wanglab/gogpt-training-data huggingface dataset:
Protein: BAG family molecular chaperone regulator 4 (BAG-4) (Bcl-2-associated athanogene 4) (Silencer of death domains) (Q8CI61)
Organism: Mus musculus (Mouse)
Function: Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Prevents constitutive TNFRSF1A signaling (By similarity). Negative regulator of PRKN translocation to damaged mitochondria (By similarity).
Subcellular location: Cytoplasm.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 1A
- Heat shock 70 kDa protein 1B
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- BAG family molecular chaperone regulator 2
- Heat shock 70 kDa protein 1-like
- BAG family molecular chaperone regulator 1
- Heat shock 70 kDa protein 4
- Heat shock 70 kDa protein 1A
- Tumor necrosis factor
- Heat shock cognate 71 kDa protein
Sequence:
MSALRRSGYGPSDGPSYGRYYGPGGGDVPVHVPPPLYPPLRPEPPQPPVSWRGRGGAPAETTWPGEGAGGDGYYPSGGAWAEASRAGGGHQEQPPYPGYNSNYWNSVRPRAPYPGSYSVRPELQGQSLNSYANGAYGPPYPPGPGASTASYSGAYYVPGYTQSNYSTEVPNTYRSPGNSPTPMSRWMYSQQDCPTEAPPLRGQVPGYPASQNPGMTLPHYPYGDGNRAVPQSGGTGRPQDDAWASSAYGMGARYPWPSAAPSAPSAGSLYMTESASPWPGNSSPQPPPSPPPQQPKDPSYSYNPSGQGLSRHSFPCSVHQYESPGAVNNDNSDLLDSQVQYSAEPQLYGNASSEHPSNQVPSNNLPEECFSSDEGTPPSIKKIIHVLEKVQFLEQEVEEFVGKKTDKAYWLLEEMLTKELLELDSVETGGQDSVRQARKEAVCKIQAILEKLEKKGL
Protein: Epididymal-specific lipocalin-5 (Androgen-dependent epididymal 18.5 kDa protein) (Epididymal retinoic acid-binding protein) (E-RABP) (Epididymal secretory protein I) (ESP-I) [Cleaved into: Epididymal-specific lipocalin-5, B form; Epididymal-specific lipocalin-5, C form] (P06911)
Organism: Rattus norvegicus (Rat)
Function: Associates with spermatozoa in the epididymal fluid but does not bind tightly to them. Binds both all-trans and 9-cis retinoic acid. May act as a retinoid carrier protein which is required for epididymal function and/or sperm maturation.
Subcellular location: Secreted. Note=Synthesized in the proximal part of the epididymis and secreted into the epididymal fluid.
Interaction partners:
Sequence:
MENIMPFALLGLCVGLAAGTEGAVVKDFDISKFLGFWYEIAFASKMGTPGLAHKEEKMGAMVVELKENLLALTTTYYSEDHCVLEKVTATEGDGPAKFQVTRLSGKKEVVVEATDYLTYAIIDITSLVAGAVHRTMKLYSRSLDDNGEALYNFRKITSDHGFSETDLYILKHDLTCVKVLQSAAESRP
Protein: UBP-type domain-containing protein (Q581T5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Polyubiquitin, putative
Sequence:
MLRCRVADVVSSDQMCEMTNFPPVQATVGYVQLLRRLSFKREFFVPFVPTKHVIFTFQTRNPLEEGKVKDEVTDLVSHYFNWIRERGVYSFQILQLYVCILSGCTVVVIECPDTLTTLDVHSFSQEPEAPTVGKRRVLVFPCDNDEISDSELESNYYIVPTCTLCAERLEPTLTGYSSPTCSCVDGRECRCLLEQSSCVVCQTSITMQHESQKVQCEQCSRTGDPWICLVCGYVGCSRYQAKHAREHYLQHKHLFSMSLLTQQIWDYDSDAFVHRVVVLLDNATGAVNRVQYPDRDNIPSSLADEYVDAAAEKVSKKHINAKFDSKVETSNEQLALMIISELNTRRVEYETEMHGGSHHLNDELMGDPSLCSVIVAERACAASRERWWQLHNANKSIQEELMQRRREEEAHQKTIDELQQELRSVVQHYATREYSLLTEINELRQTITDVETNLRTFAKLSRGLGNDTLEHVRIVGGTKEPKPRRRGGNNTRDGRA
Protein: Metalloproteinase inhibitor 1 (Collagenase inhibitor 16C8 fibroblast) (Erythroid-potentiating activity) (EPA) (TPA-S1) (TPA-induced protein) (Tissue inhibitor of metalloproteinases 1) (TIMP-1) (P12032)
Organism: Mus musculus (Mouse)
Function: Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14 (By similarity). Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling.
