dbPTM

STIP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	STIP1_HUMAN
UniProt AC	P31948
Protein Name	Stress-induced-phosphoprotein 1
Gene Name	STIP1
Organism	Homo sapiens (Human).
Sequence Length	543
Subcellular Localization	Cytoplasm . Nucleus .
Protein Description	Acts as a co-chaperone for HSP90AA1. [PubMed: 27353360 Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90 (By similarity]
Protein Sequence	MEQVNELKEKGNKALSVGNIDDALQCYSEAIKLDPHNHVLYSNRSAAYAKKGDYQKAYEDGCKTVDLKPDWGKGYSRKAAALEFLNRFEEAKRTYEEGLKHEANNPQLKEGLQNMEARLAERKFMNPFNMPNLYQKLESDPRTRTLLSDPTYRELIEQLRNKPSDLGTKLQDPRIMTTLSVLLGVDLGSMDEEEEIATPPPPPPPKKETKPEPMEEDLPENKKQALKEKELGNDAYKKKDFDTALKHYDKAKELDPTNMTYITNQAAVYFEKGDYNKCRELCEKAIEVGRENREDYRQIAKAYARIGNSYFKEEKYKDAIHFYNKSLAEHRTPDVLKKCQQAEKILKEQERLAYINPDLALEEKNKGNECFQKGDYPQAMKHYTEAIKRNPKDAKLYSNRAACYTKLLEFQLALKDCEECIQLEPTFIKGYTRKAAALEAMKDYTKAMDVYQKALDLDSSCKEAADGYQRCMMAQYNRHDSPEDVKRRAMADPEVQQIMSDPAMRLILEQMQKDPQALSEHLKNPVIAQKIQKLMDVGLIAIR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEQVNELK -------CHHHHHHH	7.99	22223895
8	2-Hydroxyisobutyrylation	MEQVNELKEKGNKAL CHHHHHHHHHCCCCC	51.72	-
8	Acetylation	MEQVNELKEKGNKAL CHHHHHHHHHCCCCC	51.72	19608861
8	Malonylation	MEQVNELKEKGNKAL CHHHHHHHHHCCCCC	51.72	30639696
8	Succinylation	MEQVNELKEKGNKAL CHHHHHHHHHCCCCC	51.72	23954790
10	Acetylation	QVNELKEKGNKALSV HHHHHHHHCCCCCCC	67.22	156463
10	Ubiquitination	QVNELKEKGNKALSV HHHHHHHHCCCCCCC	67.22	-
13	2-Hydroxyisobutyrylation	ELKEKGNKALSVGNI HHHHHCCCCCCCCCH	60.41	-
13	Ubiquitination	ELKEKGNKALSVGNI HHHHHCCCCCCCCCH	60.41	21890473
16	Phosphorylation	EKGNKALSVGNIDDA HHCCCCCCCCCHHHH	32.60	30278072
26	S-nitrosocysteine	NIDDALQCYSEAIKL CHHHHHHHHHHHHCC	4.14	-
26	Glutathionylation	NIDDALQCYSEAIKL CHHHHHHHHHHHHCC	4.14	22555962
26	S-nitrosylation	NIDDALQCYSEAIKL CHHHHHHHHHHHHCC	4.14	19483679
27	Phosphorylation	IDDALQCYSEAIKLD HHHHHHHHHHHHCCC	9.15	28796482
28	Phosphorylation	DDALQCYSEAIKLDP HHHHHHHHHHHCCCC	28.33	28796482
32	Acetylation	QCYSEAIKLDPHNHV HHHHHHHCCCCCCCC	54.61	26051181
32	Ubiquitination	QCYSEAIKLDPHNHV HHHHHHHCCCCCCCC	54.61	-
41	Phosphorylation	DPHNHVLYSNRSAAY CCCCCCEECCCCCHH	11.65	28796482
42	Phosphorylation	PHNHVLYSNRSAAYA CCCCCEECCCCCHHH	22.93	28442448
44	Methylation	NHVLYSNRSAAYAKK CCCEECCCCCHHHCC	23.02	115917937
48	Phosphorylation	YSNRSAAYAKKGDYQ ECCCCCHHHCCCCHH	20.76	18083107
50	2-Hydroxyisobutyrylation	NRSAAYAKKGDYQKA CCCCHHHCCCCHHHH	44.61	-
50	Ubiquitination	NRSAAYAKKGDYQKA CCCCHHHCCCCHHHH	44.61	21890473
54	Phosphorylation	AYAKKGDYQKAYEDG HHHCCCCHHHHHCCC	22.15	18083107
56	Ubiquitination	AKKGDYQKAYEDGCK HCCCCHHHHHCCCCC	46.86	-
58	Phosphorylation	KGDYQKAYEDGCKTV CCCHHHHHCCCCCCC	22.91	25839225
62	S-nitrosocysteine	QKAYEDGCKTVDLKP HHHHCCCCCCCCCCC	5.30	-
