wanglab/gogpt-training-data huggingface dataset:
Protein: CRIB domain-containing protein RIC5 (ROP-interactive CRIB motif-containing protein 5) (Target of ROP protein RIC5) (F4J424)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as downstream effector of Rho-related GTP binding proteins of the 'Rho of Plants' (ROPs) family. Participates in the propagation of ROP GTPase signals in specific cellular responses. Is involved in pollen tube growth regulation through its interaction with ARAC11/ROP1.
Subcellular location: Cell membrane {ECO:0000305|PubMed:11752391}; Peripheral membrane protein {ECO:0000305|PubMed:11752391}.
Interaction partners:
- Immunoglobulin E-set superfamily protein
- At1g12070
- Rac-like GTP-binding protein ARAC11
- Guanosine nucleotide diphosphate dissociation inhibitor 2
- Pollen receptor-like kinase 3
- Phosphatidylinositol 4-phosphate 5-kinase 6
- Phosphatidylinositol 4-phosphate 5-kinase 4
- Rac-like GTP-binding protein ARAC6
- Ubiquitin-conjugating enzyme family protein
- Rho GDP-dissociation inhibitor 1
Sequence:
MTSPMKGLLKGLRYIARIFEDEKEPEMQIGIPTDVKHVAHIGWEGPSATTPSWMHDFKPTDQTKTETKGTSNKKPGSSGEKHRKGRRKTSTGNNSPTESPSRVGGSVRPSKRNTGKQREQNTGSGSESGSGLELPQQTDQFVVPKQSKQKKSKGSATGGGEPPPSNEPSNKKETDISVRAVYPCAGLGSSTGR
Protein: RAR-related orphan receptor C (A0A8I6GEH3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004334}.
Interaction partners:
Sequence:
MDRAPQRHHRTSRELLAAKKTHTSQIEVIPCKICGDKSSGIHYGVITCEGCKGFFRRSQQCNVAYSCTRQQNCPIDRTSRNRCQHCRLQKCLALGMSRDAVKFGRMSKKQRDSLHAEVQKQLQQQQQREQVAKTPPAGSHGADTLTYTLGVPDGQLPLGASPDLPEASACPPGLLRASGSGPPYSNTLAKTEVQGASCHLEYSPERGKAEGRDSIYSTDGQLTLGRRGLQLGEPEQGSDSHCSPSFCSAPEAPYASLTDIEYLVQNVCKSYRETCQLRLEDLLRQRTNLFSREEVTSYQRKSMWEMWERCAHHLTEAIQYVVEFAKRLSGFMELCQNDQIILLKAGAMEVVLVRMCRAYNANNHTVFFEGKYGGVELFRALGCSELISSIFDFSHFLSALCFSEDEIALYTALVLINANRPGLQEKRRVEHLQYNLELAFHHHLCKTHRQGLLAKLPPKGKLRSLCSQHVEKLQDFQHLHPIVVQAAFPPLYKELFSTDIESSEGLSK
Protein: Methyl-CpG-binding domain-containing protein 10 (AtMBD10) (MBD10) (Methyl-CpG-binding protein MBD10) (Q9XI36)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcriptional regulator (By similarity). Required for nucleolar dominance that consist in the silencing of rRNA genes inherited from one progenitor in genetic hybrids.
Subcellular location: Nucleus {ECO:0000269|PubMed:19061642}.
Interaction partners:
- Methyl-CpG-binding domain-containing protein 6
- Methyl-CpG-binding domain-containing protein 8
- Histone deacetylase 6
- Methyl-CpG-binding domain-containing protein 1
- Methyl-CpG-binding domain-containing protein 9
- Methyl-CpG-binding domain-containing protein 7
- Methyl-CpG-binding domain-containing protein 2
- Methyl-CpG-binding domain-containing protein 13
- Methyl-CpG-binding domain-containing protein 5
- Methyl-CpG-binding domain-containing protein 4
Sequence:
MENTDELVSIELPAPASWKKLFYPKRAGTPRKTEIVFVAPTGEEISSRKQLEQYLKAHPGNPVISEFEWTTGETPRRSSRISQKVKATTPTPDKEPLLKKRRSSLTKKDNKEAAEKNEEAAVKENMDVDKDGKTENAEAEKEKEKEGVTEIAEAEKENNEGEKTEAEKVNKEGEKTEAGKEGQTEIAEAEKEKEGEKAEAENKEAEVVRDKKESMEVDTSELEKKAGSGEGAEEPSKVEGLKDTEMKEAQEVVTEADVEKKPAEEKTENKGSVTTEANGEQNVTLGEPNLDADAEADKGKESKEYDEKTTEAEANKENDTQESDEKKTEAAANKENETQESDVKKTEAAVAEEKSNDMKAEDTNRSLEANQVQQQQGAAASVSC
Protein: AT3g61200/T20K12_100 (Thioesterase superfamily protein) (Q9M2E4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- 2-carboxy-1,4-naphthoquinone phytyltransferase, chloroplastic
Sequence:
MNWAKFRETGSPEDTDMSSTPISSDTTAVSKVIDPNYVLMVADFFKAISPDESCNDFTSFDSFSVLFQNNTRALSIARGRVSCSVTVTPGISNFFKGLHGGAVASIAERVAMACVKTVVSEDKHLFIGELSMSYLSSAPISSELLVEGTVVRTGRNLSVVTVEFKIKETMKVTYLSRATFYHSPISKL
Protein: Dynactin subunit 1 (Q07DR3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cell cortex {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000256|ARBA:ARBA00004114}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}.
