wanglab/gogpt-training-data huggingface dataset:
Protein: Extracellular tyrosine-protein kinase PKDCC (EC 2.7.10.2) (Protein kinase domain-containing protein, cytoplasmic) (Protein kinase-like protein SgK493) (Sugen kinase 493) (Vertebrate lonesome kinase) (Q504Y2)
Organism: Homo sapiens (Human)
Function: Secreted tyrosine-protein kinase that mediates phosphorylation of extracellular proteins and endogenous proteins in the secretory pathway, which is essential for patterning at organogenesis stages. Mediates phosphorylation of MMP1, MMP13, MMP14, MMP19 and ERP29. Probably plays a role in platelets: rapidly and quantitatively secreted from platelets in response to stimulation of platelet degranulation. May also have serine/threonine protein kinase activity. Required for longitudinal bone growth through regulation of chondrocyte differentiation. May be indirectly involved in protein transport from the Golgi apparatus to the plasma membrane (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:25171405}. Golgi apparatus {ECO:0000250|UniProtKB:Q5RJI4}.
Interaction partners:
- Protein O-mannose kinase
- Extracellular serine/threonine protein kinase FAM20C
Sequence:
MRRRRAAVAAGFCASFLLGSVLNVLFAPGSEPPRPGQSPEPSPAPGPGRRGGRGELARQIRARYEEVQRYSRGGPGPGAGRPERRRLMDLAPGGPGLPRPRPPWARPLSDGAPGWPPAPGPGSPGPGPRLGCAALRNVSGAQYMGSGYTKAVYRVRLPGGAAVALKAVDFSGHDLGSCVREFGVRRGCYRLAAHKLLKEMVLLERLRHPNVLQLYGYCYQDSEDIPDTLTTITELGAPVEMIQLLQTSWEDRFRICLSLGRLLHHLAHSPLGSVTLLDFRPRQFVLVDGELKVTDLDDARVEETPCAGSTDCILEFPARNFTLPCSAQGWCEGMNEKRNLYNAYRFFFTYLLPHSAPPSLRPLLDSIVNATGELAWGVDETLAQLEKVLHLYRSGQYLQNSTASSSTEYQCIPDSTIPQEDYRCWPSYHHGSCLLSVFNLAEAVDVCESHAQCRAFVVTNQTTWTGRQLVFFKTGWSQVVPDPNKTTYVKASG
Protein: RuvB-like helicase 1 (EC 3.6.4.12) (Q9C0X6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: DNA helicase which participates in several chromatin remodeling complexes, including the SWR1 and the INO80 complexes. The SWR1 complex mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. The INO80 complex remodels chromatin by shifting nucleosomes and is involved in DNA repair. Also involved in pre-rRNA processing (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Chromatin-remodeling complex subunit ies6
- RuvB-like helicase 2
- Actin-like protein arp5
- TEL2-interacting protein 1
- Helicase swr1
- Actin-like protein arp6
- SWR1 complex subunit vps71
- SWR1-complex protein 4
- SWR complex protein 2
- Protein AF-9 homolog
Sequence:
MVQISEVKGNGRDNRITTHSHIKGLGLKEDGTCESVGGGFIGQEKAREACGIITDLIKSKKFGGKGVLFAGGAGTGKTALALAIAQELGPKVPFCPMVGSEVYSSEIKKTEALMENFRRAIGLRVKETKEVYEGEVTEMVPEEAENPLGGYGKTISHVLLGLKTHKGTKQLKLDPSIYESLQREQVSTGDVIYIEANTGAVKRVGRSDAYATEFDLEAEEYVPMPKGEVHKRKEIVQDVTLHDLDIANARPQGGQDIMSMMGQLMKPKKTEITDKLRGEINKVVNKYIEQGIAELIPGVLFIDEVHMLDIECFTYLNQALESTISPIVIFASNRGICTIRGTEDIQAPHGIPTDLLDRLLIVRTLPYSESEIRSILQIRAKVENIILTDECLDKLAQEGSRTSLRYVIQLLTPVSIIASLHGNKEIGVQDIEECNDLFLDARRSAQVVKSSSGFLQ