62	S-nitrosylation	QKAYEDGCKTVDLKP HHHHCCCCCCCCCCC	5.30	19483679
63	2-Hydroxyisobutyrylation	KAYEDGCKTVDLKPD HHHCCCCCCCCCCCC	58.05	-
63	Acetylation	KAYEDGCKTVDLKPD HHHCCCCCCCCCCCC	58.05	25953088
63	Malonylation	KAYEDGCKTVDLKPD HHHCCCCCCCCCCCC	58.05	26320211
68	Ubiquitination	GCKTVDLKPDWGKGY CCCCCCCCCCCCCCH	36.15	21890473
68	Ubiquitination	GCKTVDLKPDWGKGY CCCCCCCCCCCCCCH	36.15	21906983
68	Acetylation	GCKTVDLKPDWGKGY CCCCCCCCCCCCCCH	36.15	23954790
68	Malonylation	GCKTVDLKPDWGKGY CCCCCCCCCCCCCCH	36.15	26320211
68	Ubiquitination	GCKTVDLKPDWGKGY CCCCCCCCCCCCCCH	36.15	21890473
73	2-Hydroxyisobutyrylation	DLKPDWGKGYSRKAA CCCCCCCCCHHHHHH	50.88	-
73	Acetylation	DLKPDWGKGYSRKAA CCCCCCCCCHHHHHH	50.88	23236377
73	Malonylation	DLKPDWGKGYSRKAA CCCCCCCCCHHHHHH	50.88	26320211
73	Sumoylation	DLKPDWGKGYSRKAA CCCCCCCCCHHHHHH	50.88	19608861
73	Ubiquitination	DLKPDWGKGYSRKAA CCCCCCCCCHHHHHH	50.88	19608861
78	Malonylation	WGKGYSRKAAALEFL CCCCHHHHHHHHHHH	36.11	26320211
78	Ubiquitination	WGKGYSRKAAALEFL CCCCHHHHHHHHHHH	36.11	21890473
85	Ubiquitination	KAAALEFLNRFEEAK HHHHHHHHHHHHHHH	3.08	21890473
85	Ubiquitination	KAAALEFLNRFEEAK HHHHHHHHHHHHHHH	3.08	21906983
87	Methylation	AALEFLNRFEEAKRT HHHHHHHHHHHHHHH	42.36	115917945
92	Succinylation	LNRFEEAKRTYEEGL HHHHHHHHHHHHHHH	48.86	23954790
93	Methylation	NRFEEAKRTYEEGLK HHHHHHHHHHHHHHH	49.98	115917949
94	Phosphorylation	RFEEAKRTYEEGLKH HHHHHHHHHHHHHHH	34.28	28152594
95	Phosphorylation	FEEAKRTYEEGLKHE HHHHHHHHHHHHHHH	18.93	28152594
99	Ubiquitination	KRTYEEGLKHEANNP HHHHHHHHHHHCCCH	6.06	21890473
99	Ubiquitination	KRTYEEGLKHEANNP HHHHHHHHHHHCCCH	6.06	21906983
100	2-Hydroxyisobutyrylation	RTYEEGLKHEANNPQ HHHHHHHHHHCCCHH	50.70	-
100	Acetylation	RTYEEGLKHEANNPQ HHHHHHHHHHCCCHH	50.70	23749302
100	Malonylation	RTYEEGLKHEANNPQ HHHHHHHHHHCCCHH	50.70	26320211
100	Ubiquitination	RTYEEGLKHEANNPQ HHHHHHHHHHCCCHH	50.70	19608861
109	Ubiquitination	EANNPQLKEGLQNME HCCCHHHHHHHHHHH	44.48	21906983
112	Ubiquitination	NPQLKEGLQNMEARL CHHHHHHHHHHHHHH	3.31	-
115	Ubiquitination	LKEGLQNMEARLAER HHHHHHHHHHHHHHH	2.48	21906983
115	Acetylation	LKEGLQNMEARLAER HHHHHHHHHHHHHHH	2.48	19608861
115	Sulfoxidation	LKEGLQNMEARLAER HHHHHHHHHHHHHHH	2.48	30846556
115	Ubiquitination	LKEGLQNMEARLAER HHHHHHHHHHHHHHH	2.48	19608861
115	Ubiquitination	LKEGLQNMEARLAER HHHHHHHHHHHHHHH	2.48	21890473
118	Methylation	GLQNMEARLAERKFM HHHHHHHHHHHHHHC	22.56	115917929
120	Ubiquitination	QNMEARLAERKFMNP HHHHHHHHHHHHCCC	14.70	-
120	Acetylation	QNMEARLAERKFMNP HHHHHHHHHHHHCCC	14.70	19608861
123	Sumoylation	EARLAERKFMNPFNM HHHHHHHHHCCCCCC	40.23	-
123	Sumoylation	EARLAERKFMNPFNM HHHHHHHHHCCCCCC	40.23	25114211
123	Ubiquitination	EARLAERKFMNPFNM HHHHHHHHHCCCCCC	40.23	21906983
