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Protein

Protein lin-37 homolog

Gene

Lin37

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-1538133. G0 and Early G1.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein lin-37 homolog
Alternative name(s):
Antolefinin
Antolefinine
Gene namesi
Name:Lin37
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1922910. Lin37.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 246246Protein lin-37 homologPRO_0000238480Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei135 – 1351PhosphoserineCombined sources
Modified residuei138 – 1381PhosphoserineCombined sources
Modified residuei167 – 1671PhosphothreonineBy similarity
Modified residuei182 – 1821PhosphoserineBy similarity
Modified residuei202 – 2021PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9D8N6.
MaxQBiQ9D8N6.
PaxDbiQ9D8N6.
PRIDEiQ9D8N6.

PTM databases

iPTMnetiQ9D8N6.
PhosphoSiteiQ9D8N6.

Expressioni

Gene expression databases

BgeeiQ9D8N6.
CleanExiMM_LIN37.
ExpressionAtlasiQ9D8N6. baseline and differential.
GenevisibleiQ9D8N6. MM.

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 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000048557.

Structurei

3D structure databases

ProteinModelPortaliQ9D8N6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi136 – 20368Pro-richAdd
BLAST

Phylogenomic databases

eggNOGiENOG410II8K. Eukaryota.
ENOG4111QJM. LUCA.
GeneTreeiENSGT00390000002748.
HOGENOMiHOG000006536.
HOVERGENiHBG054424.
InParanoidiQ9D8N6.
OMAiVDLAQFN.
OrthoDBiEOG7TQV2M.
PhylomeDBiQ9D8N6.
TreeFamiTF329230.

Family and domain databases

InterProiIPR028226. LIN37.
[Graphical view]
PfamiPF15306. LIN37. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9D8N6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFPVKVKVEK SEMEMAKARN QLDAVLQCLL EKSHMDRERL DEEAGKTPLD
60 70 80 90 100
THNKDCSIAA TGKRPSARFP HQRRKKRREM DDGLAEGGPQ RSNTYVIKLF
110 120 130 140 150
DRSVDLAQFS ENTPLYPICR AWMRNSPTVR ERERSPGSPL PPLPEDGEGS
160 170 180 190 200
EVINSKNRDV YKLPPPTAPG PLGDACRSRI PSPLQPETEG TPDDEPSEPE
210 220 230 240
PSPSTLIYRN MQRWKRIRQR WKEASHRNQL RYSESMKILR EMYDRQ
Length:246
Mass (Da):28,378
Last modified:June 1, 2001 - v1
Checksum:i6FD6104D9945A81D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY428767 mRNA. Translation: AAR06606.1.
AK007858 mRNA. Translation: BAB25310.1.
CCDSiCCDS21098.1.
RefSeqiNP_001277498.1. NM_001290569.1.
NP_083653.1. NM_029377.2.
UniGeneiMm.379242.

Genome annotation databases

EnsembliENSMUST00000043975; ENSMUSP00000048557; ENSMUSG00000036845.
GeneIDi75660.
KEGGimmu:75660.
UCSCiuc009gex.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY428767 mRNA. Translation: AAR06606.1.
AK007858 mRNA. Translation: BAB25310.1.
CCDSiCCDS21098.1.
RefSeqiNP_001277498.1. NM_001290569.1.
NP_083653.1. NM_029377.2.
UniGeneiMm.379242.

3D structure databases

ProteinModelPortaliQ9D8N6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000048557.

PTM databases

iPTMnetiQ9D8N6.
PhosphoSiteiQ9D8N6.

Proteomic databases

EPDiQ9D8N6.
MaxQBiQ9D8N6.
PaxDbiQ9D8N6.
PRIDEiQ9D8N6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000043975; ENSMUSP00000048557; ENSMUSG00000036845.
GeneIDi75660.
KEGGimmu:75660.
UCSCiuc009gex.1. mouse.

Organism-specific databases

CTDi55957.
MGIiMGI:1922910. Lin37.

Phylogenomic databases

eggNOGiENOG410II8K. Eukaryota.
ENOG4111QJM. LUCA.
GeneTreeiENSGT00390000002748.
HOGENOMiHOG000006536.
HOVERGENiHBG054424.
InParanoidiQ9D8N6.
OMAiVDLAQFN.
OrthoDBiEOG7TQV2M.
PhylomeDBiQ9D8N6.
TreeFamiTF329230.

Enzyme and pathway databases

ReactomeiR-MMU-1538133. G0 and Early G1.

Miscellaneous databases

NextBioi343650.
PROiQ9D8N6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D8N6.
CleanExiMM_LIN37.
ExpressionAtlasiQ9D8N6. baseline and differential.
GenevisibleiQ9D8N6. MM.

Family and domain databases

InterProiIPR028226. LIN37.
[Graphical view]
PfamiPF15306. LIN37. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of a novel 821 bp cDNA from a whole mouse brain with an ORF encoding a 246 aa protein referred to as antolefinine."
    Anton B., Leff P., Matus M., Gonzaga R., Medina R., Calva J.C., Acevedo R., Martinez C., Retana I., Saavedra R., Arias A., Zavala E., Pavon L., Alagon A.
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    Tissue: Brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Pancreas.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135; SER-138 AND SER-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiLIN37_MOUSE
AccessioniPrimary (citable) accession number: Q9D8N6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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.