CPLM-019126

Genbank Nucleotide ID

Protein Synonyms/Alias

E3-14.7K-interacting protein; FIP-2; Huntingtin yeast partner L; Huntingtin-interacting protein 7; HIP-7; Huntingtin-interacting protein L; NEMO-related protein; Optic neuropathy-inducing protein; Transcription factor IIIA-interacting protein; TFIIIA-IntP

FIP2; GLC1E; HIP7; HYPL; NRP

Homo sapiens (Human)

Position	Peptide	Type	References
213	STGTALSKYRSRSAD	ubiquitination	[1]
319	ELQEAHTKLSKAELM	ubiquitination	[2]
322	EAHTKLSKAELMKKR	ubiquitination	[2]
327	LSKAELMKKRLQEKC	ubiquitination	[2]
333	MKKRLQEKCQALERK	acetylation	[3]
448	QLQMDEMKQTIAKQE	ubiquitination	[1, 2, 4]
489	REKIHEEKEQLALQL	ubiquitination	[5]
501	LQLAVLLKENDAFED	ubiquitination	[2, 5, 6]

[1] 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]
[2] 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]
[3] Regulation of cellular metabolism by protein lysine acetylation.
Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
[4] 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]
[5] 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]
[6] 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]

Functional Description

Plays an important role in the maintenance of the Golgi complex, in membrane trafficking, in exocytosis, through its interaction with myosin VI and Rab8. Links myosin VI to the Golgi complex and plays an important role in Golgi ribbon formation. Negatively regulates the induction of IFNB in response to RNA virus infection. Plays a neuroprotective role in the eye and optic nerve. Probably part of the TNF-alpha signaling pathway that can shift the equilibrium toward induction of cell death. May act by regulating membrane trafficking and cellular morphogenesis via a complex that contains Rab8 and hungtingtin (HD). May constitute a cellular target for adenovirus E3 14.7, an inhibitor of TNF-alpha functions, thereby affecting cell death.

REGION 58 209 Interaction with Rab8.
REGION 411 577 Interaction with HD.
REGION 412 520 Interaction with MYO6.
MOTIF 474 479 UBAN.
MOD_RES 177 177 Phosphoserine; by TBK1.
MOD_RES 342 342 Phosphoserine (By similarity).

3D-structure; Alternative splicing; Amyotrophic lateral sclerosis; Coiled coil; Complete proteome; Cytoplasm; Disease mutation; Glaucoma; Golgi apparatus; Neurodegeneration; Phosphoprotein; Polymorphism; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005829; C:cytosol; TAS:Reactome.
GO:0000139; C:Golgi membrane; TAS:Reactome.
GO:0005654; C:nucleoplasm; TAS:Reactome.
GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
GO:0008219; P:cell death; TAS:ProtInc.
GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO:0090161; P:Golgi ribbon formation; IDA:UniProtKB.
GO:0043001; P:Golgi to plasma membrane protein transport; IMP:UniProtKB.
GO:0000042; P:protein targeting to Golgi; IMP:UniProtKB.
GO:0007165; P:signal transduction; TAS:ProtInc.