wanglab/gogpt-training-data huggingface dataset:
Protein: Protein Aster-A (GRAM domain-containing protein 1A) (Q96CP6)
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 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). May play a role in tumor progression (By similarity). Plays a role in autophagy regulation and is required for biogenesis of the autophagosome. This function in autophagy requires its cholesterol-transfer activity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29469807}; Single-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:29469807}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:31222192}. Note=In lipid-poor conditions localizes to the ER membrane and is recruited to endoplasmic reticulum-plasma membrane contact sites (EPCS) in response to excess cholesterol in the PM (By similarity). Localizes to distinct EPCS than GRAMD2A and ESYT2/3 (PubMed:29469807). {ECO:0000250|UniProtKB:Q8VEF1, ECO:0000269|PubMed:29469807}.
Interaction partners:
Sequence:
MFDTTPHSGRSTPSSSPSLRKRLQLLPPSRPPPEPEPGTMVEKGSDSSSEKGGVPGTPSTQSLGSRNFIRNSKKMQSWYSMLSPTYKQRNEDFRKLFSKLPEAERLIVDYSCALQREILLQGRLYLSENWICFYSNIFRWETTISIQLKEVTCLKKEKTAKLIPNAIQICTESEKHFFTSFGARDRCFLLIFRLWQNALLEKTLSPRELWHLVHQCYGSELGLTSEDEDYVSPLQLNGLGTPKEVGDVIALSDITSSGAADRSQEPSPVGSRRGHVTPNLSRASSDADHGAEEDKEEQVDSQPDASSSQTVTPVAEPPSTEPTQPDGPTTLGPLDLLPSEELLTDTSNSSSSTGEEADLAALLPDLSGRLLINSVFHVGAERLQQMLFSDSPFLQGFLQQCKFTDVTLSPWSGDSKCHQRRVLTYTIPISNPLGPKSASVVETQTLFRRGPQAGGCVVDSEVLTQGIPYQDYFYTAHRYCILGLARNKARLRVSSEIRYRKQPWSLVKSLIEKNSWSGIEDYFHHLERELAKAEKLSLEEGGKDARGLLSGLRRRKRPLSWRAHGDGPQHPDPDPCARAGIHTSGSLSSRFSEPSVDQGPGAGIPSALVLISIVICVSLIILIALNVLLFYRLWSLERTAHTFESWHSLALAKGKFPQTATEWAEILALQKQFHSVEVHKWRQILRASVELLDEMKFSLEKLHQGITVSDPPFDTQPRPDDSFS
Protein: Contig An03c0130, genomic contig (A2QGV2)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MPEFKISASLEGHGDDVRAVAFPNPNAIFSASRDATVRLWKLVSTPPPAYDYTITSHGQAFINALAYYPPTPQFPDGLVLSGGQDTIIEARQPGKAADDNADAMLLGHTHNVCALDVSHDGGWVVSGSWDSTARLWKVGKWETDVVLEGHQGSVWTVLAYDKDTVITGCADKIIRIFNTSGTLLRTIENSQDVVRALCKVPASNPTGAHFASASNDGVIRLFTIQGQLVGEMHGHESFIYSLAALPSGELVSSGEDRTVRVWDGTQCVQTITHPAISVWSVAVCKETGDIVTGASDRITRVFSRSQERVASPEVVQQFEKTVKESAIPEQQIGKINKDKLPGTEFLRQKSGTKDGQVQMIREADGSVTAHTWSAASREWVAVGTVVDSAASSGRKTEYLGQDYDYVFDVDVEDGKPPLKLPYNVSQNPYEAATKFIQDNELSMNYLDQVAQFIVQNTQGATLERRYRPEDAQSPPAPEARPKVLPQKTYLSIKSANLKLIAKKLQELNQHVISSGSKDLSLSPSELETVATLCGQLESSNVEQSPAVEAGVVLLYKVATVWPVASRLPGLDLLRLSAAATPVTATADYDGKDLISGIKSSGVFDSPFNVNNAMLSIRMLANLFETDAGRDLATSKFEQILSGVKSALTNSGTTPNRNLTIAITTLYINFAVYLTSAGRESMPESSEQALVLLGELTTLITGEKDSEAVYRGLVALGTLIKGLGEEVRTAAKEVYDVDDVLKKVSSSGLGKEPRIKGIIGEIKESLSSRYKMLRPGS
Protein: WD repeat and coiled-coil-containing protein (Q9H6R7)
Organism: Homo sapiens (Human)
Interaction partners:
- ALK tyrosine kinase receptor
- RuvB-like 1
- Echinoderm microtubule-associated protein-like 4
- Kinesin-1 heavy chain
- RuvB-like 2
Sequence:
MELGKGKLLRTGLNALHQAVHPIHGLAWTDGNQVVLTDLRLHSGEVKFGDSKVIGQFECVCGLSWAPPVADDTPVLLAVQHEKHVTVWQLCPSPMESSKWLTSQTCEIRGSLPILPQGCVWHPKCAILTVLTAQDVSIFPNVHSDDSQVKADINTQGRIHCACWTQDGLRLVVAVGSSLHSYIWDSAQKTLHRCSSCLVFDVDSHVCSITATVDSQVAIATELPLDKICGLNASETFNIPPNSKDMTPYALPVIGEVRSMDKEATDSETNSEVSVSSSYLEPLDLTHIHFNQHKSEGNSLICLRKKDYLTGTGQDSSHLVLVTFKKAVTMTRKVTIPGILVPDLIAFNLKAHVVAVASNTCNIILIYSVIPSSVPNIQQIRLENTERPKGICFLTDQLLLILVGKQKLTDTTFLPSSKSDQYAISLIVREIMLEEEPSITSGESQTTYSTFSAPLNKANRKKLIESLSPDFCHQNKGLLLTVNTSSQNGRPGRTLIKEIQSPLSSICDGSIALDAEPVTQPASLPRHSSTPDHTSTLEPPRLPQRKNLQSEKETYQLSKEVEILSRNLVEMQRCLSELTNRLHNGKKSSSVYPLSQDLPYVHIIYQKPYYLGPVVEKRAVLLCDGKLRLSTVQQTFGLSLIEMLHDSHWILLSADSEGFIPLTFTATQEIIIRDGSLSRSDVFRDSFSHSPGAVSSLKVFTGLAAPSLDTTGCCNHVDGMA
Protein: TBC1 domain family member 9 (TBC1 domain family member 9A) (Q6ZT07)
Organism: Homo sapiens (Human)
Function: May act as a GTPase-activating protein for Rab family protein(s).
Interaction partners:
Sequence:
MWVNPEEVLLANALWITERANPYFILQRRKGHAGDGGGGGGLAGLLVGTLDVVLDSSARVAPYRILYQTPDSLVYWTIACGGSRKEITEHWEWLEQNLLQTLSIFENENDITTFVRGKIQGIIAEYNKINDVKEDDDTEKFKEAIVKFHRLFGMPEEEKLVNYYSCSYWKGKVPRQGWMYLSINHLCFYSFLMGREAKLVIRWVDITQLEKNATLLLPDVIKVSTRSSEHFFSVFLNINETFKLMEQLANIAMRQLLDNEGFEQDRSLPKLKRKSPKKVSALKRDLDARAKSERYRALFRLPKDEKLDGHTDCTLWTPFNKMHILGQMFVSTNYICFTSKEENLCSLIIPLREVTIVEKADSSSVLPSPLSISTRNRMTFLFANLKDRDFLVQRISDFLQQTTSKIYSDKEFAGSYNSSDDEVYSRPSSLVSSSPQRSTSSDADGERQFNLNGNSVPTATQTLMTMYRRRSPEEFNPKLAKEFLKEQAWKIHFAEYGQGICMYRTEKTRELVLKGIPESMRGELWLLLSGAINEKATHPGYYEDLVEKSMGKYNLATEEIERDLHRSLPEHPAFQNEMGIAALRRVLTAYAFRNPNIGYCQAMNIVTSVLLLYAKEEEAFWLLVALCERMLPDYYNTRVVGALVDQGVFEELARDYVPQLYDCMQDLGVISTISLSWFLTLFLSVMPFESAVVVVDCFFYEGIKVIFQLALAVLDANVDKLLNCKDDGEAMTVLGRYLDSVTNKDSTLPPIPHLHSLLSDDVEPYPEVDIFRLIRTSYEKFGTIRADLIEQMRFKQRLKVIQTLEDTTKRNVVRTIVTETSFTIDELEELYALFKAEHLTSCYWGGSSNALDRHDPSLPYLEQYRIDFEQFKGMFALLFPWACGTHSDVLASRLFQLLDENGDSLINFREFVSGLSAACHGDLTEKLKLLYKMHVLPEPSSDQDEPDSAFEATQYFFEDITPECTHVVGLDSRSKQGADDGFVTVSLKPDKGKRANSQENRNYLRLWTPENKSKSKNAKDLPKLNQGQFIELCKTMYNMFSEDPNEQELYHATAAVTSLLLEIGEVGKLFVAQPAKEGGSGGSGPSCHQGIPGVLFPKKGPGQPYVVESVEPLPASLAPDSEEHSLGGQMEDIKLEDSSPRDNGACSSMLISDDDTKDDSSMSSYSVLSAGSHEEDKLHCEDIGEDTVLVRSGQGTAALPRSTSLDRDWAITFEQFLASLLTEPALVKYFDKPVCMMARITSAKNIRMMGKPLTSASDYEISAMSG
Protein: Peptidase S28 (G5EFJ8)
Organism: Caenorhabditis elegans
Interaction partners:
- Fatty acid synthase
- Choline/ethanolamine kinase
- Putative acid phosphatase 1
- Fatty acid synthase
- ACid Phosphatase family
Sequence:
MTRNLLLLTLLVSFVLAIIPNHYHFKKHLKRGSRKYGNSETAMTTGYMAQNLDHLIGNASGTFTQRYLYSQQYTLHQRTAFLYVSGVEGPNVVLDDRTPIVKTAKQFGATIFTLEHRYYGESKPNVDKLDAYNLRHLNSFQATQDVISFIKYANVQFNMDQDVRWVVWGIGYGGIIAAEARKLDPNSVSGVIASSTPLTHEYDFWRFNHRVAIVLAETGGSLCYRKVANGFADIREAMKTPEGRLNISDLFQLNPRLNETALNYNDIQMFYLAIIAPFQEIVEFNDDFDLSIADLCTTIDKSNWTNMEVVYQAYVYLSTTLDGFAGPMDISYQDFVDSLGDQSVDSGWIDNRIWQYQVCTEFGWFYTTNDNEQGLFGPVVPASLFLNQCFDIFPDANLTATGLRDSIINYNNFYGSSYDYSGTNAVFTNGMNDPWRELGKTSTGDFSVVAYLIPDASTASDMFPGNTNNSFIIQAHNLMTENINVWLNGPRNPKTFVNTTVPWTRPYWGEYGSLRETMLKQEVESKFSKLENGRTSEKTFPEPKFKKVFLGRPPHGFLPESDFNMSPDDYPAGFETGSFRQRQDHFNNQNADFFQQRFFKNTQWAKPGGPNFLMIGGEGPDKASWVLNENLPYLIWAKKYGATVYMLEHRFYGESRVGDNTNFNRLSSLQMIYDIADFIRSVNIKSGTSNPWITFGGSYSGLISAWTREVFPELVVGAVASSAPVFAKTDFYEYLMVAENSIRSYNSTCADRIQEGFNSMRALFLTKGGRQTLSSMFKLDPPFADNVTDIDQHYFFSNIYSNFQGDVQYSGDNMGSYANSYGIPDMCKIMTNDSNTPLNNIVAFNEYMANFYNGGGPYFGLDNSYQDMINFLINAKDFGPDAEASLLWTWQTCSEFGYFQSADSGNGIFGSPTPVNFFIQICMDVFNNYYQRSAIDPMVDNTNYMYGERFHFRGSNVVFPNGNKDPWHALGLYYPTDSSVVSYLIDGTAHCADMYPARDADVPGLKVVRDLIDQNIAIWLNQAPPSTGTTQTSGTGSTASPGTGSTSQPVTATTVQATTKSTTSVTVLTPFIAMLVSYLL
Protein: Fructose-bisphosphate aldolase 7, cytosolic (AtFBA7) (EC 4.1.2.13) (P22197)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a key role in glycolysis and gluconeogenesis.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9SJQ9}.