125	Sulfoxidation	RLAERKFMNPFNMPN HHHHHHHCCCCCCCH	7.55	28183972
136	Acetylation	NMPNLYQKLESDPRT CCCHHHHHHHCCCCH	40.44	26051181
136	Ubiquitination	NMPNLYQKLESDPRT CCCHHHHHHHCCCCH	40.44	-
139	O-linked_Glycosylation	NLYQKLESDPRTRTL HHHHHHHCCCCHHHH	64.45	28510447
143	O-linked_Glycosylation	KLESDPRTRTLLSDP HHHCCCCHHHHCCCH	33.13	28510447
145	Acetylation	ESDPRTRTLLSDPTY HCCCCHHHHCCCHHH	31.29	-
145	Ubiquitination	ESDPRTRTLLSDPTY HCCCCHHHHCCCHHH	31.29	21906983
145	Phosphorylation	ESDPRTRTLLSDPTY HCCCCHHHHCCCHHH	31.29	-
147	Ubiquitination	DPRTRTLLSDPTYRE CCCHHHHCCCHHHHH	5.58	21906983
147	Acetylation	DPRTRTLLSDPTYRE CCCHHHHCCCHHHHH	5.58	19608861
147	Ubiquitination	DPRTRTLLSDPTYRE CCCHHHHCCCHHHHH	5.58	19608861
148	Phosphorylation	PRTRTLLSDPTYREL CCHHHHCCCHHHHHH	44.66	23186163
152	Phosphorylation	TLLSDPTYRELIEQL HHCCCHHHHHHHHHH	13.89	23917254
156	Ubiquitination	DPTYRELIEQLRNKP CHHHHHHHHHHHCCC	2.44	21906983
156	Ubiquitination	DPTYRELIEQLRNKP CHHHHHHHHHHHCCC	2.44	21890473
162	Ubiquitination	LIEQLRNKPSDLGTK HHHHHHCCCHHHCCC	39.19	-
164	Phosphorylation	EQLRNKPSDLGTKLQ HHHHCCCHHHCCCCC	47.26	28787133
169	Acetylation	KPSDLGTKLQDPRIM CCHHHCCCCCCHHHH	42.21	23236377
169	Ubiquitination	KPSDLGTKLQDPRIM CCHHHCCCCCCHHHH	42.21	21906983
170	Ubiquitination	PSDLGTKLQDPRIMT CHHHCCCCCCHHHHH	7.58	21906983
170	Ubiquitination	PSDLGTKLQDPRIMT CHHHCCCCCCHHHHH	7.58	21890473
186	Acetylation	LSVLLGVDLGSMDEE HHHHHCCCCCCCCCC	43.44	-
186	Ubiquitination	LSVLLGVDLGSMDEE HHHHHCCCCCCCCCC	43.44	-
198	O-linked_Glycosylation	DEEEEIATPPPPPPP CCCHHCCCCCCCCCC	41.82	OGP
198	Phosphorylation	DEEEEIATPPPPPPP CCCHHCCCCCCCCCC	41.82	26074081
205	Acetylation	TPPPPPPPKKETKPE CCCCCCCCCCCCCCC	67.15	-
207	Acetylation	PPPPPPKKETKPEPM CCCCCCCCCCCCCCC	76.12	11921037
209	Phosphorylation	PPPPKKETKPEPMEE CCCCCCCCCCCCCHH	61.86	26074081
210	Sumoylation	PPPKKETKPEPMEED CCCCCCCCCCCCHHC	48.77	-
210	Acetylation	PPPKKETKPEPMEED CCCCCCCCCCCCHHC	48.77	23749302
210	Sumoylation	PPPKKETKPEPMEED CCCCCCCCCCCCHHC	48.77	25114211
210	Ubiquitination	PPPKKETKPEPMEED CCCCCCCCCCCCHHC	48.77	-
213	Acetylation	KKETKPEPMEEDLPE CCCCCCCCCHHCCCH	43.97	-
214	Sulfoxidation	KETKPEPMEEDLPEN CCCCCCCCHHCCCHH	9.32	21406390
216	Ubiquitination	TKPEPMEEDLPENKK CCCCCCHHCCCHHHH	59.61	21906983
222	Acetylation	EEDLPENKKQALKEK HHCCCHHHHHHHHHH	44.60	-
222	Ubiquitination	EEDLPENKKQALKEK HHCCCHHHHHHHHHH	44.60	-
222	2-Hydroxyisobutyrylation	EEDLPENKKQALKEK HHCCCHHHHHHHHHH	44.60	-
222	Succinylation	EEDLPENKKQALKEK HHCCCHHHHHHHHHH	44.60	23954790
229	2-Hydroxyisobutyrylation	KKQALKEKELGNDAY HHHHHHHHHHCCHHH	57.56	-
229	Acetylation	KKQALKEKELGNDAY HHHHHHHHHHCCHHH	57.56	23749302
229	Malonylation	KKQALKEKELGNDAY HHHHHHHHHHCCHHH	57.56	26320211
237	2-Hydroxyisobutyrylation	ELGNDAYKKKDFDTA HHCCHHHHHCCHHHH	55.88	-
