wanglab/gogpt-training-data huggingface dataset:
Protein: Pyruvate ferredoxin oxidoreductase, beta subunit (EC 1.2.7.1) (Q72BR4)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Pyruvate ferredoxin oxidoreductase, alpha subunit
- Pyruvate:ferredoxin oxidoreductase
- Pyruvate ferredoxin oxidoreductase, alpha subunit, putative
- Pyruvate ferredoxin oxidoreductase, gamma subunit, putative
- Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-binding domain protein
- Pyruvate ferredoxin/flavodoxin oxidoreductase family protein
- Pyruvate ferredoxin oxidoreductase, iron-sulfur binding subunit, putative
- Succinate--CoA ligase subunit alpha
- L-lactate dehydrogenase
- Pyruvate ferredoxin oxidoreductase, beta subunit, putative
Sequence:
MTTTIESLGTFETSWCPGCGNHDIMKALRQAIVGLGLEAHKVAHVSGIGQAAKAPHYIRLNGFNGLHGRSLPPAQAIRLCNSELTVIAQSGDGCNYGEGGNHFLAAIRRNVDMTLLVHDNQIYGLTKGQASPTTGEGQVTKSQPGGVTSAPFNPVAVAVAMRCGFVARSFSGNVEHLQAMIEAAVRHRGFSLVDIFSPCVSFNKVNTFGWYRQRCREIDASHDPTDWNAAMRIADTFGDVLPIGVIYRNERPPLDERVSHVAKGPLGRQAVRHDVLRDIMASYM
Protein: FERM and PDZ domain containing 1 (D3ZW88)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- G-protein signaling modulator 2
- F-box protein 10
- G-protein-signaling modulator 1
- DDB1- and CUL4-associated factor 10
- Family with sequence similarity 222, member A
Sequence:
MEELEGGLSQTRKAHRIEQMVARWLRRSRDSSARAKVAAADGPPGNPAQALTAVQHTVTLDKDVLLQNYGFHISETLPLTVVAVTAGGSAHGKLFPGDQILQMNKELAEDLSCERAVDILRETEDALSITVVRCTSGVPKSSFLTEEKRARLKTNPVKVHFAEEVLVSGHSQGNSLLCMPNVLKVYLENGQTKAFKFEANTTVKDIILTVKEKLSIRSIEYFALALEEQYSISRLHLLHEEELIQQVVEREESQDSRCLFRVCFVPKDPLDLLKEDPVAFEYLYLQSCSDVLQERFAVEMKCNSALRLAALHIQERIYACAQPQKISLKYIEKDWGIENFISPTLLRNMKGKDIKKAISFHMKRNQNLLEPRQKQLISAAQLRLNYLQILGELKTYGGKIFNATLMLQDRESYIALLVGAKYGISQIINSKLNIMSTLAEFANISRVELTEESEKVSVVKIYLQDVKVLTLLLESSSAKDLTCLIAGYYRLFVDPANPVFLWSGNRQQTHRVSAEEGYESRACSDSEESSEVDCVLEPLSDRCLVKLSLCRPFVREEQRPGDSPTPEVTRRGPSTCGASSMTDSAESEASDSANTESRGCRTSGSSESMDALEEDDLDACSSSGTSFFHFGPPGFSKDLDTNSQEENSRVETSGFLCLLDLAQNATSRCQKIEGPQSLASEACSWGPELSMGRLDPRLYEGSRTDYYSLCSSVSPGSHLSDSGSESTTSRQGAAPPPWCPQDWMETQSGSMLETLALPALPTLALEDGSSDEEYYDAADKLTPPDTLSGPRAADLSAMRLQSHSRTRGSEESLHPDPEGGEPSRQGGVKKYAKSPRKRRSFLQTDHTSQVSFPMEPSASQENMDDVCYYDREPYLSLTAPSPTVSSLQDMKSEPGLLETKALGLLASLRETKSKNPASRIMEMEPETMETKSVIDSRVSSISAIRLRIDPGNTENLEASPSAVTTDGSSASIPHNPHPSNPGSSSPQAAQVRPLQSISPGQDAGGTTPKGLTAEPQDSTFPLSSADPNPDTPGPHHAPQGDTSELEEVRSEMGSGSVLINHIQEVTPQIAGPLCPSDGPTTSGEHGVTSEEMALDAAEVRQENAPSLFHKGFGKDSGHFKGDGLDNIPQALDDANATTGEIGSSLCSEPPATGLGRISPNSEGENQVAQEQELLAELDLGPNFLLGEQTIQSAVLPELVEAEQLDHVIGEDSVPVDTSQQVCVHTVPPLPKLSPCQEEPRSADSGHGSPAESKGDSPITCLPPERSFLCFAPESQPESSNSLSRVTSFSFAGMNEVVPAGIGIEHCRCQFPYATCFRGLQPETEEEDGDPQSHPAAPLTSPPSAGSQVTLPWRAARAYSCTTPLPRKSHIWPEYCSRALRQLKTAPANAPEGFVQLTESLLELQDILEASWGVGNKHPPDKCTWHFSESRSRLCMGSQKLLSSCQHVIRMDQSPEEMQGAVRVTFQHLVQLAGLCFQFTDCSRCSTRHREVAGNLRDVVYTYHQFVEAAKLTCERGYHDLSVKLLARQCTALTAAVFCLTQKFRASTAL
Protein: Transcription factor STKL1 (Protein Storekeeper-like 1) (Q8LG05)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription repressor that binds DNA in a sequence-specific manner, 5'-GCCT-3', to regulate the expression of PGR. Acts as a modulatory component for the glucose-triggered developmental leaf growth process.
