wanglab/gogpt-training-data huggingface dataset:
Protein: Trehalose-phosphatase (EC 3.1.3.12) (Trehalose-6-phosphate phosphatase) (TPP) (P78875)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Phosphatase catalytic subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-alpha-D-glucose in a two step process. The disaccharide trehalose serves as a storage carbohydrate that is mobilized during nutrient stress and spore germination (Probable). Together with ntp1, regulates the level of trehalose as a protectant for cell integrity during thermal, osmotic, and oxidative stress (Probable).
Interaction partners:
- Alpha,alpha-trehalose-phosphate synthase
- Cytosolic neutral trehalase
- Putative alpha,alpha-trehalose-phosphate synthase 106 kDa subunit
- Putative alpha,alpha-trehalose-phosphate synthase 100 kDa subunit
- Probable UTP--glucose-1-phosphate uridylyltransferase
- Probable UTP--glucose-1-phosphate uridylyltransferase
- Protection of telomeres protein poz1
- Trehalose-phosphatase
- Protection of telomeres protein tpz1
- Coiled-coil quantitatively-enriched protein 1
Sequence:
MSVYGKIPSTSFEHENTFELSGDLLDPEELKSLGVSGRIIYVLRHLPFKSSINEETREWDLSGRRGATTMYSSMNWLANSTYWQTTLVGWTGVIPTVSEKEENKDAVTRLDSQDVKRFEETYSQWNSGERSTEYVPVWLPGPEKGSETIINETRSQQSRWLAYAENVIRPLIHYKYWPSSEVDENEEQWWRDYVKMNHAFADKICEIYKPGDFIIVQDYSLFLVPQLIRNKIDDAVIGFYHHHPFPSSEIARCFPRRRAILRSVLGADFIGFEDYSYARHFISCCSRVLDLEIGHDWVNLNGNKVTVRAITVGIDVPRIIRSSGNVSVSEKLEELNKRYENMKVILGRDRLDELYGVPQKLRSFQRFLRTYPEWRKKVVLIQITISSAFKHPKLLSSIKKLVQAINQEFGTDDYTPVHHVEEQLEPADYFALLTRADALFINSIREGVSNLALEYVVCQRDRYGMVLLSEFTATSAMLHDVPLINPWDYNECAEIISNALSTPLERRKMIERESYKQVTTHTMQSWTSSLIRSLANKLAATKTDQRIPTLTPEHALSVYSKASKRLFMMDYDGTLTPIVRDPNAAVPSKKLLDNLATLAADPKNQVWIISGRDQQFLRNWMDDIKGLGLSAEHGSFVRKPHSTTWINLAELLDMSWKKEVRRIFQYYTDRTQGSSIEEKRCAMTWHYRKADPENGAFQALECEALLEELVCSKYDVEIMRGKANLEVRPSSINKGGIVKQILSSYPEDSLPSFIFCAGDDRTDEDMFRSLHKNTRINKETSFAVTIGSDKKLSIADWCIADPANVIDILADLANFTN
Protein: Ribonucleoside-diphosphate reductase large subunit (EC 1.17.4.1) (Protein DEFECTIVE IN POLLEN DNA DEGRADATION 2) (Ribonucleoside-diphosphate reductase R1 subunit) (AtRNR1) (Q9SJ20)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R1 contains the binding sites for both substrates and allosteric effectors and carries out the actual reduction of the ribonucleotide. Ribonucleotide reductase (RNR) complex function is essential for efficient organellar DNA degradation in pollen. Involved in chloroplast division.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22239102}.
