wanglab/gogpt-training-data huggingface dataset:
Protein: Branched-chain amino acid ABC transporter, ATP-binding protein (Q5LS32)
Organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Interaction partners:
- Branched-chain amino acid ABC transporter, permease protein
- Branched-chain amino acid ABC transporter, permease protein
- Branched-chain amino acid ABC transporter, permease protein
- Branched-chain amino acid ABC transporter, permease protein
- Branched-chain amino acid ABC transporter, periplasmic substrate-binding protein
- Branched-chain amino acid ABC transporter, permease protein
- Branched-chain amino acid ABC transporter, ATP-binding protein
- Branched-chain amino acid ABC transporter, permease protein
- Branched-chain amino acid ABC transporter, permease protein
- Branched-chain amino acid ABC transporter, permease protein
Sequence:
MCPGCFNDKRPHLFSGDEATTNKAAKHKAAPGEHMIVVEDVHKHFGGFHAVDGATLEITKGSVTGLIGPNGAGKTTLFNVIAGVLPPTSGKVTMDGEDITGLPPHELFHKGLLRTFQIAHEFSSMTCRENLMMVPGGQSGEALWNTWFGRKRIADEERALRAKADEVLEFLTIEHLADHKAGQVSGGQKKLLELGRTMMVDAKIVFLDEVGAGVNRTLLMTIADTILRLNKERGYTFVVIEHDMDFIGKICDPVICMAEGRVLAQGTLDEIKANEHVIEAYLGTGLKNKAQLEAGA
Protein: Vacuolar-sorting protein BRO1 (Amino acid sensor-independent protein 6) (BCK1-like resistance to osmotic shock protein 1) (BRO domain-containing protein 1) (Nitrogen permease inactivating protein 3) (Vacuolar protein-sorting-associated protein 31) (P48582)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. Fusion between endosomes and the vacuole will then target the cargo proteins to the vacuolar lumen. Acts as an adapter that recruits the DOA4 deubiquitinase to the endosomes, leading to deubiquitination of cargo proteins prior to the lumenal sequestration. Its association to the endosomes depends on SNF7 and its dissociation requires VPS4. Interacts functionally with the Pkc1p-mitogen-activated protein kinase pathway.
Subcellular location: Cytoplasm. Endosome.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase 4
- Vacuolar-sorting protein SNF7
- Vacuolar protein sorting-associated protein 20
- Vacuolar protein sorting-associated protein 4
- DOA4-independent degradation protein 4
- Vacuolar protein-sorting-associated protein 24
- Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease
- Regulator of free ubiquitin chains 1
- Vacuolar protein sorting-associated protein 27
- Vacuolar protein sorting-associated protein IST1
Sequence:
MKPYLFDLKLKDTEKLDWKKGLSSYLKKSYGSSQWRTFYDEKATSELDHLRNNANGELAPSSLSEQNLKYYSFLEHLYFRLGSKGSRLKMDFTWYDAEYSSAQKGLKYTQHTLAFEKSCTLFNIAVIFTQIARENINEDYKNSIANLTKAFSCFEYLSENFLNSPSVDLQSENTRFLANICHAEAQELFVLKLLNDQISSKQYTLISKLSRATCNLFQKCHDFMKEIDDDVAIYGEPKWKTTVTCKLHFYKSLSAYYHGLHLEEENRVGEAIAFLDFSMQQLISSLPFKTWLVEFIDFDGFKETLEKKQKELIKDNDFIYHESVPAVVQVDSIKALDAIKSPTWEKILEPYMQDVANKCDSLYRGIIPLDVYEKESIYSEEKATLLRKQVEETETANLEYSSFIEFTNLPRLLSDLEKQFSDGNIFSNTDTQGQLMRDQIQTWCKFIQTNEFRDIEEQMNKIVFKRKQILEILSALPNDQKENVTKLKSSLVAASNSDEKLFACVKPHIVEINLLNDNGKIWKKFDEFNRNTPPQPSLLDIDDTKNDKILELLKQVKGHAEDLRTLKEERSRNLSELRDEINNDDITKLLIINKGKSDVELKDLFEVELEKFEPLSTRIEATIYKQSSMIDDIKAKLDEIFHLSNFKDKSSGEEKFLEDRKNFFDKLQEAVKSFSIFASDLPKGIEFYDSLFNMSRDLAERVRVAKQTEDSTANSPAPPLPPLDSKASVVGGPPLLPQKSAAFQSLSRQGLNLGDQFQNLKISAGSDLPQGPGIPPRTYEASPYAATPTMAAPPVPPKQSQEDMYDLRRRKAVENEERELQENPTSFYNRPSVFDENMYSKYSS