Interaction partners:
Sequence:
MSSDGGGRPVKVGSVVEVIGKGQRGTVAYIGATLFASGKWVGVILDEAKGKNDGTVQGKRYFTCEENHGIFVRQSQIQLIDDGGSSATSPETPDSGVAKLLKKEIQETPKTAKQTGRPSVGGSALSESVLAESESSSSTQMSLAAPVVPQPSTASAPAPATPSKEEESLRAQLKDLEEKLETLRMKRSEDKAKLKEMEKYKIQLEQLQEWRSKMQEQQNDLQKQLKEAKKEAREALEAKDRYMEEMADTADAIEMATLDKEMAEERAESLQQETESLKEKLEELTMDMEILKHEIEEKGSDGAASSYHVKQLEEQNARLKEALVRMRDLSSSEKQEHVKLQKQMEKKNSELETLRSQKEKLQEEMKLAEDTIDELKEQVDAALGAEEMVETLTERNLDLEEKVRELRETVSDLESINEMNDELQENARETELELREQLDLAGARVREAQKRVEAAQETLADYQQTINKYRELTTHLQEVNRELTNQQSSSAEQLQQPAAELFDFKIKFAETKAYAKAIEMELRKMEVSQANRQVSLLTSFMPESFLRHGGDHDCILVLLLIPRLICKAELISKQAQEKFDLNGGSLERAGLRGAAGEQLSFASGLVYSLTLLQATLHKYELALSVCGVDVYKRMGTLYSEMCVHERSLDFLIDLLHKDQLDETVQVEPLTKAIKYYQHLYSVHLCDQPEDCTVQLADHIKFTQSALDCMGSEVGRLRAFLQAGQEGAELCVLLKDLDTSCGDIRQFCKKIRRRMPGTDAPGIPAALRFSEQVSEALADSRKQLARVVAVLQEVSAAGAQMMAPLQEQEGLSAVKIEDVAFKAVEQVYGTQGLNPYECLRQSCSAVIATMNKMATAMQEGEYDSERPQRPPPPVETRAAAVRAEMTDAEGLGNKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDTSTKDADERVEKIQTKLDEALNTLKKKEKEFEETMDALQADIDQLESEKAELKQRISSQSRATEGLRGQPASGIASIVTGNVAGGMLSAPAGVSGVVQVVDSPLLKQQIDVQRIAIKQLKSENYRLKAERMRAQLSSLPPLQVPNMKSVMMKENTAAGALQRKTDVLLHNLMKMSAGLKVVDITGKTTASASAQLLEQTAKMKSLSDALDKLQAEVSQHVVSQQPGASVPSDFATFPTATFVKAQQEQQSGCVLVSKLMIPCARGKEQKHTLVLSQQQLQRVHHLLMT
Protein: Shiga toxin subunit B (Q32GM0)
Organism: Shigella dysenteriae serotype 1 (strain Sd197)
Function: The B subunit is responsible for the binding of the holotoxin to specific receptors on the target cell surface, such as globotriaosylceramide (Gb3) in human intestinal microvilli.
