UniProt Accession

 PR40A_HUMAN; O75400; O43856; O75404; Q8TBQ1; Q9H782; Q9NWU9; Q9P0Q2; Q9Y5A8 

Genbank Protein ID

 AC012443; AC079344; AK000592; AK024810; AF049523; AF049524; AF049528; BC011788; BC027178; U70667; AF155096; AF151059 

Genbank Nucleotide ID

 BAA91277.1; BAB15016.1; AAC27501.1; AAC27502.1; AAC27506.1; AAH11788.1; AAH27178.1; AAB93495.1; AAD42862.1; AAF36145.1 

Protein Name

 Pre-mRNA-processing factor 40 homolog A 

Protein Synonyms/Alias

 Fas ligand-associated factor 1; Formin-binding protein 11; Formin-binding protein 3; Huntingtin yeast partner A; Huntingtin-interacting protein 10; HIP-10; Huntingtin-interacting protein A; Renal carcinoma antigen NY-REN-6 

Gene Name

 PRPF40A 

Gene Synonyms/Alias

 FBP11; FLAF1; FNBP3; HIP10; HYPA; HSPC225 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
196	EYKSDSGKPYYYNSQ	acetylation	[1]
196	EYKSDSGKPYYYNSQ	ubiquitination	[2, 3, 4, 5]
450	AYKVQTEKEEKEEAR	acetylation	[6]
596	EKEEEEEKQKSLLRE	ubiquitination	[6]
669	KFYVEDLKARYHDEK	ubiquitination	[2, 5, 6]
680	HDEKKIIKDILKDKG	acetylation	[1]
718	TLDAGNIKLAFNSLL	ubiquitination	[3, 5, 6, 7]
727	AFNSLLEKAEARERE	ubiquitination	[3, 4, 5, 6, 7]
755	SAFKSMLKQAAPPIE	ubiquitination	[7]
776	DIRERFVKEPAFEDI	ubiquitination	[2, 5, 6, 8]
925	SPKKKTGKDSGNWDT	acetylation	[9]
944	LSEGELEKRRRTLLE	ubiquitination	[8]

Reference

 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] 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]
 [3] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] 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]
 [6] 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]
 [7] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [8] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [9] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 

Functional Description

 Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing. 

Sequence Annotation

 DOMAIN 140 173 WW 1.
 DOMAIN 181 214 WW 2.
 DOMAIN 393 447 FF 1.
 DOMAIN 460 514 FF 2.
 DOMAIN 527 587 FF 3.
 DOMAIN 607 667 FF 4.
 DOMAIN 672 727 FF 5.
 DOMAIN 742 799 FF 6.
 MOD_RES 36 36 Phosphoserine (By similarity).
 MOD_RES 151 151 Phosphoserine.
 MOD_RES 196 196 N6-acetyllysine.
 MOD_RES 373 373 Phosphothreonine.
 MOD_RES 828 828 Phosphoserine (By similarity).
 MOD_RES 830 830 Phosphoserine (By similarity).
 MOD_RES 832 832 Phosphoserine (By similarity).
 MOD_RES 834 834 Phosphoserine (By similarity).
 MOD_RES 883 883 Phosphoserine.
 MOD_RES 885 885 Phosphoserine.
 MOD_RES 888 888 Phosphoserine.
 MOD_RES 932 932 Phosphothreonine.
 MOD_RES 933 933 Phosphoserine.
 MOD_RES 935 935 Phosphoserine.
 MOD_RES 938 938 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division; Complete proteome; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 957 AA 

Protein Sequence

Gene Ontology

 GO:0016363; C:nuclear matrix; IDA:UniProtKB.
 GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0016477; P:cell migration; IMP:UniProtKB.
 GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
 GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
 GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB.
 GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. 

Interpro

 IPR002713; FF_domain.
 IPR001202; WW_dom. 

Pfam

 PF01846; FF
 PF00397; WW 

SMART

 SM00441; FF
 SM00456; WW 

PROSITE

 PS51676; FF
 PS01159; WW_DOMAIN_1
 PS50020; WW_DOMAIN_2 

PRINTS