Interaction partners:
- Triosephosphate isomerase, chloroplastic
- Triosephosphate isomerase, cytosolic
- Sedoheptulose-1,7-bisphosphatase, chloroplastic
- Transketolase-1, chloroplastic
- Transketolase-2, chloroplastic
- Phosphoglycerate kinase 2, chloroplastic
- Glucose-6-phosphate isomerase, cytosolic
- Aldolase-type TIM barrel family protein
- transaldolase
- Phosphoglycerate kinase 1, chloroplastic
Sequence:
MSAFVSKYEDELIKTAKYIATPGRGILAADESTETIGKRFAGINVENTESNRQAYRELLFTSPGSYPCLSGVILFEETLYQKTSDGKPFVDLLMENGVIPGIKVDKGLVDLAGTNGETTTQGLDSLGARCQQYYEAGARFAKWRAFFKIGATEPSVLSIQEDARVLARYAIICQENGLVPIVEPEVLTGGSHDIKKCAAVTETVLAAVFKALNYHHVLLEGTLLKPNMVTPGSDSPKVAPELIAEYTVTALRRTVPPAIPGIVFLSGIQREEQATLNLNAMNKLDVLKPWTLTFSFGGALQQSAIKAWAGKPENVAKAQAKFLTRCKANKDATLGKYTGWASGDSAAFENLVVIGYRY
Protein: mRNA interferase (EC 3.1.-.-) (G1UB28)
Organism: Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Interaction partners:
- Predicted transcriptional regulator
- Transcriptional regulator/antitoxin MazE
Sequence:
MIRGEIWWVDLGIPFGSEPGFKRPVLIIQDDSFNQSNINTIVSIAITSNLNLSEAPGNVFISKKDSSLSKDSVINVSQIVTLDKERFLNKAGKLKSNKLGEVEIGLKLVTGLD
Protein: Atypical kinase COQ8B, mitochondrial (EC 2.7.-.-) (AarF domain-containing protein kinase 4) (Coenzyme Q protein 8B) (Q96D53)
Organism: Homo sapiens (Human)
Function: Atypical kinase involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration. Its substrate specificity is unclear: does not show any protein kinase activity. Probably acts as a small molecule kinase, possibly a lipid kinase that phosphorylates a prenyl lipid in the ubiquinone biosynthesis pathway. Required for podocyte migration.
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:24270420, ECO:0000269|PubMed:33988507}; Single-pass membrane protein {ECO:0000269|PubMed:24270420}. Cytoplasm, cytosol {ECO:0000269|PubMed:24270420}. Cell membrane {ECO:0000269|PubMed:24270420}.