Protein: Protein transport protein Sec23, putative (Q580Y6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Protein transport protein Sec31, putative
- ADP-ribosylation factor, putative
- Protein transport protein Sec24C, putative
- Protein transport protein Sec24A, putative
- Protein transport protein Sec13, putative
- Protein transport protein sec13, putative
- Sec16 Sec23-binding domain-containing protein
- Synaptobrevin-type vesicle transport protein, putative
- Longin domain-containing protein
- Golgi reassembly stacking protein
Sequence:
MQGHVPQQSYGGYPRQADYQGLYPTQDVKQGYVSYQDPATLMEGHNAQYGGGTAEGTYSNQYTQLQQQMNNYNYNANQTPWQQQYAPQQGIHNPANTNDTNMFAPPTAVGAAAASHVGGAVAPTGSGASATTASHVPPPPPAAECTDENGLRWTWSTYPNHTRDGKQEAPSAAALTLPEMVIPLACMYTPLFPIDASRMVIGDPTACGQQCQNCGAFWSHHCYREEGKFWVCFSCQRRNQLPPHYRPEHPALHNDTVEYILPLEQPTTAQATRGVGFSPTFVFIIDTCIAVEELEALKCNIQRCLNWLPPQSLIGLVSFGARVSVWDLSGSSLSRCYSIRGDRAYTTAELGNMLQLNDGLPARGRFLVPLEECEFTLTTSIEGLQCHDGVTPVNKRPLRATGTAVSAAVRLLEALPEVPVKKEMSGAAPAGVAPVRKAGRVLLFTGGPCTRGPGTVVSIEKESMMRFHRDIIEGETPYYEAAFKFYNEIQLRLLDVNASLSVFAESFDQIGILEMRQAVDQTGGTFICGDTFDHQMFTISLQRYFDLCDLRPPGVESSGISSAGDIDGSAPGALVANSGFGVKLHVHTSADTLVSGVLGPCVAAEKTSGTKAHRASISPIEIGVGGTTDWRVSTIDQGTTYTVVFDTATLNKVDGMPQQQQNRFIQFVTHFTTPLGESRIRVTSVALPIAPVTITADGVSTANPQYFSEYDTFDQTCAATVLARMTVSILEKHPSKWNDAKRWLDTVLVRFVRRYGSFTPGSPESLRLRPCFTLFPSFVFNLRRSEYFMVLNISPDESTFKRHWLMRESVDNCVLMIQPTLHSYDMETPTATAVPLDSCSLRPDNILLMDAFFNIHIMWGTVIFAWIQARYQDNPEYAHFAQLLETVENEATMLLDMRYPYPRFSRTDANGSEARHIKTRMNPTTTHHSGARGGNGVSDLSDVIYTDDASIVKFMESLKQAVVTPESKK
Protein: Ubiquitin-conjugating enzyme E2 E1 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme E1) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme E1) (UbcM3) (Ubiquitin carrier protein E1) (Ubiquitin-protein ligase E1) (P52482)
Organism: Mus musculus (Mouse)
Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes the covalent attachment of ISG15 to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. In vitro also catalyzes 'Lys-48'-linked polyubiquitination.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P51965}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 E3
- Ubiquitin-conjugating enzyme E2 E2
- Anaphase-promoting complex subunit 4
- E3 ubiquitin-protein ligase TRIP12
- Ubiquitin-conjugating enzyme E2 variant 1
- Cell division cycle protein 16 homolog
- Cell division cycle protein 23 homolog
- Anaphase-promoting complex subunit 11
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit 1