Interaction partners:
- Ribonucleoside-diphosphate reductase small chain C
- Ribonucleoside-diphosphate reductase small chain A
- Thymidylate kinase
- Guanylate kinase 2
- Guanylate kinase 3, chloroplastic
- At5g66005
- Guanylate kinase 1
- Putative ribonucleoside-diphosphate reductase small chain B
- Nucleoside diphosphate kinase III, chloroplastic/mitochondrial
- Nucleoside diphosphate kinase 1
Sequence:
MYVVKRDGRQETVHFDKITARLKKLSYGLSSDHCDPVLVAQKVCAGVYKGVTTSQLDELAAETAAAMTCNHPDYASLAARIAVSNLHKNTKKSFSETIKDMFYHVNDRSGLKSPLIADDVFEIIMQNAARLDSEIIYDRDFEYDYFGFKTLERSYLLKVQGTVVERPQHMLMRVAVGIHKDDIDSVIQTYHLMSQRWFTHASPTLFNAGTPRPQLSSCFLVCMKDDSIEGIYETLKECAVISKSAGGIGVSVHNIRATGSYIRGTNGTSNGIVPMLRVFNDTARYVDQGGGKRKGAFAVYLEPWHADVYEFLELRKNHGKEEHRARDLFYALWLPDLFMERVQNNGQWSLFCPNEAPGLADCWGAEFETLYTKYEREGKAKKVVQAQQLWYEILTSQVETGTPYMLFKDSCNRKSNQQNLGTIKSSNLCTEIIEYTSPTETAVCNLASIALPRFVREKGVPLDSHPPKLAGSLDSKNRYFDFEKLAEVTATVTVNLNKIIDVNYYPVETAKTSNMRHRPIGIGVQGLADAFILLGMPFDSPEAQQLNKDIFETIYYHALKASTELAARLGPYETYAGSPVSKGILQPDMWNVIPSDRWDWAVLRDMISKNGVRNSLLVAPMPTASTSQILGNNECFEPYTSNIYSRRVLSGEFVVVNKHLLHDLTDMGLWTPTLKNKLINENGSIVNVAEIPDDLKAIYRTVWEIKQRTVVDMAADRGCYIDQSQSLNIHMDKPNFAKLTSLHFYTWKKGLKTGMYYLRSRAAADAIKFTVDTAMLKEKPSVAEGDKEVEEEDNETKLAQMVCSLTNPEECLACGS
Protein: Glutathione reductase (GR) (GRase) (EC 1.8.1.7) (Q6FRV2)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Maintains high levels of reduced glutathione in the cytosol.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P41921}. Mitochondrion {ECO:0000250|UniProtKB:P41921}.
Interaction partners:
- Pyruvate dehydrogenase E1 component subunit beta
- Glutathione synthetase
- Candida glabrata strain CBS138 chromosome A complete sequence
- Glutathione hydrolase
- Thioredoxin reductase
- 2-oxoglutarate dehydrogenase, mitochondrial
- Protein URE2
- glutathione-specific gamma-glutamylcyclotransferase
- Acetyltransferase component of pyruvate dehydrogenase complex
- Thioredoxin reductase
Sequence:
MIVKRLFRTMAPVAKHFDYLVIGGGSGGVASSRRAASYGAKTLLIEGKALGGTCVNVGCVPKKVMWYASDLATRLTHAHEYGLAQNVPLSKESITFNWPEFKKKRDAYIHRLNGIYENNLKKEGVEVVFGWAKFNKDGNVEVTKHDNTTEVYSADRILVATGGKPVYPEKVPGFELGTDSDGFFRLEEQPKKVVVVGAGYIGIELAGVFHGLGSDSHLVIRGKTVLRKFDEIIQNTVTDYYVEEGINVHKETNVDKVEKDEKTGKLSVHLTNGQVLEDVDELIWTMGRRSLLGIGLENVGVKLNDKEQIITDEYQNTNVPNIYSLGDVSGRVELTPVAIAAGRKLSNRLFGPEQYRNDKLDYTNVPSVVFSHPEAGSIGLTEDEAIKQYGKDNIKVYTSKFTAMYYAMLEHKSPTRYKIICEGPNEKVVGLHIVGDSSAEILQGFGVAIKMGATKADFDNCVAIHPTSAEELVTMR
Protein: Protocadherin beta 16 (Q14BM8)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004162}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
Interaction partners:
Sequence:
MEASRKLICRQRQVLFFFLLLGFPLTTAGELRRYSVVEEKEGRSFVTNLVKDLGLGQLELSRRGAKVISKGNKLHLQLDQETGDLLLNEKVDREKLCGHTEPCLLSFQVLLDNPLDIFQAELEVTDINDHSPEFLDKEIMLKISESSLPGATFPLKNAQDMDVGQNGIDKYLISSNSYFRVLTRKRSDGKKYPELVLDRALDREEEAELRLTLTAQDGGSLPRSGTTEVHIEVLDINDNAPQFEQLFYKAQIPEDSPIGFLIITVSATDKDIGVNGQISYSLFQVSDDISKTFSIHPLTGEVRLKEHLDFEKTQSYEINIEARDAGTFSGKCTILAQVLDVNDHAPEIILSAFTNSILENLPETMVAVFSVSDLDSGENGKVSCSIQDDLPFFLKPSGENFYTLLSQKPLDRESVAEYNITITVADMGSPILKTQVNLTVQVSDINDNAPIFTQTSYTMFIRENNSPALHIGTISATDSDSGSNAHITYSLLPPHDHQLALASFISINADNGQLFVLRALDYEALQAFEFHVGATDGGSPALSSQALVRVVVLDDNDNAPFVLYPMQNASAPYTELLPRAAEPGYLVTKVVAVDRDSGQNAWLSFQLLKATEPGLFSVWAHNGEVHTSRLLSERDVHKHRLILLVKDNGDPPRSASVTLHVLLVDGFSQPYLPLPEVARDPDHEDSELTLYLVIALASVSSLFLVSVLLFVGVRLCRRAREVSLGGCSVPEGHFPGHLVDVSGTGTLSQSYQYEVCLTGDSGTGEFKYLKPILPNFQDHSFRPEMGENPNSRNDWSFGIQLK
Protein: guanylate kinase (EC 2.7.4.8) (E9PTV0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- GMP synthase
- Adenine phosphoribosyltransferase
- Ribonucleoside-diphosphate reductase
- Adenylate kinase 9
- Inosine triphosphate pyrophosphatase
- Nucleoside diphosphate kinase A
- Phosphodiesterase
- 5'-nucleotidase, cytosolic IA
- Nucleoside diphosphate kinase
- Nucleoside diphosphate kinase B
Sequence:
TETATHQVGMAGPRPVVLSGPSGAGKSTLLKKLFQEHGSVFGFSVSHTTRNPRPGEEDGKDYYFVTREMMQRDIAAGDFIEHAEFSGNLYGTSKEAVRAVQAMNRICVLDVDLQGVRSIKKTDLHPIYISVQPPSMDVLEQRLRQRNTETEESLAKRLAAAQADMESSKEPGLFDLVIVNDNLDEAYVTLKQALSEEIKKAEGTEHA
Protein: Protein transport protein Sec31B (SEC31-like protein 2) (SEC31-related protein B) (SEC31B-1) (Q9NQW1)
Organism: Homo sapiens (Human)
Function: As a component of the coat protein complex II (COPII), may function in vesicle budding and cargo export from the endoplasmic reticulum.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16495487}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000269|PubMed:16495487}; Peripheral membrane protein {ECO:0000269|PubMed:16495487}; Cytoplasmic side {ECO:0000269|PubMed:16495487}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16495487}; Peripheral membrane protein {ECO:0000269|PubMed:16495487}.
Interaction partners:
- Protein SEC13 homolog
- Protein transport protein Sec24B
- Protein transport protein Sec23B
- Protein transport protein Sec24A
- Protein transport protein Sec23A
- Small COPII coat GTPase SAR1A
- Small COPII coat GTPase SAR1B
- Protein transport protein Sec24D
- Protein transport protein Sec24C
- Protein transport protein Sec31A
Sequence:
MKLKELERPAVQAWSPASQYPLYLATGTSAQQLDSSFSTNGTLEIFEVDFRDPSLDLKHRGVLSALSRFHKLVWGSFGSGLLESSGVIVGGGDNGMLILYNVTHILSSGKEPVIAQKQKHTGAVRALDLNPFQGNLLASGASDSEIFIWDLNNLNVPMTLGSKSQQPPEDIKALSWNRQAQHILSSAHPSGKAVVWDLRKNEPIIKVSDHSNRMHCSGLAWHPDIATQLVLCSEDDRLPVIQLWDLRFASSPLKVLESHSRGILSVSWSQADAELLLTSAKDSQILCRNLGSSEVVYKLPTQSSWCFDVQWCPRDPSVFSAASFNGWISLYSVMGRSWEVQHMRQADKISSSFSKGQPLPPLQVPEQVAQAPLIPPLKKPPKWIRRPTGVSFAFGGKLVTFGLPSTPAHLVPQPCPRLVFISQVTTESEFLMRSAELQEALGSGNLLNYCQNKSQQALLQSEKMLWQFLKVTLEQDSRMKFLKLLGYSKDELQKKVATWLKSDVGLGESPQPKGNDLNSDRQQAFCSQASKHTTKEASASSAFFDELVPQNMTPWEIPITKDIDGLLSQALLLGELGPAVELCLKEERFADAIILAQAGGTDLLKQTQERYLAKKKTKISSLLACVVQKNWKDVVCTCSLKNWREALALLLTYSGTEKFPELCDMLGTRMEQEGSRALTSEARLCYVCSGSVERLVECWAKCHQALSPMALQDLMEKVMVLNRSLEQLRGPHGVSPGPATTYRVTQYANLLAAQGSLATAMSFLPRDCAQPPVQQLRDRLFHAQGSAVLGQQSPPFPFPRIVVGATLHSKETSSYRLGSQPSHQVPTPSPRPRVFTPQSSPAMPLAPSHPSPYQGPRTQNISDYRAPGPQAIQPLPLSPGVRPASSQPQLLGGQRVQVPNPVGFPGTWPLPGSPLPMACPGIMRPGSTSLPETPRLFPLLPLRPLGPGRMVSHTPAPPASFPVPYLPGDPGAPCSSVLPTTGILTPHPGPQDSWKEAPAPRGNLQRNKLPETFMPPAPITAPVMSLTPELQGILPSQPPVSSVSHAPPGVPGELSLQLQHLPPEKMERKELPPEHQSLKSSFEALLQRCSLSATDLKTKRKLEEAAQRLEYLYEKLCEGTLSPHVVAGLHEVARCVDAGSFEQGLAVHAQVAGCSSFSEVSSFMPILKAVLIIAHKLLV
Protein: Actin-3 (EC 3.6.4.-) (P0DM42)
Organism: Caenorhabditis elegans
Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
Sequence:
MCDDEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGVVLDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITVGNERFRCPEAMFQPSFLGMESAGIHETSYNSIMKCDIDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
Protein: Leucine-zipper-like transcriptional regulator 1 (LZTR-1) (Q8N653)
Organism: Homo sapiens (Human)
Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates ubiquitination of Ras (K-Ras/KRAS, N-Ras/NRAS and H-Ras/HRAS). Is a negative regulator of RAS-MAPK signaling that acts by controlling Ras levels and decreasing Ras association with membranes.
Subcellular location: Endomembrane system {ECO:0000269|PubMed:30442762, ECO:0000269|PubMed:30442766}. Recycling endosome {ECO:0000269|PubMed:30442762}. Golgi apparatus {ECO:0000269|PubMed:16356934, ECO:0000269|PubMed:30481304, ECO:0000269|PubMed:34626534}.
Interaction partners:
- Cullin-3
- Kelch-like protein 22
- GTPase KRas
- Kelch-like protein 3
- Gigaxonin
- Zinc finger SWIM domain-containing protein 8
- Kelch-like protein 21
- Kelch-like protein 8
- Kelch repeat and BTB domain-containing protein 8
- Kelch-like protein 7
Sequence:
MAGPGSTGGQIGAAALAGGARSKVAPSVDFDHSCSDSVEYLTLNFGPFETVHRWRRLPPCDEFVGARRSKHTVVAYKDAIYVFGGDNGKTMLNDLLRFDVKDCSWCRAFTTGTPPAPRYHHSAVVYGSSMFVFGGYTGDIYSNSNLKNKNDLFEYKFATGQWTEWKIEGRLPVARSAHGATVYSDKLWIFAGYDGNARLNDMWTIGLQDRELTCWEEVAQSGEIPPSCCNFPVAVCRDKMFVFSGQSGAKITNNLFQFEFKDKTWTRIPTEHLLRGSPPPPQRRYGHTMVAFDRHLYVFGGAADNTLPNELHCYDVDFQTWEVVQPSSDSEVGGAEVPERACASEEVPTLTYEERVGFKKSRDVFGLDFGTTSAKQPTQPASELPSGRLFHAAAVISDAMYIFGGTVDNNIRSGEMYRFQFSCYPKCTLHEDYGRLWESRQFCDVEFVLGEKEECVQGHVAIVTARSRWLRRKITQARERLAQKLEQEAAPVPREAPGVAAGGARPPLLHVAIREAEARPFEVLMQFLYTDKIKYPRKGHVEDVLLIMDVYKLALSFQLCRLEQLCRQYIEASVDLQNVLVVCESAARLQLSQLKEHCLNFVVKESHFNQVIMMKEFERLSSPLIVEIVRRKQQPPPRTPLDQPVDIGTSLIQDMKAYLEGAGAEFCDITLLLDGHPRPAHKAILAARSSYFEAMFRSFMPEDGQVNISIGEMVPSRQAFESMLRYIYYGEVNMPPEDSLYLFAAPYYYGFYNNRLQAYCKQNLEMNVTVQNVLQILEAADKTQALDMKRHCLHIIVHQFTKVSKLPTLRSLSQQLLLDIIDSLASHISDKQCAELGADI
Protein: Growth hormone (H6UQ57)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
MAPGSWFSPLLIAVVTLGLPQEAAATFPAMPLSNLFANAVLRAQHLHLLAAETYKEFERTYIPEDQWYTNKNSQAAFCYSETIPAPTGKDDAQQKSDMELLRFSLVLIQSWLTPVQYLSKVFTNNLVFGTKKRVFEKLKDLEEGLQPLMRELEDRSPRGPQLLRPTYDKFDIHLRNEDALLKNYGLLSCFKKDLHKVETYLKVMKCRRFGESNCTI
Protein: ADP-ribosylation factor-binding protein GGA3 (Golgi-localized, gamma ear-containing, ARF-binding protein 3) (Q8BMI3)
Organism: Mus musculus (Mouse)
Function: Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (DXXLL) motif (By similarity).