Protein: Uncharacterized calcium-binding protein C800.10c (Q9HGL2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Cytoskeletal protein syp1
- Epsin-1
- Probable clathrin heavy chain
- AP-2 complex subunit alpha
- Clathrin light chain
- Endocytosis protein end4
- AP-2 complex subunit mu
- Actin cytoskeleton-regulatory complex protein end3
- AP-2 complex subunit sigma
- Cell division control protein 42 homolog
Sequence:
MSLNLSAEEQTAFDQLFKIADKQDIGVITGEEAVPFLEKSGLAPQVLGQIWQIADAENRGFLTFSGFVIAMRLVALAQEKLPFDYKKSGKIPYFADIHISGVDSSKFVQLNRPNNVSSGDGSDGSFLPPISSDEMTRYQQMFTTVCPTDGLMDGDRASSIFGRAPLSTEILARVWNLVDTHKRGALDIREFNTGMHIINLLLNGSLKSPPVSISPSFIASAASTSSVSAPSQYPGLSRSPPVQAPNIPVSDPWAIPSQDLTSFCQLFSNVDKAHKGYVSGSEAYSFFLASKLPEDVLAQIWDLSDTNSNGKLNIGEFCISLYLIKLKLSGKELPKVLPSSMLSSVAPLMQKSKSVPTSIPSVVPANISSPNPNPTLAPNPTGPSRVTSGTEDLLSLDATPFSPTLAPQHTSSNATKHSAPPVTKSAPFPVVSPLQLNHTPGFPTSPAAKPNSPTSTFFPQSSFGQTIAKNTMDKPSAVRTSVPSQLAAPIPQVASAEQLKLAAEVPKLESQLSQVKKSNDDLQKSSRDVAANLSDVKAKVSEIRKAYDEELAKAKQISLDIETNKAQTEQVNREYSILEATLNALQKQNKQKGEVLEQVVAESEAAKNMVESSNASIQQLKSEVADKEQTLAQLHLQLDEMTQRLVSLDEESKAVSQRKLDLEYKINNSKTQLATATEEYHEHSKQLEAEKQELSKLEDGLKSVNLTEEAPKPEVDSTPRFPSFTSNGITTDKPTLPDTTSSVPTQHNSFDAMHNTLRSPSLNSNNSSAHASTVSRNPFHNLKISGASSPVSNFWESEFASAVFPRSISKTTSLSVNNSSVNPSLDSEPVQLSNMEEPQHQDSSVVDVSTSASQRGSPVLSDLSKLTGSARNTAEPVENTSAEPIENTSAPTPFEIANKQQATEPISAPFATETISTPAPVKPPVPPSRRDRSAQDGVVQQATPHIQDEFPPIQFNEIDDDESSSDEEPPMSNLSPQISIGSVTNYTSAVTELPDPNHQLEMSTTTHVQHPNSETIPSSTENQYFDTTSGAFEANSNTEVTVNSNEVSQPFDFDTANESDNDDDELPVQQVVSGSLANDAFNVDDEFDNQFANLQAAEIKDDDNSSTDEEEHAGHH
Protein: heparosan-N-sulfate-glucuronate 5-epimerase (EC 5.1.3.17) (A1Z6M8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase
- Heparan-sulfate 6-O-sulfotransferase
- Heparin sulfate O-sulfotransferase
- Extracellular sulfatase SULF-1 homolog
- Dally-like, isoform A
Sequence:
MSKYLSSQRDALSAPALPVSRENREPPKFQGVKQREPLVFFIMRLNLKAVLLVLTVAVVVITLGVYMRCAAFSFSPDFVRPLDRSARQSSSGGEATALHDIECSINQEYTVHCKRDENANEVYVPFSFLRNYFDVSGAVSTNSNEVAKFNWVHSTAKVNLPRGKYDARGVYMYFENYNVEVRDRVKCISAAEGVPVSTQWEKRGYFYPTQIAQFALSHYSKNLTEPAPRVRVLEDGDGNQMEWSTPKTSNMTRIWHHKFNTSVVQFETAPGYEGVISIALNQTLDLLLSVDLLLVTNSSSLMITVQNRDTRHNYSLHYIPADLLLSVQDTNIYYGLGGSALNKWRHITRDLHIDLQKGIMGDKRSPLKIRRSDLEVISIGFLGLGFFDNITLSTSDHLAHFYDAAEWFVHNQDPKTGGWTNPVRRSLNGFAELRPGWISAMGQGHAISVLARAYWHSGGDERYLRAAAAGLQPYRVYSRDGGVLAQFMDKFYWYEEYPTTPPSYVLNGFIYSLLGLYDLNSTAPGKIAREAGKLFAQGMHSLKKMLLLFDTGSGTSYDLRHLSLGVAPNLARWDYHATHVNQLLLLATIDSDPLIAQTAERWKGYMFGRRAKHN
Protein: Photoreceptor disk component PRCD (Progressive rod-cone degeneration protein) (Q00LT1)
Organism: Homo sapiens (Human)
Function: Involved in vision.