237	Acetylation	ELGNDAYKKKDFDTA HHCCHHHHHCCHHHH	55.88	23749302
239	2-Hydroxyisobutyrylation	GNDAYKKKDFDTALK CCHHHHHCCHHHHHH	60.52	-
246	Acetylation	KDFDTALKHYDKAKE CCHHHHHHHHHHHHH	37.34	16916647
246	Ubiquitination	KDFDTALKHYDKAKE CCHHHHHHHHHHHHH	37.34	-
248	Ubiquitination	FDTALKHYDKAKELD HHHHHHHHHHHHHCC	19.97	-
252	2-Hydroxyisobutyrylation	LKHYDKAKELDPTNM HHHHHHHHHCCCCCC	65.63	-
252	Ubiquitination	LKHYDKAKELDPTNM HHHHHHHHHCCCCCC	65.63	-
259	Sulfoxidation	KELDPTNMTYITNQA HHCCCCCCCEEECCE	3.11	30846556
260	Acetylation	ELDPTNMTYITNQAA HCCCCCCCEEECCEE	17.53	-
260	Ubiquitination	ELDPTNMTYITNQAA HCCCCCCCEEECCEE	17.53	-
261	Phosphorylation	LDPTNMTYITNQAAV CCCCCCCEEECCEEE	8.59	-
269	Phosphorylation	ITNQAAVYFEKGDYN EECCEEEEECCCCHH	10.99	29496907
272	Ubiquitination	QAAVYFEKGDYNKCR CEEEEECCCCHHHHH	47.38	-
275	Phosphorylation	VYFEKGDYNKCRELC EEECCCCHHHHHHHH	25.78	-
277	2-Hydroxyisobutyrylation	FEKGDYNKCRELCEK ECCCCHHHHHHHHHH	28.56	-
277	Acetylation	FEKGDYNKCRELCEK ECCCCHHHHHHHHHH	28.56	19608861
284	2-Hydroxyisobutyrylation	KCRELCEKAIEVGRE HHHHHHHHHHHHCHH	54.38	-
284	Acetylation	KCRELCEKAIEVGRE HHHHHHHHHHHHCHH	54.38	23749302
284	Ubiquitination	KCRELCEKAIEVGRE HHHHHHHHHHHHCHH	54.38	-
288	Acetylation	LCEKAIEVGRENRED HHHHHHHHCHHCHHH	7.76	-
288	Acetylation	LCEKAIEVGRENRED HHHHHHHHCHHCHHH	7.76	19608861
293	Acetylation	IEVGRENREDYRQIA HHHCHHCHHHHHHHH	33.15	-
293	Ubiquitination	IEVGRENREDYRQIA HHHCHHCHHHHHHHH	33.15	-
293	Methylation	IEVGRENREDYRQIA HHHCHHCHHHHHHHH	33.15	115917933
296	Phosphorylation	GRENREDYRQIAKAY CHHCHHHHHHHHHHH	10.32	28152594
301	Ubiquitination	EDYRQIAKAYARIGN HHHHHHHHHHHHHCC	43.49	21890473
301	Acetylation	EDYRQIAKAYARIGN HHHHHHHHHHHHHCC	43.49	-
301	Ubiquitination	EDYRQIAKAYARIGN HHHHHHHHHHHHHCC	43.49	-
301	Acetylation	EDYRQIAKAYARIGN HHHHHHHHHHHHHCC	43.49	19608861
301	Succinylation	EDYRQIAKAYARIGN HHHHHHHHHHHHHCC	43.49	23954790
301	Ubiquitination	EDYRQIAKAYARIGN HHHHHHHHHHHHHCC	43.49	19608861
309	Phosphorylation	AYARIGNSYFKEEKY HHHHHCCCCCCCHHH	27.08	28442448
310	Phosphorylation	YARIGNSYFKEEKYK HHHHCCCCCCCHHHH	23.75	28442448
312	Acetylation	RIGNSYFKEEKYKDA HHCCCCCCCHHHHHH	57.65	19608861
312	Methylation	RIGNSYFKEEKYKDA HHCCCCCCCHHHHHH	57.65	19608861
313	Acetylation	IGNSYFKEEKYKDAI HCCCCCCCHHHHHHH	50.23	-
313	Ubiquitination	IGNSYFKEEKYKDAI HCCCCCCCHHHHHHH	50.23	-
316	Phosphorylation	SYFKEEKYKDAIHFY CCCCCHHHHHHHHHH	19.85	28152594
317	2-Hydroxyisobutyrylation	YFKEEKYKDAIHFYN CCCCHHHHHHHHHHC	52.32	-
317	Acetylation	YFKEEKYKDAIHFYN CCCCHHHHHHHHHHC	52.32	23236377
317	Malonylation	YFKEEKYKDAIHFYN CCCCHHHHHHHHHHC	52.32	26320211
317	Ubiquitination	YFKEEKYKDAIHFYN CCCCHHHHHHHHHHC	52.32	-
320	Acetylation	EEKYKDAIHFYNKSL CHHHHHHHHHHCHHH	3.11	-
