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Q5TKA1 (LIN9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein lin-9 homolog

Short name=HuLin-9
Short name=hLin-9
Alternative name(s):
Beta subunit-associated regulator of apoptosis
TUDOR gene similar protein
Type I interferon receptor beta chain-associated protein
pRB-associated protein
Gene names
Name:LIN9
Synonyms:BARA, TGS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length542 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a tumor suppressor. Inhibits DNA synthesis. Its ability to inhibit oncogenic transformation is mediated through its association with RB1. Plays a role in the expression of genes required for the G1/S transition. Ref.1 Ref.2

Subunit structure

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. Interacts with RB1. Ref.1 Ref.6 Ref.7

Subcellular location

Nucleusnucleoplasm. Note: Found in perinucleolar structures. Associated with chromatin. Ref.1 Ref.2

Tissue specificity

Expressed in thymus and testis. Ref.1

Sequence similarities

Belongs to the lin-9 family.

Sequence caution

The sequence AAH43444.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAD97871.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5TKA1-1)

Also known as: Lin9-L; Long form;

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.
Isoform 2 (identifier: Q5TKA1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MHRGGQPLKKRRGSFKM
Isoform 3 (identifier: Q5TKA1-3)

Also known as: Lin9-S; Short form;

The sequence of this isoform differs from the canonical sequence as follows:
     54-88: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 542541Protein lin-9 homolog
PRO_0000249546

Regions

Region2 – 296295Sufficient for interaction with RB1
Coiled coil354 – 41360 Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.11
Modified residue651Phosphoserine Ref.13
Modified residue3041Phosphothreonine Ref.13
Modified residue3091Phosphoserine Ref.8 Ref.9 Ref.10 Ref.12 Ref.13
Modified residue3211Phosphoserine Ref.8 Ref.9 Ref.10 Ref.12 Ref.13

Natural variations

Alternative sequence11M → MHRGGQPLKKRRGSFKM in isoform 2.
VSP_020509
Alternative sequence54 – 8835Missing in isoform 3.
VSP_020510

Experimental info

Sequence conflict4361E → V in AAH43444. Ref.5
Sequence conflict5081S → R in AAV41873. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Lin9-L) (Long form) [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 1107865E6FF33037

FASTA54261,946
        10         20         30         40         50         60 
MAELDQLPDE SSSAKALVSL KEGSLSNTWN EKYSSLQKTP VWKGRNTSSA VEMPFRNSKR 

        70         80         90        100        110        120 
SRLFSDEDDR QINTRSPKRN QRVAMVPQKF TATMSTPDKK ASQKIGFRLR NLLKLPKAHK 

       130        140        150        160        170        180 
WCIYEWFYSN IDKPLFEGDN DFCVCLKESF PNLKTRKLTR VEWGKIRRLM GKPRRCSSAF 

       190        200        210        220        230        240 
FEEERSALKQ KRQKIRLLQQ RKVADVSQFK DLPDEIPLPL VIGTKVTARL RGVHDGLFTG 

       250        260        270        280        290        300 
QIDAVDTLNA TYRVTFDRTG LGTHTIPDYE VLSNEPHETM PIAAFGQKQR PSRFFMTPPR 

       310        320        330        340        350        360 
LHYTPPLQSP IIDNDPLLGQ SPWRSKISGS DTETLGGFPV EFLIQVTRLS KILMIKKEHI 

       370        380        390        400        410        420 
KKLREMNTEA EKLKSYSMPI SIEFQRRYAT IVLELEQLNK DLNKVLHKVQ QYCYELAPDQ 

       430        440        450        460        470        480 
GLQPADQPTD MRRRCEEEAQ EIVRHANSST GQPCVENENL TDLISRLTAI LLQIKCLAEG 

       490        500        510        520        530        540 
GDLNSFEFKS LTDSLNDIKS TIDASNISCF QNNVEIHVAH IQSGLSQMGN LHAFAANNTN 


RD 

« Hide

Isoform 2 [UniParc].

