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Protein Page:
STI1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
STI1 a protein that is apparently involved in the response to stress. Specifically interacts with the C-terminal tails of Hsp70 and Hsp90 via TPR1 and TPR2A domains. Deletion of STI1 reduces the activity of the glucocorticoid receptor, a Hsp90 target protein. Phosphorylated in vitro by p90RSK and casein kinase II. Note: This description may include information from UniProtKB.
Protein type: Chaperone
Cellular Component: Golgi apparatus; protein complex; nucleus
Molecular Function: protein C-terminus binding; protein binding; chaperone binding; Hsp70 protein binding
Biological Process: axon guidance; response to stress
Reference #:  P31948 (UniProtKB)
Alt. Names/Synonyms: Hop; Hsc70/Hsp90-organizing protein; Hsp70/Hsp90-organizing protein; IEF-SSP-3521; NY-REN-11 antigen; P60; Renal carcinoma antigen NY-REN-11; STI1; STI1L; STIP1; Stress-induced-phosphoprotein 1; stress-induced-phosphoprotein 1 (Hsp70/Hsp90-organizing protein); Transformation-sensitive protein IEF SSP 3521
Gene Symbols: STIP1
Molecular weight: 62,639 Da
Basal Isoelectric point: 6.4  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

STI1
Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


  MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


        human

 
0 1 K8-a MEQVNELkEkGNkAL
0 5 K10-a QVNELkEkGNkALsV
0 3 K13-u ELkEkGNkALsVGNI
0 3 S16-p EkGNkALsVGNIDDA
0 6 K32-u QCYSEAIkLDPHNHV
0 17 Y41-p DPHNHVLySNRSAAy
0 2 Y48-p ySNRSAAyAKKGDyQ
0 2 Y54-p AyAKKGDyQKAyEDG
0 3 Y58-p KGDyQKAyEDGCKTV
0 3 K68-a GCKTVDLkPDWGkGY
0 17 K68-u GCKTVDLkPDWGkGY
0 1 K73-a DLkPDWGkGYSRkAA
0 1 K78-u WGkGYSRkAAALEFL
0 1 K100-a RTYEEGLkHEANNPQ
0 3 K100-u RTYEEGLkHEANNPQ
0 8 K109-u EANNPQLkEGLQNME
0 6 K123-u EARLAERkFMNPFNM
0 6 K136 NMPNLYQKLESDPRT
0 1 T145-p ESDPRTRtLLSDPTY
0 13 K162 LIEQLRNKPSDLGTk
0 3 K169-u KPSDLGTkLQDPRIM
2 0 S189 LLGVDLGSMDEEEEI
2 3 T198-p DEEEEIAtPPPPPPP
0 1 K207-a PPPPPPKkETKPEPM
0 1 K237 ELGNDAYKKKDFDTA
0 2 K246-a KDFDTALkHYDKAKE
0 1 K252 LkHYDKAKELdPTNM
0 1 D255-ca YDKAKELdPTNMTYI
0 3 Y269-p ITNQAAVyFEKGDyN
0 1 Y275-p VyFEKGDyNKCRELC
0 1 K301-a EDYRQIAkAYARIGN
0 5 K312-a RIGNSYFkEEKYKDA
0 1 K317 YFkEEKYKDAIHFYN
0 4 K325-a DAIHFYNkSLAEHRT
0 1 K325-u DAIHFYNkSLAEHRT
1 0 T332 kSLAEHRTPDVLkKC
0 6 K337-a HRTPDVLkKCQQAEk
0 1 K344-a kKCQQAEkILKEQER
0 380 Y354-p KEQERLAyINPDLAL
0 1 K373 KGNECFQKGDYPQAM
0 1 K381-a GDYPQAMkHytEAIk
0 1 Y383-p YPQAMkHytEAIkRN
0 1 T384-p PQAMkHytEAIkRNP
0 1 K388-a kHytEAIkRNPKDAK
0 2 K429-a QLEPTFIkGYTRKAA
0 1 K442-u AAALEAMkDyTkAMD
0 3 Y444-p ALEAMkDyTkAMDVY
0 1 K446-a EAMkDyTkAMDVYQK
0 1 K446-u EAMkDyTkAMDVYQK
0 1 K462-a LDLDSSCkEAADGYQ
0 5 K462-u LDLDSSCkEAADGYQ
0 10 Y476-p QRCMMAQyNRHDsPE
0 16 S481-p AQyNRHDsPEDVkRR
0 2 K486-u HDsPEDVkRRAMADP
0 1 K513 LILEQMQKDPQALSE
  mouse

