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Protein

THUMP domain-containing protein 1

Gene

THUMPD1

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

Functioni

Functions as a tRNA-binding adapter to mediate NAT10-dependent tRNA acetylation (PubMed:25653167).1 Publication

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
THUMP domain-containing protein 1
Gene namesi
Name:THUMPD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:23807. THUMPD1.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134983093.

Polymorphism and mutation databases

BioMutaiTHUMPD1.
DMDMi61248576.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 353352THUMP domain-containing protein 1PRO_0000072530Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei79 – 791PhosphothreonineCombined sources
Modified residuei86 – 861PhosphoserineCombined sources
Modified residuei88 – 881PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9NXG2.
MaxQBiQ9NXG2.
PaxDbiQ9NXG2.
PRIDEiQ9NXG2.

PTM databases

iPTMnetiQ9NXG2.
PhosphoSiteiQ9NXG2.

Expressioni

Gene expression databases

BgeeiQ9NXG2.
CleanExiHS_THUMPD1.
ExpressionAtlasiQ9NXG2. baseline and differential.
GenevisibleiQ9NXG2. HS.

Organism-specific databases

HPAiHPA027851.

Interactioni

Subunit structurei

Interacts with NAT10 (PubMed:25653167).1 Publication

Protein-protein interaction databases

BioGridi120762. 24 interactions.
IntActiQ9NXG2. 3 interactions.
STRINGi9606.ENSP00000370741.

Structurei

Secondary structure

1
353
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi171 – 18818
Beta strandi195 – 2017
Helixi210 – 22415
Beta strandi232 – 2343
Beta strandi236 – 2449
Beta strandi247 – 2548

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DIRNMR-A170-254[»]
ProteinModelPortaliQ9NXG2.
SMRiQ9NXG2. Positions 170-254.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NXG2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini147 – 254108THUMPPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the THUMPD1 family.Curated
Contains 1 THUMP domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3943. Eukaryota.
COG1818. LUCA.
GeneTreeiENSGT00390000002365.
HOGENOMiHOG000139150.
HOVERGENiHBG053030.
InParanoidiQ9NXG2.
KOiK06963.
OMAiQQVVPEN.
OrthoDBiEOG7MKW6R.
PhylomeDBiQ9NXG2.
TreeFamiTF313884.

Family and domain databases

InterProiIPR004114. THUMP_dom.
[Graphical view]
PfamiPF02926. THUMP. 1 hit.
[Graphical view]
SMARTiSM00981. THUMP. 1 hit.
[Graphical view]
PROSITEiPS51165. THUMP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9NXG2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPAQQTTQ PGGGKRKGKA QYVLAKRARR CDAGGPRQLE PGLQGILITC
60 70 80 90 100
NMNERKCVEE AYSLLNEYGD DMYGPEKFTD KDQQPSGSEG EDDDAEAALK
110 120 130 140 150
KEVGDIKAST EMRLRRFQSV ESGANNVVFI RTLGIEPEKL VHHILQDMYK
160 170 180 190 200
TKKKKTRVIL RMLPISGTCK AFLEDMKKYA ETFLEPWFKA PNKGTFQIVY
210 220 230 240 250
KSRNNSHVNR EEVIRELAGI VCTLNSENKV DLTNPQYTVV VEIIKAVCCL
260 270 280 290 300
SVVKDYMLFR KYNLQEVVKS PKDPSQLNSK QGNGKEAKLE SADKSDQNNT
310 320 330 340 350
AEGKNNQQVP ENTEELGQTK PTSNPQVVNE GGAKPELASQ ATEGSKSNEN

DFS
Length:353
Mass (Da):39,315
Last modified:July 5, 2004 - v2
Checksum:i7F0BBD91D204AA1B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841Q → R in BAA91050 (PubMed:14702039).Curated
Sequence conflicti285 – 2851K → E in BAA91050 (PubMed:14702039).Curated
Sequence conflicti352 – 3521F → S in BAA91050 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti311 – 3111E → D.
Corresponds to variant rs11074471 [ dbSNP | Ensembl ].
VAR_037645

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000281 mRNA. Translation: BAA91050.1.
AC004381 Genomic DNA. No translation available.
BC000448 mRNA. Translation: AAH00448.1.
CCDSiCCDS10588.1.
RefSeqiNP_001291479.1. NM_001304550.1.
NP_060206.2. NM_017736.4.
UniGeneiHs.700004.

Genome annotation databases

EnsembliENST00000381337; ENSP00000370741; ENSG00000066654.
ENST00000396083; ENSP00000379392; ENSG00000066654.
GeneIDi55623.
KEGGihsa:55623.
UCSCiuc002dho.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000281 mRNA. Translation: BAA91050.1.
AC004381 Genomic DNA. No translation available.
BC000448 mRNA. Translation: AAH00448.1.
CCDSiCCDS10588.1.
RefSeqiNP_001291479.1. NM_001304550.1.
NP_060206.2. NM_017736.4.
UniGeneiHs.700004.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DIRNMR-A170-254[»]
ProteinModelPortaliQ9NXG2.
SMRiQ9NXG2. Positions 170-254.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120762. 24 interactions.
IntActiQ9NXG2. 3 interactions.
STRINGi9606.ENSP00000370741.

PTM databases

iPTMnetiQ9NXG2.
PhosphoSiteiQ9NXG2.

Polymorphism and mutation databases

BioMutaiTHUMPD1.
DMDMi61248576.

Proteomic databases

EPDiQ9NXG2.
MaxQBiQ9NXG2.
PaxDbiQ9NXG2.
PRIDEiQ9NXG2.

Protocols and materials databases

DNASUi55623.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000381337; ENSP00000370741; ENSG00000066654.
ENST00000396083; ENSP00000379392; ENSG00000066654.
GeneIDi55623.
KEGGihsa:55623.
UCSCiuc002dho.5. human.

Organism-specific databases

CTDi55623.
GeneCardsiTHUMPD1.
HGNCiHGNC:23807. THUMPD1.
HPAiHPA027851.
MIMi616662. gene.
neXtProtiNX_Q9NXG2.
PharmGKBiPA134983093.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3943. Eukaryota.
COG1818. LUCA.
GeneTreeiENSGT00390000002365.
HOGENOMiHOG000139150.
HOVERGENiHBG053030.
InParanoidiQ9NXG2.
KOiK06963.
OMAiQQVVPEN.
OrthoDBiEOG7MKW6R.
PhylomeDBiQ9NXG2.
TreeFamiTF313884.

Miscellaneous databases

ChiTaRSiTHUMPD1. human.
EvolutionaryTraceiQ9NXG2.
GenomeRNAii55623.
NextBioi60236.
PROiQ9NXG2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NXG2.
CleanExiHS_THUMPD1.
ExpressionAtlasiQ9NXG2. baseline and differential.
GenevisibleiQ9NXG2. HS.

Family and domain databases

InterProiIPR004114. THUMP_dom.
[Graphical view]
PfamiPF02926. THUMP. 1 hit.
[Graphical view]
SMARTiSM00981. THUMP. 1 hit.
[Graphical view]
PROSITEiPS51165. THUMP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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: Lung.
  4. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-88, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-88, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "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, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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 AND SER-88, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "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-86 AND SER-88, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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 THR-79; SER-86 AND SER-88, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "Yeast Kre33 and human NAT10 are conserved 18S rRNA cytosine acetyltransferases that modify tRNAs assisted by the adaptor Tan1/THUMPD1."
    Sharma S., Langhendries J.L., Watzinger P., Koetter P., Entian K.D., Lafontaine D.L.
    Nucleic Acids Res. 43:2242-2258(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NAT10.
  15. "Solution structure of the THUMP domain of THUMP domain-containing protein 1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (SEP-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 170-254.

Entry informationi

Entry nameiTHUM1_HUMAN
AccessioniPrimary (citable) accession number: Q9NXG2
Secondary accession number(s): Q9BWC3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 5, 2004
Last modified: May 11, 2016
This is version 109 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.