Interaction partners:
- Shiga toxin subunit A
Sequence:
MKKTLLIAASLSFFSASALATPDCVTGKVEYTKYNDDDTFTVKVGDKELFTNRWNLQSLLLSAQITGMTVTIKTNACHNGGGFSEVIFR
Protein: Down syndrome cell adhesion molecule 1, isoform CB (A0A0B4K6Y9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNMPNERLKWLMLFAAVALIACGSQTLAANPPDADQKGPVFLKEPTNRIDFSNSTGAEIECKASGNPMPEIIWIRSDGTAVGDVPGLRQISSDGKLVFPPFRAEDYRQEVHAQVYACLARNQFGSIISRDVHVRAVVAQYYDTDVNKAYVIRGNAAVLKCEIPSFVADFVSVVSWHTDQNEDFLPGSEYDGKYLVLPSGELHIREVGPEDGYKSYQCRTKHRLTGETRLSATKGRLVITEPVGSVAPKVDTRDEFTFARTRMGASKALICPAQSYPMPFFRWYKFIEGTTRKQAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGESVETVLTVTAPLSAKIDPPTQTVDFGRPAVFTCQYTGNPIKTVSWMKDGKAIGHSEPVLRIESVKKEDKGMYQCFVRNDQESAEASAELKLGGRFDPPVIRQAFQEETMEPGPSVFLKCVAGGNPTPEISWELDGKKIANNDRYQVGQYVTVNGDVVSYLNITSVHANDGGLYKCIAKSKVGVAEHSAKLNVYGLPYIRQMEKKAIVAGETLIVTCPVAGYPIDSIVWERDNRALPINRKQKVFPNGTLIIENVERNSDQATYTCVAKNQEGYSARGSLEVQVMVLPQIVPFAYEDLINMGDSIDLFCQIQKGDRPIKVHWSFERSAGDYGFDQVQPQMRTNRISEKTSMISIPSASPAHTGRDTCIASNKAGTTTYSVDLTVNVPPRWILEPTDKAFAQGSDAKVECKADGFPKPQVTWKKAVGDTPGEYKDLKKSDNIRVEEGTLHVDNIQKTNEGYYLCEAINGIGSGLSAVIMISVQAPPEFTEKLRNQTARRGEPAVLQCEAKGEKPIGILWNMNNMRLDPKNDNRYTIREEILSTGVMSSLSIKRTERSDSALFTCVATNAFGSDDASINMIVQEVPEMPYALKVLDKSGRSVQLSWAQPYDGNSPLDRYIIEFKRSRASWSEIDRVIVPGHTTEAQVQKLSPATTYNIRIVAENAIGTSQSSEAVTIITAEEAPSGKPQNIKVEPVNQTTMRVTWKPPPRTEWNGEILGYYVGYKLSNTNSSYVFETINFITEEGKEHNLELQNLRVYTQYSVVIQAFNKIGAGPLSEEEKQFTAEGTPSQPPSDTACTTLTSQTIRVGWVSPPLESANGVIKTYKVVYAPSDEWYDETKRHYKKTASSDTVLHGLKKYTNYTMQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPSRDLPELSAEDTIRIILSNLNLVVPVVAALLVIIIAIIVICILRSKGNHHKDDVVYNQTMGPGATLDKRRPDLRDELGYIAPPNRKLPPVPGSNYNTCDRIKRGRGGLRSNHSTWDPRRNPNLYEELKAPPVPMHGNHYGHAHGNAECHYRHPGMEDEICPYATFHLLGFREEMDPTKAMNFQTFPHQNGHAGPVPGHAGTMLPPGHPGHVHSRSGSQSMPRANRYQRKNSQGGQSSIYTPAPEYDDPANCAEEDQYRRYTRVNSQGGSLYSGPGPEYDDPANCAPEEDQYGSQYGGPYGQPYDHYGSRGSMGRRSIGSARNPGNGSPEPPPPPPRNHDMSNSSFNDSKESNEISEAECDRDHGPRGNYGAVKRSPQPKDQRTTEEMRKLIERNETGPKQLQLQQANGAGFTAYDTMAV
Protein: Protransforming growth factor alpha [Cleaved into: Transforming growth factor alpha (TGF-alpha) (EGF-like TGF) (ETGF) (TGF type 1)] (P48030)
Organism: Mus musculus (Mouse)
Function: TGF alpha is a mitogenic polypeptide that is able to bind to the EGF receptor/EGFR and to act synergistically with TGF beta to promote anchorage-independent cell proliferation in soft agar.
Subcellular location: [Transforming growth factor alpha]: Secreted, extracellular space.; SUBCELLULAR LOCATION: [Protransforming growth factor alpha]: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Epidermal growth factor receptor
- Pro-epidermal growth factor
- Receptor tyrosine-protein kinase erbB-3
- Receptor tyrosine-protein kinase erbB-2
- Receptor tyrosine-protein kinase erbB-4
- Insulin-like growth factor 1
- Insulin-2
- Insulin-1
- Amphiregulin
- Platelet-derived growth factor subunit B
Sequence:
MVPATGQLALLALGILLAVCQALENSTSPLSDSPVAAAVVSHFNKCPDSHTQYCFHGTCRFLVQEEKPACVCHSGYVGVRCEHADLLAVVAASQKKQAITALVVVSIVALAVLIITCVLIHCCQLRKHCEWCRALVCRHEKPSALLKGRTACCHSETVV
Protein: Transcriptional activator protein LuxR (P12746)
Organism: Aliivibrio fischeri (Vibrio fischeri)
Function: Transcriptional activator of the bioluminescence operon. Binds to the OHHL autoinducer.