Subcellular location: Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:27613864}. Membrane {ECO:0000269|PubMed:27613864}; Lipid-anchor {ECO:0000269|PubMed:27613864}; Cytoplasmic side {ECO:0000250|UniProtKB:Q00LT2}. Endoplasmic reticulum {ECO:0000269|PubMed:24992209}. Golgi apparatus {ECO:0000269|PubMed:24992209}. Note=Localizes to photoreceptor disk membranes in the photoreceptor outer segment (PubMed:27613864). The secretion in media described in PubMed:24992209 is probably an experimental artifact (PubMed:24992209). {ECO:0000269|PubMed:24992209, ECO:0000269|PubMed:27613864}.
Interaction partners:
- Guanylyl cyclase-activating protein 2
- Photoreceptor cilium actin regulator
- Interphotoreceptor matrix proteoglycan 2
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha
- Cyclic nucleotide-gated channel beta-1
- Zinc finger protein 513
- Protein eyes shut homolog
- Ceramide kinase-like protein
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
- Isocitrate dehydrogenase subunit beta, mitochondrial
Sequence:
MCTTLFLLSTLAMLWRRRFANRVQPEPSDVDGAARGSSLDADPQSSGREKEPLK
Protein: NAD(P)H oxidoreductase RTN4IP1, mitochondrial (EC 1.6.5.2) (Reticulon-4-interacting protein 1 homolog) (dRtn4ip1) (Q8IPZ3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:37884807}.
Interaction partners:
- AT25567p
Sequence:
MTAAGFNSILCLRQLVRLNRRQYSAPAKSVLSGSQTNDQATPPPTSKSADKMRGWQLHNYGDIDELQLSEMLKIPQIRCSNECLVRIRATAVNPIDLAMLRGYGATVLNKMRCQPGDGIEFPLILGREFCGELVQTGMGVSLPLGSRVWGVVPLQATIGSHAEYVAVPSYCLAPAPKELDDYEAASVLYAGLTAWSGLYITGGLGGPCGATTASGGGAHKRVLVLGGSGGVGTLAIQILKSQKVQVLATCSENAIEMVRNLGADLVVDYNNPQAMEELCKYAPYDIVLDCAGQGGQKAAESKYDFRQYITFSSPLLANIDKQGLGVGALKNVFDLFQTNVRSVTQRGGLVKWGFFSPAPQGIQFLQKLVEQRKLMPLIDSSYGFSELPKAFEKMKSGHLRGKIVVKLREETGD
Protein: Protein Aster-B (GRAM domain-containing protein 1B) (Q3KR37)
Organism: Homo sapiens (Human)
Function: Cholesterol transporter that mediates non-vesicular transport of cholesterol from the plasma membrane (PM) to the endoplasmic reticulum (ER) (By similarity). Contains unique domains for binding cholesterol and the PM, thereby serving as a molecular bridge for the transfer of cholesterol from the PM to the ER (By similarity). Plays a crucial role in cholesterol homeostasis in the adrenal gland and has the unique ability to localize to the PM based on the level of membrane cholesterol (By similarity). In lipid-poor conditions localizes to the ER membrane and in response to excess cholesterol in the PM is recruited to the endoplasmic reticulum-plasma membrane contact sites (EPCS) which is mediated by the GRAM domain (By similarity). At the EPCS, the sterol-binding VASt/ASTER domain binds to the cholesterol in the PM and facilitates its transfer from the PM to ER (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30220461}; Single-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:30220461}; Single-pass membrane protein {ECO:0000255}. Note=In lipid-poor conditions localizes to the ER membrane and in response to excess cholesterol in the PM is recruited to the endoplasmic reticulum-plasma membrane contact sites (EPCS). {ECO:0000269|PubMed:30220461}.