Sequence:
MSDDDSRASTSSSSSSSSNQQTEKEGSTPKKKESKVSMSKNSKLLSTSAKRIQKELADITLDPPPNCSAGPKGDNIYEWRSTILGPPGSVYEGGVFFLDITFTPEYPFKPPKVTFRTRIYHCNINSQGVICLDILKDNWSPALTISKVLLSICSLLTDCNPADPLVGSIATQYMTNRAEHDRMARQWTKRYAT
Protein: Fibroblast growth factor receptor 2 (FGFR-2) (EC 2.7.10.1) (Keratinocyte growth factor receptor) (KGFR) (CD antigen CD332) (P21803)
Organism: Mus musculus (Mouse)
Function: Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation, migration and apoptosis, and in the regulation of embryonic development. Required for normal embryonic patterning, trophoblast function, limb bud development, lung morphogenesis, osteogenesis and skin development. Plays an essential role in the regulation of osteoblast differentiation, proliferation and apoptosis, and is required for normal skeleton development. Promotes cell proliferation in keratinocytes and immature osteoblasts, but promotes apoptosis in differentiated osteoblasts. Phosphorylates PLCG1, FRS2 and PAK4. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. FGFR2 signaling is down-regulated by ubiquitination, internalization and degradation. Mutations that lead to constitutive kinase activation or impair normal FGFR2 maturation, internalization and degradation lead to aberrant signaling. Over-expressed FGFR2 promotes activation of STAT1.
Subcellular location: Cell membrane; Single-pass type I membrane protein. Golgi apparatus {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Note=Detected on osteoblast plasma membrane lipid rafts. After ligand binding, the activated receptor is rapidly internalized and degraded (By similarity). {ECO:0000250}.
Interaction partners:
- Fibroblast growth factor 8
- Fibroblast growth factor 7
- Fibroblast growth factor 4
- Fibroblast growth factor 2
- Fibroblast growth factor 10
- Fibroblast growth factor 1
- Fibroblast growth factor 9
- Fibroblast growth factor 3
- Fibroblast growth factor 17
- Fibroblast growth factor 18
Sequence:
MVSWGRFICLVLVTMATLSLARPSFSLVEDTTLEPEEPPTKYQISQPEAYVVAPGESLELQCMLKDAAVISWTKDGVHLGPNNRTVLIGEYLQIKGATPRDSGLYACTAARTVDSETWIFMVNVTDAISSGDDEDDTDSSEDVVSENRSNQRAPYWTNTEKMEKRLHACPAANTVKFRCPAGGNPTSTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCLVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVVGGDVEFVCKVYSDAQPHIQWIKHVEKNGSKNGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGISFHSAWLTVLPAPVREKEITASPDYLEIAIYCIGVFLIACMVVTVIFCRMKTTTKKPDFSSQPAVHKLTKRIPLRRQVTVSAESSSSMNSNTPLVRITTRLSSTADTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPTNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEEYLDLTQPLEQYSPSYPDTSSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT
Protein: Nuclear pore complex protein NUP85 (Nuclear pore complex protein NUP75) (Nucleoporin 75) (Nucleoporin 85) (Q8RXH2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as component of the nuclear pore complex (NPC).