Interaction partners:
Sequence:
MKNINADDTYRIINKIKACRSNNDINQCLSDMTKMVHCEYYLLAIIYPHSMVKSDISILDNYPKKWRQYYDDANLIKYDPIVDYSNSNHSPINWNIFENNAVNKKSPNVIKEAKTSGLITGFSFPIHTANNGFGMLSFAHSEKDNYIDSLFLHACMNIPLIVPSLVDNYRKINIANNKSNNDLTKREKECLAWACEGKSSWDISKILGCSERTVTFHLTNAQMKLNTTNRCQSISKAILTGAIDCPYFKN
Protein: [histone H3]-trimethyl-L-lysine(4) demethylase (EC 1.14.11.67) (A0A3B3ITE7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEAATTLHPGPRPALPLGGPGPLGEFLPPPECPVFEPSWEEFADPFAFIHKIRPIAEQTGICKVRPPPDWQPPFACDVDKLHFTPRIQRLNELEAQTRVKLNFLDQIAKYWELQGSTLKIPHVERKILDLFQLNKLVAEEGGFAVVCKDRKWTKIATKMGFAPGKAVGSHIRGHYERILNPYNLFLSGDSLRCLQKPNLTTDTKDKEYKPHDIPQRQSVQPSETCPPARRAKRMRAEAMNIKIEPEETTEARTHNLRRRMGCPTPKCENEKEMKSSIKQEPIERKDYIVENEKEKPKSRSKKATNAVDLYVCLLCGSGNDEDRLLLCDGCDDSYHTFCLIPPLHDVPKGDWRCPKCLAQECSKPQEAFGFEQAARDYTLRTFGEMADAFKSDYFNMPVHMVPTELVEKEFWRLVSTIEEDVTVEYGADIASKEFGSGFPVRDGKIKLSPEEEEYLDSGWNLNNMPVMEQSVLAHITADICGMKLPWLYVGMCFSSFCWHIEDHWSYSINYLHWGEPKTWYGVPGYAAEQLENVMKKLAPELFVSQPDLLHQLVTIMNPNTLMTHEVPVYRTNQCAGEFVITFPRAYHSGFNQGFNFAEAVNFCTVDWLPLGRQCVEHYRLLHRYCVFSHDEMICKMASKADVLDVVVASTVQKDMAIMIEDEKALRETVRKLGVIDSERMDFELLPDDERQCVKCKTTCFMSAISCSCKPGLLVCLHHVKELCSCPPYKYKLRYRYTLDDLYPMMNALKLRAESYNEWALNVNEALEAKINKKKSLVSFKALIEESEMKKFPDNDLLRHLRLVTQDAEKCASVAQQLLNGKRQTRYRSGGGKSQNQLTVNELRQFVTQLYALPCVLSQTPLLKDLLNRVEDFQQHSQKLLSEETPSAAELQDLLDVSFEFDVELPQLAEMRIRLEQARWLEEVQQACLDPSSLTLDDMRRLIDLGVGLAPYSAVEKAMARLQELLTVSEHWDDKAKSLLKARPRHSLNSLATAVKEIEEIPAYLPNGAALKDSVQRARDWLQDVEGLQAGGRVPVLDTLIELVTRGRSIPVHLNSLPRLETLVAEVQAWKECAVNTFLTENSPYSLLEVLCPRCDIGLLGLKRKQRKLKEPLPNGKKKSTKLESLSDLERALTESKETASAMATLGEARLREMEALQSLRLANEGKLLSPLQDVDIKICLCQKAPAAPMIQCELCRDAFHTSCVAVPSISQGLRIWLCPHCRRSEKPPLEKILPLLASLQRIRVRLPEGDALRYMIERTVNWQHRAQQLLSSGNLKFVQDRVGSGLLYSRWQASAGQVSDTNKVSQPPGTTSFSLPDDWDNRTSYLHSPFSTGRSCIPLHGVSPEVNELLMEAQLLQVSLPEIQELYQTLLAKPSPAQQTDRSSPVRPSSEKNDCCRGKRDGINSLERKLKRRLEREGLSSERWERVKKMRTPKKKKIKLSHPKDMNNFKLERERSYELVRSAETHSLPSDTSYSEQEDSEDEDAICPAVSCLQPEGDELSPSRR
Protein: Phosphomannomutase (PMM) (EC 5.4.2.8) (Asparagine-linked glycosylation protein 4) (P07283)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions such as folding and glycosylation of secretory proteins in the ER lumen.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:3905826}.
