Skip Header

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

Q5TKA1

- LIN9_HUMAN

UniProt

Q5TKA1 - LIN9_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Protein lin-9 homolog

Gene

LIN9

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

Functioni

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.2 Publications

GO - Biological processi

  1. DNA replication Source: UniProtKB-KW
  2. G2/M transition of mitotic cell cycle Source: Reactome
  3. mitotic cell cycle Source: Reactome
  4. regulation of cell cycle Source: Reactome
  5. transcription, DNA-templated Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Cell cycle, DNA synthesis

Enzyme and pathway databases

ReactomeiREACT_1006. Polo-like kinase mediated events.
REACT_111214. G0 and Early G1.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:LIN9
Synonyms:BARA, TGS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:30830. LIN9.

Subcellular locationi

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

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. transcriptional repressor complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA134970771.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 542541Protein lin-9 homologPRO_0000249546Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei65 – 651Phosphoserine1 Publication
Modified residuei304 – 3041Phosphothreonine1 Publication
Modified residuei309 – 3091Phosphoserine5 Publications
Modified residuei321 – 3211Phosphoserine5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ5TKA1.
PaxDbiQ5TKA1.
PRIDEiQ5TKA1.

PTM databases

PhosphoSiteiQ5TKA1.

Expressioni

Tissue specificityi

Expressed in thymus and testis.1 Publication

Gene expression databases

BgeeiQ5TKA1.
CleanExiHS_LIN9.
ExpressionAtlasiQ5TKA1. baseline and differential.
GenevestigatoriQ5TKA1.

Organism-specific databases

HPAiHPA030241.

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. Interacts with RB1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
E2F4Q162543EBI-1389424,EBI-448943
MYBL2P102447EBI-1389424,EBI-1389468

Protein-protein interaction databases

BioGridi130420. 17 interactions.
IntActiQ5TKA1. 14 interactions.
MINTiMINT-4054198.
STRINGi9606.ENSP00000329102.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 296295Sufficient for interaction with RB1Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili354 – 41360Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the lin-9 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG148048.
GeneTreeiENSGT00390000003188.
HOGENOMiHOG000007517.
HOVERGENiHBG057743.
InParanoidiQ5TKA1.
OrthoDBiEOG71ZP10.
PhylomeDBiQ5TKA1.
TreeFamiTF314315.

Family and domain databases

InterProiIPR010561. LIN-9/ALY1.
[Graphical view]
PANTHERiPTHR21689. PTHR21689. 1 hit.
PfamiPF06584. DIRP. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q5TKA1-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAELDQLPDE SSSAKALVSL KEGSLSNTWN EKYSSLQKTP VWKGRNTSSA
60 70 80 90 100
VEMPFRNSKR SRLFSDEDDR QINTRSPKRN QRVAMVPQKF TATMSTPDKK
110 120 130 140 150
ASQKIGFRLR NLLKLPKAHK WCIYEWFYSN IDKPLFEGDN DFCVCLKESF
160 170 180 190 200
PNLKTRKLTR VEWGKIRRLM GKPRRCSSAF FEEERSALKQ KRQKIRLLQQ
210 220 230 240 250
RKVADVSQFK DLPDEIPLPL VIGTKVTARL RGVHDGLFTG QIDAVDTLNA
260 270 280 290 300
TYRVTFDRTG LGTHTIPDYE VLSNEPHETM PIAAFGQKQR PSRFFMTPPR
310 320 330 340 350
LHYTPPLQSP IIDNDPLLGQ SPWRSKISGS DTETLGGFPV EFLIQVTRLS
360 370 380 390 400
KILMIKKEHI KKLREMNTEA EKLKSYSMPI SIEFQRRYAT IVLELEQLNK
410 420 430 440 450
DLNKVLHKVQ QYCYELAPDQ GLQPADQPTD MRRRCEEEAQ EIVRHANSST
460 470 480 490 500
GQPCVENENL TDLISRLTAI LLQIKCLAEG GDLNSFEFKS LTDSLNDIKS
510 520 530 540
TIDASNISCF QNNVEIHVAH IQSGLSQMGN LHAFAANNTN RD
Length:542
Mass (Da):61,946
Last modified:December 21, 2004 - v1
Checksum:i1107865E6FF33037
GO
Isoform 2 (identifier: Q5TKA1-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MHRGGQPLKKRRGSFKM

Show »
Length:558
Mass (Da):63,811
Checksum:i90ECE86266AF02CE
GO
Isoform 3 (identifier: Q5TKA1-3) [UniParc]FASTAAdd to Basket

Also known as: Lin9-S, Short form

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

Show »
Length:507
Mass (Da):57,733
Checksum:iB657E9DD7A2882F0
GO

Sequence cautioni

The sequence AAH43444.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAD97871.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti436 – 4361E → V in AAH43444. (PubMed:15489334)Curated
Sequence conflicti508 – 5081S → R in AAV41873. (PubMed:15538385)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MHRGGQPLKKRRGSFKM in isoform 2. 1 PublicationVSP_020509
Alternative sequencei54 – 8835Missing in isoform 3. 2 PublicationsVSP_020510Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1553.1. [Q5TKA1-2]
RefSeqiNP_001257338.1. NM_001270409.1.
NP_001257339.1. NM_001270410.1.
NP_775106.2. NM_173083.3. [Q5TKA1-2]
UniGeneiHs.120817.

Genome annotation databases

EnsembliENST00000328205; ENSP00000329102; ENSG00000183814. [Q5TKA1-2]
GeneIDi286826.
KEGGihsa:286826.
UCSCiuc001hqa.3. human. [Q5TKA1-2]
uc001hqc.4. human. [Q5TKA1-1]

Polymorphism databases

DMDMi74708186.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS1553.1. [Q5TKA1-2 ]
RefSeqi NP_001257338.1. NM_001270409.1.
NP_001257339.1. NM_001270410.1.
NP_775106.2. NM_173083.3. [Q5TKA1-2 ]
UniGenei Hs.120817.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 130420. 17 interactions.
IntActi Q5TKA1. 14 interactions.
MINTi MINT-4054198.
STRINGi 9606.ENSP00000329102.

PTM databases

PhosphoSitei Q5TKA1.

Polymorphism databases

DMDMi 74708186.

Proteomic databases

MaxQBi Q5TKA1.
PaxDbi Q5TKA1.
PRIDEi Q5TKA1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000328205 ; ENSP00000329102 ; ENSG00000183814 . [Q5TKA1-2 ]
GeneIDi 286826.
KEGGi hsa:286826.
UCSCi uc001hqa.3. human. [Q5TKA1-2 ]
uc001hqc.4. human. [Q5TKA1-1 ]

Organism-specific databases

CTDi 286826.
GeneCardsi GC01M226420.
HGNCi HGNC:30830. LIN9.
HPAi HPA030241.
MIMi 609375. gene.
neXtProti NX_Q5TKA1.
PharmGKBi PA134970771.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG148048.
GeneTreei ENSGT00390000003188.
HOGENOMi HOG000007517.
HOVERGENi HBG057743.
InParanoidi Q5TKA1.
OrthoDBi EOG71ZP10.
PhylomeDBi Q5TKA1.
TreeFami TF314315.

Enzyme and pathway databases

Reactomei REACT_1006. Polo-like kinase mediated events.
REACT_111214. G0 and Early G1.

Miscellaneous databases

ChiTaRSi LIN9. human.
GeneWikii LIN9.
GenomeRNAii 286826.
NextBioi 96300.
PROi Q5TKA1.
SOURCEi Search...

Gene expression databases

Bgeei Q5TKA1.
CleanExi HS_LIN9.
ExpressionAtlasi Q5TKA1. baseline and differential.
Genevestigatori Q5TKA1.

Family and domain databases

InterProi IPR010561. LIN-9/ALY1.
[Graphical view ]
PANTHERi PTHR21689. PTHR21689. 1 hit.
Pfami PF06584. DIRP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiLIN9_HUMAN
AccessioniPrimary (citable) accession number: Q5TKA1
Secondary accession number(s): Q5U5L8
, Q5U7E1, Q6PI55, Q6ZTV4, Q7Z3J1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: December 21, 2004
Last modified: November 26, 2014
This is version 88 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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