Interaction partners:
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- Ubiquinone biosynthesis protein COQ9
- All trans-polyprenyl-diphosphate synthase PDSS1
- Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- NADPH-dependent 3-demethoxyubiquinone 3-hydroxylase, mitochondrial
- All trans-polyprenyl-diphosphate synthase PDSS2
- Coenzyme Q-binding protein COQ10 homolog A
Sequence:
MWLKVGGLLRGTGGQLGQTVGWPCGALGPGPHRWGPCGGSWAQKFYQDGPGRGLGEEDIRRAREARPRKTPRPQLSDRSRERKVPASRISRLANFGGLAVGLGLGVLAEMAKKSMPGGRLQSEGGSGLDSSPFLSEANAERIVQTLCTVRGAALKVGQMLSIQDNSFISPQLQHIFERVRQSADFMPRWQMLRVLEEELGRDWQAKVASLEEVPFAAASIGQVHQGLLRDGTEVAVKIQYPGIAQSIQSDVQNLLAVLKMSAALPAGLFAEQSLQALQQELAWECDYRREAACAQNFRQLLANDPFFRVPAVVKELCTTRVLGMELAGGVPLDQCQGLSQDLRNQICFQLLTLCLRELFEFRFMQTDPNWANFLYDASSHQVTLLDFGASREFGTEFTDHYIEVVKAAADGDRDCVLQKSRDLKFLTGFETKAFSDAHVEAVMILGEPFATQGPYDFGSGETARRIQDLIPVLLRHRLCPPPEETYALHRKLAGAFLACAHLRAHIACRDLFQDTYHRYWASRQPDAATAGSLPTKGDSWVDPS
Protein: Serine acetyltransferase 3, mitochondrial (AtSAT-3) (AtSERAT2;2) (SAT-m) (EC 2.3.1.30) (Q39218)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:9830017}.
Interaction partners:
- Cysteine synthase, mitochondrial
- Cysteine synthase, chloroplastic/chromoplastic
- Cysteine synthase 1
- Phosphoserine phosphatase, chloroplastic
- Bifunctional cystathionine gamma-lyase/cysteine synthase
- Putative inactive cysteine synthase 2
- S-sulfo-L-cysteine synthase
- cysteine synthase
- Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic
- Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic
Sequence:
MLPVTSRRHFTMSLYMLRSSSPHINHHSFLLPSFVSSKFKHHTLSPPPSPPPPPPMAACIDTCRTGKPQISPRDSSKHHDDESGFRYMNYFRYPDRSSFNGTQTKTLHTRPLLEDLDRDAEVDDVWAKIREEAKSDIAKEPIVSAYYHASIVSQRSLEAALANTLSVKLSNLNLPSNTLFDLFSGVLQGNPDIVESVKLDLLAVKERDPACISYVHCFLHFKGFLACQAHRIAHELWTQDRKILALLIQNRVSEAFAVDFHPGAKIGTGILLDHATAIVIGETAVVGNNVSILHNVTLGGTGKQCGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLLGGKDNPKTHDKIPGLTMDQTSHISEWSDYVI
Protein: Delta(9)-fatty-acid desaturase fat-5 (EC 1.14.19.-) (Fatty acid desaturase 5) (FAT-5) (Palmitoyl-CoA fatty acid desaturase) (G5ED44)
Organism: Caenorhabditis elegans
Function: Delta(9)-fatty acid desaturase that acts preferentially on palmitoyl-CoA (hexadecanoyl-CoA) producing the monounsaturated palmitoleoyl-CoA ((9Z)-hexadecenoyl-CoA), which can be elongated to (11Z)-octadecenoyl-CoA (the most abundant monounsaturated fatty acid in Caenorhabditis elegans phospholipids and triacylglycerols). Also acts on pentadecanoyl-CoA, heptadecanoyl-CoA and myristoyl-CoA (tetradecanoyl-CoA), the monounsaturated fatty acids (MUFAs) produced are further used as substrates to synthesize polyunsaturated fatty acids (PUFAs) by several other desaturases and elongases. Unlike plants, Caenorhabditis elegans desaturases seem to use fatty acyl-CoAs as substrates (By similarity).