Subcellular location: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
Interaction partners:
- Protein SEH1
- Nuclear pore complex protein NUP107
- Protein transport protein SEC13 homolog B
- Nuclear pore complex protein NUP160
- Nuclear pore complex protein NUP155
- Nuclear pore complex protein NUP205
- Nuclear pore complex protein NUP88
- Nuclear pore complex protein NUP54
- Nuclear pore complex protein NUP93A
- Nuclear pore complex protein NUP35
Sequence:
MPGMSSESGGGELVLFSTKEKTPVLYPLSYGLKSPVHRLSISWGCGNNLRVTVLRNPELRDDDDGEVGGKVVNVRLSGEDGEISDPQWRRIAYGSVSPFALLQSRRNSISSLSKMDMSSSLYQTAWWEYVMEYSRDIKSLLSNTISLPAPLIEDPRSVIKNAEEPTSLKAAWELMELFYADKTCLSWLPERLVDWLSEYDILLSSSHPTIYSKLQDFQKELVGLQAIEDDPRYWEVMASALSVGWLEIVVKLLHLHGSYQLDQLGHRETENGLVEAVAVLISKMPRMRPQLEDGKFGECSAAKPDFMKTRERWQSQITKLECSAFWVQCAHHQTREGLRNMLKIMIGNADCLRAATCNWMELFVSHLLYLRPFTKGLDGMHSLAQKCVQSKPVNTSHKLLRLLIGILGENTEVVLAECSKEFGSWMVAHAMELLTAGSEEGEVLVHEEQRKLGGINMEELHRLVYAQVLSSHALTWQIAPIYLASCEKQGLGLLELLFYRQPVQENQMLIKSLEICRLYELSNVSAKLMKISGVHHWKHGRKGSGIFWLQQARDENCLSVIAQQLFDSVGKSLSDESLKQWEGLVELLGSESQISGGLDFLHKYRDFKRSLKVVHDGKTIDAAHEAVERLVSLMKSPSTPQRFWLPLLHDSLKLLNWPERSLLNVTQTNLMLNKLQELSIARLRPGFIESELSAQAVGSVRLALATNLGRAFLEEC
Protein: F-box/LRR-repeat protein 20 (F-box and leucine-rich repeat protein 20) (F-box/LRR-repeat protein 2-like) (Q9CZV8)
Organism: Mus musculus (Mouse)
Function: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Isoform 3 regulates neural transmission by binding and ubiquitinating RIMS1, a modulator of presynaptic plasticity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17803915}. Note=Isoform 3 is present at the presynaptic membrane.
Interaction partners:
- S-phase kinase-associated protein 1
- Cullin-1
- Regulating synaptic membrane exocytosis protein 1
Sequence:
MRRDVNGVTKSRFEMFSNSDEAVINKKLPKELLLRIFSFLDVVTLCRCAQVSRAWNVLALDGSNWQRIDLFDFQRDIEGRVVENISKRCGGFLRKLSLRGCLGVGDNALRTFAQNCRNIEVLSLNGCTKTTDATCTSLSKFCSKLRHLDLASCTSITNMSLKALSEGCPLLEQLNISWCDQVTKDGIQALVRGCGGLKALFLKGCTQLEDEALKYIGAHCPELVTLNLQTCLQITDEGLITICRGCHKLQSLCASGCSNITDAILNALGQNCPRLRILEVARCSQLTDVGFTTLARNCHELEKMDLEECVQITDSTLIQLSIHCPRLQVLSLSHCELITDDGIRHLGNGACAHDQLEVIELDNCPLITDASLEHLKSCHSLERIELYDCQQITRAGIKRLRTHLPNIKVHAYFAPVTPPPSVGGSRQRFCRCCIIL
Protein: G antigen 2D (GAGE-2D) (Cancer/testis antigen 4.8) (CT4.8) (G antigen 8) (GAGE-8) (Q9UEU5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSWRGRSTYRPRPRRYVEPPEMIGPMRPEQFSDEVEPATPEEGEPATQRQDPAAAQEGEDEGASAGQGPKPEADSQEQGHPQTGCECEDGPDGQEMDPPNPEEVKTPEEGEKQSQC
Protein: Transcription factor PRE6 (Basic helix-loop-helix protein 163) (AtbHLH163) (bHLH 163) (Protein KIDARI) (Protein PACLOBUTRAZOL RESISTANCE 6) (bHLH transcription factor bHLH163) (Q8GW32)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Atypical and probable non DNA-binding bHLH transcription factor that regulates light-mediated responses in day light conditions by binding and inhibiting the activity of the bHLH transcription factor HFR1, a critical regulator of light signaling and shade avoidance. Forms non-functional heterodimers with HFR1, causing liberation and activation of PIF4 from the transcriptionally inactive HFR1-PIF4 complex.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23224238}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:23224238}.