320	Ubiquitination	EEKYKDAIHFYNKSL CHHHHHHHHHHCHHH	3.11	-
320	Acetylation	EEKYKDAIHFYNKSL CHHHHHHHHHHCHHH	3.11	19608861
320	Ubiquitination	EEKYKDAIHFYNKSL CHHHHHHHHHHCHHH	3.11	19608861
323	Phosphorylation	YKDAIHFYNKSLAEH HHHHHHHHCHHHHHH	13.91	28152594
325	2-Hydroxyisobutyrylation	DAIHFYNKSLAEHRT HHHHHHCHHHHHHCC	35.15	-
325	Acetylation	DAIHFYNKSLAEHRT HHHHHHCHHHHHHCC	35.15	19608861
325	Malonylation	DAIHFYNKSLAEHRT HHHHHHCHHHHHHCC	35.15	26320211
325	Methylation	DAIHFYNKSLAEHRT HHHHHHCHHHHHHCC	35.15	22633797
325	Ubiquitination	DAIHFYNKSLAEHRT HHHHHHCHHHHHHCC	35.15	21890473
332	Phosphorylation	KSLAEHRTPDVLKKC HHHHHHCCHHHHHHH	26.25	21815630
337	2-Hydroxyisobutyrylation	HRTPDVLKKCQQAEK HCCHHHHHHHHHHHH	51.88	-
337	Acetylation	HRTPDVLKKCQQAEK HCCHHHHHHHHHHHH	51.88	23749302
337	Ubiquitination	HRTPDVLKKCQQAEK HCCHHHHHHHHHHHH	51.88	-
340	Acetylation	PDVLKKCQQAEKILK HHHHHHHHHHHHHHH	55.16	-
340	Acetylation	PDVLKKCQQAEKILK HHHHHHHHHHHHHHH	55.16	19608861
344	Acetylation	KKCQQAEKILKEQER HHHHHHHHHHHHHHH	57.25	19608861
344	Ubiquitination	KKCQQAEKILKEQER HHHHHHHHHHHHHHH	57.25	19608861
347	2-Hydroxyisobutyrylation	QQAEKILKEQERLAY HHHHHHHHHHHHHHH	61.91	-
347	Ubiquitination	QQAEKILKEQERLAY HHHHHHHHHHHHHHH	61.91	-
348	Acetylation	QAEKILKEQERLAYI HHHHHHHHHHHHHHC	54.98	19608861
349	Acetylation	AEKILKEQERLAYIN HHHHHHHHHHHHHCC	39.25	-
354	Nitration	KEQERLAYINPDLAL HHHHHHHHCCHHHHH	13.06	-
354	Phosphorylation	KEQERLAYINPDLAL HHHHHHHHCCHHHHH	13.06	21945579
357	Acetylation	ERLAYINPDLALEEK HHHHHCCHHHHHHHH	28.56	-
357	Acetylation	ERLAYINPDLALEEK HHHHHCCHHHHHHHH	28.56	19608861
359	Acetylation	LAYINPDLALEEKNK HHHCCHHHHHHHHCC	6.55	19608861
364	Acetylation	PDLALEEKNKGNECF HHHHHHHHCCCCCHH	55.36	-
364	2-Hydroxyisobutyrylation	PDLALEEKNKGNECF HHHHHHHHCCCCCHH	55.36	-
364	Acetylation	PDLALEEKNKGNECF HHHHHHHHCCCCCHH	55.36	23954790
364	Malonylation	PDLALEEKNKGNECF HHHHHHHHCCCCCHH	55.36	26320211
364	Succinylation	PDLALEEKNKGNECF HHHHHHHHCCCCCHH	55.36	23954790
364	Ubiquitination	PDLALEEKNKGNECF HHHHHHHHCCCCCHH	55.36	19608861
366	Acetylation	LALEEKNKGNECFQK HHHHHHCCCCCHHHC	74.34	25953088
370	Glutathionylation	EKNKGNECFQKGDYP HHCCCCCHHHCCCHH	5.19	22555962
371	Acetylation	KNKGNECFQKGDYPQ HCCCCCHHHCCCHHH	7.39	-
372	Acetylation	NKGNECFQKGDYPQA CCCCCHHHCCCHHHH	61.55	19608861
372	Ubiquitination	NKGNECFQKGDYPQA CCCCCHHHCCCHHHH	61.55	19608861
372	Ubiquitination	NKGNECFQKGDYPQA CCCCCHHHCCCHHHH	61.55	21890473
373	Acetylation	KGNECFQKGDYPQAM CCCCHHHCCCHHHHH	33.23	23749302
373	Ubiquitination	KGNECFQKGDYPQAM CCCCHHHCCCHHHHH	33.23	-
376	Phosphorylation	ECFQKGDYPQAMKHY CHHHCCCHHHHHHHH	13.10	25839225
380	Sulfoxidation	KGDYPQAMKHYTEAI CCCHHHHHHHHHHHH	2.01	30846556
381	Acetylation	GDYPQAMKHYTEAIK CCHHHHHHHHHHHHH	36.15	21466224