Subcellular location: Nucleus {ECO:0000269|PubMed:27031427}.
Interaction partners:
- Probable transcription factor At3g04930
- Transcription factor
- B3 domain-containing protein At5g60142
- Sequence-specific DNA binding transcription factor
- Trihelix transcription factor ASIL2
- Protein LOL2
Sequence:
MASLENPAIDSSSEFESSSEEISSSKESKPKEAPVTVPSTKTLNSPSAAVAVSDDSESEKQSFVLTRRKKKEGAAESPAVKSGKKEGAAESPAVKSGNNEGATESPAVKSGKKRASEGTTSRDMHVKRIKKEGDNKKGHAQRVWSEEDEISLLQAMIDFKAETGTSPWDHKDRFFDIAKKSISFDVSKVQFFDKIRSFKRKYFGDRKVRSVESDHDKKCLGLAVSFWGSDGVSLETPVKKKVKDESVLVKANSKEKNVKPLVKEDEQVVILGEDSEWFEESFLVPVIASLGLDEYSVKKKWSKVSVETKKRIQEKMKLVDAKKCELLLANMDVLKEVTSVLTQTN
Protein: Guanine nucleotide-binding protein subunit beta-like protein (Q57YE7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA damage-binding protein 1
- Cullin family profile domain-containing protein
- Cullin 4B, putative
Sequence:
MQCERFKQTKRDQLPLYCHDVRLAWRMQPLGFSTGSLRSLVHTQRAEAYQQELPHNLRGCIESVTHLDGTRESHCDPFANPEEMEHSANPIASEGAQTPSESFVRSFGLRRELEGHNGCVNSLSMNASGELLLSGSDDLAFCLYDTFEWQIKQRYRTRHSSNIFHAVFVPGNDHHVVSCARDGRTLVTDLEVGESFYKCRHSQVASSIAVSPWWPDTAYVGYLNGFISRIDTRTRRLESERTTDGNPCLPSVGEVRTLAVHDRWPFLLASGTNTEAVYLHDVRMCSLGAFAAITIPCVRRSNGVSGLSFSANGTSLAVNYREEHVYVVPWLETLYSRAVSTSASRNATCTGFSSVLDMGAVDKLTVATADGAVKMSGRRNVQTMFKDVTFMEDDSIVCSGCDSGNVFFWRTSDGKLIHTTPGDASIVNVVLYSHRTGRLLTSGIDDTIKVLGPLNGRVSQSIEHREEVEDTFSRSVVGVVDTVRRILLGEIPSTRGDRLSEILSLGDNLVTRTPDTEDRTDVRVELNTTVSDDSDDDGGGSVDDFDSHYEDESNEEVGQYQSQDRIWHVNFSRSHVEASLEQFAAAERALHMSLTDLILLTRQLVATWVFGSRRVVGGIGTVPPLFLANGAMSSTTAESDAFSGIRGMVVEGAEDDGDVDVDDMITDDATALSSARMSLPEDTSNLGDSIDRHVGSDSGVSSASGNGEDDPFLVIGTSILTPATERHISHIRAADEGTLVEELPVVGGGPGQREERGDSTSQRTGDDRNEAAIPGTDVMGTVSSWFQDMHRVFNKLRDGLKTTFRRWTLPGGGRVQIPRWDRCTFGVASGAPVVDGGWSPSQAPDVDDDTSFLFYYASGVAQAESSGNVPAAPPTFDAFLSNKQRIRCFLTLLDVVLRRKELICSSTEERRGYWMFRCVTELCYAYYFMALGEAEAAIHHVEQLERHAEYRCITALGSVDSACLRLGGKRRRQAPVPQGTGSRGTYERRGTELLRTLDCGELPPLLVPMALKIRILVLSQRGVVSGEDVLSSGSCSDHGELLRDQAGDSYLQSLVNEMRGRLSGHPNEKVKQRVVRMLRGINITLS
Protein: Mitochondrial carrier protein, putative (Q38DS0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
Sequence:
MDVICSALAGVMARAVCHPLDTAKTVTFTGFFGDSSSSLHVNSKGSLRHVASSIWRREGPGAFYRGAGVAIVGSAPGTALYLTTYTWSRDFLQGYVSASHSSSFLSTIPSSFIHLICGLFAESVSCIFWVPIDVTKERLQAQSSFVEGRYKGNWDAIRTVARYEGVRGLYKGYWSTLASFGPYSAVYFGCYEVFENVLNEHMSLGTFSSSLCAGGMGNIVACVVTNPLELVKTRLQVQRAVLSVNGKPTAVYGFPFRYKGLLDGLCAIVKSEGVCALWKGLPIRVTFAAPNAALTMGFYSYLKGNMA
Protein: Uncharacterized protein (Q386C3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPSSKSDSGDPTPVQHLANESMQSSATLSASAWASAVKRFEGPKSSGNSAPTDGGKPRHKESMFAVKQATAPETMDPIMRRLELRYEPLPAERQYSVQSSSRKQRGEQRSDVVDVSMQAVQDETVALLTRHLPCIPSTLPDVTEWKEATKSQNEPVLDDRITAQTIHRLLCKGHFRDRKRQLLKCRSKQAIEEFDELLPSNAVNALSKQVSRLEPPFVEKMMEAKMYCKQQKNDESTPREVHPASCEGTPFSRAPPGYYHSHLSAPPPSRCSFTASPKGDLSPLQKQALPGILTASEDNFSAKIPASVTLTLSTAAGDDQSIVDQVVAYAASKRRPSVAVVGGDLIETNTQGDPYGHGCDLKLHPSHKPVFSALDAVLSVSKEYEKVQQQWPGRSASRISAARRGITERITSLHSSRIPPEFWVSIHQPTLPGTRLLQHPHLAKREPSSSVPEKTLMFPAANATGRAQVYLLADTLDRMLEEGSGDLEVLADKELALLLIPEELDDGKPAGLGAVGSSEKFTNVCPLKSSDDAHAQYIQSAERVMKTIDIGLAELSRQVGSFCIERGALLDSLRIVINDLSSSCFALVSYCKDRARQELMMRRELASASSKDVEMVFELREQLKKAQSEVQALREVNNEYVKKAQKYDTLIERLMLKDSMFYKHSADLHLSMLMELEESYTESTNKGMDALYHHTSTNAAEPKVAEAPIIRLATMKQKEHQEAEKKVYEESYRLISVLSKTMDTVEKVCQPLYDHVDLPKHRSTVNVASSKWAMIASAVGSYEVEKKHRRRVFDVFAEWNSLQEPVPASALPDDKLKDDEVENKSHAVESHAYSYSTTPRGLENTHNADAQEGTFTTDVVTASQCTEVGQPSSAATRRMRPITKEDLVAMDVKDCTAEEINALYAEDFDMAAYLHPEWNPPTDVELTPMVLRDMIHDVTESLMHIALRMQALSTSSFIEQCLKPPAMPPAHPEEPCSLCGRKDRSAIGKKNRGEALQKVANEVQRRYEMLGQKCQRAEAERERLRKELQMQQAHECRLAREFGMREEELKKANAELAEENNRRGRRRRSQINTHERPRSSFMRSSVLSEMLNLSGSIDDAPVPGEEEK
Protein: GTP-binding protein RHO5 (P53879)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Small GTPase that negatively regulates a MAP kinase branch, downstream of SLT2, of the PKC1-mediated signal transduction pathway. With its specific guanine nucleotide exchange factor (GEF), the heterodimeric complex DCK1/LMO1, relocates to mitochondria upon oxidative stress and triggers cell death. The DCK1/LMO1/RHO5 signaling module that mediates mitochondrial turnover under nitrogen starvation conditions via mitophagy. The DCK1/LMO1/RHO5 signaling module also plays a role in cell wall integrity signaling.
Subcellular location: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Mitochondrion {ECO:0000269|PubMed:25598154}. Note=Localization to mitochondria occurs upon oxidative stress and is dependent of DCK1 and LMO1. {ECO:0000269|PubMed:25598154}.
