Search Results
Overview
| Uniprot ID | H0UXJ8 |
|---|---|
| Protein Name | - |
| Gene Name | HSP90AA1 |
| Organism | Cavia porcellus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 284 | KKKKIKEKYIDQEEL |
| 408 | REMLQQSKILKVIRK |
| 568 | KQEEKKTKFENLCKI |
| 586 | ILEKKVEKVVVSNRL |
| 616 | ANMERIMKAQALRDN |
Function
No function data available.
Protein Sequence
10
MPEETQTQDQ
20
PMEEEEVETF
30
AFQAEIAQLM
40
SLIINTFYSN
50
KEIFLRELIS
60
NSSDALDKIR
70
YESLTDPSKL
80
DSGKELHINL
90
IPNKQDRTLT
100
IVDTGIGMTK
110
ADLINNLGTI
120
AKSGTKAFME
130
ALQAGADISM
140
IGQFGVGFYS
150
AYLVAEKVTV
160
ITKHNDDEQY
170
AWESSAGGSF
180
TVRTDTGEPM
190
GRGTKVILHL
200
KEDQTEYLEE
210
RRIKEIVKKH
220
SQFIGYPITL
230
FVEKERDKEV
240
SDDEAEEKED
250
KEEDKEKEEK
260
ESDDKPEIED
270
VGSDEEEEEK
280
KDGDKKKKKK
290
IKEKYIDQEE
300
LNKTKPIWTR
310
NPDDITNEEY
320
GEFYKSLTND
330
WEDHLAVKHF
340
SVEGQLEFRA
350
LLFVPRRAPF
360
DLFENRKKKN
370
NIKLYVRRVF
380
IMDNCEELIP
390
EYLNFIRGVV
400
DSEDLPLNIS
410
REMLQQSKIL
420
KVIRKNLVKK
430
CLELFTELAE
440
DKENYKKFYE
450
QFSKNIKLGI
460
HEDSQNRKKL
470
SELLRYYTSA
480
SGDEMVSLKD
490
YCTRMKENQK
500
HIYYITGETK
510
DQVANSAFVE
520
RLRKHGLEVI
530
YMIEPIDEYC
540
VQQLKEFEGK
550
TLVSVTKEGL
560
ELPEDEEEKK
570
KQEEKKTKFE
580
NLCKIMKDIL
590
EKKVEKVVVS
600
NRLVTSPCCI
610
VTSTYGWTAN
620
MERIMKAQAL
630
RDNSTMGYMA
640
AKKHLEINPD
650
HSIIETLRQK
660
AEADKNDKSV
670
KDLVILLYET
680
ALLSSGFSLE
690
DPQTHANRIY
700
RMIKLGLGID
710
EDDPTADDTT
720
AAVNEEMPPL
730
EGDDDTSRME
EVD
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0042470 | melanosome |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0101031 | protein folding chaperone complex |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0016887 | ATP hydrolysis activity |
| Molecular Function | GO:0140662 | ATP-dependent protein folding chaperone |
| Molecular Function | GO:0097718 | disordered domain specific binding |
| Molecular Function | GO:0070182 | DNA polymerase binding |
| Molecular Function | GO:0051020 | GTPase binding |
| Molecular Function | GO:0042826 | histone deacetylase binding |
| Molecular Function | GO:0030235 | nitric-oxide synthase regulator activity |
| Molecular Function | GO:0042803 | protein homodimerization activity |
| Molecular Function | GO:1990782 | protein tyrosine kinase binding |
| Molecular Function | GO:0097110 | scaffold protein binding |
| Molecular Function | GO:0048156 | tau protein binding |
| Molecular Function | GO:0030911 | TPR domain binding |
| Molecular Function | GO:0031625 | ubiquitin protein ligase binding |
| Molecular Function | GO:0051082 | unfolded protein binding |
| Biological Process | GO:0002218 | activation of innate immune response |
| Biological Process | GO:0098586 | cellular response to virus |
| Biological Process | GO:0051131 | chaperone-mediated protein complex assembly |
| Biological Process | GO:1902988 | neurofibrillary tangle assembly |
| Biological Process | GO:0002230 | positive regulation of defense response to virus by host |
| Biological Process | GO:0032728 | positive regulation of interferon-beta production |
| Biological Process | GO:0045732 | positive regulation of protein catabolic process |
| Biological Process | GO:0032273 | positive regulation of protein polymerization |
| Biological Process | GO:0030150 | protein import into mitochondrial matrix |
| Biological Process | GO:0050821 | protein stabilization |
| Biological Process | GO:0042981 | regulation of apoptotic process |
| Biological Process | GO:0032880 | regulation of protein localization |
| Biological Process | GO:0031396 | regulation of protein ubiquitination |
| Biological Process | GO:0046677 | response to antibiotic |
| Biological Process | GO:0009409 | response to cold |
| Biological Process | GO:0009408 | response to heat |
| Biological Process | GO:1905323 | telomerase holoenzyme complex assembly |
Reference
[1] Feng J, Chen X, Li R, Xie Y, Zhang X et al.. Lactylome analysis reveals potential target modified proteins in the retina of form-deprivation myopia.. iScience 27(9):110606. 2024 Sep 20. PMID: 39246443.