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Protein

Gamma-taxilin

Gene

TXLNG

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

Functioni

May be involved in intracellular vesicle traffic. Inhibits ATF4-mediated transcription, possibly by dimerizing with ATF4 to form inactive dimers that cannot bind DNA. May be involved in regulating bone mass density through an ATF4-dependent pathway. May be involved in cell cycle progression.2 Publications

GO - Molecular functioni

  • protein heterodimerization activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-taxilin
Alternative name(s):
Environmental lipopolysaccharide-responding gene protein
Factor inhibiting ATF4-mediated transcription
Short name:
FIAT
Lipopolysaccharide-specific response protein 5
Gene namesi
Name:TXLNG
Synonyms:CXorf15, ELRG, LSR5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:18578. TXLNG.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • nuclear membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38588.

Polymorphism and mutation databases

BioMutaiTXLNG.
DMDMi212276476.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 528528Gamma-taxilinPRO_0000189426Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei79 – 791PhosphoserineBy similarity
Modified residuei86 – 861PhosphoserineCombined sources
Modified residuei97 – 971PhosphoserineCombined sources
Modified residuei105 – 1051PhosphoserineCombined sources
Modified residuei283 – 2831PhosphotyrosineCombined sources
Modified residuei517 – 5171PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9NUQ3.
MaxQBiQ9NUQ3.
PaxDbiQ9NUQ3.
PRIDEiQ9NUQ3.

PTM databases

iPTMnetiQ9NUQ3.
PhosphoSiteiQ9NUQ3.

Expressioni

Tissue specificityi

Ubiquitously expressed. Expressed at high level in heart and skeletal muscle. Expressed in brain, placenta, lung, liver, kidney and pancreas.1 Publication

Inductioni

By bacterial lipopolysaccharides (LPS) in Hep-G2 cells.1 Publication

Gene expression databases

BgeeiQ9NUQ3.
CleanExiHS_CXorf15.
GenevisibleiQ9NUQ3. HS.

Organism-specific databases

HPAiHPA000297.
HPA000841.

Interactioni

Subunit structurei

Binds to the C-terminal coiled coil region of syntaxin family members STX1A, STX3A and STX4A. Forms a heterodimer with ATF4 in osteoblasts.1 Publication

GO - Molecular functioni

  • protein heterodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi120901. 46 interactions.
IntActiQ9NUQ3. 17 interactions.
STRINGi9606.ENSP00000369465.

Structurei

3D structure databases

ProteinModelPortaliQ9NUQ3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili153 – 464312Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the taxilin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1850. Eukaryota.
ENOG410XQH1. LUCA.
GeneTreeiENSGT00390000001482.
HOGENOMiHOG000231384.
HOVERGENiHBG104385.
InParanoidiQ9NUQ3.
OMAiEPKSQRS.
OrthoDBiEOG70KGP6.
PhylomeDBiQ9NUQ3.
TreeFamiTF318595.

Family and domain databases

InterProiIPR026183. Taxilin_fam.
[Graphical view]
PANTHERiPTHR16127. PTHR16127. 1 hit.
PfamiPF09728. Taxilin. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NUQ3-1) [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
MATRVEEAAR GRGGGAEEAT EAGRGGRRRS PRQKFEIGTM EEAGICGLGV
60 70 80 90 100
KADMLCNSQS NDILQHQGSN CGGTSNKHSL EEDEGSDFIT ENRNLVSPAY
110 120 130 140 150
CTQESREEIP GGEARTDPPD GQQDSECNRN KEKTLGKEVL LLMQALNTLS
160 170 180 190 200
TPEEKLAALC KKYADLLEES RSVQKQMKIL QKKQAQIVKE KVHLQSEHSK
210 220 230 240 250
AILARSKLES LCRELQRHNK TLKEENMQQA REEEERRKEA TAHFQITLNE
260 270 280 290 300
IQAQLEQHDI HNAKLRQENI ELGEKLKKLI EQYALREEHI DKVFKHKELQ
310 320 330 340 350
QQLVDAKLQQ TTQLIKEADE KHQREREFLL KEATESRHKY EQMKQQEVQL
360 370 380 390 400
KQQLSLYMDK FEEFQTTMAK SNELFTTFRQ EMEKMTKKIK KLEKETIIWR
410 420 430 440 450
TKWENNNKAL LQMAEEKTVR DKEYKALQIK LERLEKLCRA LQTERNELNE
460 470 480 490 500
KVEVLKEQVS IKAAIKAANR DLATPVMQPC TALDSHKELN TSSKRALGAH
510 520
LEAEPKSQRS AVQKPPSTGS APAIESVD
Length:528
Mass (Da):60,586
Last modified:November 4, 2008 - v2
Checksum:i4EAC314330CE4490
GO
Isoform 2 (identifier: Q9NUQ3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     35-166: Missing.

Show »
Length:396
Mass (Da):46,252
Checksum:iE05B3ED888BEE3A6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti249 – 2491N → D in BAA92068 (PubMed:14702039).Curated
Sequence conflicti296 – 2961H → R in BAA92068 (PubMed:14702039).Curated
Sequence conflicti402 – 4021K → I in AAF70546 (Ref. 6) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti246 – 2461I → V.
Corresponds to variant rs5969783 [ dbSNP | Ensembl ].
VAR_019809

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei35 – 166132Missing in isoform 2. 1 PublicationVSP_039391Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY739713 mRNA. Translation: AAW65982.1.
AK002071 mRNA. Translation: BAA92068.1.
AL929302, BX004861 Genomic DNA. Translation: CAI41279.1.
BX004861, AL929302 Genomic DNA. Translation: CAI41713.1.
CH471074 Genomic DNA. Translation: EAW98918.1.
BC101572 mRNA. Translation: AAI01573.1.
BC101576 mRNA. Translation: AAI01577.1.
AF143740 mRNA. Translation: AAF70546.2.
CCDSiCCDS14178.1. [Q9NUQ3-1]
CCDS55373.1. [Q9NUQ3-2]
RefSeqiNP_001162154.1. NM_001168683.1. [Q9NUQ3-2]
NP_060830.2. NM_018360.2. [Q9NUQ3-1]
UniGeneiHs.555961.

