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Protein

Protein lin-54 homolog

Gene

LIN54

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the DREAM complex, a multiprotein complex that can both act as a transcription activator or repressor depending on the context. In G0 phase, the complex binds to more than 800 promoters and is required for repression of E2F target genes. In S phase, the complex selectively binds to the promoters of G2/M genes whose products are required for mitosis and participates in their cell cycle dependent activation. In the complex, acts as a DNA-binding protein that binds the promoter of CDK1 in a sequence-specific manner.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-1538133. G0 and Early G1.
R-HSA-156711. Polo-like kinase mediated events.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein lin-54 homolog
Alternative name(s):
CXC domain-containing protein 1
Gene namesi
Name:LIN54
Synonyms:CXCDC1, KIAA2037
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:25397. LIN54.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi525 – 5251C → Y: Abolishes DNA-binding to the CDK1 promoter; when associated with Y-527. 1 Publication
Mutagenesisi527 – 5271C → Y: Abolishes DNA-binding to the CDK1 promoter; when associated with Y-525. 1 Publication

Organism-specific databases

PharmGKBiPA162394056.

Polymorphism and mutation databases

DMDMi313104222.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 749749Protein lin-54 homologPRO_0000341389Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei244 – 2441N6-acetyllysineCombined sources
Modified residuei249 – 2491N6-acetyllysineCombined sources
Modified residuei310 – 3101PhosphoserineCombined sources
Modified residuei314 – 3141PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ6MZP7.
MaxQBiQ6MZP7.
PaxDbiQ6MZP7.
PRIDEiQ6MZP7.

PTM databases

iPTMnetiQ6MZP7.
PhosphoSiteiQ6MZP7.

Expressioni

Gene expression databases

BgeeiQ6MZP7.
CleanExiHS_LIN54.
ExpressionAtlasiQ6MZP7. baseline and differential.
GenevisibleiQ6MZP7. HS.

Organism-specific databases

HPAiHPA056606.

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 MYBL2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MYBL2P102444EBI-1389411,EBI-1389468
RBL2Q0899910EBI-1389411,EBI-971439

Protein-protein interaction databases

BioGridi126328. 25 interactions.
IntActiQ6MZP7. 35 interactions.
MINTiMINT-7239317.
STRINGi9606.ENSP00000341947.

Structurei

3D structure databases

ProteinModelPortaliQ6MZP7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini521 – 634114CRCPROSITE-ProRule annotationAdd
BLAST

Domaini

The CXC domains mediate DNA-binding.1 Publication

Sequence similaritiesi

Belongs to the lin-54 family.Curated
Contains 1 CRC domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1171. Eukaryota.
ENOG4110UR5. LUCA.
GeneTreeiENSGT00390000013974.
HOGENOMiHOG000082518.
HOVERGENiHBG108088.
InParanoidiQ6MZP7.
OMAiTPGIQTQ.
OrthoDBiEOG7DFXBK.
PhylomeDBiQ6MZP7.
TreeFamiTF313189.

Family and domain databases

InterProiIPR005172. CRC.
IPR028307. Lin-54_fam.
IPR033467. Tesmin/TSO1-like_CXC.
[Graphical view]
PANTHERiPTHR12446. PTHR12446. 1 hit.
PfamiPF03638. TCR. 2 hits.
[Graphical view]
SMARTiSM01114. CXC. 2 hits.
[Graphical view]
PROSITEiPS51634. CRC. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6MZP7-1) [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

        10         20         30         40         50
MEVVPAEVNS LLPEEIMDTG ITLVDDDSIE AVIVSSPIPM ETELEEIVNI
60 70 80 90 100
NSTGDSTATP ISTEPITVYS NHTNQVAVNT TITKADSNTT VKPAFPSGLQ
110 120 130 140 150
KLGAQTPVTI SANQIILNKV SQTSDLKLGN QTLKPDGQKL ILTTLGKSGS
160 170 180 190 200
PIVLALPHSQ LPQAQKVTTQ AQSGDAKLPP QQIKVVTIGG RPEVKPVIGV
210 220 230 240 250
SALTPGSQLI NTTTQPSVLQ TQQLKTVQIA KKPRTPTSGP VITKLIFAKP
260 270 280 290 300
INSKAVTGQT TQVSPPVIAG RVLSQSTPGT PSKTITISES GVIGSTLNST
310 320 330 340 350
TQTPNKIAIS PLKSPNKAVK STVQTITVGG VSTSQFKTII PLATAPNVQQ
360 370 380 390 400
IQVPGSKFHY VRLVTATSAS SSTQPVSQNP STNTQPLQQA KPVVVNTTPV
410 420 430 440 450
RMSVPIVSAQ AVKQVVPKPI NPTSQIVTTS QPQQRLIMPA TPLPQIQPNL
460 470 480 490 500
TNLPPGTVLA PAPGTGNVGY AVLPAQYVTQ LQQSSYVSIA SNSTFTGTSG
510 520 530 540 550
IQTQARLPFN GIIPSESASR PRKPCNCTKS LCLKLYCDCF ANGEFCNNCN
560 570 580 590 600
CTNCYNNLEH ENERQKAIKA CLDRNPEAFK PKIGKGKEGE SDRRHSKGCN
610 620 630 640 650
CKRSGCLKNY CECYEAKIMC SSICKCIGCK NFEESPERKT LMHLADAAEV
660 670 680 690 700
RVQQQTAAKT KLSSQISDLL TRPTPALNSG GGKLPFTFVT KEVAEATCNC
710 720 730 740
LLAQAEQADK KGKSKAAAER MILEEFGRCL MSVINSAGKA KSDPCAMNC
Length:749
Mass (Da):79,494
Last modified:November 30, 2010 - v3
Checksum:iA3E4513CB0118B78
GO
Isoform 2 (identifier: Q6MZP7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     229-317: Missing.

