHHRDRRE
510 520
RSRSFERSHK SKHHGGSRSG HGRHRR
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.Probable cloning artifact.Curated
The sequence AAQ89026.1 differs from that shown.Probable cloning artifact.Curated

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:
EMBLi
GenBanki
DDBJi
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_020307.3. [Q9UK58-1]
XP_005247707.1. XM_005247650.2.
XP_005247708.1. XM_005247651.2. [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]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_020307.3. [Q9UK58-1]
XP_005247707.1. XM_005247650.2.
XP_005247708.1. XM_005247651.2. [Q9UK58-4]
UniGeneiHs.4859.

3D structure databases

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

Protein-protein interaction databases

BioGridi121327. 11 interactions.
IntActiQ9UK58. 10 interactions.
MINTiMINT-4541433.
STRINGi9606.ENSP00000295926.

PTM databases

PhosphoSiteiQ9UK58.

Polymorphism and mutation databases

BioMutaiCCNL1.
DMDMi74753368.

Proteomic databases

MaxQBiQ9UK58.
PaxDbiQ9UK58.
PRIDEiQ9UK58.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi57018.
GeneCardsiGC03M156864.
HGNCiHGNC:20569. CCNL1.
HPAiHPA034752.
HPA057911.
MIMi613384. gene.
neXtProtiNX_Q9UK58.
PharmGKBiPA134980948.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5333.
GeneTreeiENSGT00760000119191.
HOVERGENiHBG056044.
InParanoidiQ9UK58.
OMAiCELIQSA.
PhylomeDBiQ9UK58.
TreeFamiTF101011.

Enzyme and pathway databases

SignaLinkiQ9UK58.

Miscellaneous databases

ChiTaRSiCCNL1. human.
GeneWikiiCCNL1.
GenomeRNAii57018.
NextBioi62766.
PROiQ9UK58.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UK58.
CleanExiHS_CCNL1.
ExpressionAtlasiQ9UK58. baseline and differential.
GenevisibleiQ9UK58. HS.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR015429. Cyclin_C/H/T/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.
ProtoNetiSearch...

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].
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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: June 24, 2015
This is version 129 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.