UniProt Accession

 TSAP1_HUMAN; Q9NX07; Q86SU7 

Genbank Protein ID

 AK000510; AL513497; CH471059; BC000680; BC039879 

Genbank Nucleotide ID

 BAA91217.1; CAI22288.1; EAX07689.1; AAH00680.1; AAH39879.1 

Protein Name

 tRNA selenocysteine 1-associated protein 1 

Protein Synonyms/Alias

 SECp43; tRNA selenocysteine-associated protein 1 

Gene Name

 TRNAU1AP 

Gene Synonyms/Alias

 SECP43; TRSPAP1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
68	CLHKINGKPLPGATP	ubiquitination	[1, 2]
77	LPGATPAKRFKLNYA	ubiquitination	[1]
80	ATPAKRFKLNYATYG	ubiquitination	[1]
127	YPSCRGGKVVLDQTG	ubiquitination	[1, 2, 3]
137	LDQTGVSKGYGFVKF	ubiquitination	[1, 3]
143	SKGYGFVKFTDELEQ	ubiquitination	[1]
151	FTDELEQKRALTECQ	ubiquitination	[1, 3, 4, 5]
166	GAVGLGSKPVRLSVA	ubiquitination	[1, 2, 5]
176	RLSVAIPKASRVKPV	ubiquitination	[1]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 

Functional Description

 Involved in the early steps of selenocysteine biosynthesis and tRNA(Sec) charging to the later steps resulting in the cotranslational incorporation of selenocysteine into selenoproteins. Stabilizes the SECISBP2, EEFSEC and tRNA(Sec) complex. May be involved in the methylation of tRNA(Sec). Enhances efficiency of selenoproteins synthesis (By similarity). 

Sequence Annotation

 DOMAIN 3 86 RRM 1.
 DOMAIN 96 175 RRM 2.  

Keyword

 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Nucleus; Protein biosynthesis; Reference proteome; Repeat; RNA-binding. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 287 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; ISS:HGNC.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0001514; P:selenocysteine incorporation; ISS:HGNC. 

Interpro

 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 

Pfam

 PF00076; RRM_1 

SMART

 SM00360; RRM 

PROSITE

 PS50102; RRM 

PRINTS