Subcellular location: Secreted {ECO:0000269|PubMed:23522389}.
Interaction partners:
- Matrix metalloproteinase-9
- CD63 antigen
- Stromelysin-1
- Matrix metalloproteinase-14
- 72 kDa type IV collagenase
- Integrin beta-1
- Macrophage metalloelastase
- C-C motif chemokine 2
- Interstitial collagenase B
- Neutrophil collagenase
Sequence:
MMAPFASLASGILLLLSLIASSKACSCAPPHPQTAFCNSDLVIRAKFMGSPEINETTLYQRYKIKMTKMLKGFKAVGNAADIRYAYTPVMESLCGYAHKSQNRSEEFLITGRLRNGNLHISACSFLVPWRTLSPAQQRAFSKTYSAGCGVCTVFPCLSIPCKLESDTHCLWTDQVLVGSEDYQSRHFACLPRNPGLCTWRSLGAR
Protein: Transcription initiation factor TFIID subunit 10 (STAF28) (Transcription initiation factor TFIID 30 kDa subunit) (TAF(II)30) (TAFII-30) (TAFII30) (Q12962)
Organism: Homo sapiens (Human)
Function: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription. TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. TAF10 is also component of the PCAF histone acetylase complex, the TATA-binding protein-free TAF complex (TFTC) and the STAGA transcription coactivator-HAT complex. May regulate cyclin E expression (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:11564863, ECO:0000269|PubMed:25959397, ECO:0000269|PubMed:9674425}.
Interaction partners:
- Transcription initiation factor TFIID subunit 7
- Transcription initiation factor TFIID subunit 3
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 8
- Transformation/transcription domain-associated protein
- Transcription initiation factor TFIID subunit 6
- SAGA-associated factor 29
- Transcription factor SPT20 homolog
- Transcription initiation factor TFIID subunit 2
- TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L
Sequence:
MSCSGSGADPEAAPASAASAPGPAPPVSAPAALPSSTAAENKASPAGTAGGPGAGAAAGGTGPLAARAGEPAERRGAAPVSAGGAAPPEGAISNGVYVLPSAANGDVKPVVSSTPLVDFLMQLEDYTPTIPDAVTGYYLNRAGFEASDPRIIRLISLAAQKFISDIANDALQHCKMKGTASGSSRSKSKDRKYTLTMEDLTPALSEYGINVKKPHYFT
Protein: Integral membrane protein 2B (Immature BRI2) (imBRI2) (Protein E25B) (Transmembrane protein BRI) (Bri) [Cleaved into: BRI2, membrane form (Mature BRI2) (mBRI2); BRI2 intracellular domain (BRI2 ICD); BRI2C, soluble form; Bri23 peptide (Bri2-23) (ABri23) (C-terminal peptide) (P23 peptide)] (Q9Y287)
Organism: Homo sapiens (Human)
Function: Plays a regulatory role in the processing of the amyloid-beta A4 precursor protein (APP) and acts as an inhibitor of the amyloid-beta peptide aggregation and fibrils deposition. Plays a role in the induction of neurite outgrowth. Functions as a protease inhibitor by blocking access of secretases to APP cleavage sites.