Interaction partners:
- Transcription factor HFR1
- Transcription factor IBH1
- Transcription factor HBI1
- Transcription factor PIF4
- EMBRYO SURROUNDING FACTOR 1-like protein 3
- Transcription factor bHLH49
- Transcription factor bHLH150
- Transcription factor bHLH147
- Transcription factor PAR1
- Cytochrome P450 83B1
Sequence:
MSSRRSSRSRQSGSSRISDDQISDLVSKLQHLIPELRRRRSDKVSASKVLQETCNYIRNLHREVDDLSDRLSELLASTDDNSAEAAIIRSLLNY
Protein: ADAM metallopeptidase with thrombospondin type 1 motif 6 (A0A286YEC9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MEISWKTLTWILSLIMASSEFYSDHRLSYSSQEEFLTYLEHYQLTIPIRVDQNGAFLSFTVKNDKHSRRRRSMDLLDPQQAVSKLFFKLSAYGKHFHLNLTLNTNFVSKHFTVEYWGKDGPQWKHDFLDNCHYTGYLQDQHSTTKVALSNCVGLHGIIATEDEEYFIEPLKNTTEDSKHFSYENGHPHVIYKKSTLQQQHIYDHSHCGVSDLTGSGKPWWLNKTSSFPSLPPINDTHIHHRKRRSVSTERFVETLVVADKMMVGYHGRKDIEHYILSVMNIVAKLYRDSSLGNVVNIIVARLIVLTEDQPNLEINHHADKSLDSFCKWQKSILSHQSDGNTIPENGIAHHDNAVLITRYDICTYKNKPCGTLGLASVAGMCEPERSCSINEDIGLGSAFTIAHEIGHNFGMNHDGIGNSCGTKGHEAAKLMAAHITANTNPFSWSACSRDYITSFLEFLKLGDSISGS
Protein: Aluminum-activated malate transporter 1 (AtALMT1) (Q9SJE9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Malate transporter critical for aluminum tolerance. The STOP1 transcription factor is required for ALMT1 expression.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Protein SENSITIVE TO PROTON RHIZOTOXICITY 1
- Protein DETOXIFICATION 42
- Protein ALUMINUM SENSITIVE 3
- Protein SENSITIVE TO PROTON RHIZOTOXICITY 2
- Multicopper oxidase LPR2
- Probable manganese-transporting ATPase PDR2
- Probable WRKY transcription factor 46
- Major facilitator superfamily protein
- Protein RAE1
- Calmodulin-binding transcription activator 2
Sequence:
MEKVREIVREGIRVGNEDPRRIIHAFKVGLALVLVSSFYYYQPFGPFTDYFGINAMWAVMTVVVVFEFSVGATLGKGLNRGVATLVAGGLGIGAHQLARLSGATVEPILLVMLVFVQAALSTFVRFFPWVKTKFDYGILIFILTFALISLSGFRDEEIMDLAESRLSTVVIGGVSCILISIFVCPVWAGQDLHSLLASNFDTLSHFLQDFGDEYFEAREKGDYKVVEKRKKNLERYKSVLDSKSDEEALANYAEWEPPHGQFRFRHPWKQYVAVGALLRQCAYRIDALNSYINSDFQIPVDIKKKLETPLRRMSSESGNSMKEMSISLKQMIKSSSSDIHVSNSQAACKSLSTLLKSGILNDVEPLQMISLMTTVSMLIDIVNLTEKISESVHELASAARFKNKMRPTVLYEKSDSGSIGRAMPIDSHEDHHVVTVLHDVDNDRSNNVDDSRGGSSQDSCHHVAIKIVDDNSNHEKHEDGEIHVHTLSNGHLQ
Protein: Serine/threonine-protein kinase PrkC (Ser/Thr-protein kinase PrkC) (EC 2.7.11.1) (O34507)
Organism: Bacillus subtilis (strain 168)
Function: Protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing m-Dpm (meso-diaminopimelate), which act as spore germinants. Autophosphorylates and phosphorylates EF-G (elongation factor G, fusA); the latter modification is likely necessary for germination in response to peptidoglycan. Another group did not detect phosphorylation of EF-G. PrkC is a substrate in vitro of the cotranscribed phosphatase PrpC, which suggests that they form a functional couple in vivo. Might also be involved in sporulation and biofilm formation. Does not seem to be involved in stress response.
Subcellular location: Spore membrane {ECO:0000269|PubMed:18984160}; Single-pass type II membrane protein {ECO:0000269|PubMed:18984160}. Note=Is associated with the inner membrane of the spore.