Interaction partners:
- NPC intracellular cholesterol transporter 1
- GRAM domain-containing protein 2B
- Protein Aster-C
Sequence:
MKGFKLSCTASNSNRSTPACSPILRKRSRSPTPQNQDGDTMVEKGSDHSSDKSPSTPEQGVQRSCSSQSGRSGGKNSKKSQSWYNVLSPTYKQRNEDFRKLFKQLPDTERLIVDYSCALQRDILLQGRLYLSENWICFYSNIFRWETLLTVRLKDICSMTKEKTARLIPNAIQVCTDSEKHFFTSFGARDRTYMMMFRLWQNALLEKPLCPKELWHFVHQCYGNELGLTSDDEDYVPPDDDFNTMGYCEEIPVEENEVNDSSSKSSIETKPDASPQLPKKSITNSTLTSTGSSEAPVSFDGLPLEEEALEGDGSLEKELAIDNIMGEKIEMIAPVNSPSLDFNDNEDIPTELSDSSDTHDEGEVQAFYEDLSGRQYVNEVFNFSVDKLYDLLFTNSPFQRDFMEQRRFSDIIFHPWKKEENGNQSRVILYTITLTNPLAPKTATVRETQTMYKASQESECYVIDAEVLTHDVPYHDYFYTINRYTLTRVARNKSRLRVSTELRYRKQPWGLVKTFIEKNFWSGLEDYFRHLESELAKTESTYLAEMHRQSPKEKASKTTTVRRRKRPHAHLRVPHLEEVMSPVTTPTDEDVGHRIKHVAGSTQTRHIPEDTPNGFHLQSVSKLLLVISCVICFSLVLLVILNMMLFYKLWMLEYTTQTLTAWQGLRLQERLPQSQTEWAQLLESQQKYHDTELQKWREIIKSSVMLLDQMKDSLINLQNGIRSRDYTSESEEKRNRYH
Protein: Keratin, type I cuticular Ha6 (Keratin-36) (K36) (Keratin-5) (MHRa-1) (Type I keratin 48 kDa) (B1AQ75)
Organism: Mus musculus (Mouse)
Interaction partners:
- Keratin, type I cytoskeletal 14
- Loricrin
Sequence:
MATQICTPTFSAGSAKGLCGTSGSFSRISSIHSMGSCRAPSLVGTVGSVSSFRTGFSGPGSCLPGSYLSSGCHSSGFAGSGGWFCEGAFNGNEKATMQILNDRLANYLEKVRQLEQENTQLECRIREWYECQIPYICPDYQSYFKTAEELQQKILLTKSENARLILQIDNAKLAADDFRTKYETELSLRQLVEADINGLRRILDELTLCKADLEAQVESLKEELLCLKRNHEEEVNALRSQLGDRLNVEVDAAPPVDLNKILDDMRCQYETLVENNRRDVEAWFNTQTEELNQQVVSSSEQLQCCQTEIIELRRTVNSLEIELQAQQSMRNSLESTLAETEARYSSQLGQMQCLITNVESQLAEIRCDLERQNHEYQVLLDVKARLESEIATYRRLLDGEDCKLPAHPCSTECKPAVRVPYIPSTTCTPAGPCTPAGPCTPAPQVSTQIRTITEEIRDGRVISSREHVVPRAM
Protein: ESCRT-related protein CHMP1B (Protein CHARGED MULTIVESICULAR BODY PROTEIN 1B) (Protein CHROMATIN MODIFYING PROTEIN 1B) (Vacuolar protein-sorting-associated protein 46.2) (Q9SSM4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in ESCRT-dependent multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. Mediates the MVB sorting of the auxin carriers PIN1, PIN2 and AUX1. Required for embryonic axis establishment and seedling growth. Required for autophagic degradation of plastid proteins. Promotes the efficient sequestration of cargo from plastids into autophagosomes. Mediates the efficient delivery of autophagic plastid bodies to the vacuole, but not into the cytoplasm.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9HD42}. Endosome membrane {ECO:0000250|UniProtKB:Q9HD42}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9HD42}.
