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Q9NXG2 (THUM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
THUMP domain-containing protein 1
Gene names
Name:THUMPD1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length353 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the THUMPD1 family.

Contains 1 THUMP domain.

Ontologies

Keywords
   Coding sequence diversityPolymorphism
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 353352THUMP domain-containing protein 1
PRO_0000072530

Regions

Domain147 – 254108THUMP

Amino acid modifications

Modified residue21N-acetylalanine Ref.8
Modified residue861Phosphoserine Ref.3 Ref.4 Ref.6 Ref.7 Ref.8 Ref.9
Modified residue881Phosphoserine Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

Natural variations

Natural variant3111E → D.
Corresponds to variant rs11074471 [ dbSNP | Ensembl ].
VAR_037645

Experimental info

Sequence conflict841Q → R in BAA91050. Ref.1
Sequence conflict2851K → E in BAA91050. Ref.1
Sequence conflict3521F → S in BAA91050. Ref.1

Secondary structure

............... 353
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9NXG2 [UniParc].

Last modified July 5, 2004. Version 2.
Checksum: 7F0BBD91D204AA1B

FASTA35339,315
        10         20         30         40         50         60 
MAAPAQQTTQ PGGGKRKGKA QYVLAKRARR CDAGGPRQLE PGLQGILITC NMNERKCVEE 

        70         80         90        100        110        120 
AYSLLNEYGD DMYGPEKFTD KDQQPSGSEG EDDDAEAALK KEVGDIKAST EMRLRRFQSV 

       130        140        150        160        170        180 
ESGANNVVFI RTLGIEPEKL VHHILQDMYK TKKKKTRVIL RMLPISGTCK AFLEDMKKYA 

       190        200        210        220        230        240 
ETFLEPWFKA PNKGTFQIVY KSRNNSHVNR EEVIRELAGI VCTLNSENKV DLTNPQYTVV 

       250        260        270        280        290        300 
VEIIKAVCCL SVVKDYMLFR KYNLQEVVKS PKDPSQLNSK QGNGKEAKLE SADKSDQNNT 

       310        320        330        340        350 
AEGKNNQQVP ENTEELGQTK PTSNPQVVNE GGAKPELASQ ATEGSKSNEN DFS 

« Hide

References

« Hide 'large scale' references
[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. 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[3]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-88, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[4]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-88, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[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: 19367720] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, MASS SPECTROMETRY.
Tissue: T-cell.
[6]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-88, MASS SPECTROMETRY.
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: 18318008] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-88, MASS SPECTROMETRY.
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: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-88, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-88, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK000281 mRNA. Translation: BAA91050.1.
BC000448 mRNA. Translation: AAH00448.1.
IPIIPI00550243.
RefSeqNP_060206.2. NM_017736.3.
UniGeneHs.460232.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DIRNMR-A170-254[»]
ProteinModelPortalQ9NXG2.
SMRQ9NXG2. Positions 170-254.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9NXG2.

PTM databases

PhosphoSiteQ9NXG2.

Polymorphism databases

DMDM61248576.

Proteomic databases

PRIDEQ9NXG2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000381337; ENSP00000370741; ENSG00000066654.
ENST00000396083; ENSP00000379392; ENSG00000066654.
ENST00000431224; ENSP00000392282; ENSG00000066654.
GeneID55623.
KEGGhsa:55623.
NMPDRfig|9606.3.peg.11828.
UCSCuc002dho.1. human.

Organism-specific databases

CTD55623.
GeneCardsGC16M020744.
H-InvDBHIX0019394.
HGNCHGNC:23807. THUMPD1.
HPAHPA027851.
neXtProtNX_Q9NXG2.
GenAtlasSearch...

Phylogenomic databases

GeneTreeENSGT00390000002365.
HOVERGENHBG053030.
InParanoidQ9NXG2.
OrthoDBEOG4P8FJT.
PhylomeDBQ9NXG2.

Gene expression databases

ArrayExpressQ9NXG2.
BgeeQ9NXG2.
CleanExHS_THUMPD1.
GenevestigatorQ9NXG2.
GermOnlineENSG00000066654. Homo sapiens.

Family and domain databases

InterProIPR004114. THUMP.
[Graphical view]
KOK06963.
PfamPF02926. THUMP. 1 hit.
[Graphical view]
SMARTSM00981. THUMP. 1 hit.
[Graphical view]
PROSITEPS51165. THUMP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio60236.

Entry information

Entry nameTHUM1_HUMAN
AccessionPrimary (citable) accession number: Q9NXG2
Secondary accession number(s): Q9BWC3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 70 of the entry and version 2 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.

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Human chromosome 16: entries, gene names and cross-references to MIM

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families