Genome annotation databases

EnsembliENST00000380122; ENSP00000369465; ENSG00000086712. [Q9NUQ3-1]
ENST00000398155; ENSP00000381222; ENSG00000086712. [Q9NUQ3-2]
GeneIDi55787.
KEGGihsa:55787.
UCSCiuc004cxq.3. human. [Q9NUQ3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY739713 mRNA. Translation: AAW65982.1.
AK002071 mRNA. Translation: BAA92068.1.
AL929302, BX004861 Genomic DNA. Translation: CAI41279.1.
BX004861, AL929302 Genomic DNA. Translation: CAI41713.1.
CH471074 Genomic DNA. Translation: EAW98918.1.
BC101572 mRNA. Translation: AAI01573.1.
BC101576 mRNA. Translation: AAI01577.1.
AF143740 mRNA. Translation: AAF70546.2.
CCDSiCCDS14178.1. [Q9NUQ3-1]
CCDS55373.1. [Q9NUQ3-2]
RefSeqiNP_001162154.1. NM_001168683.1. [Q9NUQ3-2]
NP_060830.2. NM_018360.2. [Q9NUQ3-1]
UniGeneiHs.555961.

3D structure databases

ProteinModelPortaliQ9NUQ3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120901. 46 interactions.
IntActiQ9NUQ3. 17 interactions.
STRINGi9606.ENSP00000369465.

PTM databases

iPTMnetiQ9NUQ3.
PhosphoSiteiQ9NUQ3.

Polymorphism and mutation databases

BioMutaiTXLNG.
DMDMi212276476.

Proteomic databases

EPDiQ9NUQ3.
MaxQBiQ9NUQ3.
PaxDbiQ9NUQ3.
PRIDEiQ9NUQ3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000380122; ENSP00000369465; ENSG00000086712. [Q9NUQ3-1]
ENST00000398155; ENSP00000381222; ENSG00000086712. [Q9NUQ3-2]
GeneIDi55787.
KEGGihsa:55787.
UCSCiuc004cxq.3. human. [Q9NUQ3-1]

Organism-specific databases

CTDi55787.
GeneCardsiTXLNG.
H-InvDBHIX0020474.
HGNCiHGNC:18578. TXLNG.
HPAiHPA000297.
HPA000841.
MIMi300677. gene.
neXtProtiNX_Q9NUQ3.
PharmGKBiPA38588.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1850. Eukaryota.
ENOG410XQH1. LUCA.
GeneTreeiENSGT00390000001482.
HOGENOMiHOG000231384.
HOVERGENiHBG104385.
InParanoidiQ9NUQ3.
OMAiEPKSQRS.
OrthoDBiEOG70KGP6.
PhylomeDBiQ9NUQ3.
TreeFamiTF318595.

Miscellaneous databases

ChiTaRSiTXLNG. human.
GenomeRNAii55787.
PROiQ9NUQ3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NUQ3.
CleanExiHS_CXorf15.
GenevisibleiQ9NUQ3. HS.

Family and domain databases

InterProiIPR026183. Taxilin_fam.
[Graphical view]
PANTHERiPTHR16127. PTHR16127. 1 hit.
PfamiPF09728. Taxilin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Anti-leukemia-specific humoral immune response in children with T-lineage acute lymphoblastic leukemia."
    Dohnal A.M., Panzer-Gruemayer R.E.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  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 1).
    Tissue: Placenta.
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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] (ISOFORM 1).
    Tissue: Brain.
  6. "New Homo sapiens gene from dental pulp cells."
    Chai Y.B., Zhao Z.L., Zhu F., Yan W., Chen N.C., Wang Q., Yue L., Chen S.M.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 343-528.
  7. Cited for: TISSUE SPECIFICITY, INTERACTION WITH STX1A; STX3A AND STX4A.
  8. "FIAT represses ATF4-mediated transcription to regulate bone mass in transgenic mice."
    Yu V.W., Ambartsoumian G., Verlinden L., Moir J.M., Prud'homme J., Gauthier C., Roughley P.J., St-Arnaud R.
    J. Cell Biol. 169:591-601(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
  9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND SER-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Over-expression and siRNA of a novel environmental lipopolysaccharide-responding gene on the cell cycle of the human hepatoma-derived cell line HepG2."
    Du K., Chai Y., Hou L., Chang W., Chen S., Luo W., Cai T., Zhang X., Chen N., Chen Y., Chen J.
    Toxicology 243:303-310(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  12. "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].
  13. "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-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "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-97 AND TYR-283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTXLNG_HUMAN
AccessioniPrimary (citable) accession number: Q9NUQ3
Secondary accession number(s): Q2KQ75, Q5JNZ7, Q9P0X1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: November 4, 2008
Last modified: June 8, 2016
This is version 116 of the entry and version 2 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

Miscellaneous

Depletion of TXLNG by siRNA decreases the percentage of Hep-G2 cells arrested in G1 phase.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.