Interaction partners:
- Protein HOMOLOG OF MAMMALIAN LYST-INTERACTING PROTEIN 5
- Protein SUPPRESSOR OF K
- Vacuolar protein sorting-associated protein 2 homolog 2
- Vacuolar protein sorting-associated protein 32 homolog 1
- Vacuolar protein sorting-associated protein
- Vacuolar protein sorting-associated protein 2 homolog 1
- Vacuolar protein sorting-associated protein 60.2
- Vacuolar protein sorting-associated protein 24 homolog 1
- Vacuolar protein sorting-associated protein 32 homolog 2
- Vacuolar protein sorting-associated protein 2 homolog 3
Sequence:
MGNTDKLMNQIFDLKFTSKSLQRQSRKCEKEEKAEKLKVKKAIEKGNMDGARIYAENAIRKRSEQMNYLRLASRLDAVVARLDTQAKMTTITKSMTNIVKSLESSLATGNLQKMSETMDSFEKQFVNMEVQAEFMENAMAGSTSLSTPEGEVNSLMQQVADDYGLEVSVGLPQPAGHAIPTKTEEKVDEDDLSRRLAELKARG
Protein: Neural cell adhesion molecule 1 (A0A087X1V2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
TISWFRDGQLLPSSNYSNIKIYNTPSASYLEVTPDSENDFGNYNCTAVNRIGQESLEFILVQADTPSSPSIDQVEPYSSTAQVQFDEPEATGGVPILKYKAEWRAVGEEVWHSKWYDAKEASMEGIVTIVGLKPETTYAVRLAALNGKGLGEISAASEFKTQPVHSPPPREPSAPKLEGQMGEDGNSIKVNLIKQDDGGSPIRHYLVRYRALSSEWKPEIRLPSGSDH
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A8I6A623)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell projection, dendrite {ECO:0000256|ARBA:ARBA00004279}.
Interaction partners:
Sequence:
MSSRTALAPGNDRNSDTHGTLGSGRSSDKGPSWSSRSLGARCRNSIASCPEEQPHVGNYRLLRTIGKGNFAKVKLARHILTGREVAIKIIDKTQLNPSSLQKLFREVRIMKGLNHPNIVKLFEVIETEKTLYLVMEYASAGEVFDYLVSHGRMKEKEARAKFRQIVSAVHYCHQKNIVHRDLKAENLLLDAEANIKIADFGFSNEFTLGSKLDTFCGSPPYAAPELFQGKKYDGPEVDIWSLGVILYTLVSGSLPFDGHNLKELRERVLRGKYRVPFYMSTDCESILRRFLVLNPAKRCTLEQIMKDKWINIGYEGEELKPYTEPEEDFGDTKRIEVMVGMGYTREEIKEALTNQKYNEVTATYLLLGRKTEEGGDRGAPGLALARVRAPSDTTNGTSSSKGSSHNKGQRTSSSTYHRQRRHSDFCGPSPAPLHPKRSPTSTGDTELKEERLPGRKASCSAAGSGSRGLPPSSPMVSSAHNPNKAEIPERRKDSTSTPNNLPPSMMTRRNTYVCTERPGSERQSLLPNGKENSSGTSRVPPASPSSHSLAPPSGERSRLARGSTIRSTFHGGQVRDRRAGGGSGGGVQNGPPASPTLAHEAAPLPSGRPRPTTNLFTKLTSKLTRRVTLDPSKRQNSNRCVSGASLPQGSKIRSQTNLRESGDLRSQVAIYLGIKRKPPPGCSDSPGV
Protein: Mating-type M-specific polypeptide Mc (mat-Mc) (P0CY17)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. Positive regulator of MFM genes. The HMG box recognizes the DNA sequence 5'-AACAAAG-3'. Required for conjugation and efficient meiosis.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:16823372}.