Subcellular location: [Integral membrane protein 2B]: Golgi apparatus membrane {ECO:0000269|PubMed:14656991, ECO:0000269|PubMed:19114711}; Single-pass type II membrane protein {ECO:0000269|PubMed:10526337}. Note=Immature BRI2 (imBRI2) is cleaved by furin in the Golgi into mBRI2 and a Bri23 peptide. mBRI2 is transported to the plasma membrane and Bri23 peptide is secreted.; SUBCELLULAR LOCATION: [BRI2, membrane form]: Cell membrane {ECO:0000269|PubMed:18440095, ECO:0000269|PubMed:19748705, ECO:0000269|PubMed:21752865}; Single-pass type II membrane protein {ECO:0000269|PubMed:10526337}. Endosome membrane {ECO:0000269|PubMed:19748705}; Single-pass type II membrane protein {ECO:0000269|PubMed:10526337}. Note=Mature BRI2 (mBRI2) needs to be transported from the endoplasmic reticulum compartment to the cell membrane in order to be able to inhibit APP processing. {ECO:0000269|PubMed:19748705}.; SUBCELLULAR LOCATION: [Bri23 peptide]: Secreted {ECO:0000269|PubMed:10526337, ECO:0000269|PubMed:14656991, ECO:0000269|PubMed:18524908}. Note=Detected in the cerebral spinal fluid (CSF). {ECO:0000269|PubMed:18524908}.; SUBCELLULAR LOCATION: [BRI2C, soluble form]: Secreted {ECO:0000269|PubMed:17965014}.
Interaction partners:
- Amyloid-beta precursor protein
- Cystatin-C
Sequence:
MVKVTFNSALAQKEAKKDEPKSGEEALIIPPDAVAVDCKDPDDVVPVGQRRAWCWCMCFGLAFMLAGVILGGAYLYKYFALQPDDVYYCGIKYIKDDVILNEPSADAPAALYQTIEENIKIFEEEEVEFISVPVPEFADSDPANIVHDFNKKLTAYLDLNLDKCYVIPLNTSIVMPPRNLLELLINIKAGTYLPQSYLIHEHMVITDRIENIDHLGFFIYRLCHDKETYKLQRRETIKGIQKREASNCFAIRHFENKFAVETLICS
Protein: Mitochondrial import inner membrane translocase subunit TIM50-C (Tiny tim 50) (Q9W4V8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
- SD19278p
- Mitochondrial import inner membrane translocase subunit Tim21
- AT05822p
- Protein preli-like
- Mitochondrial import inner membrane translocase subunit TIM44
- Probable mitochondrial import inner membrane translocase subunit Tim17 3
- Translocase of the inner mitochondrial membrane 17b, isoform A
- Probable mitochondrial import inner membrane translocase subunit Tim17 4
- Heat shock 70 kDa protein cognate 5
- MIP34364p1
Sequence:
MSMSMAPATVLQLLRGLSTPRLLTHIHQHRALGNHYHHYHQHYQHQHHLLHHQQQYLRLFTCTALPAAAPALFSILHTARGYSSTTKQEAGATGPNDAPEVAPNAPLLAKLFPQTSPEVDSNAEQERKKREEEEEKENERAWKRMKLGFAIFGGSAVAAGFWAVYEFGKPEVDPNGQPIEDEFTHKPLVQQYLQRMWKSIHYYQRMIQEPSRAKLLPDPLKPPYVQPRYTLVLEMKDVLVHPDWTYQTGWRFKKRPGVDHFLAECAKDFEIVVFTAEQGMTVFPILDALDPNGYIMYRLVRDATHFVDGHHVKNLDNLNRDLKKVIVVDWDANATKMHPDNTFGLARWHGNDDDGQLLDLIAFLKIIAQNNVDDVREVLHYYRQFDDPINQFRENQRKLAEQMLEAERIEQSKTKPMVKQWSRNILGR