Checksum: 90ECE86266AF02CE
Show »

FASTA55863,811
Isoform 3 (Lin9-S) (Short form) [UniParc].

Checksum: B657E9DD7A2882F0
Show »

FASTA50757,733

References

« Hide 'large scale' references
[1]"Inhibition of oncogenic transformation by mammalian Lin-9, a pRB-associated protein."
Gagrica S., Hauser S., Kolfschoten I., Osterloh L., Agami R., Gaubatz S.
EMBO J. 23:4627-4638(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH RB1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Cervix carcinoma.
[2]"A mutant allele of BARA/LIN-9 rescues the cdk4-/- phenotype by releasing the repression on E2F-regulated genes."
Sandoval R., Xue J., Tian X., Barrett K., Pilkinton M., Ucker D.S., Raychaudhuri P., Kineman R.D., Luque R.M., Baida G., Zou X., Valli V.E., Cook J.L., Kiyokawa H., Colamonici O.R.
Exp. Cell Res. 312:2465-2475(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, SUBCELLULAR LOCATION.
Tissue: Myeloma.
[3]"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. expand/collapse author list , 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).
Tissue: Thymus.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Heart.
[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 1 AND 2).
Tissue: Testis.
[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-309 AND SER-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309 AND SER-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309 AND SER-321, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [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-309 AND SER-321, 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-65; THR-304; SER-309 AND SER-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY786184 mRNA. Translation: AAV41873.1.
AF190323 mRNA. Translation: AAQ13710.1.
AF190324 mRNA. Translation: AAQ13711.1.
AK126177 mRNA. Translation: BAC86475.1.
BX537869 mRNA. Translation: CAD97871.1. Different initiation.
BC043444 mRNA. Translation: AAH43444.1. Different initiation.
BC045625 mRNA. Translation: AAH45625.1.
RefSeqNP_001257338.1. NM_001270409.1.
NP_001257339.1. NM_001270410.1.
NP_775106.2. NM_173083.3.
UniGeneHs.120817.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid130420. 15 interactions.
IntActQ5TKA1. 14 interactions.
MINTMINT-4054198.
STRING9606.ENSP00000329102.

PTM databases

PhosphoSiteQ5TKA1.

Polymorphism databases

DMDM74708186.

Proteomic databases

PaxDbQ5TKA1.
PRIDEQ5TKA1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000328205; ENSP00000329102; ENSG00000183814. [Q5TKA1-2]
ENST00000366801; ENSP00000355766; ENSG00000183814. [Q5TKA1-3]
GeneID286826.
KEGGhsa:286826.
UCSCuc001hqa.3. human. [Q5TKA1-2]
uc001hqc.4. human. [Q5TKA1-1]

Organism-specific databases

CTD286826.
GeneCardsGC01M226420.
HGNCHGNC:30830. LIN9.
HPAHPA030241.
MIM609375. gene.
neXtProtNX_Q5TKA1.
PharmGKBPA134970771.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG148048.
HOGENOMHOG000007517.
HOVERGENHBG057743.
InParanoidQ5TKA1.
OrthoDBEOG71ZP10.
PhylomeDBQ5TKA1.
TreeFamTF314315.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.

Gene expression databases

ArrayExpressQ5TKA1.
BgeeQ5TKA1.
CleanExHS_LIN9.
GenevestigatorQ5TKA1.

Family and domain databases

InterProIPR010561. LIN-9/ALY1.
[Graphical view]
PANTHERPTHR21689. PTHR21689. 1 hit.
PfamPF06584. DIRP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiLIN9.
GenomeRNAi286826.
NextBio96300.
PROQ5TKA1.
SOURCESearch...

Entry information

Entry nameLIN9_HUMAN
AccessionPrimary (citable) accession number: Q5TKA1
Secondary accession number(s): Q5U5L8 expand/collapse secondary AC list , Q5U7E1, Q6PI55, Q6ZTV4, Q7Z3J1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM