dbPTM

KRI1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KRI1_HUMAN
UniProt AC	Q8N9T8
Protein Name	Protein KRI1 homolog
Gene Name	KRI1
Organism	Homo sapiens (Human).
Sequence Length	703
Subcellular Localization
Protein Description
Protein Sequence	MPEPRGSSQLRVNAAFAARYNRYREREELQRLKDRYGDRDSSSDSSSESDSSDERVEFDPQQERDFYKTLSLLKKKDPRIYQKDATFYNRTASSSDSEEDPEALEKQKKVRPMYLKDYERKVILEKAGKYVDEENSDGETSNHRLQETSSQSYVEEQKQLKESFRAFVEDSEDEDGAGEGGSSLLQKRAKTRQEKAQEEADYIEWLKGQKEIRNPDSLKELTHLKEYWNDPELDEGERFLRDYILNKRYEEEEEEEEDEEEMEEEEGVHGPPVQLAVDDSSDEGELFLKKQEDFEQKYNFRFEEPDSASVKTYPRSIASSVRRKDERRKEKREETRERKKREKAKKQEELKQLKNLKRKEILAKLEKLRKVTGNEMLGLEEGDLEDDFDPAQHDQLMQKCFGDEYYGAVEEEKPQFEEEEGLEDDWNWDTWDGPEQEGDWSQQELHCEDPNFNMDADYDPSQPRKKKREAPLTGKKKRKSPFAAAVGQEKPVFEPGDKTFEEYLDEYYRLDYEDIIDDLPCRFKYRTVVPCDFGLSTEEILAADDKELNRWCSLKKTCMYRSEQEELRDKRAYSQKAQNSWKKRQVFKSLCREEAETPAEATGKPQRDEAGPQRQLPALDGSLMGPESPPAQEEEAPVSPHKKPAPQKRRRAKKARLLGPTVMLGGCEFSRQRLQAFGLNPKRLHFRQLGRQRRKQQGPKNSS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MPEPRGSSQLRVNAA CCCCCCCCHHHHHHH	46.07	27282143
33	Ubiquitination	REELQRLKDRYGDRD HHHHHHHHHHHCCCC	59.30	-
47	Phosphorylation	DSSSDSSSESDSSDE CCCCCCCCCCCCCCC	32.41	30177828
49	Phosphorylation	SSDSSSESDSSDERV CCCCCCCCCCCCCCC	45.52	18452278
51	Phosphorylation	DSSSESDSSDERVEF CCCCCCCCCCCCCCC	37.40	20068231
52	Phosphorylation	SSSESDSSDERVEFD CCCCCCCCCCCCCCC	43.02	30177828
55	Phosphorylation	ESDSSDERVEFDPQQ CCCCCCCCCCCCHHH	44.75	18452278
71	Phosphorylation	RDFYKTLSLLKKKDP HHHHHHHHHHHHCCC	50.94	20860994
83	Acetylation	KDPRIYQKDATFYNR CCCCCCCCCCCEECC	46.74	26051181
86	Phosphorylation	RIYQKDATFYNRTAS CCCCCCCCEECCCCC	5.34	29514088
88	Phosphorylation	YQKDATFYNRTASSS CCCCCCEECCCCCCC	34.48	29514088
89	Ubiquitination	QKDATFYNRTASSSD CCCCCEECCCCCCCC	32.15	-
91	Phosphorylation	DATFYNRTASSSDSE CCCEECCCCCCCCCC	13.47	23927012
93	Phosphorylation	TFYNRTASSSDSEED CEECCCCCCCCCCCC	5.65	23927012
94	Phosphorylation	FYNRTASSSDSEEDP EECCCCCCCCCCCCH	10.20	25159151
95	Phosphorylation	YNRTASSSDSEEDPE ECCCCCCCCCCCCHH	30.54	25159151
97	Phosphorylation	RTASSSDSEEDPEAL CCCCCCCCCCCHHHH	27.53	28355574
99	Phosphorylation	ASSSDSEEDPEALEK CCCCCCCCCHHHHHH	29.75	19651622
100	Phosphorylation	SSSDSEEDPEALEKQ CCCCCCCCHHHHHHH	35.38	19651622
101	Phosphorylation	SSDSEEDPEALEKQK CCCCCCCHHHHHHHH	42.53	19651622
103	Phosphorylation	DSEEDPEALEKQKKV CCCCCHHHHHHHHHC	44.85	18767875
