CPLM-021285

Genbank Nucleotide ID

EH domain-containing protein 4

Protein Synonyms/Alias

Hepatocellular carcinoma-associated protein 10/11; PAST homolog 4

HCA10; HCA11; PAST4; FKSG7

Homo sapiens (Human)

Position	Peptide	Type	References
35	LRSLYLRKVLPLEEA	ubiquitination	[1, 2, 3]
165	PGILSGEKQRISRGY	ubiquitination	[4, 5]
223	KIRVVLNKADQVDTQ	ubiquitination	[4, 5, 6]
291	DIQSLPQKAAVRKLN	ubiquitination	[2, 4]
296	PQKAAVRKLNDLIKR	ubiquitination	[2]
327	EMPSVFGKENKKREL	acetylation	[7]
508	EEEFALAKHLIKIKL	ubiquitination	[2]

[1] 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]
[2] 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]
[3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[4] 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]
[5] 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]
[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]
[7] 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]

Functional Description

Plays a role in early endosomal transport.

DOMAIN 447 535 EH.
DOMAIN 479 514 EF-hand.
NP_BIND 68 75 ATP (By similarity).
BINDING 223 223 ATP (By similarity).
BINDING 261 261 ATP (By similarity).
MOD_RES 451 451 Phosphotyrosine.
MOD_RES 459 459 Phosphoserine.

ATP-binding; Calcium; Cell membrane; Complete proteome; Endosome; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO:0005783; C:endoplasmic reticulum; IDA:LIFEdb.
GO:0005634; C:nucleus; TAS:ProtInc.
GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO:0005509; F:calcium ion binding; IEA:InterPro.
GO:0005525; F:GTP binding; IEA:InterPro.
GO:0003924; F:GTPase activity; IEA:InterPro.
GO:0003676; F:nucleic acid binding; TAS:ProtInc.
GO:0071363; P:cellular response to growth factor stimulus; IEA:Compara.
GO:0032456; P:endocytic recycling; IGI:UniProtKB.
GO:0006184; P:GTP catabolic process; IEA:GOC.
GO:0006907; P:pinocytosis; IEA:Compara.
GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Compara.
GO:0051260; P:protein homooligomerization; IPI:UniProtKB.
GO:0030100; P:regulation of endocytosis; IEA:Compara.

IPR001401; Dynamin_GTPase.
IPR011992; EF-hand-like_dom.
IPR018247; EF_Hand_1_Ca_BS.
IPR002048; EF_hand_dom.
IPR000261; EPS15_homology.
IPR027417; P-loop_NTPase.

PS00018; EF_HAND_1
PS50222; EF_HAND_2
PS50031; EH