Note: No experimental confirmation available.
Show »
Length:660
Mass (Da):70,378
Checksum:iF34917B51B87B370
GO
Isoform 3 (identifier: Q6MZP7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     8-228: Missing.

Show »
Length:528
Mass (Da):56,284
Checksum:i7EEAFDD538973450
GO
Isoform 4 (identifier: Q6MZP7-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-401: Missing.

Note: No experimental confirmation available.
Show »
Length:348
Mass (Da):37,613
Checksum:iB65DCCA3258768FB
GO
Isoform 5 (identifier: Q6MZP7-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     229-243: IAKKPRTPTSGPVIT → VGFFHSLLPELHQRP
     244-749: Missing.

Note: No experimental confirmation available.
Show »
Length:243
Mass (Da):25,743
Checksum:i6ECC642FE3E55419
GO

Sequence cautioni

The sequence BAC98377.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91N → S in CAE45981 (PubMed:17974005).Curated
Sequence conflicti743 – 7431D → A in CAE45981 (PubMed:17974005).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 401401Missing in isoform 4. 1 PublicationVSP_034272Add
BLAST
Alternative sequencei8 – 228221Missing in isoform 3. 2 PublicationsVSP_034273Add
BLAST
Alternative sequencei229 – 31789Missing in isoform 2. 1 PublicationVSP_034274Add
BLAST
Alternative sequencei229 – 24315IAKKP…GPVIT → VGFFHSLLPELHQRP in isoform 5. 1 PublicationVSP_034275Add
BLAST
Alternative sequencei244 – 749506Missing in isoform 5. 1 PublicationVSP_034276Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB111889 mRNA. Translation: BAC98377.1. Different initiation.
AK292769 mRNA. Translation: BAF85458.1.
BX640657 mRNA. Translation: CAE45799.1.
BX640966 mRNA. Translation: CAE45981.1.
AC021105 Genomic DNA. No translation available.
BC109277 mRNA. Translation: AAI09278.1.
BC109278 mRNA. Translation: AAI09279.1.
CCDSiCCDS3599.1. [Q6MZP7-1]
CCDS47089.1. [Q6MZP7-3]
CCDS75157.1. [Q6MZP7-2]
RefSeqiNP_001108479.1. NM_001115007.2. [Q6MZP7-3]
NP_001108480.1. NM_001115008.2. [Q6MZP7-3]
NP_001275925.1. NM_001288996.1. [Q6MZP7-2]
NP_001275926.1. NM_001288997.1. [Q6MZP7-3]
NP_919258.2. NM_194282.3. [Q6MZP7-1]
XP_005262807.1. XM_005262750.3. [Q6MZP7-1]
XP_006714144.1. XM_006714081.2. [Q6MZP7-1]
UniGeneiHs.96952.

Genome annotation databases

EnsembliENST00000340417; ENSP00000341947; ENSG00000189308. [Q6MZP7-1]
ENST00000442461; ENSP00000398265; ENSG00000189308. [Q6MZP7-3]
ENST00000446851; ENSP00000407139; ENSG00000189308. [Q6MZP7-3]
ENST00000505397; ENSP00000425844; ENSG00000189308. [Q6MZP7-1]
ENST00000506560; ENSP00000423475; ENSG00000189308. [Q6MZP7-2]
ENST00000508171; ENSP00000427413; ENSG00000189308. [Q6MZP7-5]
ENST00000510557; ENSP00000421045; ENSG00000189308. [Q6MZP7-3]
GeneIDi132660.
KEGGihsa:132660.
UCSCiuc003hnx.5. human. [Q6MZP7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB111889 mRNA. Translation: BAC98377.1. Different initiation.
AK292769 mRNA. Translation: BAF85458.1.
BX640657 mRNA. Translation: CAE45799.1.
BX640966 mRNA. Translation: CAE45981.1.
AC021105 Genomic DNA. No translation available.
BC109277 mRNA. Translation: AAI09278.1.
BC109278 mRNA. Translation: AAI09279.1.
CCDSiCCDS3599.1. [Q6MZP7-1]
CCDS47089.1. [Q6MZP7-3]
CCDS75157.1. [Q6MZP7-2]
RefSeqiNP_001108479.1. NM_001115007.2. [Q6MZP7-3]
NP_001108480.1. NM_001115008.2. [Q6MZP7-3]
NP_001275925.1. NM_001288996.1. [Q6MZP7-2]
NP_001275926.1. NM_001288997.1. [Q6MZP7-3]
NP_919258.2. NM_194282.3. [Q6MZP7-1]
XP_005262807.1. XM_005262750.3. [Q6MZP7-1]
XP_006714144.1. XM_006714081.2. [Q6MZP7-1]
UniGeneiHs.96952.