Interaction partners:
- Protein phosphatase PrpC
- Small ribosomal subunit biogenesis GTPase RsgA
- Serine/threonine-protein kinase YabT
- Cell cycle protein GpsB
- Probable dual-specificity RNA methyltransferase RlmN
- Probable ribosomal RNA small subunit methyltransferase B
- Ribulose-phosphate 3-epimerase
- Methionyl-tRNA formyltransferase
- Septum site-determining protein DivIVA
- Peptide deformylase 1
Sequence:
MLIGKRISGRYQILRVIGGGGMANVYLAEDIILDREVAIKILRFDYANDNEFIRRFRREAQSASSLDHPNIVSIYDLGEEDDIYYIVMEYVEGMTLKEYITANGPLHPKEALNIMEQIVSAIAHAHQNQIVHRDIKPHNILIDHMGNIKVTDFGIATALSSTTITHTNSVLGSVHYLSPEQARGGLATKKSDIYALGIVLFELLTGRIPFDGESAVSIALKHLQAETPSAKRWNPSVPQSVENIILKATAKDPFHRYETAEDMEADIKTAFDADRLNEKRFTIQEDEEMTKAIPIIKDEELAKAAGEKEAEVTTAQENKTKKNGKRKKWPWVLLTICLVFITAGILAVTVFPSLFMPKDVKIPDVSGMEYEKAAGLLEKEGLQVDSEVLEISDEKIEEGLMVKTDPKADTTVKEGATVTLYKSTGKAKTEIGDVTGQTVDQAKKALKDQGFNHVTVNEVNDEKNAGTVIDQNPSAGTELVPSEDQVKLTVSIGPEDITLRDLKTYSKEAASGYLEDNGLKLVEKEAYSDDVPEGQVVKQKPAAGTAVKPGNEVEVTFSLGPEKKPAKTVKEKVKIPYEPENEGDELQVQIAVDDADHSISDTYEEFKIKEPTERTIELKIEPGQKGYYQVMVNNKVVSYKTIEYPKDE
Protein: Cell division cycle protein 20 homolog (mmCdc20) (p55CDC) (Q9JJ66)
Organism: Mus musculus (Mouse)
Function: Required for full ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) and may confer substrate specificity upon the complex. Is regulated by MAD2L1: in metaphase the MAD2L1-CDC20-APC/C ternary complex is inactive and in anaphase the CDC20-APC/C binary complex is active in degrading substrates. The CDC20-APC/C complex positively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 induces presynaptic differentiation.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:34298015}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q12834}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q12834}.
Interaction partners:
- Anaphase-promoting complex subunit 2
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Cell division cycle protein 27 homolog
- Cell division cycle protein 16 homolog
- F-box only protein 5
- Ubiquitin-conjugating enzyme E2 C
- Cell division cycle protein 23 homolog
- G2/mitotic-specific cyclin-B2
- Mitotic spindle assembly checkpoint protein MAD2A
- Cyclin-A2
Sequence:
MAQFVFESDLHSLLQLDAPIPNAPVARWQRKAKEATGPAPSPMRAANRSHSAGRTPGRTPGKSSSKVQTTPSKPGGDRFIPQRSASQMEVASFLLSKENQPEDRGTPTKKEHQKAWSLNLNGFDVEEAKILRLSGKPQNAPEGYQNRLKVLYSQKATPGSSRKTCRYIPSLPDRILDAPEIRNDYYLNLVDWSSGNVLAVALDNSVYLWNAGSGDILQLLQMEQPGDYISSVAWIKEGNYLAVGTSNAEVQLWDVQQQKRLRNMTSHSARVSSLSWNSYILSSGSRSGHIHHHDVRVAEHHVATLSGHSQEVCGLRWAPDGRHLASGGNDNIVNVWPSGPGESGWAPLQTFTQHQGAVKAVAWCPWQSNILATGGGTSDRHIRIWNVCSGACLSAVDVHSQVCSILWSPHYKELISGHGFAQNQLVIWKYPTMAKVAELKGHTARVLGLTMSPDGATVASAAADETLRLWRCFEMDPALRREREKASVAKSSLIHQGIR
Protein: Protein RESISTANCE TO PHYTOPHTHORA 1, chloroplastic (StRPH1) (M1C5M7)
Organism: Solanum tuberosum (Potato)
Function: Plays a positive role in the immune response to the oomycetes P.infestans, including induced oxidative burst and enhanced expression of defense-related genes.
Subcellular location: Plastid, chloroplast {ECO:0000250|UniProtKB:Q9ZU82}. Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MNSATTMSASVLNYQILKFFPPQKNGFLKSPLIRGKICRFCVSASSNELNKQVIEDPKEETQEKSDGVIVNSTEEEEERSGENSTSTGPSTVLDNKELKKAVLKTASTFAPRASTATKNPAKPGTVLYTVFEVQAYASMLIGGALSFNLIFPSTEPDIWRLMGMWSIWMFTIPSLRARDCSKDEKEALNYLFLLVPLLNVAIPFFLKSFAVVWSADTVAFLGMYAWKLGWLQKER
Protein: Diacylglycerol acyltransferase, putative (Q386T8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
Sequence:
MAGTQAAVDYTKVLVKNTVRFILLVLFLISLVVSLLLCMLADIFQAYAPVFPLWPMVFASVALNVACAVSTSLYHRVTCKASRSYKSSGSNHAYLAMQGFGYGLLFICPAVLFLYIELLASPVAVYRYGLITALGGSCAVANGLLIASLRYSEKTQRRVKEGGLGGGERPQRDSGLWRRRLLLLPDGETAIVVLLCIIALTCSIIAEYFTHLRRALTIVGMLLLVVSAAITRVGTGYRSATGEHPFSISRCSFRTGIVQGLGWFLGGATLCFDLVLCNSGAGAPPSWHIISGLSSMVSVAALLFARFHRFTEPTFKQGLQLSSDGPYVMTATSLFQLTFVWCLTLLLSTEYCELGMQLRQGLITCQTLTAVSMFALPLCTHFLGRVVFGKEYGIWISLDCRLEFAILQRLAWFCYSIAIFFAVLHMTESNHFRFVVIQALLVGVSQCLVHASLWAFGGGTLGRYSSDVEDQESLSRTTSTKSTSQEEDSEGEASVSYEGGRSALPLVLNAEMVTAIAVCVCGIALRLVADVESMDGAFVGALLGVPRKSLLNLARVMATVAVPLAHISSRDRVPLWQPFVGCGGYVSMQAVGWSVYAINTLIEAANYFHEERRSLASPVFGTQSMPLEHTVDGVCATVPFICIFLGSLFETWAQQSEKIHQRKMQQKIVELNSLLQHVIADPEDRERTKSLLKVVIGPRWKDLRSSGSSDEDERAEEVETRKEGMRNIVAILCVCVMMLFATSAFSATHQPAFTLIFGISGMMMTSVSCFSLQLFYGSIVHGATGTYSYFMPFSGGQKFVAFQTAGWSCYAAALLLILISCLEGRGSPTAFVCMGFFSVAAQFLILNSIPHFDSTPRPASLLEQNAEAALAVFALVGSFTFGVVWNAYTGGGIPGQAPSPLPIIVTAIAASCAAPLGIVSLKRHMERSAMFAVADGLESSSEASDGEEEIRSDGHTDAIAHVSNGSGHQFPSSLMQGQVNTGVDSERGTNDSFDTQASRSFPGSTGSFGSGKRCRSVQHMEVIPGTLYTICLILALLATLIWVIFVPIVLFYMFYSYAYSGLAVFHMTFTTFHIVLFLLSIAVVTPVLVQIIYDRRCKGLRGKFWSPLVAFTVYSLPTIVVSTVLVVWTQVDTMGAEVFALNMVFMSCLSFLSCAYLVASLFNTCFLGYVLHFYLYTCLVQGLAPLVVWKCVTDVGFTVFWLWYLRGYGKLPHITGCMCGAKSRDLFRTYLSPAIVDYFSARLIVDGRGKAGRGKTVIYSNSEGEEENAGPDHNDPSNKYIYSFHPHGVFPGTALWLPMSPQWEELIGRNEETIVTTHGADVIFAVPFMRDALMSVGTMSVSRKGIENCLKQNNSPIIVTGGMAEMVYQKGSDTEMHIVMHHSGFVRMALQHGVPIVPILCFAEQNVMMNVPFPRLQRLTSRKLGFPFPTMPYGRWFLPLPHARPLTVVVGKPILPDPAMCNADDPDHVVHYRLRYFGELQRLFFKYRDEAGYPNMVLHLHCHNETHIVTEFKGSESVKDDQNQ
Protein: Membrane-associated phosphatidylinositol transfer protein 2 (Phosphatidylinositol transfer protein, membrane-associated 2) (PITPnm 2) (Pyk2 N-terminal domain-interacting receptor 3) (NIR-3) (Q9BZ72)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes (in vitro). Binds calcium ions.
