RIMB2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RIMB2_HUMAN
• UniProt AC: O15034
• Protein Name: RIMS-binding protein 2
• Gene Name: RIMBP2
• Organism: Homo sapiens (Human).
• Sequence Length: 1052
• Subcellular Localization: Cell membrane. Cell junction, synapse. Synaptic plasma membrane..
• Protein Description: Plays a role in the synaptic transmission as bifunctional linker that interacts simultaneously with RIMS1, RIMS2, CACNA1D and CACNA1B..
• Protein Sequence: MREAAERRQQLQLEHDQALAVLSAKQQEIDLLQKSKVRELEEKCRTQSEQFNLLSRDLEKFRQHAGKIDLLGGSAVAPLDISTAPSKPFPQFMNGLATSLGKGQESAIGGSSAIGEYIRPLPQPGDRPEPLSAKPTFLSRSGSARCRSESDMENERNSNTSKQRYSGKVHLCVARYSYNPFDGPNENPEAELPLTAGKYLYVYGDMDEDGFYEGELLDGQRGLVPSNFVDFVQDNESRLASTLGNEQDQNFINHSGIGLEGEHILDLHSPTHIDAGITDNSAGTLDVNIDDIGEDIVPYPRKITLIKQLAKSVIVGWEPPAVPPGWGTVSSYNVLVDKETRMNLTLGSRTKALIEKLNMAACTYRISVQCVTSRGSSDELQCTLLVGKDVVVAPSHLRVDNITQISAQLSWLPTNSNYSHVIFLNEEEFDIVKAARYKYQFFNLRPNMAYKVKVLAKPHQMPWQLPLEQREKKEAFVEFSTLPAGPPAPPQDVTVQAGVTPATIRVSWRPPVLTPTGLSNGANVTGYGVYAKGQRVAEVIFPTADSTAVELVRLRSLEAKGVTVRTLSAQGESVDSAVAAVPPELLVPPTPHPRPAPQSKPLASSGVPETKDEHLGPHARMDEAWEQSRAPGPVHGHMLEPPVGPGRRSPSPSRILPQPQGTPVSTTVAKAMAREAAQRVAESSRLEKRSVFLERSSAGQYAASDEEDAYDSPDFKRRGASVDDFLKGSELGKQPHCCHGDEYHTESSRGSDLSDIMEEDEEELYSEMQLEDGGRRRPSGTSHNALKILGNPASAGRVDHMGRRFPRGSAGPQRSRPVTVPSIDDYGRDRLSPDFYEESETDPGAEELPARIFVALFDYDPLTMSPNPDAAEEELPFKEGQIIKVYGDKDADGFYRGETCARLGLIPCNMVSEIQADDEEMMDQLLRQGFLPLNTPVEKIERSRRSGRRHSVSTRRMVALYDYDPRESSPNVDVEAELTFCTGDIITVFGEIDEDGFYYGELNGQKGLVPSNFLEEVPDDVEVYLSDAPSHYSQDTPMRSKAKRKKSVHFTP