383	Phosphorylation	YPQAMKHYTEAIKRN HHHHHHHHHHHHHHC	10.76	28152594
384	Phosphorylation	PQAMKHYTEAIKRNP HHHHHHHHHHHHHCH	20.75	28152594
388	2-Hydroxyisobutyrylation	KHYTEAIKRNPKDAK HHHHHHHHHCHHCHH	53.85	-
388	Acetylation	KHYTEAIKRNPKDAK HHHHHHHHHCHHCHH	53.85	23749302
388	Ubiquitination	KHYTEAIKRNPKDAK HHHHHHHHHCHHCHH	53.85	19608861
391	Ubiquitination	TEAIKRNPKDAKLYS HHHHHHCHHCHHHHC	39.68	-
391	Acetylation	TEAIKRNPKDAKLYS HHHHHHCHHCHHHHC	39.68	19608861
391	Ubiquitination	TEAIKRNPKDAKLYS HHHHHHCHHCHHHHC	39.68	19608861
395	2-Hydroxyisobutyrylation	KRNPKDAKLYSNRAA HHCHHCHHHHCCHHH	59.08	-
395	Acetylation	KRNPKDAKLYSNRAA HHCHHCHHHHCCHHH	59.08	23749302
397	Phosphorylation	NPKDAKLYSNRAACY CHHCHHHHCCHHHHH	11.82	29496907
405	Acetylation	SNRAACYTKLLEFQL CCHHHHHHHHHHHHH	18.33	-
405	Ubiquitination	SNRAACYTKLLEFQL CCHHHHHHHHHHHHH	18.33	-
410	Ubiquitination	CYTKLLEFQLALKDC HHHHHHHHHHHHCCH	7.91	-
411	Acetylation	YTKLLEFQLALKDCE HHHHHHHHHHHCCHH	19.22	19608861
418	Ubiquitination	QLALKDCEECIQLEP HHHHCCHHHHHHHCC	67.07	21890473
418	Ubiquitination	QLALKDCEECIQLEP HHHHCCHHHHHHHCC	67.07	-
420	Ubiquitination	ALKDCEECIQLEPTF HHCCHHHHHHHCCCC	0.82	-
422	Ubiquitination	KDCEECIQLEPTFIK CCHHHHHHHCCCCHH	51.97	21890473
422	Acetylation	KDCEECIQLEPTFIK CCHHHHHHHCCCCHH	51.97	-
422	Ubiquitination	KDCEECIQLEPTFIK CCHHHHHHHCCCCHH	51.97	-
422	Acetylation	KDCEECIQLEPTFIK CCHHHHHHHCCCCHH	51.97	19608861
422	Ubiquitination	KDCEECIQLEPTFIK CCHHHHHHHCCCCHH	51.97	19608861
428	Acetylation	IQLEPTFIKGYTRKA HHHCCCCHHCCHHHH	3.58	19608861
429	2-Hydroxyisobutyrylation	QLEPTFIKGYTRKAA HHCCCCHHCCHHHHH	41.49	-
429	Acetylation	QLEPTFIKGYTRKAA HHCCCCHHCCHHHHH	41.49	23954790
429	Ubiquitination	QLEPTFIKGYTRKAA HHCCCCHHCCHHHHH	41.49	-
434	2-Hydroxyisobutyrylation	FIKGYTRKAAALEAM CHHCCHHHHHHHHHH	34.28	-
434	Malonylation	FIKGYTRKAAALEAM CHHCCHHHHHHHHHH	34.28	26320211
434	Ubiquitination	FIKGYTRKAAALEAM CHHCCHHHHHHHHHH	34.28	-
435	Acetylation	IKGYTRKAAALEAMK HHCCHHHHHHHHHHH	8.48	19608861
438	Acetylation	YTRKAAALEAMKDYT CHHHHHHHHHHHHHH	3.55	-
438	Ubiquitination	YTRKAAALEAMKDYT CHHHHHHHHHHHHHH	3.55	21906983
441	Sulfoxidation	KAAALEAMKDYTKAM HHHHHHHHHHHHHHH	2.18	30846556
442	2-Hydroxyisobutyrylation	AAALEAMKDYTKAMD HHHHHHHHHHHHHHH	55.41	-
442	Acetylation	AAALEAMKDYTKAMD HHHHHHHHHHHHHHH	55.41	25953088
442	Malonylation	AAALEAMKDYTKAMD HHHHHHHHHHHHHHH	55.41	30639696
442	Ubiquitination	AAALEAMKDYTKAMD HHHHHHHHHHHHHHH	55.41	21906983
444	Phosphorylation	ALEAMKDYTKAMDVY HHHHHHHHHHHHHHH	12.48	29496907
446	Acetylation	EAMKDYTKAMDVYQK HHHHHHHHHHHHHHH	35.17	19608861
446	Ubiquitination	EAMKDYTKAMDVYQK HHHHHHHHHHHHHHH	35.17	21890473
453	2-Hydroxyisobutyrylation	KAMDVYQKALDLDSS HHHHHHHHHHCCCHH	32.98	-