Interaction partners:
- M-factor
- Mating-type M-specific polypeptide Mi
- Small ribosomal subunit protein eS21
- Silenced mating-type M-specific polypeptide Mi
- Putative protein disulfide-isomerase C1F5.02
- M cell-type agglutination protein mam3
Sequence:
MDSHQELSAGSPISYDFLDPDWCFKRYLTKDALHSIETGKGAAYFVPDGFTPILIPNSQSYLLDGNSAQLPRPQPISFTLDQCKVPGYILKSLRKDTTSTERTPRPPNAFILYRKEKHATLLKSNPSINNSQVSKLVGEMWRNESKEVRMRYFKMSEFYKAQHQKMYPGYKYQPRKNKVKR
Protein: Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex (EC 2.3.1.-) (F4J5T2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MVLPLFRRAAIARTSSLLRARLFAPASEFHSRFSNGLYHLDDKISSSNGVRSASIDLITRMDDSSPKPILRFGVQNFSSTAIRLTNTDVKWVIRIINGNFRLTCRKIEMLIDAGAKTSISLFSLMFVLPSYLRYSDRRCNQLYKILPLNYYFLWVVGPISQTVLAMPALSPTMSHGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSKDIPVNEPIAIMVEEEDDIKNVPATIEGGRDGKEETSAHQVMKPDESTQQKSSIQPDASDLPPHVVLEMPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKDVAVGKPIALIVEDAESIEAIKSSSAGSSEVDTVKEVPDSVVDKPTERKAGFTKISPAAKLLILEHGLEASSIEASGPYGTLLKSDVVAAIASGKASKSSASTKKKQPSKETPSKSSSTSKPSVTQSDNNYEDFPNSQIRKIIAKRLLESKQKIPHLYLQSDVVLDPLLAFRKELQENHGVKVSVNDIVIKAVAVALRNVRQANAFWDAEKGDIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEVKELAQKARSGKLAPHEFQGGTFSISNLGMYPVDNFCAIINPPQAGILAVGRGNKVVEPVIGLDGIEKPSVVTKMNVTLSADHRIFDGQVGASFMSELRSNFEDVRRLLL
Protein: Pre-mRNA-processing factor 39 (P39682)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Function prior to stable branch point recognition by the U1 snRNP particle to facilitate or stabilize the U1 snRNP/5'-splice site interaction. Has a direct role in the assembly or function of a catalytically active spliceosome.
Subcellular location: Nucleus.
Interaction partners:
- Protein NAM8
- Nuclear cap-binding protein subunit 2
- Pre-mRNA-processing protein PRP40
- Small nuclear ribonucleoprotein-associated protein B
- U1 small nuclear ribonucleoprotein component PRP42
- U1 small nuclear ribonucleoprotein C
- 56 kDa U1 small nuclear ribonucleoprotein component
- U1 small nuclear ribonucleoprotein component SNU71
- Protein LUC7
- U2 small nuclear ribonucleoprotein A'
Sequence:
MPDETNFTIEDIEPRPDALRGLDTQFLQDNTALVQAYRGLDWSDISSLTQMVDVIEQTVVKYGNPNDSIKLALETILWQILRKYPLLFGFWKRFATIEYQLFGLKKSIAVLATSVKWFPTSLELWCDYLNVLCVNNPNETDFIRNNFEIAKDLIGKQFLSHPFWDKFIEFEVGQKNWHNVQRIYEYIIEVPLHQYARFFTSYKKFLNEKNLKTTRNIDIVLRKTQTTVNEIWQFESKIKQPFFNLGQVLNDDLENWSRYLKFVTDPSKSLDKEFVMSVFDRCLIPCLYHENTWMMYIKWLTKKNISDEVVVDIYQKANTFLPLDFKTLRYDFLRFLKRKYRSNNTLFNNIFNETVSRYLKIWPNDILLMTEYLCMLKRHSFKNSLDQSPKEILEKQTSFTKILETSITNYINNQIDAKVHLQTLINDKNLSIVVVELIKTTWLVLKNNMQTRKYFNLYQKNILIKNSVPFWLTYYKFEKSNVNFTKLNKFIRELGVEIYLPTTVMNDILTDYKTFYLTHSNIVTYESSIIDSNTFDPILYPELKMSNPKYDPVLNTTANVDWHKKTEWKEAGHIGITTERPQISNSIIECNSGTLIQKPISLPNFRNLEKINQVKINDLYTEEFLKEGK