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
74	Phosphorylation	KIDLLGGSAVAPLDI CCEECCCCCEECCCC	20.12	30243723
82	Phosphorylation	AVAPLDISTAPSKPF CEECCCCCCCCCCCC	20.41	30243723
83	Phosphorylation	VAPLDISTAPSKPFP EECCCCCCCCCCCCH	42.81	30243723
98	Phosphorylation	QFMNGLATSLGKGQE HHHHHHHHHCCCCCC	29.53	22210691
99	Phosphorylation	FMNGLATSLGKGQES HHHHHHHHCCCCCCC	29.53	25348772
112	Phosphorylation	ESAIGGSSAIGEYIR CCCCCCCCHHHHHCC	27.47	22210691
117	Phosphorylation	GSSAIGEYIRPLPQP CCCHHHHHCCCCCCC	9.30	22210691
176	Phosphorylation	VHLCVARYSYNPFDG EEEEEEECCCCCCCC	13.03	27732954
177	Phosphorylation	HLCVARYSYNPFDGP EEEEEECCCCCCCCC	16.93	27732954
178	Phosphorylation	LCVARYSYNPFDGPN EEEEECCCCCCCCCC	20.23	27732954
345	Phosphorylation	KETRMNLTLGSRTKA CCCCCCCCCCHHHHH	24.86	23403867
348	Phosphorylation	RMNLTLGSRTKALIE CCCCCCCHHHHHHHH	39.63	23403867
350	Phosphorylation	NLTLGSRTKALIEKL CCCCCHHHHHHHHHH	23.51	23403867
376	Phosphorylation	QCVTSRGSSDELQCT EEEECCCCCCCEEEE	33.24	-
377	Phosphorylation	CVTSRGSSDELQCTL EEECCCCCCCEEEEE	37.62	-
599	Phosphorylation	HPRPAPQSKPLASSG CCCCCCCCCCCCCCC	34.87	24719451
628	Phosphorylation	MDEAWEQSRAPGPVH HHHHHHHCCCCCCCC	20.92	-
649	Phosphorylation	PVGPGRRSPSPSRIL CCCCCCCCCCHHHCC	28.50	25921289
651	Phosphorylation	GPGRRSPSPSRILPQ CCCCCCCCHHHCCCC	36.43	25921289
653	Phosphorylation	GRRSPSPSRILPQPQ CCCCCCHHHCCCCCC	35.97	25921289
662	Phosphorylation	ILPQPQGTPVSTTVA CCCCCCCCCCHHHHH	18.44	27732954
665	O-linked_Glycosylation	QPQGTPVSTTVAKAM CCCCCCCHHHHHHHH	21.40	28657654
665	Phosphorylation	QPQGTPVSTTVAKAM CCCCCCCHHHHHHHH	21.40	27732954
666	O-linked_Glycosylation	PQGTPVSTTVAKAMA CCCCCCHHHHHHHHH	26.06	28657654
666	Phosphorylation	PQGTPVSTTVAKAMA CCCCCCHHHHHHHHH	26.06	27732954
667	O-linked_Glycosylation	QGTPVSTTVAKAMAR CCCCCHHHHHHHHHH	15.80	28657654
667	Phosphorylation	QGTPVSTTVAKAMAR CCCCCHHHHHHHHHH	15.80	27732954
690	Phosphorylation	SSRLEKRSVFLERSS HHHHHHEEEEEECCC	28.43	-
696	Phosphorylation	RSVFLERSSAGQYAA EEEEEECCCCCCCCC	18.37	27732954
697	Phosphorylation	SVFLERSSAGQYAAS EEEEECCCCCCCCCC	42.51	27732954
701	Phosphorylation	ERSSAGQYAASDEED ECCCCCCCCCCCCCC	11.83	27732954
704	Phosphorylation	SAGQYAASDEEDAYD CCCCCCCCCCCCCCC	37.07	27732954
710	Phosphorylation	ASDEEDAYDSPDFKR CCCCCCCCCCCCHHH	29.31	27732954
712	Phosphorylation	DEEDAYDSPDFKRRG CCCCCCCCCCHHHCC	17.43	24076635
721	Phosphorylation	DFKRRGASVDDFLKG CHHHCCCCHHHHHCC	28.98	23312004
727	Ubiquitination	ASVDDFLKGSELGKQ CCHHHHHCCCCCCCC	61.45	17370265
733	Ubiquitination	LKGSELGKQPHCCHG HCCCCCCCCCCCCCC	73.59	17370265
745	Phosphorylation	CHGDEYHTESSRGSD CCCCCCCCCCCCCCC	36.34	-
747	Phosphorylation	GDEYHTESSRGSDLS CCCCCCCCCCCCCHH	26.87	-
748	Phosphorylation	DEYHTESSRGSDLSD CCCCCCCCCCCCHHH	34.13	-
751	Phosphorylation	HTESSRGSDLSDIME CCCCCCCCCHHHHCH	33.98	30576142
754	Phosphorylation	SSRGSDLSDIMEEDE CCCCCCHHHHCHHCH	30.04	30576142
794	Phosphorylation	KILGNPASAGRVDHM HHHCCCCCCCCCCCC	32.29	24670416
832	Phosphorylation	DYGRDRLSPDFYEES HCCCCCCCCCHHCCC	24.26	26657352
836	Phosphorylation	DRLSPDFYEESETDP CCCCCCHHCCCCCCC	26.60	27732954
839	Phosphorylation	SPDFYEESETDPGAE CCCHHCCCCCCCCHH	33.58	27732954
841	Phosphorylation	DFYEESETDPGAEEL CHHCCCCCCCCHHHC	57.69	27732954

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

Oops, there are no upstream regulatory protein records of RIMB2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RIMB2_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 RIMB2_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of RIMB2_HUMAN !!

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
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Ubiquitylation

"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry.";
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
Proteomics 7:868-874(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-727 AND LYS-733, AND MASSSPECTROMETRY.
PubMed: 17370265