RABP2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RABP2_HUMAN
• UniProt AC: P29373
• Protein Name: Cellular retinoic acid-binding protein 2
• Gene Name: CRABP2
• Organism: Homo sapiens (Human).
• Sequence Length: 138
• Subcellular Localization: Cytoplasm. Endoplasmic reticulum. Nucleus. Upon ligand binding, a conformation change exposes a nuclear localization motif and the protein is transported into the nucleus.
• Protein Description: Transports retinoic acid to the nucleus. Regulates the access of retinoic acid to the nuclear retinoic acid receptors..
• Protein Sequence: MPNFSGNWKIIRSENFEELLKVLGVNVMLRKIAVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPCKSLVKWESENKMVCEQKLLKGEGPKTSWTRELTNDGELILTMTADDVVCTRVYVRE

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Succinylation	PNFSGNWKIIRSENF CCCCCCCEEECCCCH	32.05	23954790
13	Phosphorylation	GNWKIIRSENFEELL CCCEEECCCCHHHHH	26.87	24505115
21	Ubiquitination	ENFEELLKVLGVNVM CCHHHHHHHHCHHHH	48.30	21906983
31	Ubiquitination	GVNVMLRKIAVAAAS CHHHHHHHHHHHHHC	30.93	21906983
38	Phosphorylation	KIAVAAASKPAVEIK HHHHHHHCCCCEEEE	34.15	28348404
39	Ubiquitination	IAVAAASKPAVEIKQ HHHHHHCCCCEEEEE	32.06	23000965
45	Sumoylation	SKPAVEIKQEGDTFY CCCCEEEEECCCEEE	28.88	-
45	Sumoylation	SKPAVEIKQEGDTFY CCCCEEEEECCCEEE	28.88	-
45	Ubiquitination	SKPAVEIKQEGDTFY CCCCEEEEECCCEEE	28.88	23000965
52	Phosphorylation	KQEGDTFYIKTSTTV EECCCEEEEEECCEE	12.00	20068231
62	Phosphorylation	TSTTVRTTEINFKVG ECCEEEEEEEEEEEC	25.05	27251275
83	Ubiquitination	TVDGRPCKSLVKWES ECCCEECCHHEEEEC	49.89	21906983
87	Acetylation	RPCKSLVKWESENKM EECCHHEEEECCCCE	51.00	30587861
87	Sumoylation	RPCKSLVKWESENKM EECCHHEEEECCCCE	51.00	-
87	Ubiquitination	RPCKSLVKWESENKM EECCHHEEEECCCCE	51.00	22817900
87	Sumoylation	RPCKSLVKWESENKM EECCHHEEEECCCCE	51.00	-
90	Phosphorylation	KSLVKWESENKMVCE CHHEEEECCCCEEEE	45.41	24719451
99	Ubiquitination	NKMVCEQKLLKGEGP CCEEEEEHHHCCCCC	33.23	23000965
102	Sumoylation	VCEQKLLKGEGPKTS EEEEHHHCCCCCCCC	66.41	-
102	Ubiquitination	VCEQKLLKGEGPKTS EEEEHHHCCCCCCCC	66.41	23000965
102	Sumoylation	VCEQKLLKGEGPKTS EEEEHHHCCCCCCCC	66.41	21998312
107	Ubiquitination	LLKGEGPKTSWTREL HHCCCCCCCCEEEEE	67.08	23000965
115	Phosphorylation	TSWTRELTNDGELIL CCEEEEECCCCCEEE	26.89	28348404
124	Sulfoxidation	DGELILTMTADDVVC CCCEEEEEECCCEEE	2.32	30846556

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RABP2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RABP2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RABP2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CCND3_HUMAN	CCND3	physical	12482873
UBC9_HUMAN	UBE2I	physical	21998312
KASH5_HUMAN	CCDC155	physical	25416956

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• DB00523: Alitretinoin
• DB00755: Tretinoin

Related Literatures of Post-Translational Modification

Sumoylation

"Nuclear translocation of cellular retinoic acid-binding protein II isregulated by retinoic acid-controlled SUMOylation.";
Majumdar A., Petrescu A.D., Xiong Y., Noy N.;
J. Biol. Chem. 286:42749-42757(2011).
Cited for: SUMOYLATION AT LYS-102.
PubMed: 21998312