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Delta
- Delta
- Nuclear hormone receptor family member nhr-49
- Sterol regulatory element binding protein sbp-1
- Nuclear hormone receptor family member nhr-80
- Mediator of RNA polymerase II transcription subunit 15
- Acetyl-CoA carboxylase
- Delta
- Omega-3 fatty acid desaturase fat-1
- Long chain fatty acid elongase 2
Sequence:
MTQIKVDAIISKQFLAADLNEIRQMQEESKKQVIKMEIVWKNVALFVALHIGALVGLYQLVFQAKWATVGWVFLLHTLGSMGVTGGAHRLWAHRAYKATLSWRVFLMLINSIAFQNDIIDWARDHRCHHKWTDTDADPHSTNRGMFFAHMGWLLVKKHDQLKIQGGKLDLSDLYEDPVLMFQRKNYLPLVGIFCFALPTFIPVVLWGESAFIAFYTAALFRYCFTLHATWCINSVSHWVGWQPYDHQASSVDNLWTSIAAVGEGGHNYHHTFPQDYRTSEHAEFLNWTRVLIDFGASIGMVYDRKTTPEEVIQRQCKKFGCETEREKMLHKLG
Protein: Ras-like protein 1 (EC 3.6.5.2) (P01119)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The S.cerevisiae Ras proteins modulate the activity of the adenylate cyclase catalytic subunit and therefore affect the biosynthesis of cyclic-AMP.
Subcellular location: Cell membrane; Lipid-anchor.
Interaction partners:
- Adenylate cyclase
- cAMP-dependent protein kinase type 1
- Cell division control protein 25
- cAMP-dependent protein kinase type 2
- Inhibitory regulator protein IRA2
- cAMP-dependent protein kinase type 3
- Inhibitory regulator protein IRA1
- Ras-like protein 2
- G protein-coupled receptor GPR1
- cAMP-dependent protein kinase regulatory subunit
Sequence:
MQGNKSTIREYKIVVVGGGGVGKSALTIQFIQSYFVDEYDPTIEDSYRKQVVIDDKVSILDILDTAGQEEYSAMREQYMRTGEGFLLVYSVTSRNSFDELLSYYQQIQRVKDSDYIPVVVVGNKLDLENERQVSYEDGLRLAKQLNAPFLETSAKQAINVDEAFYSLIRLVRDDGGKYNSMNRQLDNTNEIRDSELTSSATADREKKNNGSYVLDNSLTNAGTGSSSKSAVNHNGETTKRTDEKNYVNQNNNNEGNTKYSSNGNGNRSDISRGNQNNALNSRSKQSAEPQKNSSANARKESSGGCCIIC
Protein: SOSS complex subunit B2 (Nucleic acid-binding protein 1) (Oligonucleotide/oligosaccharide-binding fold-containing protein 2A) (Sensor of single-strand DNA complex subunit B2) (Sensor of ssDNA subunit B2) (Single-stranded DNA-binding protein 2) (H7C0W4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XRVTKTKDGHEVRSCKVADKTGSITISVWDEIGGLIQPGDIIRLTRGYASMWKGCLTLYTGRGGELQKIGEFCMVYSEVPNFSEPNPDYRGQQNKGAQSEQKNNSMNSNMGTGNGVHTGPESREHQFSHAGRSNGRGLINPQLQGTASNQTVMTTISNGRDPRRAFKR
Protein: At3g05070 (Cwf18 pre-mRNA splicing factor) (T12H1.3 protein) (Q9MAB2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Pre-mRNA-processing protein 40C
- Cell division cycle 5-like protein
- Pre-mRNA-splicing factor SYF2
- Pre-mRNA-processing factor 17
- Transducin/WD40 repeat-like superfamily protein
- G patch domain-containing protein TGH
- At2g29210/F16P2.41
- Peptidyl-prolyl cis-trans isomerase CYP18-2
