UniProt Accession

 HENMT_HUMAN; Q5T8I9; A8MRR6; B1AM16; B1AM17; Q96EJ7; Q96NN0 

Genbank Protein ID

 AK055087; AL160171; AL160171; AL160171; CH471122; BC012198; BC088366 

Genbank Nucleotide ID

 BAB70852.1; CAI12929.1; CAI12930.1; CAI12931.1; EAW56326.1; AAH12198.1; AAH88366.1 

Protein Name

 Small RNA 2'-O-methyltransferase 

Protein Synonyms/Alias

 HEN1 methyltransferase homolog 1 

Gene Name

 HENMT1 

Gene Synonyms/Alias

 C1orf59 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
28	RETAIQFKPPLYRQR	ubiquitination	[1]
40	RQRYQFVKNLVDQHE	ubiquitination	[1, 2]
50	VDQHEPKKVADLGCG	ubiquitination	[1, 3]
100	PFLGDFLKPRDLNLT	ubiquitination	[1, 2]
182	TLRDSDHKFEWTRME	ubiquitination	[1]
235	IFRKNGGKATESCLS	ubiquitination	[1, 3, 4]
251	QHDQHVYKAVFTTSY	ubiquitination	[1, 2]
308	PKDIGGSKAPVPCFG	ubiquitination	[1, 2, 3, 4]
323	PVFTEVEKAKIENSP	ubiquitination	[1, 2]
325	FTEVEKAKIENSPTP	ubiquitination	[1, 4]
338	TPFCVGDKFFVPLQR	ubiquitination	[1, 2, 3, 4]
351	QRLLAYPKLNRLCAN	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] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [3] 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]
 [4] 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] 

Functional Description

 Methyltransferase that adds a 2'-O-methyl group at the 3'-end of piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. This probably protects the 3'-end of piRNAs from uridylation activity and subsequent degradation. Stabilization of piRNAs is essential for gametogenesis (By similarity). 

Sequence Annotation

 METAL 132 132 Magnesium (By similarity).
 METAL 135 135 Magnesium (By similarity).
 METAL 136 136 Magnesium; via tele nitrogen (By
 METAL 181 181 Magnesium; via tele nitrogen (By
 BINDING 60 60 S-adenosyl-L-methionine (By similarity).
 BINDING 78 78 S-adenosyl-L-methionine (By similarity).
 BINDING 114 114 S-adenosyl-L-methionine (By similarity).  

Keyword

 Complete proteome; Cytoplasm; Metal-binding; Methyltransferase; Polymorphism; Reference proteome; RNA-binding; RNA-mediated gene silencing; S-adenosyl-L-methionine; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 393 AA 

Protein Sequence

Gene Ontology

 GO:0043186; C:P granule; ISS:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0008171; F:O-methyltransferase activity; ISS:UniProtKB.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0008173; F:RNA methyltransferase activity; ISS:UniProtKB.
 GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
 GO:0034587; P:piRNA metabolic process; ISS:UniProtKB. 

Interpro

 IPR026610; Hen1. 

Pfam

  

SMART

  

PROSITE

  

PRINTS