STIP1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: STIP1_MOUSE
• UniProt AC: Q60864
• Protein Name: Stress-induced-phosphoprotein 1
• Gene Name: Stip1
• Organism: Mus musculus (Mouse).
• Sequence Length: 543
• Subcellular Localization: Cytoplasm . Nucleus .
• Protein Description: Acts as a co-chaperone for HSP90AA1. Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90..
• Protein Sequence: MEQVNELKEKGNKALSAGNIDDALQCYSEAIKLDPQNHVLYSNRSAAYAKKGDYQKAYEDGCKTVDLKPDWGKGYSRKAAALEFLNRFEEAKRTYEEGLKHEANNLQLKEGLQNMEARLAERKFMNPFNLPNLYQKLENDPRTRSLLSDPTYRELIEQLQNKPSDLGTKLQDPRVMTTLSVLLGVDLGSMDEEEEAATPPPPPPPKKEPKPEPMEEDLPENKKQALKEKELGNDAYKKKDFDKALKHYDRAKELDPTNMTYITNQAAVHFEKGDYNKCRELCEKAIEVGRENREDYRQIAKAYARIGNSYFKEEKYKDAIHFYNKSLAEHRTPDVLKKCQQAEKILKEQERLAYINPDLALEEKNKGNECFQKGDYPQAMKHYTEAIKRNPRDAKLYSNRAACYTKLLEFQLALKDCEECIQLEPTFIKGYTRKAAALEAMKDYTKAMDVYQKALDLDSSCKEAADGYQRCMMAQYNRHDSPEDVKRRAMADPEVQQIMSDPAMRLILEQMQKDPQALSEHLKNPVIAQKIQKLMDVGLIAIR

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
1	Acetylation	-------MEQVNELK -------CHHHHHHH	7.99	-
8	Acetylation	MEQVNELKEKGNKAL CHHHHHHHHHHHHHH	51.72	-
10	Acetylation	QVNELKEKGNKALSA HHHHHHHHHHHHHHC	67.22	23576753
13	Ubiquitination	ELKEKGNKALSAGNI HHHHHHHHHHHCCCH	60.41	-
16	Phosphorylation	EKGNKALSAGNIDDA HHHHHHHHCCCHHHH	38.70	26745281
26	S-nitrosylation	NIDDALQCYSEAIKL CHHHHHHHHHHHHCC	4.14	22178444
26	Glutathionylation	NIDDALQCYSEAIKL CHHHHHHHHHHHHCC	4.14	24333276
26	S-palmitoylation	NIDDALQCYSEAIKL CHHHHHHHHHHHHCC	4.14	28526873
26	S-nitrosocysteine	NIDDALQCYSEAIKL CHHHHHHHHHHHHCC	4.14	-
32	Ubiquitination	QCYSEAIKLDPQNHV HHHHHHHCCCCCCCE	54.61	-
62	Glutathionylation	QKAYEDGCKTVDLKP HHHHCCCCCCCCCCC	5.30	24333276
68	Acetylation	GCKTVDLKPDWGKGY CCCCCCCCCCCCCCH	36.15	22826441
68	Ubiquitination	GCKTVDLKPDWGKGY CCCCCCCCCCCCCCH	36.15	27667366
73	Malonylation	DLKPDWGKGYSRKAA CCCCCCCCCHHHHHH	50.88	26320211
73	Acetylation	DLKPDWGKGYSRKAA CCCCCCCCCHHHHHH	50.88	23236377
78	Acetylation	WGKGYSRKAAALEFL CCCCHHHHHHHHHHH	36.11	23806337
78	Succinylation	WGKGYSRKAAALEFL CCCCHHHHHHHHHHH	36.11	23806337
100	Ubiquitination	RTYEEGLKHEANNLQ HHHHHHHHHHHHHHH	50.70	27667366
109	Ubiquitination	EANNLQLKEGLQNME HHHHHHHHHHHHHHH	36.45	-
123	Ubiquitination	EARLAERKFMNPFNL HHHHHHHHHCCCCCC	40.23	27667366
136	Ubiquitination	NLPNLYQKLENDPRT CCHHHHHHHHCCHHH	44.18	-