Interaction partners:
- Mannose-1-phosphate guanyltransferase
- Mannose-6-phosphate isomerase
- Hexokinase-2
- N-acetylglucosamine kinase
- Putative glucokinase-2
- Glucokinase-1
- Hexokinase-1
- Dolichol-phosphate mannosyltransferase
- Glucose-6-phosphate isomerase
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
Sequence:
MSIAEFAYKEKPETLVLFDVDGTLTPARLTVSEEVRKTLAKLRNKCCIGFVGGSDLSKQLEQLGPNVLDEFDYSFSENGLTAYRLGKELASQSFINWLGEEKYNKLAVFILRYLSEIDLPKRRGTFLEFRNGMINVSPIGRNASTEERNEFERYDKEHQIRAKFVEALKKEFPDYGLTFSIGGQISFDVFPAGWDKTYCLQHVEKDGFKEIHFFGDKTMVGGNDYEIFVDERTIGHSVQSPDDTVKILTELFNL
Protein: Outer membrane usher protein YraJ (P42915)
Organism: Escherichia coli (strain K12)
Function: Part of the yraHIJK fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches. Increases adhesion to eukaryotic T24 bladder epithelial cells in the absence of fim operon. Probably involved in the export and assembly of fimbrial subunits across the outer membrane.
Subcellular location: Cell outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Probable fimbrial chaperone YraI
- Uncharacterized fimbrial-like protein YraK
- Chaperone protein FimC
- Probable fimbrial chaperone SfmC
- Uncharacterized fimbrial chaperone YqiH
- Probable fimbrial chaperone YfcS
- Uncharacterized fimbrial chaperone YcbF
- Probable fimbrial chaperone YadV
- Uncharacterized fimbrial chaperone YbgP
- Probable fimbrial chaperone protein ElfD
Sequence:
MPQRHHQGHKRTPKQLALIIKRCLPMVLTGSGMLCTTANAEEYYFDPIMLETTKSGMQTTDLSRFSKKYAQLPGTYQVDIWLNKKKVSQKKITFTANAEQLLQPQFTVEQLRELGIKVDEIPALAEKDDDSVINSLEQIIPGTAAEFDFNHQQLNLSIPQIALYRDARGYVSPSRWDDGIPTLFTNYSFTGSDNRYRQGNRSQRQYLNMQNGANFGPWRLRNYSTWTRNDQTSSWNTISSYLQRDIKALKSQLLLGESATSGSIFSSYTFTGVQLASDDNMLPNSQRGFAPTVRGIANSSAIVTIRQNGYVIYQSNVSAGAFEINDLYPSSNSGDLEVTIEESDGTQRRFIQPYSSLPMMQRPGHLKYSATAGRYRADANSDSKEPEFAEATAIYGLNNTFTLYGGLLGSEDYYALGIGIGGTLGALGALSMDINRADTQFDNQHSFHGYQWRTQYIKDIPETNTNIAVSYYRYTNDGYFSFNEANTRNWDYNSRQKSEIQFNISQTIFDGVSLYASGSQQDYWGNNDKNRNISVGVSGQQWGVGYSLNYQYSRYTDQNNDRALSLNLSIPLERWLPRSRVSYQMTSQKDRPTQHEMRLDGSLLDDGRLSYSLEQSLDDDNNHNSSLNASYRSPYGTFSAGYSYGNDSSQYNYGVTGGVVIHPHGVTLSQYLGNAFALIDANGASGVRIQNYPGIATDPFGYAVVPYLTTYQENRLSVDTTQLPDNVDLEQTTQFVVPNRGAMVAARFNANIGYRVLVTVSDRNGKPLPFGALASNDDTGQQSIVDEGGILYLSGISSKSQSWTVRWGNQADQQCQFAFSTPDSEPTTSVLQGTAQCH
Protein: Negative elongation factor complex member A (A0A0C4DFX9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPGQRRALSPKMASMRESDTGLWLHNKLGATDELWAPPSIASLLTAAVIDNIRLCFHGLSSAVKLKLLLGTLHLPRRTVDEMKGALMEIIQLASLDSDPWVLMVADILKSFPDTGSLNLELEEQNPNVQDILGELREKVGECEASAMLPLECQYLNKNALTTLAGPLTPPVKHFQLKRKPKSATLRAELLQKSTETAQQLKRSAGVPFHAKGRGLLRKMDTTTPLKGIPKQAPFRSPTAPSVFSPTGNRTPIPPSRTLLRKERGVKLLDISELDMVGAGREAKRRRKTLDAEVVEKPAKEETVVENATPDYAAGLVSTQKLGSLNNEPALPSTSYLPSTPSVVPASSYIPSSETPPAPSSREASRPPEEPSAPSPTLPAQFKQRAPMYNSGLSPATPTPAAPTSPLTPTTPPAVAPTTQTPPVAMVAPQTQAPAQQQPKKNLSLTREQMFAAQEMFKTANKVTRPEKALILGFMAGSRENPCQEQGDVIQIKLSEHTEDLPKADGQGSTTMLVDTVFEMNYATGQWTRFKKYKPMTNVS