- Crooked neck protein, putative / cell cycle protein
- Crooked neck protein, putative / cell cycle protein
Sequence:
MASEDESIEQKAAARKEALKALRAAQELSETKEDGEDEAVEEDGPAMKFRNYVPQAKELQDGKLAPPELPKFEDPIVALPPAVEKKEDPFVNIAPKKPNWDLRRDVQKKLDKLERRTQKAMHKLMEEQEKEREMAEADGNTIES
Protein: cDNA FLJ57801, highly similar to Homo sapiens AHNAK nucleoprotein (desmoyokin) (AHNAK), transcript variant 1, mRNA (B4DTV0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEKEETTRELLLPNWQGSGSHGLTIAQRDDGVFVQEVTQNSPAARTGVVKEGDQIVGATIYFDNLQSGEVTQLLNTMGHHTVGLKLHRKGDRSPEPGQTWTREVFSSCSSEVVLSGDDEEYQRIYTTKIKPRLKSEDGVEGDLGETQSRTITVTRRVTAYTVDVTGREGAKDIDISSPEFKIKIPRHELTEISNVDVDTQSGKTVIRLPSGSGAASPTGSAVDIRAGAISASGPELQGAGHSKLQVTMPGIKVGGSGVNVNAKGLDLGGRGGVQVPAVDISSSLGGRAVEVQGPSLESGDHGKIKFPTMKVPKFGVSTGREGQTPKAGLRVSAPEVSVGHKGGKPGLTIQAPQLEVSVPSANIEGLEGKLKGPQITGPSLEGDLGLKGAKPQGHIGVDASAPQIGGSITGPSVEVQAPDIDVQGPGSKLNVPKMKVPKFSVSGAKGEETGIDVTLPTGEVTVPGVSGDVSLPEIATGGLEGKMKGTKVKTPEMIIQKPKISMQDVDLSLGSPKLKGDIKVSAPGVQGDVKGPQVALKGSRVDIETPNLEGTLTGPRLGSPSGKTGTCRISMSEVDLNVAAPKVKGGVDVTLPRVEGKVKVPEVDVRGPKVDVSAPDVEAHGPEWNLKMPKMKMPTFSTPGAKGEGPDVHMTLPKGDISISGPKVNVEAPDVNLEGLGGKLKGPDVKLPDMSVKTPKISMPDVDLHVKGTKVKGEYDVTVPKLEGELKGPKVDIDAPDVDVHGPDWHLKMPKMKMPKFSVPGFKAEGPEVDVNLPKADVDISGPKIDVTAPDVSIEEPEGKLKGPKFKMPEMNIKVPKISMPDVDLHLKGPNVKGEYDVTMPKVESEIKVPDVELKSAKMDIDVPDVEVQGPDWHLKMPKMKMPKFSMPGFKAEGPEVDVNLPKADVDISGPKVGVEVPDVNIEGPEGKLKGPKFKMPEMNIKAPKISMPDVDLHMKGPKVKGEYDMTVPKLEGDLKGPKVDVSAPDVEMQGPDWNLKMPKIKMPKFSMPSLKGEGPEFDVNLSKANVDISAPKVDTNAPDLSLEGPEGKLKGPKFKMPEMHFRAPKMSLPDVDLDLKGP
Protein: Elongation factor 1-alpha (Q3LUM4)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
- Elongation factor 1-gamma-like
- Elongation factor 1-gamma-like
- Elongation factor 1-gamma-like
- Elongation factor 1-beta 2-like isoform X1
- Elongation factor 1-beta 2-like
- Elongation factor 1-delta-like
- Elongation factor 1-delta-like
- Elongation factor 1-beta 2-like
- GTP-binding nuclear protein
- GTP-binding nuclear protein
Sequence:
MGKEKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIVKEVSSYLKKVGYNPEKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGTLKPGMVVTFGPSGLTTEVKSVEMHHEALQEALPGDNVGFNVKNVAVKDLKRGFVASNSKDDPAKEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAELLTKIDRRSGKELEKEPKFLKNGDAGMIKMVPTKPMVVETFSAYPPLGRFAVRDMRQTVAVGVIKSVEKKDPTGAKVTKSAAKKGK
Protein: Uncharacterized protein C1711.08 (Q9P782)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Heat shock protein 90 homolog
- Heat shock protein sti1 homolog
- 40 kDa peptidyl-prolyl cis-trans isomerase
- Protein wos2
- Heat shock protein 104
- Hsp90 co-chaperone Cdc37