Protein: Serine/threonine-protein kinase vps15 (EC 2.7.11.1) (O42900)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Vacuolar protein sorting-associated protein 38
- Phosphatidylinositol 3-kinase pik3
- Vacuolar protein sorting-associated protein atg6
- Serine/threonine-protein kinase atg1
- PtdIns3K complex I subunit atg38
- Autophagy-related protein 101
- Ubiquitin-like protein ATG12
- Autophagy-related protein 14
- Autophagy-related protein 3
- Autophagy-related protein 8
Sequence:
MGIQLSTIQTPQFHELFEEELPEYHNERSLGDSHFLRTFRMQDRKGYDVLIKVFVNKLPEISLSSIVNLLKEEQENISYRVPNAVPYIKTLVTLRAAYLVRPYVTHNLYDRISTRPFLELTEKKWIMFQLLKGISDCHRLGVCHGDIKSENILITSWNWAYLSDFSSFKPTYLPEDNPADYGYFFDTSSRRVCNIAPERFVPASQLQPAPLSPAMDIFSLGCVFAELLLEESPLFTLSQLFSYKAHGSYDLQSVLEQIEDKSTQNMILSMLDRDPSQRLSADAYLQKYRGTVFPACFYDTLYDYCIGLVDPSGILSAKQPNDACSLYGSRIDDIYRDIMPPNNNDISNLMHTPHEYNGIDSYSVPLFTTLDEFYNKNPAAKNWYLRLYNTMQEKKGFEDKEQGSTPAPSPSVIEDISSIETDENHLYGAAVLLPIVLSTIRHVNTRESKINALSLVQILSRNICDESKLDTVLPFVMTLLRDQYADVRISALITITRLVSNVTSIAPINAFLFQEYLFPDLQHFLFDMNSRTRATYASCLPILAKQASKFLNLAQSLRNAGILSFPESEYENINHGKAELLFETGRHDLVVTVERHVSTLLADSSSIVRRSLLNALAPLCVFFGKAKSNDLILSHLITYLNDTDWMLRCAFFESITGLSIFIGPRSVDEYILPLMLQALVDPEPAVLESVLGSFSGLIELHLFEKLVVVDILQLVLPLVAVPNAYIRRAALSVIYSAYQSFDDIDRDCIVTPLLRPYLMSNLCDINSLEKLDQFILPMVSDSVWSTLTRWYEESENSSFWKCDKDASYSSLDVSNDSLLGRTKNLQKREIMHHAEVYTHKKISLTGHVIITSTEMLELSEDDQKWADIIKEMGVDVKHLWVLANLRDYVKKTKINLNGINYKRQSGLRELNTYPNAPLHILPETIFWNPERPPSSSIANETFLDRNSYAESIQTSRSYNDDLIARDPIAYVGTDMTNAFGTTTKPKDVSQSDIKVDINRESNSDNGETITGTHDVYRQTDNPEIKLPSDTASSKVDTHNPTVTQPTDDTGGLNSYNTENPLLTNNTLEPSSVEAIVSSKDSDKHAKESKGKSLAPLISSRVSTNDTTNVAGIRSQRSFTTHIDLKKLTTRQNGAKKSSYTGTNPCVLNYLNKIYAEAAASTLNVGAAVSPSWASNIPLRRRTKVSAKAANKIVQTHEWHPEGSRVAQIYLGSLLDGGTKKVLVSPDSSFFVTLGSDGVVRAWQLVESVRHISTMRCECRLSYGHTRRNGERNRFSVVNGCFLGNTYAFASVTQDGSVEVHRLDVNNQRHTLISAGRIPNLDFSDSVTSMEASTFHDGSIRLVVVTKWSRIVYLDVGMMRVLSSDQLPLQCGSATSVVVSEGCNWALIGTTKGWLLLWDLRFGTLSCSWHMPARIDQMHLLLDVTKKRSNVNEYTSGNNNSPVTKVPGSSSTSSSSTQPINSTIPINPLENHGMLNSFGSTTVSISFSVLTNLDNKEVNLEDAVPASHRSASGIVNFDVEKGKTEEVFLENWNSSLTSPIPVSVGIDAFNEKKKFDIDSGNDMGLRDLNTKFDSPWPCISSPIYRYRGPSAGSVEREPLFLIAASGSPHAFIWNPHNVSASSSVTNDSESSKLSLIHNKPPIYQKVSEQQNVRPKSSGVSRPLLFLQQQKNLPSENRLHPIVDMAFLYQPYAIVLIVDAFGSLELWT
Protein: Kallikrein-6 (EC 3.4.21.-) (Neurosin) (Protease M) (SP59) (Serine protease 18) (Serine protease 9) (Zyme) (Q92876)
Organism: Homo sapiens (Human)