Protein: Uncharacterized protein (Q38FH3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MHVASPEDIKHEIEDGRGEWRYVPPCVRQALALVLPTTPKRCSRSRSVTSGCCAPRMLLPLRGSGPKTDVMEAVEAAQLAEQPLAVAGRELLSSSKVLAKHLPKQRRIPPGKPVVRVCSSCGGPLQETGAPGKRCEERPRSGRKGRSASCVLDAHSMGERTQLPGDTSSSVPGVTRRTSSGEQTSRRTHNTARVVQPINMEASKIKRVECIRHRREVTDALLHMVEAVKVLSKEVDTTVVKSVTDAMRLDPRRAKDVRGEVAPVASPSEEQQEALKGLSNSVRWLTNATNELVAVFLTPEEKRFLGLNTHRLQTRKERSTMYQYAKTYRRRDGGLPPPPPGVGENITGDLKEGPRENQDGEGDADEEDVSGKGKSRGEGVQRSEGGKSAEVSSKGAIGKTECGAGVRSPSGAAAGAEDHNPEVGMKGGCVEMSNNTQRSSQLSSVQASRREEKLSEDNQVKKRLSVSTRGTAEEVSASNAQGSPGQAKLSVGRASASDVANPSVSSTGARNSLPKRRKASDSQSRARESMESLTGQEPPGSAVSGASLAQAETTASAGDLANKNLNKFAVASDSDSDSD
Protein: Phragmoplastin interacting protein 1 (Q9M3B8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: RNA-binding protein which mediates polarized mRNA (e.g. Ran2 transcripts mRNA) transport from the nucleus to the vicinity of the cell plate during cytokinesis and phragmoplast formation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Cell membrane {ECO:0000269|PubMed:18621982}; Peripheral membrane protein {ECO:0000269|PubMed:18621982}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:18621982}. Note=Associates with the forming cell plate during cytokinesis; may shuttle between the nucleus and the forming cell plate. {ECO:0000269|PubMed:18621982}.
Interaction partners:
- GTP-binding nuclear protein Ran-2
- Mitotic checkpoint protein BUB3.2
- Microtubule-associated protein RP/EB family member 1A
- Mitotic checkpoint protein BUB3.1
- Microtubule-associated protein RP/EB family member 1C
- Kinesin-like protein KIN-12A
- Importin subunit beta-1
- Serine/threonine-protein kinase RUNKEL
- Transportin MOS14
- Serine/threonine-protein kinase Aurora-2
Sequence:
MVLSNKKLKQRIRQDLAESLSVSVSETNPQSQSLKLLLDSSSHKPRLSKREKRRNCETFAREDDEIRENEVGNGGSSEKTDTKIKKKRKRDDAVEVDELEGDEGTKEEQKPQKKKNKKKKKKRKVNKTPKKAEEGNVEEKVKVEEIEVNTDNKEEDGVVPNKLYVGGIPYQSTEDEIRSYFRSCGVIIKVDCKMRPEDGAFSGIAFITFDTEDGAKRALAFDRAAMGDRYLTIQQYVKTTTPSIPRRKTSSGFAPEMVDGYNRVYIGNLAWDTTERDIRKLFSDCVINSVRLGKNKETGEFKGYAHVDFKDSVSVAIALKLDQQVICGRPVKICCALKDRPATDHTPGETNNAGSYNMEDTYAAADPVPALAGRSEVDDGNYFATTVSSSKVKRRVCYECGEKGHLSTACPIKLQKADDQANSKLGQETVDGRPAMQSYGLPKNSGDSYYMNETYASTNETYNGGYSASAVGTGKVKRRNCYECGEKGHLSTACPIKLQNTSHTNSTLDHQTVEAGPTQVTSYSLQKKTRDTENNGGSFMDESYATVPISIDVTNGANDASLTSAVSTGKIKKRNCYECGEKGHLSSACPNKLQKQG
Protein: Flavin-dependent thymidylate synthase (FDTS) (EC 2.1.1.148) (FAD-dependent thymidylate synthase) (Thymidylate synthase thy1) (TS) (TSase) (P15808)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NADPH and FADH(2) as the reductant.
Interaction partners:
- Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial
- dihydrofolate reductase
- Thymidylate kinase
- Thymidine kinase 1
- Aminomethyltransferase, mitochondrial
- methionyl-tRNA formyltransferase
- Serine hydroxymethyltransferase 2
- Serine hydroxymethyltransferase 1
- Bifunctional purine biosynthesis protein purH
- Phosphoribosylglycinamide formyltransferase
Sequence:
MGLDIQTEIDKIVIEKVKPEVEYYDVMGGSHRWEVKVHDHGKVALVDTMPRLAPVGQTADFSICQAARVSYGAGTKKVTEDKGLIRYLYRHQHTSPFEMVEFKFHCVMPVFIARQWIRHRTANVNEYSARYSVLPDKFYHPSIEEVRKQSTSNRQGGEEALEPKTAQEFLDYLDKVEENYKTYNELLEKGLSRELGRIGLPVSIYTEWYWKIDLHNLFHFLRLRMDSHSQKEIRDYANTIFALIRPIVPVACEAFIDYAFESLKLTRLEIEAIRTGSPLNTTNKREIEEFEEKKKLLFPNTQA
Protein: Acyl-CoA synthetase X4 (EC 6.2.1.3) (Q9VDU0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
Interaction partners:
Sequence:
MNRSTTQFDKYTKIWSGPRPASFFDADCSIGKILFAFMRNHPNSICQISDTEGTALTNGEAITFAIRIAQQLKAMGLKQDDVVGIVGTNTTYLMPVVLGCLLNGTPFHAVSPWQDEDTIKHLFSITRPKLIFCDGKCFQRLSIIARILKSHVYTLKDHRLGMPRVEDLLEPTTAELYYVPETLLLGGDHTVAILCTSGTTGLPKAVCISNSACLFDFGFVTGQDVLLSFSTIDWSAGMFNMLFSCCHGSTRIITDRPYTPEYMIQLVEKYKVTLLTVVPQQVASLLKTPTLNKQRLASIRFVSVGGGSCYVANLLKLQEFLITGQISYGYALTECGGVAANMGVAKPSSVGRIVPGVRVKILDEAGRSLGHGETGEILVHNGKVWNGYYANPNESKRMQDYQGWFHTGDMGYFDNENYLHIVERKEDLLRFHGAQYSPQEIEQVIAELPDVIEACVFGLWNEVDGDPAAAAVVKIPGSRLTEMDIVEYVAKRLVVDHKQLHCGVFFLPELPKTGSGKVLRQQARDQALGKKWADHGNGH
Protein: Phosphatidylinositol 4-kinase type 2-alpha (EC 2.7.1.67) (Phosphatidylinositol 4-kinase type II-alpha) (Q9BTU6)
Organism: Homo sapiens (Human)
Function: Membrane-bound phosphatidylinositol-4 kinase (PI4-kinase) that catalyzes the phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P), a lipid that plays important roles in endocytosis, Golgi function, protein sorting and membrane trafficking and is required for prolonged survival of neurons. Besides, phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P) is the first committed step in the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3).
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:12324459, ECO:0000269|PubMed:16443754, ECO:0000269|PubMed:22535966}; Lipid-anchor {ECO:0000269|PubMed:22535966}. Membrane raft {ECO:0000269|PubMed:11279162}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q2TBE6}. Presynaptic cell membrane {ECO:0000250|UniProtKB:Q2TBE6}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q2TBE6}. Mitochondrion {ECO:0000250|UniProtKB:Q2TBE6}. Endosome {ECO:0000269|PubMed:16443754, ECO:0000269|PubMed:23146885}. Endosome membrane {ECO:0000269|PubMed:35880319}. Cytoplasmic vesicle {ECO:0000269|PubMed:16443754}. Membrane {ECO:0000269|PubMed:24675427}; Lipid-anchor {ECO:0000269|PubMed:24675427}. Cell membrane {ECO:0000269|PubMed:11279162, ECO:0000269|PubMed:16443754}. Perikaryon {ECO:0000250|UniProtKB:Q2TBE6}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q2TBE6}. Note=Found in subdomains of the plasma membrane termed non-caveolar membrane rafts. Transported from neuronal cell body to neuron projections and neurite tips in a BLOC-1- and AP-3-complexes-dependent manner. {ECO:0000250|UniProtKB:Q2TBE6}.
Interaction partners:
- Phosphatidylinositol 4-kinase beta
- Phosphatidylinositol 4-kinase alpha
- Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha
- Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Phosphatidylinositol 4-phosphate 5-kinase type-1 beta
- Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha
- Phosphatidylinositol 3-kinase regulatory subunit beta
Sequence:
MDETSPLVSPERAQPPDYTFPSGSGAHFPQVPGGAVRVAAAAGSGPSPPGSPGHDRERQPLLDRARGAAAQGQTQTVAAQAQALAAQAAAAAHAAQAHRERNEFPEDPEFEAVVRQAELAIERCIFPERIYQGSSGSYFVKDPQGRIIAVFKPKNEEPYGHLNPKWTKWLQKLCCPCCFGRDCLVLNQGYLSEAGASLVDQKLELNIVPRTKVVYLASETFNYSAIDRVKSRGKRLALEKVPKVGQRFNRIGLPPKVGSFQLFVEGYKDADYWLRRFEAEPLPENTNRQLLLQFERLVVLDYIIRNTDRGNDNWLIKYDCPMDSSSSRDTDWVVVKEPVIKVAAIDNGLAFPLKHPDSWRAYPFYWAWLPQAKVPFSQEIKDLILPKISDPNFVKDLEEDLYELFKKDPGFDRGQFHKQIAVMRGQILNLTQALKDNKSPLHLVQMPPVIVETARSHQRSSSESYTQSFQSRKPFFSWW
Protein: Uncharacterized protein C16E8.08 (O13743)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Uncharacterized protein C3G9.05
Sequence:
MAFSPANSFLINKSICESKEVEPLEANLFGKLHNKLLICKAKKENLEKKLAYQMMYSKLLKSLPKLSSLEENKLTKLKAPIEDMENTKKELEEIRKQSTETELRYLKSLSNTLSFGTLSLSNEINKVGPSASFMLKEVHDSVQVLEQRLEKMGLIEKPSESSESSIYSILASLKHTNDSLQKKELSPHEIAESPSSHSTSPMGRNVDTETLSFLLIDWQRLCAEQNTFLRDITNNMSSSVPQDVLSQLRQFFFRSELLSDKLSNLCSES
Protein: Delta(7)-sterol 5(6)-desaturase (EC 1.14.19.20) (C-5 sterol desaturase) (Ergosterol Delta(5,6) desaturase) (Sterol-C5-desaturase) (P50860)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Catalyzes the introduction of a C-5 double bond in the B ring of ergosterol. May contribute to the regulation of ergosterol biosynthesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome K complete sequence
- Sterol 24-C-methyltransferase
- C-8 sterol isomerase
- C-22 sterol desaturase ERG5
- Squalene synthase
- Delta
- 3-keto-steroid reductase
- Terpene cyclase/mutase family member
- Sterol-4-alpha-carboxylate 3-dehydrogenase ERG26, decarboxylating
- Candida glabrata strain CBS138 chromosome J complete sequence
Sequence:
MDLVLETLDHYIFDDVYAKIAPVELQRGIDDSLVNALSLNKIVSNSTLLHETLSITNSLKRVNKDVYGLTPFLFDFTEKTYASLLPRNNLIREFFSLWAVVTVFGLLLYLITASLSYVFVFDRTIFNHPKYLKNQMYLEIKLAVSAIPTMSLLTVPWFMLELNGYSKLYYDVDWEHHGLRKLLIEYATFIFFTDCGIYLAHRWLHWPRVYKALHKPHHKWLVCTPFASHAFHPVDGYFQSLSYHIYPMILPLHKISYLILFTFVNFWSVMIHDGQHMSNNPVVNGTACHTVHHLYFNYNYGQFTTLWDRLGGSYRRPEDSLFDPKLKMDKKVLEKQARETAAYIQEVEGDDTDRVYNTDKKKTN
Protein: Protein CROC-4 (Contingent replication of cDNA 4) (MIR9-1 host gene) (Q13536)
Organism: Homo sapiens (Human)
Function: May play a role in FOS signaling pathways involved in development and remodeling of neurons. Promotes transcription of the FOS promoter.
Subcellular location: Nucleus {ECO:0000269|PubMed:10995546}. Note=Associates within the nuclear transcriptional apparatus during proliferation and differentiation.
Interaction partners:
Sequence:
MFLTEDLITFNLRNFLLFQLWESSFSPGAGGFCTTLPPSFLRVDDRATSSTTDSSRAPSSPRPPGSTSHCGISTRCTERCLCVLPLRTSQVPDVMAPQHDQEKFHDLAYSCLGKSFSMSNQDLYGYSTSSLALGLAWLSWETKKKNVLHLVGLDSL