Interaction partners:
- DOCK-like protein 1
- Rho GDP-dissociation inhibitor
- Protein kinase C-like 1
- Serine/threonine-protein kinase STE20
- Cell division control protein 24
- RHO GTPase-activating protein RGD1
- Rho-GTPase-activating protein RGD2
- ELMO family protein LMO1
- Ras GTPase-activating-like protein IQG1
- Proline-rich protein LAS17
Sequence:
MRSIKCVIIGDGAVGKTSLLISYTTNSFPTDYVPTVFDNYSTTIAIPNGTASSPLELDNGNDKRGSLSSASSSPSTDRKLYKINLWDTAGQEDYDRLRPLCYPQTDIFLICFSVSEHASFANVTEKWLPELKQTSNIEGTSLYTKLGKYPILLVGTKSDLRDDPATQKKLQEANSDYVSQEEIDELVQRCGFMGYTECSAATQAGVREVFEQAVRYAIYEPESPNQKSANHTLTDELTTATTNTNGDKNIREQKQQPHHNNSTDSTLPKGSLQQEKEALNIKPTKKGQKDKIHEQSKSKGSKIASNNHHNKQAKPKTRNDKKKKKSKCVIL
Protein: CD44 antigen (Extracellular matrix receptor III) (ECMR-III) (GP90 lymphocyte homing/adhesion receptor) (HUTCH-I) (Hermes antigen) (Hyaluronate receptor) (Lymphocyte antigen 24) (Ly-24) (Phagocytic glycoprotein 1) (PGP-1) (Phagocytic glycoprotein I) (PGP-I) (CD antigen CD44) (P15379)
Organism: Mus musculus (Mouse)
Function: Cell-surface receptor that plays a role in cell-cell interactions, cell adhesion and migration, helping them to sense and respond to changes in the tissue microenvironment. Participates thereby in a wide variety of cellular functions including the activation, recirculation and homing of T-lymphocytes, hematopoiesis, inflammation and response to bacterial infection. Engages, through its ectodomain, extracellular matrix components such as hyaluronan/HA, collagen, growth factors, cytokines or proteases and serves as a platform for signal transduction by assembling, via its cytoplasmic domain, protein complexes containing receptor kinases and membrane proteases. Such effectors include PKN2, the RhoGTPases RAC1 and RHOA, Rho-kinases and phospholipase C that coordinate signaling pathways promoting calcium mobilization and actin-mediated cytoskeleton reorganization essential for cell migration and adhesion (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:17403031, ECO:0000269|PubMed:25065622}; Single-pass type I membrane protein {ECO:0000269|PubMed:17403031}. Cell projection, microvillus {ECO:0000269|PubMed:9472040}. Secreted {ECO:0000250|UniProtKB:P16070}. Note=Colocalizes with actin in membrane protrusionFs at wounding edges. Co-localizes with RDX, EZR and MSN in microvilli. {ECO:0000269|PubMed:17403031, ECO:0000269|PubMed:9472040}.
Interaction partners:
- Osteopontin
- Fibronectin
- H-2 class II histocompatibility antigen gamma chain
- Matrix metalloproteinase-9
- Receptor tyrosine-protein kinase erbB-2
- Radixin
- E-selectin
- Epidermal growth factor receptor
- Ezrin
- Moesin
Sequence:
MDKFWWHTAWGLCLLQLSLAHQQIDLNVTCRYAGVFHVEKNGRYSISRTEAADLCQAFNSTLPTMDQMKLALSKGFETCRYGFIEGNVVIPRIHPNAICAANHTGVYILVTSNTSHYDTYCFNASAPPEEDCTSVTDLPNSFDGPVTITIVNRDGTRYSKKGEYRTHQEDIDASNIIDDDVSSGSTIEKSTPEGYILHTYLPTEQPTGDQDDSFFIRSTLATIASTVHSKSHAAAQKQNNWIWSWFGNSQSTTQTQEPTTSATTALMTTPETPPKRQEAQNWFSWLFQPSESKSHLHTTTKMPGTESNTNPTGWEPNEENEDETDTYPSFSGSGIDDDEDFISSTIATTPRVSARTEDNQDWTQWKPNHSNPEVLLQTTTRMADIDRISTSAHGENWTPEPQPPFNNHEYQDEEETPHATSTTPNSTAEAAATQQETWFQNGWQGKNPPTPSEDSHVTEGTTASAHNNHPSQRITTQSQEDVSWTDFFDPISHPMGQGHQTESKDTDSSHSTTLQPTAAPNTHLVEDLNRTGPLSVTTPQSHSQNFSTLHGEPEEDENYPTTSILPSSTKSSAKDARRGGSLPTDTTTSVEGYTFQYPDTMENGTLFPVTPAKTEVFGETEVTLATDSNVNVDGSLPGDRDSSKDSRGSSRTVTHGSELAGHSSANQDSGVTTTSGPMRRPQIPEWLIILASLLALALILAVCIAVNSRRRCGQKKKLVINGGNGTVEDRKPSELNGEASKSQEMVHLVNKEPSETPDQCMTADETRNLQSVDMKIGV