Function: Serine protease which exhibits a preference for Arg over Lys in the substrate P1 position and for Ser or Pro in the P2 position. Shows activity against amyloid precursor protein, myelin basic protein, gelatin, casein and extracellular matrix proteins such as fibronectin, laminin, vitronectin and collagen. Degrades alpha-synuclein and prevents its polymerization, indicating that it may be involved in the pathogenesis of Parkinson disease and other synucleinopathies. May be involved in regulation of axon outgrowth following spinal cord injury. Tumor cells treated with a neutralizing KLK6 antibody migrate less than control cells, suggesting a role in invasion and metastasis.
Subcellular location: Secreted. Nucleus, nucleolus. Cytoplasm. Mitochondrion. Microsome. Note=In brain, detected in the nucleus of glial cells and in the nucleus and cytoplasm of neurons. Detected in the mitochondrial and microsomal fractions of HEK-293 cells and released into the cytoplasm following cell stress.
Interaction partners:
- Amyloid-beta precursor protein
- Alpha-2-macroglobulin-like protein 1
- Corneodesmosin
- Serine protease inhibitor Kazal-type 5
- Alpha-synuclein
- Cornifin-B
Sequence:
MKKLMVVLSLIAAAWAEEQNKLVHGGPCDKTSHPYQAALYTSGHLLCGGVLIHPLWVLTAAHCKKPNLQVFLGKHNLRQRESSQEQSSVVRAVIHPDYDAASHDQDIMLLRLARPAKLSELIQPLPLERDCSANTTSCHILGWGKTADGDFPDTIQCAYIHLVSREECEHAYPGQITQNMLCAGDEKYGKDSCQGDSGGPLVCGDHLRGLVSWGNIPCGSKEKPGVYTNVCRYTNWIQKTIQAK
Protein: Thioredoxin (Trx) (Q9DGI3)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Function: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (By similarity). Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P10599}. Cytoplasm {ECO:0000250|UniProtKB:P10599}. Secreted {ECO:0000250|UniProtKB:P10599}. Note=Shuttles between the nucleus and nucleolus. {ECO:0000250|UniProtKB:Q811S9}.
Interaction partners:
- Thioredoxin-interacting protein
- Thioredoxin-interacting protein
- Thioredoxin, mitochondrial
- Peroxiredoxin-5
- Mitochondrial peptide methionine sulfoxide reductase
- Thioredoxin
- thioredoxin-disulfide reductase
- thioredoxin-dependent peroxiredoxin
- Peroxiredoxin-2
- thioredoxin-disulfide reductase
Sequence:
MVVHIENLNAFSAALKNAGDKLVVVDFTATWCGPCQKIGPIFETLSKSEDYQNVVFLKVDVDDAADVSSHCDIKCMPTFHFYKNGQKIDEFSGANEQTLKQKINDHK
Protein: Probable glucan endo-1,3-beta-glucosidase eglC (EC 3.2.1.39) (Endo-1,3-beta-glucanase eglC) (Laminarinase eglC) (Q4WG16)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation and also function biosynthetically as a transglycosylase (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Secreted, cell wall {ECO:0000250}. Note=Covalently-linked GPI-modified cell wall protein. {ECO:0000250}.