114	Phosphorylation	QKKVRPMYLKDYERK HHHCCCCHHHHHCHH	65.39	30576142
118	Phosphorylation	RPMYLKDYERKVILE CCCHHHHHCHHHHHH	20.82	20068231
120	Phosphorylation	MYLKDYERKVILEKA CHHHHHCHHHHHHHH	17.18	20068231
124	Phosphorylation	DYERKVILEKAGKYV HHCHHHHHHHHCCCC	18.95	20068231
130	Phosphorylation	ILEKAGKYVDEENSD HHHHHCCCCCCCCCC	6.55	23927012
136	Phosphorylation	KYVDEENSDGETSNH CCCCCCCCCCCCCCH	16.53	29255136
140	Phosphorylation	EENSDGETSNHRLQE CCCCCCCCCCHHHHH	58.53	22167270
141	Phosphorylation	ENSDGETSNHRLQET CCCCCCCCCHHHHHH	43.27	22167270
142	Phosphorylation	NSDGETSNHRLQETS CCCCCCCCHHHHHHH	50.72	19691289
147	Phosphorylation	TSNHRLQETSSQSYV CCCHHHHHHHCHHHH	26.74	18669648
148	Phosphorylation	SNHRLQETSSQSYVE CCHHHHHHHCHHHHH	31.55	23927012
149	Phosphorylation	NHRLQETSSQSYVEE CHHHHHHHCHHHHHH	31.43	25159151
150	Phosphorylation	HRLQETSSQSYVEEQ HHHHHHHCHHHHHHH	42.17	17525332
152	Phosphorylation	LQETSSQSYVEEQKQ HHHHHCHHHHHHHHH	52.45	25159151
153	Phosphorylation	QETSSQSYVEEQKQL HHHHCHHHHHHHHHH	56.07	23663014
156	Phosphorylation	SSQSYVEEQKQLKES HCHHHHHHHHHHHHH	30.48	17525332
158	Acetylation	QSYVEEQKQLKESFR HHHHHHHHHHHHHHH	32.85	26051181
158	Phosphorylation	QSYVEEQKQLKESFR HHHHHHHHHHHHHHH	32.85	18669648
163	Phosphorylation	EQKQLKESFRAFVED HHHHHHHHHHHHHCC	25.86	30576142
164	Ubiquitination	QKQLKESFRAFVEDS HHHHHHHHHHHHCCC	61.96	-
169	Phosphorylation	ESFRAFVEDSEDEDG HHHHHHHCCCCCCCC	20.60	20068231
171	Phosphorylation	FRAFVEDSEDEDGAG HHHHHCCCCCCCCCC	36.07	19664994
177	Phosphorylation	DSEDEDGAGEGGSSL CCCCCCCCCCCHHHH	33.18	19664994
182	Phosphorylation	DGAGEGGSSLLQKRA CCCCCCHHHHHHHHH	33.17	23927012
183	Phosphorylation	GAGEGGSSLLQKRAK CCCCCHHHHHHHHHH	25.78	25159151
188	Phosphorylation	GSSLLQKRAKTRQEK HHHHHHHHHHHHHHH	28.77	18669648
191	Phosphorylation	LLQKRAKTRQEKAQE HHHHHHHHHHHHHHH	6.44	26074081
202	Phosphorylation	KAQEEADYIEWLKGQ HHHHHHHHHHHHCCC	22.67	28796482
207	Acetylation	ADYIEWLKGQKEIRN HHHHHHHCCCCCCCC	48.50	7964333
208	Phosphorylation	DYIEWLKGQKEIRNP HHHHHHCCCCCCCCC	14.05	-
213	Ubiquitination	LKGQKEIRNPDSLKE HCCCCCCCCCCHHHH	61.44	-
217	Phosphorylation	KEIRNPDSLKELTHL CCCCCCCHHHHHHHH	39.01	20873877
222	Phosphorylation	PDSLKELTHLKEYWN CCHHHHHHHHHHHHC	70.88	20873877
223	Phosphorylation	DSLKELTHLKEYWND CHHHHHHHHHHHHCC	42.47	-
225	Ubiquitination	LKELTHLKEYWNDPE HHHHHHHHHHHCCCC	55.41	-