143	Phosphorylation	KLENDPRTRSLLSDP HHHCCHHHHHHHCCH	29.96	25777480
145	Phosphorylation	ENDPRTRSLLSDPTY HCCHHHHHHHCCHHH	32.80	28066266
148	Phosphorylation	PRTRSLLSDPTYREL HHHHHHHCCHHHHHH	47.00	25777480
162	Ubiquitination	LIEQLQNKPSDLGTK HHHHHHCCCHHHCCC	32.70	27667366
162	Acetylation	LIEQLQNKPSDLGTK HHHHHHCCCHHHCCC	32.70	23236377
164	Phosphorylation	EQLQNKPSDLGTKLQ HHHHCCCHHHCCCCC	47.26	28066266
168	Phosphorylation	NKPSDLGTKLQDPRV CCCHHHCCCCCCHHH	35.56	28066266
169	Ubiquitination	KPSDLGTKLQDPRVM CCHHHCCCCCCHHHH	42.21	27667366
180	Phosphorylation	PRVMTTLSVLLGVDL HHHHHHHHHHHCCCC	14.50	26643407
189	Phosphorylation	LLGVDLGSMDEEEEA HHCCCCCCCCHHHHH	30.29	14754904
198	Phosphorylation	DEEEEAATPPPPPPP CHHHHHCCCCCCCCC	43.29	14754904
237	Acetylation	ELGNDAYKKKDFDKA HHCCHHHHHHHHHHH	55.88	15618337
237	Succinylation	ELGNDAYKKKDFDKA HHCCHHHHHHHHHHH	55.88	23954790
243	Malonylation	YKKKDFDKALKHYDR HHHHHHHHHHHHHHH	56.46	26320211
252	Ubiquitination	LKHYDRAKELDPTNM HHHHHHHHHCCCCCC	60.75	-
284	Acetylation	KCRELCEKAIEVGRE HHHHHHHHHHHHCHH	54.38	22826441
301	Malonylation	EDYRQIAKAYARIGN HHHHHHHHHHHHHCC	43.49	26320211
301	Acetylation	EDYRQIAKAYARIGN HHHHHHHHHHHHHCC	43.49	-
312	Malonylation	RIGNSYFKEEKYKDA HHCCCCCCCHHHHHH	57.65	26320211
312	Acetylation	RIGNSYFKEEKYKDA HHCCCCCCCHHHHHH	57.65	21728379
317	Malonylation	YFKEEKYKDAIHFYN CCCCHHHHHHHHHHC	52.32	26320211
317	Ubiquitination	YFKEEKYKDAIHFYN CCCCHHHHHHHHHHC	52.32	-
317	Acetylation	YFKEEKYKDAIHFYN CCCCHHHHHHHHHHC	52.32	22826441
325	Malonylation	DAIHFYNKSLAEHRT HHHHHHCHHHHHHCC	35.15	26320211
325	Acetylation	DAIHFYNKSLAEHRT HHHHHHCHHHHHHCC	35.15	23806337
332	Phosphorylation	KSLAEHRTPDVLKKC HHHHHHCCHHHHHHH	26.25	14754904
337	Acetylation	HRTPDVLKKCQQAEK HCCHHHHHHHHHHHH	51.88	7987709
337	Ubiquitination	HRTPDVLKKCQQAEK HCCHHHHHHHHHHHH	51.88	27667366
344	Acetylation	KKCQQAEKILKEQER HHHHHHHHHHHHHHH	57.25	-
347	Ubiquitination	QQAEKILKEQERLAY HHHHHHHHHHHHHHH	61.91	27667366
354	Phosphorylation	KEQERLAYINPDLAL HHHHHHHHCCHHHHH	13.06	29514104
364	Malonylation	PDLALEEKNKGNECF HHHHHHHHCCCCCHH	55.36	26320211
364	Acetylation	PDLALEEKNKGNECF HHHHHHHHCCCCCHH	55.36	23236377
366	Acetylation	LALEEKNKGNECFQK HHHHHHCCCCCHHHC	74.34	23806337
370	S-nitrosylation	EKNKGNECFQKGDYP HHCCCCCHHHCCCHH	5.19	21278135
370	Glutathionylation	EKNKGNECFQKGDYP HHCCCCCHHHCCCHH	5.19	24333276