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9NZ52}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NZ52}. Endosome membrane {ECO:0000250|UniProtKB:Q9NZ52}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NZ52}. Early endosome membrane {ECO:0000250|UniProtKB:A0A0G2JV04}; Peripheral membrane protein {ECO:0000305}. Recycling endosome membrane {ECO:0000250|UniProtKB:A0A0G2JV04}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- ADP-ribosylation factor 6
- ADP-ribosylation factor-binding protein GGA1
- ADP-ribosylation factor-binding protein GGA2
- Cation-independent mannose-6-phosphate receptor
- Rab GTPase-binding effector protein 1
- Cation-dependent mannose-6-phosphate receptor
- ADP-ribosylation factor 1
- Polyubiquitin-B
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin-C
Sequence:
MAEAEGESLESWLNKATNPSNRQEDWEYIIGFCDQINKELEGPQIAVRLLAHKIQSPQEWEAVQALTVLEACMKNCGRRLHNEVGKFRFLNELIKVVSPKYLGDRVSEKVKTKVIELLFSWTLALPEEAKIKDAYHMLKRQGIVQSDPPIPMDRTLIPSPPPRPKNPVFDDEEKSKLLARLLKSKNPDDLQEANRLIKSMVKEDEARIQKVTKRLHTLEEVNNNVKLLHEMLLHYSQEYSSDADKELMKELFDRCENKRRTLFKLASETEDNDNSLGDILQASDNLSRVINSYKTIIEGQIVNGEVTTSTMPDSEGNSHCGNQGALIDLAELDAPSNSSPALAPPTSGIPILPPPPQTSGPPRSRSSSQAEAPPGSDSTNNALSLLDEELLCLGLTDPAPTAPKESPGSSQWHLFQNEPPSDLDFFSPRPVPAASCPSDGPQLPPPVSTSSMSQAPLPAAFPAPVVPASAPTHSTGSFMFSSGPAPALAPKAEPKGPEYPSSSTSHRLDALDQLLEEAKVTSGLVKPVSCFSPGPTASPLLPASAPARPLLPFSTGPGSPLFQSQGSPQKGPELSLASVHVPLESIKPSSALPVTAYDKNGFRILFHFAKECPPGRPDVLVVVVSMLNTAPLPVKSIVLQAAVPKSMKVKLQPPSGTELSPFSPIQPPAAITQVMLLANPMKEKVRLRYKLTFALGEQLSTELGEVDQFPPVEQWGNL
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (A0A8I6AFL3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MGSLGALALCLLRLLLLGLQRPPLPGAGAQSAAGGCSFDEHYSNCGYSVALGTNGFTWEQINTWEKPMLDPAVPTGSFMMVNSSGRASGQKAHLLLPTLKENDTHCIDFHYYFSSRDRSSPGALNVYVKVNGGPQGNPVWNVSGVVTEGWVKAELAISTFWPHFYQVIFESVSLKGHPGYIAVDEVRVLAHPCRKAPHFLRLQNVEVNVGQNATFQCIAGGKWSQHDKLWLQQWNGRDTALMVTRVVNHRRFSATVSVADTSQRSVSKYRCVIRSDGGSGVSNYAELIVKEPPTPIAPPELLAVGATYLWIKPNANSIIGDGPIILKEVEYRTTTGTWAETHIVDSPNYKLWHLDPDVEYEIRVLLTRPGEGGTGPPGPPLTTRTKCADPVHGPQNVEIVDIRARQLTLQWEPFGYAVTRCHSYNLTVQYQYVFNQQQYEAEEVIQTSSHYTLRGLRPFMTIRLRLLLSNPEGRMESEELVVQTEEDVPGAVPLESIQGGPFEEKIYIQWKPPNETNGVITLYEINYKAVGSLDPSADLSSQRGKVFKLRNETHHLFVGLYPGTTYSFTIKASTAKGFGPPVTTRIATKISAPSMPEYDADSPLNETDTTITVMLKPAQSRGAPVSVYQLVVKEERLQKSRRAADIIECFSVPVSYRNASNLDSLHYFAAELKPSNLPVTQPFTVGDNKTYNGYWNPPLSPLKSYSIYFQALSKANGETKINCVRLATKGASTQNSNTVEPEKQVDNTVKMAGVIAGLLMFIIILLGVMLTIKRRKLAKKQKETQSGAQREMGPVASTDKPTTKLSTNRNDEGFSSSSQDVNGFTDGSRGELSQPTLTIQTHPYRTCDPVEMSYPRDQFQPAIRVADLLQHITQMKRGQGYGFKEEYEALPEGQTASWDTAKEDENRNKNRYGNIISYDHSRVRLLVLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASIVMVTNLVEVGRHPAEHTVGTATLGRAASPGMVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIRELRLFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPEAGPIVVHCSAGAGRTGCFIAIDTMLDMAENEGVVDIFNCVRELRAQRVNLVQTEEQYVFVHDAILEACLCGNTAIPVCEFRSLYYNISRLDPQTNSSQIKDEFQTLNIVTPRVRPEDCSIGLLPRNHDKNRSMDVLPLDRCLPFLISVDGESSNYINAALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDTAQLCMQYWPEKTSGCYGPIQVEFVSADIDEDIIHRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSLLKAVRRLEKWQEEYDGREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTLRNNKSNMVETLEQYKFVYEVALEYLSSF
Protein: NAD(P)-linked oxidoreductase superfamily protein (Q8VZ23)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- NAD
- At2g21260
- Aldo-keto reductase family 4 member C10
- NAD
- Aldo/keto reductase family protein
- Aldo/keto reductase
- Nuclear pore complex protein NUP107
Sequence:
MASSYVTYSTVTPVVSSSNIRGVFRLAFTRRRVTLSPNARRRILRVSAKASTKNAMEYRKLGDSDLNISEVTMGTMTFGEQNTEKESHEMLSYAIEEGINCIDTAEAYPIPMKKETQGKTDLYISSWLKSQQRDKIVLATKVCGYSERSAYIRDSGEILRVDAANIKESVEKSLKRLGTDYIDLLQIHWPDRYVPLFGDFYYETSKWRPSVPFAEQLRAFQDLIVEGKVRYIGVSNETSYGVTEFVNTAKLEGLPKIVSIQNGYSLLVRCRYEVDLVEVCHPKNCNVGLLAYSPLGGGSLSGKYLATDQEATKNARLNLFPGYMERYKGSLAKEATIQYVEVAKKYGLTPVELALGFVRDRPFVTSTIIGATSVKQLKEDIDAFLMTERPFSQEVMADIDAVFKRFKDPSFV
Protein: Suppressor of zyg-1 protein 20 (G5EGU9)
Organism: Caenorhabditis elegans
Function: RNA binding protein that is required for normal cell division and cytokinesis during embryonic development. Functions with RNA-binding protein atx-2 to ensure embryonic cell division, and to this end, plays a role in the regulation of centrosome assembly, position and size, and in astral microtubule outgrowth and nucleation. Furthermore, negatively regulates the levels of the protein kinase zyg-1 at the centrosome. Also involved in ensuring centrosome attachment to the nuclear envelope.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:27689799}. Note=Co-localizes with atx-2 in the cytoplasm. {ECO:0000269|PubMed:27689799}.; SUBCELLULAR LOCATION: [Isoform f]: Cytoplasm {ECO:0000269|PubMed:19081077}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:19081077}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:19081077}. Nucleus, nucleolus {ECO:0000269|PubMed:19081077}. Chromosome {ECO:0000269|PubMed:19081077}. Note=Co-localizes with sas-4 at centrioles. Localizes to nucleoli during interphase and to the surface of chromosomes during meiosis and mitosis. Localizes in puncta adjacent to the male pronucleus at the centrosome during meiosis. Localization at the centrosome peaks at prometaphase and metaphase, but then decreases and expression is at its most minimal during interphase. {ECO:0000269|PubMed:19081077}.