453	Acetylation	KAMDVYQKALDLDSS HHHHHHHHHHCCCHH	32.98	25953088
453	Ubiquitination	KAMDVYQKALDLDSS HHHHHHHHHHCCCHH	32.98	-
461	Glutathionylation	ALDLDSSCKEAADGY HHCCCHHHHHHHHHH	5.52	22555962
462	Ubiquitination	LDLDSSCKEAADGYQ HCCCHHHHHHHHHHH	52.95	21906983
462	2-Hydroxyisobutyrylation	LDLDSSCKEAADGYQ HCCCHHHHHHHHHHH	52.95	-
462	Acetylation	LDLDSSCKEAADGYQ HCCCHHHHHHHHHHH	52.95	23749302
462	Malonylation	LDLDSSCKEAADGYQ HCCCHHHHHHHHHHH	52.95	26320211
462	Ubiquitination	LDLDSSCKEAADGYQ HCCCHHHHHHHHHHH	52.95	-
471	Glutathionylation	AADGYQRCMMAQYNR HHHHHHHHHHHHHCC	0.98	22555962
476	Phosphorylation	QRCMMAQYNRHDSPE HHHHHHHHCCCCCHH	12.48	22617229
481	Phosphorylation	AQYNRHDSPEDVKRR HHHCCCCCHHHHHHH	24.86	29255136
486	Acetylation	HDSPEDVKRRAMADP CCCHHHHHHHHHCCH	48.79	25953088
486	Ubiquitination	HDSPEDVKRRAMADP CCCHHHHHHHHHCCH	48.79	2190698
489	Acetylation	PEDVKRRAMADPEVQ HHHHHHHHHCCHHHH	11.10	-
489	Ubiquitination	PEDVKRRAMADPEVQ HHHHHHHHHCCHHHH	11.10	-
489	Ubiquitination	PEDVKRRAMADPEVQ HHHHHHHHHCCHHHH	11.10	21890473
490	Sulfoxidation	EDVKRRAMADPEVQQ HHHHHHHHCCHHHHH	4.05	21406390
493	Acetylation	KRRAMADPEVQQIMS HHHHHCCHHHHHHHC	33.83	19608861
493	Ubiquitination	KRRAMADPEVQQIMS HHHHHCCHHHHHHHC	33.83	19608861
493	Ubiquitination	KRRAMADPEVQQIMS HHHHHCCHHHHHHHC	33.83	21890473
499	Ubiquitination	DPEVQQIMSDPAMRL CHHHHHHHCCHHHHH	3.02	-
499	Sulfoxidation	DPEVQQIMSDPAMRL CHHHHHHHCCHHHHH	3.02	28183972
500	Phosphorylation	PEVQQIMSDPAMRLI HHHHHHHCCHHHHHH	41.91	20068231
506	Acetylation	MSDPAMRLILEQMQK HCCHHHHHHHHHHHH	3.17	-
509	Ubiquitination	PAMRLILEQMQKDPQ HHHHHHHHHHHHCHH	36.69	-
509	Ubiquitination	PAMRLILEQMQKDPQ HHHHHHHHHHHHCHH	36.69	21906983
511	Sulfoxidation	MRLILEQMQKDPQAL HHHHHHHHHHCHHHH	3.79	21406390
513	Acetylation	LILEQMQKDPQALSE HHHHHHHHCHHHHHH	67.06	23954790
513	Malonylation	LILEQMQKDPQALSE HHHHHHHHCHHHHHH	67.06	30639696
513	Ubiquitination	LILEQMQKDPQALSE HHHHHHHHCHHHHHH	67.06	-
523	2-Hydroxyisobutyrylation	QALSEHLKNPVIAQK HHHHHHHCCHHHHHH	62.20	-
523	Acetylation	QALSEHLKNPVIAQK HHHHHHHCCHHHHHH	62.20	25953088
523	Malonylation	QALSEHLKNPVIAQK HHHHHHHCCHHHHHH	62.20	30639696
523	Ubiquitination	QALSEHLKNPVIAQK HHHHHHHCCHHHHHH	62.20	-
530	Acetylation	KNPVIAQKIQKLMDV CCHHHHHHHHHHHHC	37.77	25953088
530	Ubiquitination	KNPVIAQKIQKLMDV CCHHHHHHHHHHHHC	37.77	-
533	Ubiquitination	VIAQKIQKLMDVGLI HHHHHHHHHHHCCCE	49.61	21906983
533	Ubiquitination	VIAQKIQKLMDVGLI HHHHHHHHHHHCCCE	49.61	-
535	Sulfoxidation	AQKIQKLMDVGLIAI HHHHHHHHHCCCEEE	5.17	21406390
543	Methylation	DVGLIAIR------- HCCCEEEC-------	31.31	115917941
560	Ubiquitination	------------------------ ------------------------		-