 
K8 MEQVNELKEkGNkAL
K10-a QVNELKEkGNkALsA
K13-u ELKEkGNkALsAGNI
S16-p EkGNkALsAGNIDDA
K32-u QCYSEAIkLDPQNHV
Y41 DPQNHVLYSNRSAAY
Y48 YSNRSAAYAKKGDYQ
Y54 AYAKKGDYQKAYEDG
Y58 KGDYQKAYEDGCKTV
K68 GCKTVDLKPDWGKGY
K68-u GCKTVDLkPDWGKGY
K73 DLkPDWGKGYSRKAA
K78 WGKGYSRKAAALEFL
K100 RTYEEGLKHEANNLQ
K100-u RTYEEGLkHEANNLQ
K109-u EANNLQLkEGLQNME
K123-u EARLAERkFMNPFNL
K136-u NLPNLYQkLENDPRT
S145 ENDPRTRSLLSDPTY
K162-u LIEQLQNkPSDLGTk
K169-u kPSDLGTkLQDPRVM
S189-p LLGVDLGsMDEEEEA
T198-p DEEEEAAtPPPPPPP
K207 PPPPPPKKEPKPEPM
K237-a ELGNDAYkKKDFDKA
K246 KDFDKALKHYDRAkE
K252-u LKHYDRAkELDPTNM
D255 YDRAkELDPTNMTYI
H269 ITNQAAVHFEKGDYN
Y275 VHFEKGDYNKCRELC
K301 EDYRQIAKAYARIGN
K312-a RIGNSYFkEEKYkDA
K317-u YFkEEKYkDAIHFYN
K325 DAIHFYNKSLAEHRt
K325 DAIHFYNKSLAEHRt
T332-p KSLAEHRtPDVLkKC
K337-a HRtPDVLkKCQQAEK
K344 kKCQQAEKILKEQER
Y354 KEQERLAYINPDLAL
K373-u KGNECFQkGDYPQAM
K381 GDYPQAMKHYTEAIK
Y383 YPQAMKHYTEAIKRN
T384 PQAMKHYTEAIKRNP
K388 KHYTEAIKRNPRDAK
K429 QLEPTFIKGYTRKAA
K442 AAALEAMKDyTKAMD
Y444-p ALEAMKDyTKAMDVY
K446 EAMKDyTKAMDVYQK
K446 EAMKDyTKAMDVYQK
K462 LDLDSSCKEAADGYQ
K462-u LDLDSSCkEAADGYQ
Y476 QRCMMAQYNRHDsPE
S481-p AQYNRHDsPEDVKRR
K486 HDsPEDVKRRAMADP
K513-u LILEQMQkDPQALSE
  rat

 
K8 MEQVNELKEKGNKAL
K10 QVNELKEKGNKALSA
K13 ELKEKGNKALSAGNI
S16 EKGNKALSAGNIDDA
K32 QCYSEAIKLDPQNHV
Y41 DPQNHVLYSNRSAAY
Y48 YSNRSAAYAKKGDYQ
Y54 AYAKKGDYQKAYEDG
Y58 KGDYQKAYEDGCKTV
K68 GCKTVDLKPDWGKGY
K68 GCKTVDLKPDWGKGY
K73 DLKPDWGKGYSRKAA
K78 WGKGYSRKAAALEFL
K100 RTYEEGLKHEANNLQ
K100 RTYEEGLKHEANNLQ
K109 EANNLQLKEGLQNME
K123 EARLAERKFMNPFNL
K136 NLPNLYQKLENDPRT
T145 ENDPRTRTLLSDPTY
K162 LIEQLQNKPSDLGTK
K169 KPSDLGTKLQDPRVM
S189 LLGVDLGSMDEEEEA
T198 DEEEEAATPPPPPPP
K207 PPPPPPKKEAKPEPM
K237 ELGNDAYKKKDFDKA
K246 KDFDKALKHYDKAKE
K252 LKHYDKAKELDPTNM
D255 YDKAKELDPTNMTYI
H269 ITNQAAVHFEKGDYN
Y275 VHFEKGDYNKCRELC
K301 EDYRQIAKAYARIGN
K312 RIGNSYFKEERYKDA
K317 YFKEERYKDAIHFYN
K325 DAIHFYNKSLAEHRT
K325 DAIHFYNKSLAEHRT
T332 KSLAEHRTPDVLKKC
K337 HRTPDVLKKCQQAEK
K344 KKCQQAEKILKEQER
Y354-p KEQERLAyINPDLAL
K373 KGNECFQKGDYPQAM
K381 GDYPQAMKHYTEAIK
Y383 YPQAMKHYTEAIKRN
T384 PQAMKHYTEAIKRNP
K388 KHYTEAIKRNPRDAK
K429 QLEPTFIKGYTRKAA
K442 AAALEAMKDYTKAMD
Y444 ALEAMKDYTKAMDVY
K446 EAMKDYTKAMDVYQK
K446 EAMKDYTKAMDVYQK
K462 LDLDSSCKEAADGYQ
K462 LDLDSSCKEAADGYQ
Y476 QRCMMAQYNRHDSPE
S481 AQYNRHDSPEDVKRR
K486 HDSPEDVKRRAMADP
K513 LILEQMQKDPQALSE
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