Interaction partners:
- Probable serine/threonine-protein kinase zyg-1
- Spindle assembly abnormal protein 4
- Spindle assembly abnormal protein 6
- Spindle-defective protein 2
- Spindle-defective protein 5
- Spindle assembly abnormal protein 5
Sequence:
MSKENVVADSWDDADADPVKELMDKVEKVKLLQRKEEKKEAFFEKVKAEESSGVVSKLQTEEGLGPSAEEPKRVFLRRPKDGFAASENVIEASPPTSADTEEQPVTNVRSRSHHKLNQKEKQPAPTYEERQAAYQAARNRILGTEYKPDNQEIKEIKFIDRSKSPETLKMTQQNMVEHYGEELSRELMEQPAEIVPPERQYTPDFTQPPPSVSESGGVYNGPPGFQQKQPNFQPTLQQQSLHQQQYLDNQYMMQMNVQIPIQYHNQTQHQFVPHEASAISTTSQNSNGDGQNDQAIYYYQAPTQQPMNYIPYNLPNMAYPPPNFQPQGQLHHQMNAGQLHQIQQQQQQCQQIQHQPPQQHQQVINGQVMNQQNQRNQVNSYPQQNGAGRGQNRQPMMYQMPCNSGPTAKPPPLMNQMQNRCMTNNGQNYQNRNMQQQGQQRSYSSQPQNGQFYQNGNSNQNNPNNGRKQQHQPQQQQNKSGKFGQNRNDMQKNNYQPNLQQPPMSQNPIPFGCPPRNVNAIREQHANNGSPNTGAGILGPHPMMSASQWPALQQNRPQ
Protein: Uncharacterized protein At5g25580 (Q84JN0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- PHD finger family protein
- DDT domain-containing protein DDR4
- DDT domain-containing protein PTM
- DDT domain-containing protein
- WD-40 repeat-containing protein MSI3
- AT5g38690/MBB18_24
- Zinc-finger domain of monoamine-oxidase A repressor R1 protein
- PHD-finger and DNA binding domain-containing protein
- Homeobox-DDT domain protein RLT2
- Homeobox-DDT domain protein RLT1
Sequence:
MVTLRQRTMVVTGEPEQKKEEERLCEDLTILSSDSDNDSSSDSAVKHLRGRWELASVLNFFNVFGPLVSEKLKFTAEEIEMGLIESNTTNAQLHIALLKGIPPVNKTLDDANAWITVLCKKLAPWWPWIAKGEIHITVNKGEEISEYQGLDSINRLKILKALCELRVQQDDARSYIQENTKEGDWDSSLRKRKLGGDGKKTSYWFDGNDIQGYRLYREVNGISKKNAGSDLSCLSWETEATNLDEFQSVARELSSSKASSLAATGQMIETEAIPVVEKYHKKRERAIKKKMKEEMVVNVNFSRPLRTTRSCRNHMPATYTFDEYDKMISDAVEETEDTDGDEVEGRDQQSASLDSNDKSTEVEAAEIHNDDDKENEISKEDAEPKEEFGAKNRLRQRVTRNSAIC
Protein: Small GTP-binding protein Rab1, putative (D6XMQ7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Vacuolar protein sorting 33, putative
- Trafficking protein particle complex subunit
- Rab GDP dissociation inhibitor
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit
- Transport protein particle
- Uncharacterized protein
- Transport protein particle
- Trafficking protein particle complex subunit
- TBC1 domain family member 7
Sequence:
MSTEYDHLFKLLLIGDSGVGKSCLLLRFADDSYTESYISTIGVDFKIRTLDIDGKVIKLQIWDTAGQERFRTITSSYYRGAHGIIIVYDTTDMESFNNVKTWLSEIDKFASENVNKLLVGNKCDLVTKKAVDTQMAQEFADSLGIPFLETSAKESSNVETAFIEMAKNIKKRVAAQGANSGATAGGRPLLTGNNRPATNSGGQKSGCC
Protein: NOSA (U box domain-containing protein) (O44007)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Ubiquitin fusion degradation protein 1 homolog
- UV excision repair protein RAD23 homolog
- HECT-type E3 ubiquitin transferase
- Nuclear protein localization protein 4 homolog
- Ubiquitin thioesterase OTU1
- Ubiquilin
- NSFL1 cofactor p47 homolog
- Coronin-A
Sequence:
MKKMFLKFRGGGDDDGDDDNNNNDENNNNNDSNKDKMETDEQALAEERRRKRLEKFQINDEELIAAAAAQQQLQQQQQQSQQSQQQQKGNTSPVRTPNTTTTTTTTTTSPLKPVTPTPITTNKPVTPTPITTNKPVAPAPTTKDSIRQCDIPMTESNYYVLEKIFLIYLQPNNNLPEKSIYLPSVNEQIKEEIKDGQLKLDKPVLDRILVERLSTKVQGVPAVEYLISCFNRIQQTIKKKMAIDQQILKDSTELVLLYFGLVLTIPDMFQNTSSSYGIGPVQLMPYLCGETTEELTDEFIFKFLSEYQEDLTPIFEPIFLDLIKILSTTTLTGNVFPYYKVFSRLVQFKAVSDLVVTLQCWNSPNFNGKEMERNTILGSLFSPSSASDDGSTIKQYFSNASTMNKNTIGDAFISIRQIQMNIHNGLVDLLKGFLKVQQENKEAFLSWLASAVEKNLERNKLQVDRTKACSDGFALNLCAVLVLLCEAFVDIDCSKVSMVDTNFLLSGKRHDITKDTRLCATSEEADQWVKDGTIEKPLAHTNFITETFFSTLRALHIGINSTYEKLKLIGRNLQDIENNKRVLLDSKIKWQNTPQGRLFEGQLDLLTKKEDMLKGITYTIDAQLFEPTFLQKTASFLLFATNWILKVINPKNTPLPLPLPAPPQFAALPEFCIEDIVDFFTFVITNFSQVLQYIKLEQLMKFFITILATPEYVKNPYLKAKIIEIISQFVPSKYSKGNPILLECNQDVKDHMVLALMRFYVDIEFTGGHNQFYEKFSYRHYSSLILKYLWSIPDFRKKFTETPKDPIFIKFINMLINDSIYVLDEALAKLAKIKENQTLFDDPNWDKDLTPEQRKEKIEQNDLNERICKSNLSLANSNIDMMLFLSSDKTIISGFMRPELIDRISAMMNYFLALIVGPKCTNLKVREPEKYHFNPKVLLNQLTEIYVNFGRDPRFLQSVVRDGRSFKNSLFQTCEKILQRERLKNDHELDEFSKLVIKLEQVAKEEEQAEEDLGDIPDEFCDPILSTLMTDPVILPSSKTVIDRQTILRHLLSDQTDPFNRSHLTPEMLIDDVETKKKIDEWLASKKKQ
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q5U0E6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAHSPVQSGLPGMQNLKADPEELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSALDLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRNTFVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEGNYSKPLKEFVEACLNKEPSFRPTAKELLKHKFILRNAKKTSYLTELIDRYKRWKAEQSHDDSSSEDSDAETDGQASGGSDSGDWIFTIREKDPKNLENGALQPSDLDRNKMKDIPKRPFSQCLSTIISPLFAELKEKSQACGGNLGSIEELRGAIYLAEEACPGISDTMVAQLVQRLQRYSLSGGGTSSH
Protein: Protease Do-like 1, chloroplastic (EC 3.4.21.-) (Protein DEGRADATION OF PERIPLASMIC PROTEINS 1) (DEGP PROTEASE 1) (O22609)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine protease that is required at high temperature. May be involved in the degradation of damaged proteins. In vivo, can degrade beta-casein.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:21877139, ECO:0000269|PubMed:9507020}; Peripheral membrane protein {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:9507020}; Lumenal side {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:9507020}.
Interaction partners:
- Protease Do-like 7
- ATP-dependent zinc metalloprotease FTSH 1, chloroplastic
- UPF0603 protein At1g54780, chloroplastic
- Putative protease Do-like 6, chloroplastic
- Putative Do-like 15 protein
- ATP-dependent zinc metalloprotease FTSH 5, chloroplastic
- ATP-dependent zinc metalloprotease FTSH 8, chloroplastic
- Putative protease Do-like 11, mitochondrial
- ATP-dependent Clp protease proteolytic subunit 3, chloroplastic
- Putative protease Do-like 12, mitochondrial
Sequence:
MATTTSCSLLLSSTLFLHSPPSSHLSFFNLSSSRSSPISLYPIRSKRYFRILSKLSLNDNNRDDDDDTLHFTPFSAVKPFFLLCTSVALSFSLFAASPAVESASAFVVSTPKKLQTDELATVRLFQENTPSVVYITNLAVRQDAFTLDVLEVPQGSGSGFVWDKQGHIVTNYHVIRGASDLRVTLADQTTFDAKVVGFDQDKDVAVLRIDAPKNKLRPIPVGVSADLLVGQKVFAIGNPFGLDHTLTTGVISGLRREISSAATGRPIQDVIQTDAAINPGNSGGPLLDSSGTLIGINTAIYSPSGASSGVGFSIPVDTVGGIVDQLVRFGKVTRPILGIKFAPDQSVEQLGVSGVLVLDAPPSGPAGKAGLQSTKRDGYGRLVLGDIITSVNGTKVSNGSDLYRILDQCKVGDEVTVEVLRGDHKEKISVTLEPKPDES