Interaction partners:
- Probable beta-glucosidase A
- Probable glucan 1,3-beta-glucosidase A
- Probable glucan 1,3-beta-glucosidase D
- Probable beta-glucosidase L
- glucan 1,3-beta-glucosidase
- Exo-beta-1,3-glucanase Exg0
- beta-glucosidase
- Probable beta-glucosidase F
- Probable beta-glucosidase E
- Probable beta-glucosidase M
Sequence:
MQFTHLVALALALATSEAAHQGFNYGNTKSDGSAKSQADFQAEFSTAKNLVGTSGFTSARLYTMIQGGTANTPISAIPAAITEQTSLLLGLWASGGNFANEIAALKAAIAQYGDDLAKLVVGISVGSEDLYRNSVDGVKANAGIGTNPDEIVSYINEVRSTIAGTKLSGAPIGHVDTWTAWVNGSNSAVIDACDWLGFDGYPYFQNTMANSISDAKALFDESVAKTQAVAKGKEVWITETGWPVSGKTENLAVANLANAKTYWDEVGCPLFGKTNTWWYILQDADPVTPNPSFGIVGSTLSTTPLFDLSCSASSSSSAAAAASSTAGPSASSVIGGKASGFTTAAANSAKPTFTVGKGPGGSYNGTGFWNSTSSARPSSSAISGSSSGSAAGSSGAGASGASGQSSSSTGSSSAPSTSNILSNAASGLSGSIFGAVVAVCLALAAL
Protein: Photosystem I reaction center subunit III, chloroplastic (Light-harvesting complex I 17 kDa protein) (P21 protein) (PSI-F) (P12356)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Probably participates in efficiency of electron transfer from plastocyanin to P700 (or cytochrome c553 in algae and cyanobacteria). This plastocyanin-docking protein contributes to the specific association of plastocyanin to PSI.
Subcellular location: Plastid, chloroplast thylakoid lumen.
Interaction partners:
Sequence:
MALTMRNPAVKASSRVAPSSRRALRVACQAQKNETASKVGTALAASALAAAVSLSAPSAAMADIAGLTPCSESKAYAKLEKKELKTLEKRLKQYEADSAPAVALKATMERTKARFANYAKAGLLCGNDGLPHLIADPGLALKYGHAGEVFIPTFGFLYVAGYIGYVGRQYLIAVKGEAKPTDKEIIIDVPLATKLAWQGAGWPLAAVQELQRGTLLEKEENITVSPR
Protein: Phosphodiesterase (EC 3.1.4.-) (Q38F46)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Adenosine kinase
- Adenosine kinase
- AMP deaminase, putative
- Adenosine monophosphate deaminase, putative
- AMP deaminase
- adenine phosphoribosyltransferase
- adenine phosphoribosyltransferase
- Phosphodiesterase
- Adenylosuccinate lyase
- 3', 5'-cyclic nucleotide phosphodiesterase, putative
Sequence:
MFMNKPFGSKRCEPFHESEHLCEAFAITEAILARYQRGKRSFTSSEKSGLAALIKRIPYDILVEVLDQSGFTPTSNATPPVDYLAMMEHTMTHGASITHALQYLNDLMTKCTGCPGIRTYYHNPNDDVLADPVHDTAALIDETTAVGKSVVTKQYLNIAGAHYIPLIHGDIVVGCVEVPRFSGNLEELPSFPSLIRAVTCTAHKFIEEARINWNREKAEAMLQMATRLARDNLDETVLASSIMNTVKSLTESARCSLFLVKDDKLEAHFEDGNVVSIPKGTGIVGYVAQTGETVNIVDAYADDRFNREVDKATGYRTKTILCMPVMYEGTIVAVTQLINKLDLTTESGLRLPRVFGKRDEELFQTFSMFAGASLRNCRINDRLLKEKKKSDVILDVVTVLSNTDIRDVDGIVRHALHGAKKLLNADRSTLFLVDKERNELCSRMADSVAGKEIRFPCGQGIAGTVAASGVGENIQDAYQDPRFNREVDKQLGYRTQTILCEPIILNGEILAVVQLVNKLDTSGEVTVFTEDDRETFRVFSLFAGISINNSHLLEFAVKAGREVMELNEHRATLFNKNVPSRAVKRVTAITKVEREAVLVCELPSFDVTDVEFDLFRARDTTDKPLDVAAAIAYRLLLGSGLPQKFGCSDEVLLNFILQCRKKYRNVPYHNFYHVVDVCQTIHTFLYRGNVYEKLTELECFVLLITALVHDLDHMGLNNSFYLKTESPLGILSSASGNTSVLEVHHCNLAVEILSDPESDVFGGLEGAERTLAFRSMIDCVLATDMAKHGSALEAFLASAADQSSDEAAFHRMTMEILLKAGDISNVTKPFDISRQWAMAVTEEFYRQGDMEKERGVEVLPMFDRSKNMELAKGQIGFIDFVAAPFFQKIVDACLQGMQWTVDRIKSNRAQWERVLETRLSTSSGNNSSTR
Protein: Methyltransferase like 17 (H0YJW1)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
XPGFVFAPCPHELPCPQLTNLACSFSQAYHPIPFSWNKKPKEEKFSMVILARGSPEEAHRWPRITQPVLKRPRHVHCHLCCPDGHMQHAVLTARRHGSSWGDLLPVLTPSAFPPSTAQDPSES
Protein: Recyclin-1 (P39531)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in recycling plasma membrane proteins internalized by endocytosis. Required for recycling of the v-SNARE SNC1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11287615}. Bud neck {ECO:0000269|PubMed:11287615}. Cell tip {ECO:0000269|PubMed:11287615}. Note=In unpolarized G1 cells this protein is found in patches in the cytoplasm, while after bud emergence it is concentrated in nascent buds and at the mother-bud neck. Accumulates at the shmoo tips of cells treated with pheromone. Localization depends on an intact actin cytoskeleton and a functional secretory pathway.
Interaction partners:
- Synaptobrevin homolog 1
- Suppressor of kinetochore protein 1
- GTP-binding protein YPT31/YPT8
- Exocyst complex component SEC5
- Exocyst complex component EXO70
- Exocyst complex component EXO84
- Exocyst complex component SEC8
- Exocyst complex component SEC15
- Phospholipid-transporting ATPase accessory subunit CDC50
- Phospholipid-transporting ATPase DRS2
Sequence:
MDDLLKVPEIVTNIASYLSTVDYLSFQQVNKRVYAIINGKNDSKYWSLKLTRMGLQQVHSNEEEEITLLDENDNQNSLRIFEIYKSFTAQNSKKIFVKFYRCYNSYARKLYNNNLANFFPTSYSNDPLKQTRILNFIKKYNFSNKNDIETFTRIETNFNILREIFINSVLKESELNYQSNNLAAVARFMKILLISNEESNAIEFFKSKADLPPSLTVLPSNDELFWAEQPREEDSGGSTVIFNSKNLDTFLNQLRDFLNEKIKLADILFKDEFPVILQFIESFIQDILLDILNNILLSYSEFLKENGKDSKANYECVPELYFTFIKKFDTELNDSVNAGANFRKVVRDLLNLYLEPFVVNYMNQTTRVFESLINSQLANYDTQVQDKQREQNAKIYNTLKDQTDASSASNNELPNDLSIITETSKTVPEADSKPSTIHQSVHSTDISNDKLDFLSSFTKIFKFSNNENQRLKQQLQLAYNLNLISNNLQNIKSLISLDLCYKILQETSEKTDQIYKFHTIESLLPLIKLRCQEIFKILITQLNKNHVKPAFEKAILLLQKYNPNEIEQIEIKFNSLSPANTQVEPLVQFTELINIGDIILQMISIFYKNELIPKKIIDKNKDFLNDVIQLKKNFETSIDDFVAEGLNIGINKLMDEISFVFKTLQLPDDYNPPPPSRNSPIRDIKPTKCAIRVVELLSNHCFLLTGATDKGTIDVYQQEIGERFFNEIVKHLKKCFISTEGAIWLICDLNYFYDFIANKLKQKNVVPYFVGLKSIGQLYIISGKDSKELGKLISDLGKFNGIFTQEEIYEFVQRRSDWVRVRKDVEKVMYGLGIRDCCIM
