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Protein

Protein lin-52 homolog

Gene

LIN52

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Biological processi

Complete GO annotation...

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-52 homolog
Gene namesi
Name:LIN52
Synonyms:C14orf46
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:19856. LIN52.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162394039.

Polymorphism and mutation databases

BioMutaiLIN52.
DMDMi74754720.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 116116Protein lin-52 homologPRO_0000252154Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei28 – 281PhosphoserineCombined sources
Modified residuei53 – 531PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ52LA3.
MaxQBiQ52LA3.
PaxDbiQ52LA3.
PeptideAtlasiQ52LA3.
PRIDEiQ52LA3.

PTM databases

iPTMnetiQ52LA3.
PhosphoSiteiQ52LA3.

Expressioni

Gene expression databases

BgeeiQ52LA3.
CleanExiHS_LIN52.
ExpressionAtlasiQ52LA3. baseline and differential.
GenevisibleiQ52LA3. HS.

Organism-specific databases

HPAiHPA000900.

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

Protein-protein interaction databases

BioGridi124874. 9 interactions.
IntActiQ52LA3. 6 interactions.
STRINGi9606.ENSP00000451812.

Structurei

Secondary structure

1
116
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi28 – 314Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4YOOX-ray2.40X15-34[»]
ProteinModelPortaliQ52LA3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the lin-52 family.Curated

Phylogenomic databases

eggNOGiKOG4402. Eukaryota.
ENOG4111VPU. LUCA.
GeneTreeiENSGT00390000008402.
HOGENOMiHOG000006570.
HOVERGENiHBG081917.
InParanoidiQ52LA3.
OMAiDKIKSMH.
OrthoDBiEOG7SJD6W.
PhylomeDBiQ52LA3.
TreeFamiTF320091.

Family and domain databases

InterProiIPR018737. DREAM_LIN52.
[Graphical view]
PANTHERiPTHR31489. PTHR31489. 1 hit.
PfamiPF10044. LIN52. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q52LA3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGWKMASPTD GTDLEASLLS FEKLDRASPD LWPEQLPGVA EFAASFKSPI
60 70 80 90 100
TSSPPKWMAE IERDDIDMLK ELGSLTTANL MEKVRGLQNL AYQLGLDESR
110
EMTRGKFLNI LEKPKK
Length:116
Mass (Da):13,001
Last modified:May 24, 2005 - v1
Checksum:iF9D1F2CA524975D0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC094003 mRNA. Translation: AAH94003.1.
BC094005 mRNA. Translation: AAH94005.1.
CCDSiCCDS32120.1.
RefSeqiNP_001019845.1. NM_001024674.2.
UniGeneiHs.612866.

Genome annotation databases

EnsembliENST00000555028; ENSP00000451812; ENSG00000205659.
GeneIDi91750.
KEGGihsa:91750.
UCSCiuc001xpp.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC094003 mRNA. Translation: AAH94003.1.
BC094005 mRNA. Translation: AAH94005.1.
CCDSiCCDS32120.1.
RefSeqiNP_001019845.1. NM_001024674.2.
UniGeneiHs.612866.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4YOOX-ray2.40X15-34[»]
ProteinModelPortaliQ52LA3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124874. 9 interactions.
IntActiQ52LA3. 6 interactions.
STRINGi9606.ENSP00000451812.

PTM databases

iPTMnetiQ52LA3.
PhosphoSiteiQ52LA3.

Polymorphism and mutation databases

BioMutaiLIN52.
DMDMi74754720.

Proteomic databases

EPDiQ52LA3.
MaxQBiQ52LA3.
PaxDbiQ52LA3.
PeptideAtlasiQ52LA3.
PRIDEiQ52LA3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000555028; ENSP00000451812; ENSG00000205659.
GeneIDi91750.
KEGGihsa:91750.
UCSCiuc001xpp.3. human.

Organism-specific databases

CTDi91750.
GeneCardsiLIN52.
HGNCiHGNC:19856. LIN52.
HPAiHPA000900.
neXtProtiNX_Q52LA3.
PharmGKBiPA162394039.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4402. Eukaryota.
ENOG4111VPU. LUCA.
GeneTreeiENSGT00390000008402.
HOGENOMiHOG000006570.
HOVERGENiHBG081917.
InParanoidiQ52LA3.
OMAiDKIKSMH.
OrthoDBiEOG7SJD6W.
PhylomeDBiQ52LA3.
TreeFamiTF320091.

Enzyme and pathway databases

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

Miscellaneous databases

GenomeRNAii91750.
PROiQ52LA3.

Gene expression databases

BgeeiQ52LA3.
CleanExiHS_LIN52.
ExpressionAtlasiQ52LA3. baseline and differential.
GenevisibleiQ52LA3. HS.

Family and domain databases

InterProiIPR018737. DREAM_LIN52.
[Graphical view]
PANTHERiPTHR31489. PTHR31489. 1 hit.
PfamiPF10044. LIN52. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Tissue: Brain.
  2. "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.
  3. "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.
  4. "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].
  5. "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-28, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  7. "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-28, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiLIN52_HUMAN
AccessioniPrimary (citable) accession number: Q52LA3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: May 24, 2005
Last modified: July 6, 2016
This is version 85 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.