wanglab/gogpt-training-data huggingface dataset:
Protein: Integral membrane bound transporter domain-containing protein (Q4GYI9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- 50S ribosomal protein L7Ae, putative
- Centromere/microtubule binding protein cbf5, putative
- Nucleolar protein 10
- Guanine nucleotide-binding protein subunit beta-like protein
- Nucleolar RNA binding protein, putative
- H/ACA ribonucleoprotein complex subunit 2
- Uncharacterized protein
- Nucleolar protein 56
- Fibrillarin, putative
- Fibrillarin, putative
Sequence:
MSDDSATGNLGSPTRLGGSSSPPAFSVSCDNGVSDTRLASSGRCNIDPSRSAAIERFLLGAQTTTAPPLGGGLATSVASTSAPGGDYIRGPQSAVDNVSFVSVKHPESADAPLSEPKPAASPKNTFTVAKSSGTVVGRSSRLGEKSLEPSAGAEAKIKSPKEIPPEAEPRGRTPPSRGRVKLVLDTPVQLRSPVSERSPTPPVEVRSALAQPRTTTLTKCSSVGRPAAVFYGSPDGTRKCGIKRTKSLGDLSQALLRGDRAADVSEWLAECSSHRRADRSAASVAGSGVYQRGSGFSEFVSLGPVTARSDRGGKSGVRTQLRAVDRVRRGEDLSRADAHFDPSPGLGRGGRHEWQRGGFARGRFAEDRAYGHVGPGSPGLQSHASAPQLPYFGGMRGAERDMDTSIGGRSLGAPSVHGAMSDQFVGQHIRVRATSVTRAARPESPTTAFTPGTQGSGFASPGVGGKGSQPSPSHVAASNLGQAHPPVGQATHAERMFMSLIADRSRERRQHFQRTPSTFSLPVNCSTDVSPVRDLSSPGSFQSPSVCHGASGGGVGGGGKGGDGSGGGGGKGGGGGGDRGGNKKGGRAGKVASSAGDEEENEERQYKERSCTALHSIPWDQRAFLPVGGFGMKRFSIFSAPLFWEKLDWTVRASLFTVLPLMILTLEPKTEHIFPMPSSVAFLAFWISMPTFGSGLREFIIALKGYALSLLLLLFVVLVDPQSTWLILLLLFIFVLSTAFFAEELKKTCAYCLTVFLMERQAKPAETGIEFVKDYFITLLIALAFGLAAFFIPSIRWSSDLAKAKVSFLGNSLSIFVQGTCSSFWTRSPLERELHILRLRQLQFTAKKAADKAREFLEEADYEPHTGHQMEGIKQRLDFFTNMHGILSSMVQVVELVNDDPGRIETPVCISFGEAIEEDLAIISSAMDSTILKISDFKNGVNEEDIHLFCEARERFQDRLAEVRQQVILNNEMYETGESDVLLGFFMFSVDELCEVISSFNPSIEAKSRFLSLSREFLSSFKSPYEALRRLVMTIIHRRTITRRAKEAIKLALCMTLPSIFQVYALDNNATSPVAGAAIIAFVYSSTGAQSFTYAVNRVLGTVLGSLCALIAVQVADGRRLVLYVAVAIISFLGAYVQTSKEYYAAGNAICNSVISVITQYKNSEAAMVRIQQNLFAIIIYFCITMVLWPMRARNKVYMSFDISLRCFREATCRLLRNLDMPEDVNEVDATTTEALAQWNKKISRQAFFLPGAATEPTLVGASFPEPAWSRLIDVQWKLWAIVSMMRFAYVTFMASKVDDETELSVHWVVLRRISPFAKDMCDLLYATVDLCLLILNKTAIVPSAHLTRLRHGMLDAEHSIVETYIQTLAHKIAGDGGSANNSCSDMGSGPGGGSDGVSSHLDMHSPRGVSHPDSGVAQRRRKPRVTDGYFVYNVTEEEEELMRTFRNRTCNARQLTQTCDNDSHGGRSDNGSDGDGGRKPGHRKGSDSSRDVRTPDKDDGNGSGNKSFEKAEDIEEITHEHGEKGGVRRALRQLLRRRTTGRPSDAETDRRKEASSNAPAVAACHSQTDEAADVHNSDDDVEPLVKGPRRDRKKEGGERLYSESEVTLVHSQSDNSQVETREYTMEKSSKAGKQLEKQSKNETLRPSAAAAASPAPAADICTRSEDGSSSHSVGGDGVFPACSFFDAKEKELVLSNRDIHSLEAFLFGVRALTVQLGDLQKALLEMVHSNELEKTM
Protein: Metallo-hydrolase/oxidoreductase superfamily protein (Q9C535)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Vacuolar protein sorting-associated protein 32 homolog 1
- Vacuolar protein sorting-associated protein 32 homolog 2
- At2g14110 superfamily protein)
- Protein SUPPRESSOR OF K
Sequence:
MALVVSGGKAAMMPLHANSLPLSINTKSRVLSASAFPLFSSTPHLPSRSLSIRLSPNVSRSLTVVSSVLSEDRATNVSGSGTDAFKLTYLEGNSWLWETAGLKILVDPILVGNLDFGIPWLYDAAKRYLKAFKLDDLPEVDCLLITQSLDDHCHLNTLRPLSEKSPGIKVIATPNAKPLLDPLFSNVTYLEPGDSFELNARNGSKVRVKATAGPVLGPPWQRPENGYLLVSPEDQISLYYEPHCVCNMELLKNERADIVITPVIKQLLPRFTLVSGQEDAVQLAKLLKAKFVVPMQNGELEAKGLLASLVKKEGTIESFKELLLKELPEAQVLEPIAGIPLEILVPSSDI
Protein: Ras GTPase-activating-like protein IQGAP1 (p195) (P46940)
Organism: Homo sapiens (Human)
Function: Plays a crucial role in regulating the dynamics and assembly of the actin cytoskeleton. Binds to activated CDC42 but does not stimulate its GTPase activity. It associates with calmodulin. Could serve as an assembly scaffold for the organization of a multimolecular complex that would interface incoming signals to the reorganization of the actin cytoskeleton at the plasma membrane. May promote neurite outgrowth. May play a possible role in cell cycle regulation by contributing to cell cycle progression after DNA replication arrest.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15355962, ECO:0000269|PubMed:29033352}. Nucleus {ECO:0000269|PubMed:20883816, ECO:0000269|PubMed:29033352}. Cytoplasm {ECO:0000269|PubMed:20883816, ECO:0000269|PubMed:29033352}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9JKF1}. Apical cell membrane {ECO:0000269|PubMed:35601831}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q9JKF1}. Note=Subcellular distribution is regulated by the cell cycle, nuclear levels increase at G1/S phase (PubMed:20883816). {ECO:0000269|PubMed:20883816}.
Interaction partners:
- Cell division control protein 42 homolog
- Catenin beta-1
- CAP-Gly domain-containing linker protein 1
- Cadherin-1
- Calmodulin-1
- Calmodulin-like protein 3
- Calmodulin-like protein 5
- Calmodulin-like protein 6
- Calmodulin-like protein 4
- Mitogen-activated protein kinase 1
Sequence:
MSAADEVDGLGVARPHYGSVLDNERLTAEEMDERRRQNVAYEYLCHLEEAKRWMEACLGEDLPPTTELEEGLRNGVYLAKLGNFFSPKVVSLKKIYDREQTRYKATGLHFRHTDNVIQWLNAMDEIGLPKIFYPETTDIYDRKNMPRCIYCIHALSLYLFKLGLAPQIQDLYGKVDFTEEEINNMKTELEKYGIQMPAFSKIGGILANELSVDEAALHAAVIAINEAIDRRIPADTFAALKNPNAMLVNLEEPLASTYQDILYQAKQDKMTNAKNRTENSERERDVYEELLTQAEIQGNINKVNTFSALANIDLALEQGDALALFRALQSPALGLRGLQQQNSDWYLKQLLSDKQQKRQSGQTDPLQKEELQSGVDAANSAAQQYQRRLAAVALINAAIQKGVAEKTVLELMNPEAQLPQVYPFAADLYQKELATLQRQSPEHNLTHPELSVAVEMLSSVALINRALESGDVNTVWKQLSSSVTGLTNIEEENCQRYLDELMKLKAQAHAENNEFITWNDIQACVDHVNLVVQEEHERILAIGLINEALDEGDAQKTLQALQIPAAKLEGVLAEVAQHYQDTLIRAKREKAQEIQDESAVLWLDEIQGGIWQSNKDTQEAQKFALGIFAINEAVESGDVGKTLSALRSPDVGLYGVIPECGETYHSDLAEAKKKKLAVGDNNSKWVKHWVKGGYYYYHNLETQEGGWDEPPNFVQNSMQLSREEIQSSISGVTAAYNREQLWLANEGLITRLQARCRGYLVRQEFRSRMNFLKKQIPAITCIQSQWRGYKQKKAYQDRLAYLRSHKDEVVKIQSLARMHQARKRYRDRLQYFRDHINDIIKIQAFIRANKARDDYKTLINAEDPPMVVVRKFVHLLDQSDQDFQEELDLMKMREEVITLIRSNQQLENDLNLMDIKIGLLVKNKITLQDVVSHSKKLTKKNKEQLSDMMMINKQKGGLKALSKEKREKLEAYQHLFYLLQTNPTYLAKLIFQMPQNKSTKFMDSVIFTLYNYASNQREEYLLLRLFKTALQEEIKSKVDQIQEIVTGNPTVIKMVVSFNRGARGQNALRQILAPVVKEIMDDKSLNIKTDPVDIYKSWVNQMESQTGEASKLPYDVTPEQALAHEEVKTRLDSSIRNMRAVTDKFLSAIVSSVDKIPYGMRFIAKVLKDSLHEKFPDAGEDELLKIIGNLLYYRYMNPAIVAPDAFDIIDLSAGGQLTTDQRRNLGSIAKMLQHAASNKMFLGDNAHLSIINEYLSQSYQKFRRFFQTACDVPELQDKFNVDEYSDLVTLTKPVIYISIGEIINTHTLLLDHQDAIAPEHNDPIHELLDDLGEVPTIESLIGESSGNLNDPNKEALAKTEVSLTLTNKFDVPGDENAEMDARTILLNTKRLIVDVIRFQPGETLTEILETPATSEQEAEHQRAMQRRAIRDAKTPDKMKKSKSVKEDSNLTLQEKKEKIQTGLKKLTELGTVDPKNKYQELINDIARDIRNQRRYRQRRKAELVKLQQTYAALNSKATFYGEQVDYYKSYIKTCLDNLASKGKVSKKPREMKGKKSKKISLKYTAARLHEKGVLLEIEDLQVNQFKNVIFEISPTEEVGDFEVKAKFMGVQMETFMLHYQDLLQLQYEGVAVMKLFDRAKVNVNLLIFLLNKKFYGK
Protein: Uncharacterized protein YER034W (P40022)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Putative zinc metalloproteinase YIL108W
- Succinate dehydrogenase assembly factor 4, mitochondrial
- Protein BOP3
Sequence:
MDAFSLKKDNRKKFQDKQKLKRKHATPSDRKYRLLNRQKEEKATTEEKDQDQEQPALKSNEDRYYEDPVLEDPHSAVANAELNKVLKDVLKNRLQQNDDATAVNNVANKDTLKIKDLKQMNTDELNRWLGRQNTTSAITAAEPESLVVPIHVQGDHDRAGKKISAPSTDLPEELETDQDFLDGLL
Protein: Carmine, isoform A (Carmine, isoform B) (Clathrin-associated adaptor complex AP-3 medium chain) (LD09732p) (Mu3 subunit of clathrin-associated protein complex AP-3) (O76928)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
- Adaptor protein complex AP-3 small chain sigma3
- AP-3 complex subunit beta
- AP-3 complex subunit delta
- AP-1 complex subunit gamma
- AP-2 complex subunit alpha
- AP complex subunit sigma
- AP complex subunit sigma
- AP complex subunit beta
- Adaptor protein complex 1, mu subunit
- Non-lysosomal glucosylceramidase
Sequence:
MIHSLFIVNSGGEVFLEKHWRSVVSRSVCEYFLDAQRAAPYDVPPVIATPHYYLITVQRDTVSLVAACKQEVPPLFVIEFLHRVVDTFQDYFGDCSESVIKDNYVVVYELLDEMLDNGFPLATESNILKELIKPPNILRTIANTVTGKSNVSTTLPSGQLSAVRWRRSGVRYTNNEAYFDVIEEVDAIIDKSGSTVFAEIQGHIDCCIKLSGMPDLTLSFMNPRLFDDVSFHPCVRYKRWEAERLLSFIPPDGNFRLMSYHISSQSVVAIPIYIRHNFSIKTGEQGRLDLTIGPRNTLGRTVDKVKLELTMPRCVLNCLLTPNQGKYTFDSVTKTLSWDVGRIDVSKLPNIRGSVSITPGTTNIDANPSVNVQFQISQLAVSGLKVNRLDMYGEKYKPFKGVKYLTKAGKFQVRM
Protein: Uclacyanin-2 (Blue copper-binding protein II) (BCB II) (Phytocyanin 2) (Uclacyanin-II) (O80517)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably acts as an electron carrier involved in oxygen activation and/or lignin formation.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
Sequence:
MAMNGLSKMAVAAATALLLVLTIVPGAVAVTYTIEWTTGVDYSGWATGKTFRVGDILEFKYGSSHTVDVVDKAGYDGCDASSSTENHSDGDTKIDLKTVGINYFICSTPGHCRTNGGMKLAVNVVAGSAGPPATPTPPSSTPGTPTTPESPPSGGSPTPTTPTPGAGSTSPPPPPKASGASKGVMSYVLVGVSMVLGYGLWM
Protein: Aldehyde dehydrogenase family 3 member B1 (EC 1.2.1.28) (EC 1.2.1.5) (EC 1.2.1.7) (Aldehyde dehydrogenase 7) (Long-chain fatty aldehyde dehydrogenase) (EC 1.2.1.48) (Medium-chain fatty aldehyde dehydrogenase) (P43353)
Organism: Homo sapiens (Human)
Function: Oxidizes medium and long chain saturated and unsaturated aldehydes. Metabolizes also benzaldehyde. Low activity towards acetaldehyde and 3,4-dihydroxyphenylacetaldehyde. May not metabolize short chain aldehydes. Can use both NADP(+) and NAD(+) as electron acceptor. May have a protective role against the cytotoxicity induced by lipid peroxidation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23721920}; Lipid-anchor {ECO:0000269|PubMed:23721920}. Note=Primarily in the plasma membrane as well as in some punctate structures in the cytoplasm.
Interaction partners:
- Aldehyde dehydrogenase family 3 member B2
- Catechol O-methyltransferase
- Amine oxidase [flavin-containing] A
- Amine oxidase [flavin-containing] B
- Aldo-keto reductase family 1 member A1
- Acetyl-coenzyme A synthetase, cytoplasmic
- Acetyl-coenzyme A synthetase 2-like, mitochondrial
- 4-aminobutyrate aminotransferase, mitochondrial
- Cytochrome P450 2E1
- Amine oxidase [copper-containing] 2
Sequence:
MDPLGDTLRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEVSEVAISQGEVTLALRNLRAWMKDERVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQYVDQSCFAVVLGGPQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGCGRVAIGGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGVGASGMGRYHGKFSFDTFSHHRACLLRSPGMEKLNALRYPPQSPRRLRMLLVAMEAQGCSCTLL
Protein: Ribosome production factor 2 homolog (Brix domain-containing protein 1 homolog) (Novel nucleolar protein 3) (Ribosome biogenesis protein RPF2 homolog) (Q9VEB3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for normal assembly of the mitotic spindle. May be involved in both centrosome-dependent and centrosome-independent spindle assembly programs.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:24255106}. Note=Found in the nucleolus during interphase. {ECO:0000269|PubMed:24255106}.
Interaction partners:
- Ribosome biogenesis regulatory protein
- Ribosome assembly factor mrt4
- Probable rRNA-processing protein EBP2 homolog
- RRM domain-containing protein
- Probable ribosome biogenesis protein RLP24
- Nucleolar GTP-binding protein 1
- Nucleolar GTP-binding protein 2
- Nucleolar complex protein 2
- Guanine nucleotide-binding protein-like 3 homolog
- Probable ATP-dependent RNA helicase pitchoune
Sequence:
MSLLRIRKPKTRKGKKVLLAREPQLIESARTMLFLDGRKCGGNVKLCMKDLQALKKPLVKVLNRKNDITPFDDPSSLEFLTMKNDAALFTFGSTSKKRPDNIILGRIFENEVLDMFELGIKRYQAISEFKNEKIGACVKPCLVFNGPKWAQTEELRRLRNLFIDTFQREKVDSIRLQGIEHVLSFTVTDDMNILMRSYRILLKKSGQRTPRIELEEIGPSADFSIRRTKIASEDLYKQARKQPKQLKVGKKKNISTDALGNTKGRVHLGKQQTGSIQTRRVKALRKTPEEKKENRQRKKVALKAAAAEALASQGNNPFSS
Protein: monodehydroascorbate reductase (NADH) (EC 1.6.5.4) (F4J849)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAEKSFKYIILGGGVSASILKTSDSVLVLLLLLSVRKVYLCKITCRWLIGYAAKEFANQGVQPGELAVISKEAVAPYERPALSKGYLFPEGAARLPGFHCCVGSGGEKLLPESYKQKGIELILSTEIVKADLSAKSLVSATGDVFKYQTLIIATGSTVLRLTDFGVKGADSKNILYLREIDDADKLVEAIKAKKGGKAVVVGGGYIGLELSAVLRINNLDVTMVFPEPWCMPRLFTADIAAFYETYYTNKGVKIIKGTVASGFTAQPNGEVKEVQLKDGRTLEADIVIVGVGAKPLTSLFKGQVEEDKGGIKTDAFFKTSVPDVYAVGDVATFPLKMYGDVRRVEHVDHSRKSAEQAVKAIKAAEGGAAVEEYDYLPFFYSRSFDLSWQFYGDNVGDSVLFGDSNPSNPKPRFGAYWVQGGKVVGAFMEGGSGDENKALAKVAKARPSAESLDELVKQGISFAAKI
Protein: RBBP7 protein (Retinoblastoma binding protein 7) (Q6FHQ0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MASKEMFEDTVEERVINEEYKIWKKNTPFLYDLVMTHALQWPSLTVQWLPEVTKPEGKDYALHWLVLGTHTSDEQNHLVVARVHIPNDDAQFDASHCDSDKGEFGGFGSVTGKIECEIKINHEGEVNRARYMPQNPHIIATKTPSSDVLVFDYTKHPAKPDPSGECNPDLRLRGHQKEGYGLSWNSNLSGHLLSASDDHTVCLWDINAGPKEGKIVDAKAIFTGHSAVVEDVAWHLLHESLFGSVADDQKLMIWDTRSNTTSKPSHLVDAHTAEVNCLSFNPYSEFILATGSADKTVALWDLRNLKLKLHTFESHKDEIFQVHWSPHNETILASSGTDRRLNVWDLSKIGEEQSAEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWVICSVSEDNIMQIWQMAENIYNDEESDVTTSELEGQGS
Protein: Mesoderm posterior ab (Mesp-ab) (I2AVV9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MEFNLPPYLLQAARCKLEPISSADCGYFSACGSLSPSSSIDSGCFSPPWGAGRQLEGPENANVDCLQAKKLKLALPVDSKRRSRSKNPGMKRQSASEREKLRMRDLTKALHHLRSFLPPSVAPAGQTLTKIETLRLAISYISHLSDQLRQAEVPNYEMCCSAEASDRFQSGLVFENVCMDGQQGLMQDNVQYCPTLTSFGDSREQMENSFPATSHFRDAQSYMFPCTTMDDASYSHQFYQ
Protein: Peroxisomal acyl-coenzyme A oxidase 1 (ACO) (AOX) (EC 1.3.3.6) (Palmitoyl-CoA oxidase) (Peroxisomal fatty acyl-CoA oxidase) (Straight-chain acyl-CoA oxidase) [Cleaved into: Peroxisomal acyl-CoA oxidase 1, A chain; Peroxisomal acyl-CoA oxidase 1, B chain; Peroxisomal acyl-CoA oxidase 1, C chain] (P07872)
Organism: Rattus norvegicus (Rat)
Function: Involved in the initial and rate-limiting step of peroxisomal beta-oxidation of straight-chain saturated and unsaturated very-long-chain fatty acids. Catalyzes the desaturation of fatty acyl-CoAs such as palmitoyl-CoA (hexadecanoyl-CoA) to 2-trans-enoyl-CoAs ((2E)-enoyl-CoAs) such as (2E)-hexadecenoyl-CoA, and donates electrons directly to molecular oxygen (O(2)), thereby producing hydrogen peroxide (H(2)O(2)).
Subcellular location: Peroxisome {ECO:0000269|PubMed:11872165}.
Interaction partners:
- Peroxisomal bifunctional enzyme
- Trifunctional enzyme subunit beta, mitochondrial
- Enoyl-CoA hydratase, mitochondrial
- Peroxisomal multifunctional enzyme type 2
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- Carnitine O-palmitoyltransferase 2, mitochondrial
- Trifunctional enzyme subunit alpha, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- Long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MNPDLRKERASATFNPELITHILDGSPENTRRRREIENLILNDPDFQHEDYNFLTRSQRYEVAVKKSATMVKKMREYGISDPEEIMWFKKLYLANFVEPVGLNYSMFIPTLLNQGTTAQQEKWMRPSQELQIIGTYAQTEMGHGTHLRGLETTATYDPKTQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITQGECYGLHAFVVPIREIGTHKPLPGITVGDIGPKFGYEEMDNGYLKMDNYRIPRENMLMKYAQVKPDGTYVKPLSNKLTYGTMVFVRSFLVGNAAQSLSKACTIAIRYSAVRRQSEIKQSEPEPQILDFQTQQYKLFPLLATAYAFHFVGRYMKETYLRINESIGQGDLSELPELHALTAGLKAFTTWTANAGIEECRMACGGHGYSHSSGIPNIYVTFTPACTFEGENTVMMLQTARFLMKIYDQVRSGKLVGGMVSYLNDLPSQRIQPQQVAVWPTMVDINSLEGLTEAYKLRAARLVEIAAKNLQTHVSHRKSKEVAWNLTSVDLVRASEAHCHYVVVKVFSDKLPKIQDKAVQAVLRNLCLLYSLYGISQKGGDFLEGSIITGAQLSQVNARILELLTLIRPNAVALVDAFDFKDMTLGSVLGRYDGNVYENLFEWAKKSPLNKTEVHESYHKHLKPLQSKL
Protein: Large ribosomal subunit protein uL16z (60S ribosomal protein L10-1) (Ribosomal protein RPL10A) (Suppressor of ACAULIS 52) (Q93VT9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ribosomal protein involved in translational regulation. Contribute to general translation under UV-B stress. Involved in the NIK1-mediated defense response to geminivirus infection. Acts coordinately with LIMYB as a transcriptional repressor.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19112492, ECO:0000269|PubMed:23886624}. Nucleus {ECO:0000269|PubMed:19112492, ECO:0000269|PubMed:23886624}. Note=Phosphorylation by NIK1 relocates the cytosolic protein to the nucleus. {ECO:0000269|PubMed:19112492}.
Interaction partners:
- Large ribosomal subunit protein eL8y
- Large ribosomal subunit protein uL4y
- Large ribosomal subunit protein uL23y
- Large ribosomal subunit protein uL10y
- Large ribosomal subunit protein uL24z
- Large ribosomal subunit protein uL10x
- Large ribosomal subunit protein uL22y
- Large ribosomal subunit protein eL38z/eL38y
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein uL1y
Sequence:
MGRRPARCYRQIKGKPYPKSRYCRGVPDPKIRIYDVGMKRKGVDEFPFCVHLVSWEKENVSSEALEAARIACNKYMVKSAGKDAFHLRIRVHPFHVLRINKMLSCAGADRLQTGMRGAFGKALGTCARVAIGQVLLSVRCKDAHGHHAQEALRRAKFKFPGRQKIIVSRKWGFTKFNRADFTKLRQEKRVVPDGVNAKFLSCHGPLANRQPGSAFLPAHY
Protein: Putative uncharacterized protein YJR120W (P47157)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Putative uncharacterized protein YOR186W
Sequence:
MRWDVIILYAISRPYATRRTGSHTHPRDSRYIAANQRRPPSACRVGPSPAKQRKDIPIFELLDTTLIKNALFALTSFLYYRTNILTCPFLNFLYLSRTGQLDKFCKDQTVTQILAT
Protein: GOLD domain-containing protein (Q57U42)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- GOLD domain-containing protein
- COP-coated vesicle membrane protein erv25, putative
- Cytosolic coat protein, putative
Sequence:
MNKMHILPPLLVVTALLFAYNTANAVTTAVAPREVFCVREVAPPHTRVTFQFNVMDADGREIRATLHDQNGTELTRWDSASTGNYDVPATVGATVAHACFENTESGGTPKRISFHFRFHVDYQSVAGPEALDPVESLVESVAKRMRDVEVKQKDLQAIQHTHLEIIGAAEWWLMLWSLFQVASLLLVSVFQLLFLKRFLERKSFV
Protein: ATP-binding cassette protein, putative (Q38AM7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MEGNGSSPCFTQFTDAEEEETSFLVKGPKQEDPASLGPEKPVALTFRNITYTVQGDKGRPKEILRGISGYVRGGELLALLGPSGAGKSTLLDIMAQRQKSGTIGGEVLLQGHPIHLGSFRRISAYVQQEDLLWPYLTVKESISYAAQLRTPPSFTRSVLETHIQRVMRLLGIDHVQNSRIGSQMVRGISGGEKKRCAIAMELVSQPSILFLDEPTTGLDTFTAQHLLTVLKEIAAGGVAVVFSIHQPRKSIFQLFDKLLLLTGSGEQAYFGPASAVMRFLEGVGVAPPQLDNPADVLLDAVALPPSEEFFKSGVGQNCALAMSRTCSGIVTAFHTSLLAVVEREIGAINERCSYGYDGLPGGDPSPYYRGITKQIYVVAWRAVLSKLRDSSAAVARIVAAAFFGTVIGSVYFQLGNDQLSIRNRMGSLFFVTMNTALSCLATLNLFIEERAIFVREHRAGMYCVLAYYIGKIVQDVPITVVTNLLFDIIVYFTMGLQQGVGKFLLFSCTCTFVVLNSYFLCLFLSSLSRNIQVANIVAPLVLVLLLLPSGGVLMGTQSLPFFWRWLKYVSFVRYGLAGLVVNEFDGLKFVCEPKVPFCFPDGATYARLQGYFPEELPEYIVACAASVAVYMVLAFFALLARAKYLQ
Protein: Prepilin peptidase PppA (Q46836)
Organism: Escherichia coli (strain K12)
Function: A pre-pilin peptidase involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of folded proteins across the outer membrane.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein.
Interaction partners:
- Lipoprotein YghG
- Putative lipoprotein AcfD homolog
- Type II secretion system core protein G
- Putative type II secretion system protein E
- Putative type II secretion system protein F
- Protein transport protein HofB homolog
- Protein transport protein HofC homolog
- Putative type II secretion system protein K
- Uncharacterized protein YggR
- Putative type II secretion system protein C
Sequence:
MLFDVFQQYPTAMPVLATVGGLIIGSFLNVVIWRYPIMLRQQMAEFHGEMSSAQSKISLALPRSHCPHCQQTIRIRDNIPLFSWLMLKGRCRDCQAKISKRYPLVELLTALAFLLASLVWPESGWGLAVMILSAWLIAASVIDLDHQWLPDVFTQGVLWTGLIAAWAQQSPLTLQDAVTGVLVGFITFYSLRWIAGIVLRKEALGMGDVLLFAALGGWVGALSLPNVALIASCCGLIYAVITKRGSTTLPFGPCLSLGGIATLYLQALF
Protein: Dual specificity mitogen-activated protein kinase kinase mek-1 (EC 2.7.12.2) (Q21307)
Organism: Caenorhabditis elegans
Function: Dual specificity protein kinase which may phosphorylate kgb-1 and thereby is an essential component of the JNK pathway composed of mlk-1, mek-1 and kgb-1. May also have a synergistic role with sek-1 in phosphorylating pmk-1. Involved in the response to environmental stress including heavy metal ions (Cu(2+) and Cd(2+)), oxidative stress and starvation. In association with sek-1, regulates germline cell apoptosis in response to oxidative, osmotic and heat shock stresses. Involved in resistance to pathogenic bacteria infection. Involved in axon regeneration after injury.
Interaction partners:
- GLH-binding kinase 1
- Stress-activated protein kinase jnk-1
- Stress-activated protein kinase JNK
- Mitogen-activated protein kinase kinase kinase dlk-1
- Mitogen-activated protein kinase pmk-1
- Mitogen-activated protein kinase kinase kinase zak-1
- Mitogen-activated protein kinase pmk-3
- Mitogen-activated protein kinase kinase kinase nsy-1
- Mitogen-activated protein kinase pmk-2
- Tyrosine-protein phosphatase vhp-1
Sequence:
MERDFDLGMGRPGGLGGLGGEPIMQQMPQPAPHHPSRSSNDHNVKNLMKQAEENSGYLTLQGNRRKADLKELQFVEDIGHGSCGTVTKCRYKSVIMAVKTMPRTSNSYEMSRILMDLDVICLSFDCPYIVRCFGYFITNFDVRVCMECMATCLDRLLIRIKQPIPERIIGKLSVSIIKALHYLKTKHQIMHRDVKPSNILLDWSGVIKLCDFGIAGRLIESRAHSKQAGCPLYMGPERLDPNNFDSYDIRSDVWSFGVTLVELATGQYPYAGTEFDMMSKILNDEPPRLDPAKFSPDFCQLVESCLQRDPTMRPNYDMLLQHPFVVHHEKIETDVEEWFADVMGECG
Protein: Protein virB8 (P17798)
Organism: Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Function: VirB proteins are suggested to act at the bacterial surface and there play an important role in directing T-DNA transfer to plant cells.