227	Phosphorylation	ELTHLKEYWNDPELD HHHHHHHHHCCCCCC	3.32	-
231	Ubiquitination	LKEYWNDPELDEGER HHHHHCCCCCCHHHH	40.95	-
233	Phosphorylation	EYWNDPELDEGERFL HHHCCCCCCHHHHHH	14.13	-
249	Phosphorylation	DYILNKRYEEEEEEE HHHHHHCCHHHHHHH	10.81	27251275
253	Ubiquitination	NKRYEEEEEEEEDEE HHCCHHHHHHHHHHH	53.57	-
280	Phosphorylation	VQLAVDDSSDEGELF EEEEEECCCCCCCEE	29.49	22617229
281	Phosphorylation	QLAVDDSSDEGELFL EEEEECCCCCCCEEE	5.23	22617229
286	Phosphorylation	DSSDEGELFLKKQED CCCCCCCEEEEEHHH	34.91	17081983
287	Phosphorylation	SSDEGELFLKKQEDF CCCCCCEEEEEHHHH	46.83	17081983
303	Ubiquitination	QKYNFRFEEPDSASV HHHCCCCCCCCCCCC	34.66	-
307	Phosphorylation	FRFEEPDSASVKTYP CCCCCCCCCCCCCCC	34.13	29255136
309	Phosphorylation	FEEPDSASVKTYPRS CCCCCCCCCCCCCCC	65.45	29255136
313	Phosphorylation	DSASVKTYPRSIASS CCCCCCCCCCCHHHH	32.91	-
315	Phosphorylation	ASVKTYPRSIASSVR CCCCCCCCCHHHHHH	28.26	-
319	O-linked_Glycosylation	TYPRSIASSVRRKDE CCCCCHHHHHHHHHH	7.31	29351928
319	Phosphorylation	TYPRSIASSVRRKDE CCCCCHHHHHHHHHH	7.31	22210691
320	O-linked_Glycosylation	YPRSIASSVRRKDER CCCCHHHHHHHHHHH	28.86	29351928
320	Phosphorylation	YPRSIASSVRRKDER CCCCHHHHHHHHHHH	28.86	26434776
326	Phosphorylation	SSVRRKDERRKEKRE HHHHHHHHHHHHHHH	15.60	-
343	Acetylation	RERKKREKAKKQEEL HHHHHHHHHHHHHHH	76.03	12433745
345	Acetylation	RKKREKAKKQEELKQ HHHHHHHHHHHHHHH	51.97	12433755
346	Acetylation	KKREKAKKQEELKQL HHHHHHHHHHHHHHH	72.51	12433765
359	Acetylation	QLKNLKRKEILAKLE HHHHHCHHHHHHHHH	3.67	130357
364	Acetylation	KRKEILAKLEKLRKV CHHHHHHHHHHHHHH	45.03	130353
419	Sumoylation	EKPQFEEEEGLEDDW CCCCCCCCCCCCCCC	47.61	-
473	Phosphorylation	KKREAPLTGKKKRKS CCCCCCCCCCCCCCC	59.51	23312004
475	Acetylation	REAPLTGKKKRKSPF CCCCCCCCCCCCCCC	64.62	25953088
479	Phosphorylation	LTGKKKRKSPFAAAV CCCCCCCCCCCHHHC	45.99	-
480	Phosphorylation	TGKKKRKSPFAAAVG CCCCCCCCCCHHHCC	47.68	22199227
486	Phosphorylation	KSPFAAAVGQEKPVF CCCCHHHCCCCCCCC	29.32	-
496	Ubiquitination	EKPVFEPGDKTFEEY CCCCCCCCCCCHHHH	38.30	-
499	Phosphorylation	VFEPGDKTFEEYLDE CCCCCCCCHHHHHHH	14.74	28509920
503	Phosphorylation	GDKTFEEYLDEYYRL CCCCHHHHHHHHHCC	58.50	28509920
507	Phosphorylation	FEEYLDEYYRLDYED HHHHHHHHHCCCHHH	51.46	-
512	Phosphorylation	DEYYRLDYEDIIDDL HHHHCCCHHHHHHCC	41.70	22817900
518	Phosphorylation	DYEDIIDDLPCRFKY CHHHHHHCCCCCCEE	21.79	-
536	Phosphorylation	VPCDFGLSTEEILAA EECCCCCCHHHHHHC	13.97	28348404