Protein: Keap1, isoform A (Keap1, isoform C) (Q9VEN5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSNTSESCSISCGGRFGSAHSTLDDHDATDDDMTFCMSNYAKEALKMMYMMRSHGMLTDVVLEVKKELFPAHKVVLSAASPYFKAMFTGGLKESEMSRVQLQGVCPTAMSRILYFMYTGQIRVTEVTVCQLLPAATMFQVPNVIDACCAFLERQLDPTNAIGIAHFAEQHGCVELQKKANVFIERNFTQVCQEEEFLQLSAYQLIALIRRDELNVQEEREVYNAVLKWVKYDEDNRHCKMEHILGAVRCQFLTPNFLKEQMKNCDVLRKVPACREYLAKIFKDLTLHKCPGVKERTPNTTRMIFVAGGFFRHSLDILEAYNVDDMTWTTLANLRIPRSGLGAAFLKGKFYAVGGRNNNIGSSYDSDWVDRYSAVTETWRPCAPMSVPRHRVGVAVMDELMYAVGGSAGMEYHNTVEYYDPDLDRWTLVQPMHAKRLGVGVVVVNRLLYAIGGFDGNERLASVECYHPENNEWSFLPPLQTGRSGAGVAAINQYIYVVGGFDGTRQLATVERYDTENDTWDMVAPIQIARSALSLTPLDEKLYAIGGFDGNNFLSIVEVYDPRTNTWTTGTPLKSGRSGHASAVIYQPACSTTFMDYEDSDAPHPDGSNNGERNAHTPQNTYGSGSPHYPGTASNMQFHTSYGMSGCNNCDSEMDIKPYIPAEHHSFQIPAIRSEELVNPNCPWSRMQERFRRTPPASFTDDERNANDMRHKLKKAQKECLFSTAAKVFHHHIEGRLRKLTSAAT
Protein: Guanine nucleotide-binding protein alpha-4 subunit (Q9BIG5)
Organism: Caenorhabditis elegans
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta-1
- Guanine nucleotide-binding protein subunit beta-2
- Guanine nucleotide-binding protein alpha-16 subunit
- Guanine nucleotide-binding protein subunit gamma
- G protein gamma domain-containing protein
- Probable glycylpeptide N-tetradecanoyltransferase
- Receptor-type guanylate cyclase gcy-27
- G Protein, Alpha subunit
- Tyrosine protein-kinase src-1
- Regulator of G-protein signaling 7
Sequence:
MGCFHSTGSEAKKRSKLIDEQLRHDHERCVGEIKLLLLGAGESGKSTIVRQMRILHETGFNKQEQMAYRPVVFSNMVQSMLAILKAMQPLNISFTDAAREEDARMFISHFLHVNNAELSEAFSLELSDLMKQLWMDEGVKKCVKRAHEYQLNDSAEYYFNALDRISSSSYLPTQDDILRARVKSTGIVETTFMYKDLCFKMFDVGGQRSERKKWIHCFDSVTAVIFCVALSEYDLRLAEDQTMNRMHESMQLFDSIVNNCWFTETSIILFLNKMDIFEERIRYTPLTVCFPEYQGGMTITETSTFIQSRFEILNKRQTPAQKEIYSHFTCATDTNNIRFVFDAVTDIIIRNNLYLCGLY
Protein: Proline-tRNA ligase (DUF1680) (Q9LXU4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein RALF-like 22
- Putative beta-glucosidase 41
- Protein BIIDXI
- BIIDXI-like protein At5g11420
- At4g12520
- Protein DUF642 L-GALACTONO-1,4-LACTONE-RESPONSIVE GENE 2
- Probable pectinesterase 48
- Signal peptide peptidase-like 3
- Peroxidase 69
- GDSL esterase/lipase 22
Sequence:
MKSGLIITIALLLYTSSFVLVSVAKECTNTPTQLSSHTFRSELLQSKNETLKTELFSHYHLTPADDSAWSSLLPRKMLKEEADEFAWTMLYRKFKDSNSSGNFLKDVSLHDVRLDPDSFHWRAQQTNLEYLLMLDVDGLAWSFRKEAGLDAPGDYYGGWERPDSELRGHFVGHYLSATAYMWASTHNDTLKEKMSALVSALSECQQKSGTGYLSAFPSSFFDRFEAITPVWAPYYTIHKILAGLVDQYKLAGNSQALKMATGMADYFYGRVRNVIRKYSVERHWQSLNEETGGMNDVLYQLYSITGDSKYLLLAHLFDKPCFLGVLAIQADDISGFHANTHIPIVVGSQQRYEITGDLLHKEISMFFMDIFNASHSYATGGTSVSEFWQDPKRMATALQTENEESCTTYNMLKVSRNLFRWTKEVSYADYYERALTNGVLGIQRGTQPGLMIYMLPLGKGVSKAVTYHGWGTPYDSFWCCYGTGIESFSKLGDSIYFQEDGATPALYVTQYISSSLDWKSAGLSISQKVNPVVSWDPYMRVTFTLSSSKVGVAKESTLNLRIPVWTNSIGAKVSLNGRPLNVPTSGNFLSIKQKWKSGDQVTMELPMSIRTEAIKDDRPEYASLQAILYGPYLLAGHTSRDWSITTQAKPGKWITPIPETQNSYLVTLSQQSGNVSYVFSNSNQTITMRVSPEPGTQDAVAATFRLVTDNSKPRISGPEGLIGRLVMLEPFDFPGMIVKQATDSSLTVQASSPSDKGASSFRLVSGLDGKLGSVSLRLESKKGCFVYSDQTLKQGTKLRLECGSDATDEKFKEAASFSLKTGMHQYNPMSFVMSGTQRNFVLSPLFSLRDETYNVYFSVQT
Protein: ATP synthase subunit b (Q08ET0)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|RuleBase:RU368017}. Mitochondrion inner membrane {ECO:0000256|RuleBase:RU368017}.