Protein: SHSP domain-containing protein (Q86GU1)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSERRIDVNRSNYSVIDNEFGNMRDRFEQEMRRVEEEMKRLRSEFEGYRPNGGPPAAISNQPYNAYSNTSSHHETSNRTGGFGSPLPPPSFHGPSDLMAHRPTYDPYLDNLKSPLIKDESDGKTLRLRFDVANYKPEEVTVKTIDNRLLVHAKHEEKTPQRTVFREYNQEFLLPRGTNPEQISSTLSTDGVLTVEAPLPQLAIQQ
Protein: Small integral membrane protein 14 (Q91VT8)
Organism: Mus musculus (Mouse)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MAEGGFDPCECVCSHEHAMRRLINLLRQSQSYCTDTECLRELPGPSSDSGISITVILMAWMVIAMLLFLLRPPNLRGSSLPGKPSSPHSGQDPPAPPVD
Protein: Large ribosomal subunit protein uL6 (60S ribosomal protein L9) (P51410)
Organism: Mus musculus (Mouse)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:36517592}.
Interaction partners:
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL18
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL24
- Small ribosomal subunit protein uS7
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein eL19
Sequence:
MKTILSNQTVDIPENVEITLKGRTVIVKGPRGTLRRDFNHINVELSLLGKKKKRLRVDKWWGNRKELATVRTICSHVQNMIKGVTLGFRYKMRSVYAHFPINVVIQENGSLVEIRNFLGEKYIRRVRMRTGVACSVSQAQKDELILEGNDIELVSNSAALIQQATTVKNKDIRKFLDGIYVSEKGTVQQADE
Protein: Glutarate-semialdehyde dehydrogenase (EC 1.2.1.-) (Q9I6M5)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the conversion of 5-oxopentanoate (glutarate semialdehyde) to glutarate. Involved in L-lysine degradation.
Interaction partners:
- 5-aminovalerate aminotransferase DavT
- Succinate dehydrogenase flavoprotein subunit
- Succinate dehydrogenase iron-sulfur subunit
- Probable coenzyme A transferase
- HpcH/HpaI aldolase/citrate lyase domain-containing protein
- Succinate dehydrogenase cytochrome b556 subunit
- Succinate dehydrogenase hydrophobic membrane anchor subunit
- Phosphoenolpyruvate carboxykinase
- Citrate synthase
- FAD dependent oxidoreductase domain-containing protein
Sequence:
MQLKDAKLFRQQAYVDGAWVDADNGQTIKVNNPATGEIIGSVPKMGAAETRRAIEAADKALPAWRALTAKERANKLRRWFDLMIENQDDLARLMTIEQGKPLAEAKGEIAYAASFLEWFGEEAKRIYGDTIPGHQPDKRIIVIKQPIGVTAAITPWNFPSAMITRKAGPALAAGCTMVLKPASQTPYSALALAELAERAGIPKGVFSVVTGSAGEVGGELTSNPIVRKLTFTGSTEIGRQLMAECAQDIKKVSLELGGNAPFIVFDDADLDAAVEGALISKYRNNGQTCVCANRLYVQDGVYDAFVDKLKAAVAKLNIGNGLEAGVTTGPLIDAKAVAKVEEHIADAVSKGAKVVSGGKPHALGGTFFEPTILVDVPKNALVSKDETFGPLAPVFRFKDEAEVIAMSNDTEFGLASYFYARDLARVFRVAEQLEYGMVGINTGLISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYLCLGGI