RUND1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RUND1_HUMAN
• UniProt AC: Q96C34
• Protein Name: RUN domain-containing protein 1
• Gene Name: RUNDC1
• Organism: Homo sapiens (Human).
• Sequence Length: 613
• Protein Description: May play a role as p53/TP53 inhibitor and thus may have oncogenic activity..
• Protein Sequence: MAAVEAAAEPVTVVAAVGPKAKDEEEEEEEPLPPCEAVRWAPVGAVAEARPGATAFLEEATAEEPGAAPGSPPDSPGRTLRRLRAERRRLDSALLALSSHFAQVQFRLRQVVRGAPAEQQRLLRELEDFAFRGCPHVLGYEGPGDPASDEGDGLPGDRPWLRGEDQSEQEKQERLETQREKQKELILQLKTQLDDLETFAYQEGSYDSLPQSVVLERQRVIIDELIKKLDMNLNEDISSLSTEELRQRVDAAVAQIVNPARVKEQLVEQLKTQIRDLEMFINFIQDEVGSPLQTGGGHCECKAGGKTGNGCSRTGSSRTPPGNSKTKAEDVKKVRETGLHLMRRALAVLQIFAVSQFGCATGQIPPTLWQRVQADRDYSPLLKRLEVSVDRVKQLALRQQPHDHVITSANLQDLSLGGKDELTMAVRKELTVAVRDLLAHGLYASSPGMSLVMAPIACLLPAFSSAPEAMHPWELFVKYYHAKNGRAYVESPARKLSQSFALPVTGGTVVTPKQSLLTAIHMVLTEHDPFKRSADSELKALVCMALNEQRLVSWVNLICKSGSLIEPHYQPWSYMAHTGFESALNLLSRLSSLKFSLPVDLAVRQLKNIKDAF

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
54	Phosphorylation	AEARPGATAFLEEAT EECCCCCCCHHHHHH	24.69	21406692
61	Phosphorylation	TAFLEEATAEEPGAA CCHHHHHHCCCCCCC	37.57	26552605
71	Phosphorylation	EPGAAPGSPPDSPGR CCCCCCCCCCCCCCH	32.00	29255136
75	Phosphorylation	APGSPPDSPGRTLRR CCCCCCCCCCHHHHH	34.72	29255136
79	Phosphorylation	PPDSPGRTLRRLRAE CCCCCCHHHHHHHHH	30.45	21406692
92	Phosphorylation	AERRRLDSALLALSS HHHHHHHHHHHHHHH	25.96	24719451
167	Phosphorylation	WLRGEDQSEQEKQER CCCCCCHHHHHHHHH	54.27	29691806
183	Ubiquitination	ETQREKQKELILQLK HHHHHHHHHHHHHHH	66.61	-
228	Ubiquitination	IIDELIKKLDMNLNE HHHHHHHHHCCCCCC	42.60	-
263	Ubiquitination	IVNPARVKEQLVEQL HHCHHHHHHHHHHHH	33.90	-
271	Ubiquitination	EQLVEQLKTQIRDLE HHHHHHHHHHHHHHH	37.77	-
290	Phosphorylation	FIQDEVGSPLQTGGG HHHHCCCCCCCCCCC	27.84	25159151
307	Phosphorylation	ECKAGGKTGNGCSRT EEECCCCCCCCCCCC	38.87	-
314	Phosphorylation	TGNGCSRTGSSRTPP CCCCCCCCCCCCCCC	25.73	28348404
316	Phosphorylation	NGCSRTGSSRTPPGN CCCCCCCCCCCCCCC	18.94	28102081
317	Phosphorylation	GCSRTGSSRTPPGNS CCCCCCCCCCCCCCC	41.33	28102081
319	Phosphorylation	SRTGSSRTPPGNSKT CCCCCCCCCCCCCCC	35.46	28348404
337	Phosphorylation	DVKKVRETGLHLMRR HHHHHHHHHHHHHHH	34.18	-
379	Phosphorylation	VQADRDYSPLLKRLE HHCCCCCHHHHHHHC	17.23	24719451
383	Ubiquitination	RDYSPLLKRLEVSVD CCCHHHHHHHCCCHH	63.72	-
393	Ubiquitination	EVSVDRVKQLALRQQ CCCHHHHHHHHHHCC	40.25	-
419	Ubiquitination	QDLSLGGKDELTMAV HHHHCCCHHHHHHHH	46.35	-
428	Ubiquitination	ELTMAVRKELTVAVR HHHHHHHHHHHHHHH	50.94	-
491	Phosphorylation	NGRAYVESPARKLSQ CCCEEEECHHHHHHH	17.51	21815630
495	Ubiquitination	YVESPARKLSQSFAL EEECHHHHHHHCCCC	55.38	-
497	Phosphorylation	ESPARKLSQSFALPV ECHHHHHHHCCCCCC	27.15	26657352
499	Phosphorylation	PARKLSQSFALPVTG HHHHHHHCCCCCCCC	14.76	26657352
505	Phosphorylation	QSFALPVTGGTVVTP HCCCCCCCCCCEECC	28.14	23090842
508	Phosphorylation	ALPVTGGTVVTPKQS CCCCCCCCEECCCHH	17.10	23090842
511	Phosphorylation	VTGGTVVTPKQSLLT CCCCCEECCCHHHHH	22.04	23090842
591	Phosphorylation	LNLLSRLSSLKFSLP HHHHHHHHHCCCCCC	32.30	24719451
594	Ubiquitination	LSRLSSLKFSLPVDL HHHHHHCCCCCCHHH	34.55	-
607	Acetylation	DLAVRQLKNIKDAF- HHHHHHHHCCHHHC-	48.57	7974827
610	Ubiquitination	VRQLKNIKDAF---- HHHHHCCHHHC----	53.01	-

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

Oops, there are no upstream regulatory protein records of RUND1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RUND1_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 RUND1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of RUND1_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

Phosphorylation

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71 AND SER-75, AND MASSSPECTROMETRY.
PubMed: 18669648