Interaction partners:
Sequence:
MLSRVVLSAAATAAPSLKNAAFLGPGVLQATRTFHTGQPHLVPVPPLPEYGGKVRYGLIPEEFFQFLYPKTGVTGPYVLGTGLILYALSKEIYVISAETFTALSVLGVMVYGIKKYGPFVADFADKLNEQKLAQLEEAKQASIQHIQNAIDTEKSQQALVQKRHYLFDVQRNNIAMALEVTYRERLYRVYKEVKNRLDYHISVQNMMRRKEQEHMINWVEKHVVQSISTQQEKETIAKCIADLKLLAKKAQAQPVM
Protein: Paxillin (P49024)
Organism: Gallus gallus (Chicken)
Function: Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion). Binds in vitro to vinculin as well as to the SH3 domain of c-SRC and, when tyrosine phosphorylated, to the SH2 domain of v-CRK.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:7525621}. Cell junction, focal adhesion {ECO:0000269|PubMed:7525621}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q8VI36}.
Interaction partners:
Sequence:
MDDLDALLADLESTTSHISKRPVFLTEETPYSYPTGNHTYQEIAVPPPVPPPPSSEALNGTVIDPLDQWQPSVSRYGHQQPQSQSPIYSSSAKSSSASVPRDGLSSPSPRASEEEHVYSFPNKQKSAEPSPTMTSTSLGSNLSELDRLLLELNAVQHNPPSGFSADEVSRSPSLPNVTGPHYVIPESSSSAGGKAAPPTKEKPKRNGGRGIEDVRPSVESLLDELESSVPSPVPAITVSQGEVSSPQRVNASQQQTRISASSATRELDELMASLSDFKFMAQGKAGGSSSPPSTTPKPGSQLDTMLGSLQSDLNKLGVATVAKGVCGACKKPIAGQVVTAMGKTWHPEHFVCTHCQEEIGSRNFFERDGQPYCEKDYHNLFSPRCYYCNGPILDKVVTALDRTWHPEHFFCAQCGVFFGPEGFHEKDGKAYCRKDYFDMFAPKCGGCARAILENYISALNTLWHPECFVCRECFTPFINGSFFEHDGQPYCEVHYHERRGSLCSGCQKPITGRCITAMGKKFHPEHFVCAFCLKQLNKGTFKEQNDKPYCQNCFLKLFC
Protein: Conserved protein (O53494)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable transmembrane protein FxsA
- Bifunctional apolipoprotein N-acyltransferase/polyprenol monophosphomannose synthase
Sequence:
MSQIPVKLLVNGRVYSPTHPEATAMAVRGDVVAWLGSDDVGRDQFPDADVQDLDGRFVAPGFVDSHIHLTATGLMLSGLDLRPATSRAQCLRMVADYAADHPGQPLWGHGWDESAWPENAAPSTADLDAVLGDCPAYLARIDSHSALVSSGLRRLVPELAAATGYTAQRPLTGDAHHLARAAARYLLTDVQLADARAVALQAIAAAGVVAVHECAGPEIGGLDDWLRLRALEHGVEVIGYWGEAVATPAQARDLVTETGARGLAGDLFVDGALGSRTAWLHEPYADAPDCIGTCHLDVDGIEAHVRACTKAEVTAGFHVIGDAAVSAAVAAFERVVADLGVVAVARCGHRLEHVEMVTADQAAKLGAWGVIASVQPNFDELWGGGDGMYARRLGAQRGSELNPLALLASQGVPLALGSDAPVTGFDPWASVRAAVNHRTPGSGVSARAAFAAATRGGWRAGGVRDGRIGTLVPGAPASYAIWDAGDFDVDAPRDAVQRWSTDPRSRVPALPRLGPTDALPRCRQTVHRGAVIYG