Subcellular location: Cell inner membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MKGSEYALLVARETLAEHYKEVEAFQTARAKSARRLSKVIAAVATIAVLGNVAQAFTIATMVPLIRLVPVYLWIRPDGTVDSEVSVSRLPATQEEAVVNASLWEYVRLRESYDADTAQYAYDLVSNFSAPMVRQNYQQFFNYPNPTSPQVILGKHGRLEVEHIASNDVTPGVQQIRYKRTLIVDGKMPMASTWTATVRYEKVTSLPGRLRLTNPGGLVVTSYQTSEDTVSNAGHSEP
Protein: Uncharacterized protein C4G3.03 (P87229)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MTVDNRCSNSSLCLRNVTPKQHPARVCSNHWQLKNLISTQNTGEESNPIYYTNSVFVWKIYPNSEKVVQVGQGLSFKPLSLLGKCGYIAAGGQLGEFDYWSPTSKQTHMKLCDQHNNGIEIHRRNCDSHAEALISSNDHTIKVVDLEHGLLRKQLHFPVNMNHASVSNDGRFMVCVGDSPQVFFYEIDRSGEYHLRHTTVADTTDSSFCTSISQRNELFAVASQDSSLSVFDVRYLRTPMLTKTSSRPDPNGSIRSCHFTPPNGGPLDLLLYSEGFSYSHLLDLRTGKDVELVLPSEDRFFSPASQDIFGSCFADDGSSVYVASATHLYEWNIDKRSRICFPSYQLL
Protein: Urokinase plasminogen activator surface receptor (U-PAR) (uPAR) (CD antigen CD87) (P49616)
Organism: Rattus norvegicus (Rat)
Function: Acts as a receptor for urokinase plasminogen activator. Plays a role in localizing and promoting plasmin formation. Mediates the proteolysis-independent signal transduction activation effects of U-PA.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:1321734}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:1321734}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305|PubMed:8307160}.
Interaction partners:
- Urokinase-type plasminogen activator
- Aa1018
- Plasminogen activator inhibitor 1
- Plasminogen
- Tissue-type plasminogen activator
- Glia-derived nexin
- Integrin beta-1
- Plasminogen activator
- Plasminogen activator inhibitor 2 type A
- Prothrombin
Sequence:
MGLLRRRLLLLVVVVTTCVPASQGLRCIQCESNQDCLVEECALGQDLCRTTVLREWEDAEELEVVTRGCAHKEKTNRTMSYRMGSVIVSLTETVCATNLCNRPRPGARGRPFPRGRYLECASCTSLDQSCERGREQSLQCRYPTEHCIEVVTLQSTERSVKDEPYTKGCGSLPGCPGTAGFHSNQTFHFLKCCNFTQCNGGPVLDLQSLPPNGFQCYSCEGNSTFGCSYEETSLIDCRGPMNQCLEATGLDVLGNRSYTVRGCATASWCQGSHVADSFQTHVNLSISCCNGSGCNRPTGGAPGPGPAHLILIASLLLTLRLWGIPLWT
Protein: Dynein light intermediate chain (G5ED34)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|RuleBase:RU366047}.
Interaction partners:
- WD_REPEATS_REGION domain-containing protein
- Dynein heavy chain, cytoplasmic
- Zygote defective protein 12
- Dynactin subunit 1
- Cytoplasmic dynein 2 heavy chain 1
- Cytoplasmic dynein 2 light intermediate chain 1
- DYnein Light chain
- Protein bicaudal D homolog
- Dynein light chain roadblock
- DYnein Light chain
Sequence:
MPPTAQPLEFDDTANAVLPVLYSSTDEEVGIWRELLASKKTNTNQGSTVIVLGDNRSGKSSLLSRLDKSDRTVKPKSLLGYRVLHVQNDARDASYAYQLGTAGANLNPSELLQIPVWSLDGNAACASLLKHALPATPAEAIFILTASIDNPNLIHSLKRWANVCTEQAQKHFTKEDLKAGRSQQEKMWQEYVDPVQSQMSTSVVGSFADEHNLLPLDQGTLTENCGVTFMVVITKSDLVLGKEFTDAQFAKISIQLRKFCLSLGATLVFTSAKETKNIQLLQKYIVHRSFGTAFTSAAQVIERESIFVPAGWDGEKKIDIIRESIPDVDSALEPTRDKLRPVAKEQLIEAEEDQAFLKKLMDILATSTTTAAPKPRTMQEEPTDKDSPLANFFSNLLNKDKPSKVSSPSTVSQPMDAAATQAQLDRLLKSAQSPKPQPRDSDA