Protein: Multicopper oxidase (Q5B233)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MLRSSFLLFFYALYASASWVFEHDFQPEERSLLFGTDVSPLKRRQEEGSSSASDSILSVAGGGGGRSSGRPQPTSTSFTQTRTTSTRPTSTNTRTGTRSSSNTTTRTSTSATSTPTTTATGTPCAGNTPDTRREWCDYSIDTNYHDITPDTGVVREYWLELDEITVSPDGISRPAVAVNGTIPGPTIFADWGDEVVVHIKNNLHETLNGSTIHWHGIRQLNTNEHDGVVSITQCPITPDHEYTYRWRAQQYGTTWYHSHISLQAWDGVVGPIIINGPATENYDVDAGTIFLNDWTHQTFEELFWYAQIVGPPLLNNSLINGTGVYGSSFSGHRAKGQKETGERFSMKVEEGTSYRLRLINGAIDTHYKFMIDSHELTVIAMDLVPVKPYKTTAVSLAMGQRYDVIVTANQRSKSDSFWLRSIPQQSCSDVEDPGNIRGIFYYGDRPSTPKTEPYPFEDSCMDEPMASLVPHVARDVQPPDYQNNALASVSFNEDHFFRWFLNSTTMQVYWEDPTLLQILNGDDSFENSSAVIELPNANEWVYMIVNTTIPVSHPIHLHGHDFFILAQGTNPWDGKYQTSNPPRRDTAVLPGNGYLVMAWETDNPGAWLMHCHIGWHTTEGFALQFVERIDEIRENVDRDFVVNACNTWNGYGEEYGVEQYDSGV
Protein: PTS system glucitol/sorbitol-specific EIIB component (EC 2.7.1.198) (EII-Gut) (Enzyme II-Gut) (Glucitol/sorbitol-specific phosphotransferase enzyme IIB component) (P56580)
Organism: Escherichia coli (strain K12)
Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II complex composed of SrlA, SrlB and SrlE is involved in glucitol/sorbitol transport. It can also use D-mannitol.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:3553176}; Multi-pass membrane protein {ECO:0000255, ECO:0000305|PubMed:3553176}.
Interaction partners:
- Sorbitol-6-phosphate 2-dehydrogenase
- PTS system glucitol/sorbitol-specific EIIC component
- PTS system glucitol/sorbitol-specific EIIA component
- Glucitol operon activator protein
- Uncharacterized protein YggP
- Phosphocarrier protein HPr
- Glucitol operon repressor
- PTS system galactitol-specific EIIB component
- PTS system galactitol-specific EIIA component
- Putative phosphotransferase enzyme IIB component SgcB
Sequence:
MTHIRIEKGTGGWGGPLELKATPGKKIVYITAGTRPAIVDKLAQLTGWQAIDGFKEGEPAEAEIGVAVIDCGGTLRCGIYPKRRIPTINIHSTGKSGPLAQYIVEDIYVSGVKEENITVVGDATPQPSSVGRDYDTSKKITEQSDGLLAKVGMGMGSTVAVLFQSGRDTIDTVLKTILPFMAFVSALIGIIMASGLGDWIAHGLAPLASHPLGLVMLALICSFPLLSPFLGPGAVIAQVIGVLIGVQIGLGNIPPHLALPALFAINAQAACDFIPVGLSLAEARQDTVRVGVPSVLVSRFLTGAPTVLIAWFVSGFIYQ
Protein: Retinaldehyde-binding protein 1 (Cellular retinaldehyde-binding protein) (E1C1U1)
Organism: Gallus gallus (Chicken)
Function: Soluble retinoid carrier essential the proper function of both rod and cone photoreceptors. Participates in the regeneration of active 11-cis-retinol and 11-cis-retinaldehyde, from the inactive 11-trans products of the rhodopsin photocycle and in the de novo synthesis of these retinoids from 11-trans metabolic precursors. The cycling of retinoids between photoreceptor and adjacent pigment epithelium cells is known as the 'visual cycle'.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P12271}.