537	Phosphorylation	PCDFGLSTEEILAAD ECCCCCCHHHHHHCC	4.59	28348404
562	Phosphorylation	KKTCMYRSEQEELRD HHHHHHHHHHHHHHH	52.85	20363803
568	Phosphorylation	RSEQEELRDKRAYSQ HHHHHHHHHHHHHHH	26.58	-
574	Phosphorylation	LRDKRAYSQKAQNSW HHHHHHHHHHHHHHH	51.16	24505115
580	Phosphorylation	YSQKAQNSWKKRQVF HHHHHHHHHHHHHHH	24.99	24505115
582	Ubiquitination	QKAQNSWKKRQVFKS HHHHHHHHHHHHHHH	46.10	-
588	Acetylation	WKKRQVFKSLCREEA HHHHHHHHHHHHHHC	37.59	25953088
589	Phosphorylation	KKRQVFKSLCREEAE HHHHHHHHHHHHHCC	41.63	28555341
597	Glutathionylation	LCREEAETPAEATGK HHHHHCCCHHHHCCC	7.12	22555962
597	Phosphorylation	LCREEAETPAEATGK HHHHHCCCHHHHCCC	7.12	25159151
603	Phosphorylation	ETPAEATGKPQRDEA CCHHHHCCCCCCCCC	34.54	-
604	Acetylation	TPAEATGKPQRDEAG CHHHHCCCCCCCCCC	21.43	26051181
622	Phosphorylation	QLPALDGSLMGPESP CCCCCCCCCCCCCCC	2.67	30266825
628	Phosphorylation	GSLMGPESPPAQEEE CCCCCCCCCCCCCCC	18.17	29255136
634	Phosphorylation	ESPPAQEEEAPVSPH CCCCCCCCCCCCCCC	39.04	18691976
639	Phosphorylation	QEEEAPVSPHKKPAP CCCCCCCCCCCCCCC	60.97	29255136
645	Phosphorylation	VSPHKKPAPQKRRRA CCCCCCCCCHHHHHH	21.89	18691976
673	Glutathionylation	GCEFSRQRLQAFGLN CCHHHHHHHHHCCCC	4.53	22555962
682	2-Hydroxyisobutyrylation	QAFGLNPKRLHFRQL HHCCCCHHHHHHHHH	12.69	-

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of KRI1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KRI1_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of KRI1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
MPP10_HUMAN	MPHOSPH10	physical	26344197
SP16H_HUMAN	SUPT16H	physical	26344197

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.

Regulatory Network of KRI1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-286; SER-287;SER-634 AND SER-645, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-634 ANDSER-645, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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 THR-97; SER-99; SER-100;SER-101; SER-103; SER-142; SER-147; SER-177; SER-286; SER-287 ANDSER-645, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634 AND SER-645, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND MASSSPECTROMETRY.	19007248 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177, AND MASSSPECTROMETRY.	17287340 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; SER-177 ANDSER-634, AND MASS SPECTROMETRY.	17081983 [Abstract]