370	S-nitrosocysteine	EKNKGNECFQKGDYP HHCCCCCHHHCCCHH	5.19	-
373	Acetylation	KGNECFQKGDYPQAM CCCCHHHCCCHHHHH	33.23	22826441
373	Ubiquitination	KGNECFQKGDYPQAM CCCCHHHCCCHHHHH	33.23	-
381	Acetylation	GDYPQAMKHYTEAIK CCHHHHHHHHHHHHH	36.15	22826441
395	Malonylation	KRNPRDAKLYSNRAA HHCCCCHHHHCCHHH	52.85	26320211
403	Glutathionylation	LYSNRAACYTKLLEF HHCCHHHHHHHHHHH	4.29	24333276
429	Acetylation	QLEPTFIKGYTRKAA HHCCCCHHCCHHHHH	41.49	23236377
434	Ubiquitination	FIKGYTRKAAALEAM CHHCCHHHHHHHHHH	34.28	27667366
444	Phosphorylation	ALEAMKDYTKAMDVY HHHHHHHHHHHHHHH	12.48	-
446	Succinylation	EAMKDYTKAMDVYQK HHHHHHHHHHHHHHH	35.17	23806337
446	Acetylation	EAMKDYTKAMDVYQK HHHHHHHHHHHHHHH	35.17	23806337
453	Acetylation	KAMDVYQKALDLDSS HHHHHHHHHHCCCHH	32.98	22826441
461	Glutathionylation	ALDLDSSCKEAADGY HHCCCHHHHHHHHHH	5.52	24333276
461	S-nitrosylation	ALDLDSSCKEAADGY HHCCCHHHHHHHHHH	5.52	22178444
461	S-nitrosocysteine	ALDLDSSCKEAADGY HHCCCHHHHHHHHHH	5.52	-
462	Ubiquitination	LDLDSSCKEAADGYQ HCCCHHHHHHHHHHH	52.95	-
471	Glutathionylation	AADGYQRCMMAQYNR HHHHHHHHHHHHHCC	0.98	24333276
471	S-nitrosylation	AADGYQRCMMAQYNR HHHHHHHHHHHHHCC	0.98	24926564
471	S-nitrosocysteine	AADGYQRCMMAQYNR HHHHHHHHHHHHHCC	0.98	-
476	Phosphorylation	QRCMMAQYNRHDSPE HHHHHHHHCCCCCHH	12.48	23984901
481	Phosphorylation	AQYNRHDSPEDVKRR HHHCCCCCHHHHHHH	24.86	25521595
513	Acetylation	LILEQMQKDPQALSE HHHHHHHHCHHHHHH	67.06	23236377
513	Ubiquitination	LILEQMQKDPQALSE HHHHHHHHCHHHHHH	67.06	-
530	Acetylation	KNPVIAQKIQKLMDV CCHHHHHHHHHHHHC	37.77	23806337
533	Acetylation	VIAQKIQKLMDVGLI HHHHHHHHHHHCCCE	49.61	22826441

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
189	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
189	S	Phosphorylation	Kinase	CSK21	Q60737	PhosphoELM
198	T	Phosphorylation	Kinase	CDK1	P06493	PSP
198	T	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
198	T	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
332	T	Phosphorylation	Kinase	CDK1	P06493	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of STIP1_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of STIP1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AF9_MOUSE	Mllt3	physical	20159978

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND MASSSPECTROMETRY.
PubMed: 19367708