Interaction partners:
Sequence:
MSAVTGTFRIVSEEEQALRTKLERLTTKDHGPVFGRCQQIPPHTLQKAKDELNETEEQREAAVKALRELVQERAGSEDVCKAVAEKMQGKDDSFFLRFIRARKFDVHRAYDLLKGYVNFRQQYPELFDNLTPEAVRSTIEAGYPGILASRDKYGRVVMLFNIENWDYEEITFDEILRAYCVILEKLLENEETQINGFCIIENFKGFTMQQASGIKPSELKKMVDMLQDSFPARFKAVHFIHQPWYFTTTYNVVKPFLKSKLLERVFVHGEELESFYQEIDADILPADFGGNLPKYDGKATAEQLFGPRIEAEDTAL
Protein: G2-specific protein kinase nimA (EC 2.7.11.1) (Never in mitosis) (P11837)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Protein kinase that plays an important role in mitotic regulation. Seems to be phosphorylated and thereby activated by CDC2/cyclin B during mitotic activation. It is also required for spindle formation and for nuclear envelope breakdown.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Anaphase-promoting complex subunit 4
- Negative regulator of mitosis
- Protein bimA
- Mitotic spindle checkpoint protein
- Uncharacterized protein
- 20S cyclosome subunit
- Anaphase-promoting complex subunit 2
- Kinesin-like protein bimC
- Anaphase-promoting complex subunit 5
- Mitotic checkpoint regulator, MAD2B-interacting-domain-containing protein
Sequence:
MAIALAEADKYEVLEKIGCGSFGIIRKVKRKSDGFILCRKEINYIKMSTKEREQLTAEFNILSSLRHPNIVAYYHREHLKASQDLYLYMEYCGGGDLSMVIKNLKRTNKYAEEDFVWRILSQLVTALYRCHYGTDPAEVGSNLLGPAPKPSGLKGKQAQMTILHRDLKPENIFLGSDNTVKLGDFGLSKLMHSHDFASTYVGTPFYMSPEICAAEKYTLRSDIWAVGCIMYELCQREPPFNARTHIQLVQKIREGKFAPLPDFYSSELKNVIASCLRVNPDHRPDTATLINTPVIRLMRREVELNNLSRAARKREEATMQKAKDVEQAFAKLEKEKQQIRSELENSIRREWEVKARLEIDRQVQNELDKLRKRFECEVQDRVAQEVEKQRRNANYREDASLRSSGHSSQMSSSNSEDSDFPSSTDISQLSLESPTNKAAKLPKKESRTPFTRSKTVVDSPMDIQMAEPSPISIASLSLSPRRTSATYSGKNIFAEGERKRPKFEPTLAYSDDEDDTPELPSPTRPKVKPDPFKAPSRPLLRQNTTALMQKLSTQPPIFPANPSRLPQMSAPDVRESKSRSPHRRLSKIPSSANLAADAGSPTRKNGVKSSPSKMNGGDEMFKAVMQRNMGGRTLVELAQARAGGRPIDEVKRCASDSRSGCSVPMKSADRDPPAVWDPERDEMPSPFLARGRKVIRNLR
Protein: Armadillo segment polarity protein (P18824)
Organism: Drosophila melanogaster (Fruit fly)
Function: Isoform neural may associate with CadN and participate in the transmission of developmental information. Can associate with alpha-catenin. Isoform cytoplasmic accumulates through wg signaling; arm function in wg signal transduction is required early in development for determination of neuroblast fate. Arm and Abl proteins function cooperatively at adherens junctions in both the CNS and epidermis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8666669}. Cell membrane {ECO:0000269|PubMed:8666669}; Peripheral membrane protein {ECO:0000269|PubMed:8666669}; Cytoplasmic side {ECO:0000269|PubMed:8666669}. Cell junction, adherens junction {ECO:0000269|PubMed:16598259, ECO:0000269|PubMed:25653389}. Note=Inner surface of cell membrane and adherens junction.