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 STIP1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of STIP1_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 STIP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HSP7E_HUMAN	HSPA14	physical	10786835
HS90A_HUMAN	HSP90AA1	physical	10786835
HSP74_HUMAN	HSPA4	physical	9452498
HS90A_HUMAN	HSP90AA1	physical	9452498
APRIO_HUMAN	PRNP	physical	12093732
PRIO_HUMAN	PRNP	physical	12093732
A4_HUMAN	APP	physical	21832049
STMN1_HUMAN	STMN1	physical	22939629
KCNQ4_HUMAN	KCNQ4	physical	23431407
PWP2_YEAST	PWP2	genetic	21850170
HSP7C_HUMAN	HSPA8	physical	9774640
HSP74_HUMAN	HSPA4	physical	21235734
HS90A_HUMAN	HSP90AA1	physical	21235734
CC117_HUMAN	CCDC117	physical	25036637
BAG2_HUMAN	BAG2	physical	25036637
HS90B_HUMAN	HSP90AB1	physical	25036637
HS90A_HUMAN	HSP90AA1	physical	25036637
DNJB6_HUMAN	DNAJB6	physical	25036637
MLF2_HUMAN	MLF2	physical	25036637
HS90A_HUMAN	HSP90AA1	physical	10642522
HSP74_HUMAN	HSPA4	physical	10642522
ALDR_HUMAN	AKR1B1	physical	26344197
AK1BF_HUMAN	AKR1B15	physical	26344197
DNJA2_HUMAN	DNAJA2	physical	26344197
DUT_HUMAN	DUT	physical	26344197
ENOG_HUMAN	ENO2	physical	26344197
ENOB_HUMAN	ENO3	physical	26344197
FABP5_HUMAN	FABP5	physical	26344197
HSP74_HUMAN	HSPA4	physical	26344197
CH10_HUMAN	HSPE1	physical	26344197
MAOX_HUMAN	ME1	physical	26344197
MSI2H_HUMAN	MSI2	physical	26344197
PCBP1_HUMAN	PCBP1	physical	26344197
PCBP2_HUMAN	PCBP2	physical	26344197
PGK1_HUMAN	PGK1	physical	26344197
PGP_HUMAN	PGP	physical	26344197
PLST_HUMAN	PLS3	physical	26344197
PPID_HUMAN	PPID	physical	26344197
KS6A3_HUMAN	RPS6KA3	physical	26344197
SUMO3_HUMAN	SUMO3	physical	26344197
SUMO4_HUMAN	SUMO4	physical	26344197
TPIS_HUMAN	TPI1	physical	26344197
HS90A_HUMAN	HSP90AA1	physical	18285346
HS90B_HUMAN	HSP90AB1	physical	18285346
HS90A_HUMAN	HSP90AA1	physical	22504172
HS90A_HUMAN	HSP90AA1	physical	28514442
HS90B_HUMAN	HSP90AB1	physical	28514442
ADHX_HUMAN	ADH5	physical	26637637

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 STIP1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-8; LYS-68; LYS-73;LYS-100; LYS-301; LYS-312; LYS-325; LYS-344; LYS-388 AND LYS-446, ANDMASS SPECTROMETRY.	19608861 [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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-246, AND MASS SPECTROMETRY.	16916647 [Abstract]
Phosphorylation
Reference	PubMed
"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-16 AND SER-481, AND MASSSPECTROMETRY.	18669648 [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-481, AND MASSSPECTROMETRY.	17081983 [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 THR-198, AND MASSSPECTROMETRY.	17287340 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-354, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-354, AND MASSSPECTROMETRY.	15592455 [Abstract]