Subcellular location: Endomembrane system {ECO:0000269|PubMed:22361696}; Peripheral membrane protein {ECO:0000269|PubMed:22361696}.
Interaction partners:
- Protein-tyrosine kinase 2-beta
- Vesicle-associated membrane protein-associated protein A
- Vesicle-associated membrane protein-associated protein B/C
Sequence:
MIIKEYRIPLPMTVEEYRIAQLYMIQKKSRNETYGEGSGVEILENRPYTDGPGGSGQYTHKVYHVGMHIPSWFRSILPKAALRVVEESWNAYPYTRTRFTCPFVEKFSIDIETFYKTDAGENPDVFNLSPVEKNQLTIDFIDIVKDPVPHNEYKTEEDPKLFQSTKTQRGPLSENWIEEYKKQVFPIMCAYKLCKVEFRYWGMQSKIERFIHDTGLRRVMVRAHRQAWCWQDEWYGLSMENIRELEKEAQLMLSRKMAQFNEDGEEATELVKHEAVSDQTSGEPPEPSSSNGEPLVGRGLKKQWSTSSKSSRSSKRGASPSRHSISEWRMQSIARDSDESSDDEFFDAHEDLSDTEEMFPKDITKWSSNDLMDKIESPEPEDTQDGLYRQGAPEFRVASSVEQLNIIEDEVSQPLAAPPSKIHVLLLVLHGGTILDTGAGDPSSKKGDANTIANVFDTVMRVHYPSALGRLAIRLVPCPPVCSDAFALVSNLSPYSHDEGCLSSSQDHIPLAALPLLATSSPQYQEAVATVIQRANLAYGDFIKSQEGMTFNGQVCLIGDCVGGILAFDALCYSNQPVSESQSSSRRGSVVSMQDNDLLSPGILMNAAHCCGGGGGGGGGGGSSGGGGSSGGSSLESSRHLSRSNVDIPRSNGTEDPKRQLPRKRSDSSTYELDTIQQHQAFLSSLHASVLRTEPCSRHSSSSTMLDGTGALGRFDFEITDLFLFGCPLGLVLALRKTVIPALDVFQLRPACQQVYNLFHPADPSASRLEPLLERRFHALPPFSVPRYQRYPLGDGCSTLLADVLQTHNAAFQEHGAPSSPGTAPASRGFRRASEISIASQVSGMAESYTASSIAQKAPDALSHTPSVRRLSLLALPAPSPTTPGPHPPARKASPGLERAPGLPELDIGEVAAKWWGQKRIDYALYCPDALTAFPTVALPHLFHASYWESTDVVSFLLRQVMRHDNSSILELDGKEVSVFTPSKPREKWQRKRTHVKLRNVTANHRINDALANEDGPQVLTGRFMYGPLDMVTLTGEKVDVHIMTQPPSGEWLYLDTLVTNNSGRVSYTIPESHRLGVGVYPIKMVVRGDHTFADSYITVLPKGTEFVVFSIDGSFAASVSIMGSDPKVRAGAVDVVRHWQDLGYLIIYVTGRPDMQKQRVVAWLAQHNFPHGVVSFCDGLVHDPLRHKANFLKLLISELHLRVHAAYGSTKDVAVYSAISLSPMQIYIVGRPTKKLQQQCQFITDGYAAHLAQLKYSHRARPARNTATRMALRKGSFGLPGQGDFLRSRNHLLRTISAQPSGPSHRHERTQSQADGEQRGQRSMSVAAGCWGRAMTGRLEPGAAAGPK