Interaction partners:
- Catenin alpha
- Protein pangolin, isoform J
- Adenomatous polyposis coli 2
- Axin
- DE-cadherin
- Protein kinase shaggy
- Supernumerary limbs, isoform B
- APC-like, isoform A
- Protein pygopus
- Protein BCL9 homolog
Sequence:
MSYMPAQNRTMSHNNQYNPPDLPPMVSAKEQTLMWQQNSYLGDSGIHSGAVTQVPSLSGKEDEEMEGDPLMFDLDTGFPQNFTQDQVDDMNQQLSQTRSQRVRAAMFPETLEEGIEIPSTQFDPQQPTAVQRLSEPSQMLKHAVVNLINYQDDAELATRAIPELIKLLNDEDQVVVSQAAMMVHQLSKKEASRHAIMNSPQMVAALVRAISNSNDLESTKAAVGTLHNLSHHRQGLLAIFKSGGIPALVKLLSSPVESVLFYAITTLHNLLLHQDGSKMAVRLAGGLQKMVTLLQRNNVKFLAIVTDCLQILAYGNQESKLIILASGGPNELVRIMRSYDYEKLLWTTSRVLKVLSVCSSNKPAIVDAGGMQALAMHLGNMSPRLVQNCLWTLRNLSDAATKVEGLEALLQSLVQVLGSTDVNVVTCAAGILSNLTCNNQRNKATVCQVGGVDALVRTIINAGDREEITEPAVCALRHLTSRHVDSELAQNAVRLNYGLSVIVKLLHPPSRWPLIKAVIGLIRNLALCPANHAPLREHGAIHHLVRLLMRAFQDTERQRSSIATTGSQQPSAYADGVRMEEIVEGTVGALHILARESHNRALIRQQSVIPIFVRLLFNEIENIQRVAAGVLCELAADKEGAEIIEQEGATGPLTDLLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSIELTNSLLREDNNIWANADLGMGPDLQDMLGPEEAYEGLYGQGPPSVHSSHGGRAFHQQGYDTLPIDSMQGLEISSPVGGGGAGGAPGNGGAVGGASGGGGNIGAIPPSGAPTSPYSMDMDVGEIDAGALNFDLDAMPTPPNDNNNLAAWYDTDC
Protein: Glypican-1 (HSPG M12) [Cleaved into: Secreted glypican-1] (P35053)
Organism: Rattus norvegicus (Rat)
Function: Cell surface proteoglycan that bears heparan sulfate. May act as a catalyst in increasing the rate of conversion of prion protein PRPN(C) to PRNP(Sc) via associating (via the heparan sulfate side chains) with both forms of PRPN, targeting them to lipid rafts and facilitating their interaction. Required for proper skeletal muscle differentiation by sequestering FGF2 in lipid rafts preventing its binding to receptors (FGFRs) and inhibiting the FGF-mediated signaling. Binds Cu(2+) or Zn(2+) ions (By similarity). Binds, via the heparan sulfate side chains, alpha-4 (V) collagen and participates in Schwann cell myelination.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. Endosome {ECO:0000250}. Note=S-nitrosylated form recycled in endosomes. Localizes to CAV1-containing vesicles close to the cell surface. Cleavage of heparan sulfate side chains takes place mainly in late endosomes. Associates with both forms of PRNP in lipid rafts. Colocalizes with APP in perinuclear compartments and with CP in intracellular compartments (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Secreted glypican-1]: Secreted, extracellular space {ECO:0000250}.
Interaction partners:
- Syndecan-1
- Fibroblast growth factor 2
- Syndecan-4
- Syndecan-2
- Proheparin-binding EGF-like growth factor
- Epithelial cell adhesion molecule
- Receptor protein-tyrosine kinase
- Syndecan-3
- Decorin
Sequence:
MELRARGWWLLCAAAALVACTRGDPASKSRSCSEVRQIYGAKGFSLSDVPQAEISGEHLRICPQGYTCCTSEMEENLANHSRMELETALHDSSRALQATLATQLHGIDDHFQRLLNDSERTLQDAFPGAFGDLYTQNTRAFRDLYAELRLYYRGANLHLEETLAEFWARLLERLFKQLHPQLLLPDDYLDCLGKQAEALRPFGDAPRELRLRATRAFVAARSFVQGLGVASDVVRKVAQVPLAPECSRAVMKLVYCAHCRGVPGARPCPDYCRNVLKGCLANQADLDAEWRNLLDSMVLITDKFWGPSGAEYVIGSVHMWLAEAINALQDNKDTLTAKVIQGCGNPKVNPHGSGPEEKRRRAKLALQEKSSTGTLEKLVSEAKAQLRDIQDYWISLPGTLCSEKMAMSPASDDRCWNGISKGRYLPEVMGDGLANQINNPEVEVDITKPDMTIRQQIMQLKIMTNRLRGAYGGNDVDFQDASDDGSGSGSGGGCPDDACGRRVSKKSSSSRTPLIHALPGLSEQEGQKTSAATRPEPHYFFLLFLFTLVLAAARPRWR
Protein: Basigin (Basic immunoglobulin superfamily) (HT7 antigen) (Membrane glycoprotein gp42) (CD antigen CD147) (P18572)
Organism: Mus musculus (Mouse)