3D structure databases

ProteinModelPortaliQ6MZP7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126328. 25 interactions.
IntActiQ6MZP7. 35 interactions.
MINTiMINT-7239317.
STRINGi9606.ENSP00000341947.

PTM databases

iPTMnetiQ6MZP7.
PhosphoSiteiQ6MZP7.

Polymorphism and mutation databases

DMDMi313104222.

Proteomic databases

EPDiQ6MZP7.
MaxQBiQ6MZP7.
PaxDbiQ6MZP7.
PRIDEiQ6MZP7.

Protocols and materials databases

DNASUi132660.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000340417; ENSP00000341947; ENSG00000189308. [Q6MZP7-1]
ENST00000442461; ENSP00000398265; ENSG00000189308. [Q6MZP7-3]
ENST00000446851; ENSP00000407139; ENSG00000189308. [Q6MZP7-3]
ENST00000505397; ENSP00000425844; ENSG00000189308. [Q6MZP7-1]
ENST00000506560; ENSP00000423475; ENSG00000189308. [Q6MZP7-2]
ENST00000508171; ENSP00000427413; ENSG00000189308. [Q6MZP7-5]
ENST00000510557; ENSP00000421045; ENSG00000189308. [Q6MZP7-3]
GeneIDi132660.
KEGGihsa:132660.
UCSCiuc003hnx.5. human. [Q6MZP7-1]

Organism-specific databases

CTDi132660.
GeneCardsiLIN54.
H-InvDBHIX0024607.
HGNCiHGNC:25397. LIN54.
HPAiHPA056606.
MIMi613367. gene.
neXtProtiNX_Q6MZP7.
PharmGKBiPA162394056.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1171. Eukaryota.
ENOG4110UR5. LUCA.
GeneTreeiENSGT00390000013974.
HOGENOMiHOG000082518.
HOVERGENiHBG108088.
InParanoidiQ6MZP7.
OMAiTPGIQTQ.
OrthoDBiEOG7DFXBK.
PhylomeDBiQ6MZP7.
TreeFamiTF313189.

Enzyme and pathway databases

ReactomeiR-HSA-1538133. G0 and Early G1.
R-HSA-156711. Polo-like kinase mediated events.

Miscellaneous databases

ChiTaRSiLIN54. human.
GenomeRNAii132660.
PROiQ6MZP7.
SOURCEiSearch...

Gene expression databases

BgeeiQ6MZP7.
CleanExiHS_LIN54.
ExpressionAtlasiQ6MZP7. baseline and differential.
GenevisibleiQ6MZP7. HS.

Family and domain databases

InterProiIPR005172. CRC.
IPR028307. Lin-54_fam.
IPR033467. Tesmin/TSO1-like_CXC.
[Graphical view]
PANTHERiPTHR12446. PTHR12446. 1 hit.
PfamiPF03638. TCR. 2 hits.
[Graphical view]
SMARTiSM01114. CXC. 2 hits.
[Graphical view]
PROSITEiPS51634. CRC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of a long cDNA clone isolated from human."
    Nagase T., Kikuno R., Ohara O.
    Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Brain.
  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 3).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Tissue: Uterine endothelium.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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 2 AND 5).
  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-310 AND SER-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "LIN54 is an essential core subunit of the DREAM/LINC complex that binds to the cdc2 promoter in a sequence-specific manner."
    Schmit F., Cremer S., Gaubatz S.
    FEBS J. 276:5703-5716(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING TO CDK1 PROMOTER, DOMAIN CXC, CELL CYCLE INVOLVEMENT, MUTAGENESIS OF CYS-525 AND CYS-527.
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-244 AND LYS-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-310 AND SER-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiLIN54_HUMAN
AccessioniPrimary (citable) accession number: Q6MZP7
Secondary accession number(s): Q32M68
, Q32M69, Q6N071, Q76B60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: November 30, 2010
Last modified: June 8, 2016
This is version 97 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, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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

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 one 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.