Function: Essential for normal retinal maturation and development. Acts as a retinal cell surface receptor for NXNL1 and plays an important role in NXNL1-mediated survival of retinal cone photoreceptors. In association with glucose transporter SLC16A1/GLUT1 and NXNL1, promotes retinal cone survival by enhancing aerobic glycolysis and accelerating the entry of glucose into photoreceptors.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:11273674, ECO:0000269|PubMed:25957687}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P26453}. Photoreceptor inner segment {ECO:0000269|PubMed:11853760, ECO:0000269|PubMed:25957687}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:25957687}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:12601063}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P26453}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P35613}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P26453}. Basolateral cell membrane {ECO:0000250|UniProtKB:P35613}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P26453}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase A
- Monocarboxylate transporter 1
- Monocarboxylate transporter 4
- 5-hydroxytryptamine receptor 1A
- Guanine nucleotide-binding protein G
- Monocarboxylate transporter 3
- 5-hydroxytryptamine receptor 2A
- Integrin beta-1
- 5-hydroxytryptamine receptor 2B
- 5-hydroxytryptamine receptor 1B
Sequence:
MAAALLLALAFTLLSGQGACAAAGFLKAPLSQERWAGGSVVLHCEAVGSPIPEIQWWFEGNAPNDSCSQLWDGARLDRVHIHAAYRQHAASSLSVDGLTAEDTGTYECRASSDPDRNHLTRPPRVKWVRAQASVVVLEPGTIQTSVQEVNSKTQLTCSLNSSGVDIVGHRWMRGGKVLQEDTLPDLHTKYIVDADDRSGEYSCIFLPEPVGRSEINVEGPPRIKVGKKSEHSSEGELAKLVCKSDASYPPITDWFWFKTSDTGEEEAITNSTEANGKYVVVSTPEKSQLTISNLDVNVDPGTYVCNATNAQGTTRETISLRVRSRMAALWPFLGIVAEVLVLVTIIFIYEKRRKPDQTLDEDDPGAAPLKGSGTHMNDKDKNVRQRNAT
Protein: Oxalate--CoA ligase (EC 6.2.1.8) (4-coumarate--CoA ligase isoform 8) (At4CL8) (4-coumarate--CoA ligase-like 10) (Acyl-activating enzyme 3) (Adenosine monophosphate binding protein 3) (AtMPBP3) (Oxalyl-CoA synthetase) (Q9SMT7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Oxalyl-CoA synthetase acting exclusively against oxalate. Follows a two-step reaction mechanism, wherein oxalate first undergoes adenylation by ATP, followed by a thioesterification in the presence of CoA to yield oxalyl-CoA (By similarity). No activity with malonate, succinate, malate, acetate, formate, lactate, glycolate, glyoxylate or glutarate. Required for oxalate degradation, normal seed development and defense against oxalate-producing fungal pathogens.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22447686}.
Interaction partners:
- 2-hydroxyacyl-CoA lyase
- tRNA-5-taurinomethyluridine 2-sulfurtransferase
- Putative acyl-activating enzyme 19
- CASP-like protein 1D1
- Plant intracellular Ras-group-related LRR protein 3
Sequence:
MDSDTLSGLLENVAKKFPDRRALSVSGKFNLTHARLHDLIERAASRLVSDAGIKPGDVVALTFPNTVEFVIMFLAVIRARATAAPLNAAYTAEEFEFYLSDSDSKLLLTSKEGNAPAQEAASKLKISHVTATLLDAGSDLVLSVADSDSVVDSATELVNHPDDGALFLHTSGTTSRPKGVPLTQLNLASSVKNIKAVYKLTESDSTVIVLPLFHVHGLLAGLLSSLGAGAAVTLPAAGRFSATTFWPDMKKYNATWYTAVPTIHQIILDRHASHPETEYPKLRFIRSCSASLAPVILSRLEEAFGAPVLEAYAMTEATHLMSSNPLPEEGPHKPGSVGKPVGQEMAILNEKGEIQEPNNKGEVCIRGPNVTKGYKNNPEANKAGFEFGWFHTGDIGYFDTDGYLHLVGRIKELINRGGEKISPIEVDAVLLTHPDVSQGVAFGVPDEKYGEEINCAVIPREGTTVTEEDIKAFCKKNLAAFKVPKRVFITDNLPKTASGKIQRRIVAQHFLEKP