- Tuberous sclerosis 1 protein homolog
- NAD reductase coq12
- Protein psi1
- Hsp70 nucleotide exchange factor fes1
Sequence:
MSATSINPNNWHWTSKDCRVWSHEYFNKELPKIQASEGPTSARITQVNSCEGDVDVSMRKRKVITIFDLKIQMEFKGETKDGVEATGSITCPELSYDLGYSDYVFDIDIYSASKEKEPIKELVREKIIPQIRQLFSGFSQVLLQTHGDDVYLSTEEHNGNAARGLPVHSSFKQNNSSQTSSNKGTTTVAAGSGSDGSRVSAVVNTADISENYTFDAPANELYATFLDPARVAAWSRAPPQLDVRPQGAFSLFHGNVVGKFLVLEENKKIVQTWRLSSWPTGHYAEITFTFDQADSYTTLRMIMKGVPIGEEEVVQGNIQDYYIRPIKTVFGFGAVL
Protein: Putative COX1/OXI3 intron 2 protein (P03876)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Intron-encoded DNA endonuclease aI5 beta
- Intron-encoded RNA maturase bI4
- Cytochrome b mRNA maturase bI2
- Intron-encoded DNA endonuclease aI5 alpha
- Intron-encoded DNA endonuclease aI4
- Intron-encoded DNA endonuclease aI3
- ATP synthase subunit a
- Putative COX1/OXI3 intron 1 protein
- Cytochrome b
- Cytochrome b mRNA maturase bI3
Sequence:
MVQRWLYSTNAKDIAVLYFMLAIFSGMAGTAMSLIIRLELAAPGSQYLHGNSQLFNVLVVGHAVLMIFCAPFRLIYHCIEVLIDKHISVYSINENFTVSFWFWLLVVTYMVFRYVNHMAYPVGANSTGTMACHKSAGVKQPAQGKNCPMARLTNSCKECLGFSLTPSHLGIVIHAYVLEEEVHELTKNESLALSKSWHLEGCTSSNGKLRNTGLSERGNPGDNGVFMVPKFNLNKVRYFSTLSKLNARKEDSLAYLTKINTTDFSELNKLMENNHNKTETINTRILKLMSDIRMLLIAYNKIKSKKGNMSKGSNNITLDGINISYLNKLSKDINTNMFKFSPVRRVEIPKTSGGFRPLSVGNPREKIVQESMRMMLEIIYNNSFSYYSHGFRPNLSCLTAIIQCKNYMQYCNWFIKVDLNKCFDTIPHNMLINVLNERIKDKGFMDLLYKLLRAGYVDKNNNYHNTTLGIPQGSVVSPILCNIFLDKLDKYLENKFENEFNTGNMSNRGRNPIYNSLSSKIYRCKLLSEKLKLIRLRDHYQRNMGSDKSFKRAYFVRYADDIIIGVMGSHNDCKNILNDINNFLKENLGMSINMDKSVIKHSKEGVSFLGYDVKVTPWEKRPYRMIKKGDNFIRVRHHTSLVVNAPIRSIVMKLNKHGYCSHGILGKPRGVGRLIHEEMKTILMHYLAVGRGIMNYYRLATNFTTLRGRITYILFYSCCLTLARKFKLNTVKKVILKFGKVLVDPHSKVSFSIDDFKIRHKMNMTDSNYTPDEILDRYKYMLPRSLSLFSGICQICGSKHDLEVHHVRTLNNAANKIKDDYLLGRMIKMNRKQITICKTCHFKVHQGKYNGPGL
Protein: Activin receptor type-2B (EC 2.7.11.30) (Activin receptor type IIB) (ACTR-IIB) (P27040)
Organism: Mus musculus (Mouse)
Function: Transmembrane serine/threonine kinase activin type-2 receptor forming an activin receptor complex with activin type-1 serine/threonine kinase receptors (ACVR1, ACVR1B or ACVR1c). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, the type-2 receptors act as a primary activin receptors (binds activin-A/INHBA, activin-B/INHBB as well as inhibin-A/INHA-INHBA). The type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q13705}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Bone morphogenetic protein 7
- Activin receptor type-1B
- Growth/differentiation factor 8
- Growth/differentiation factor 11
- TGF-beta receptor type-1
- Inhibin beta A chain
- Activin receptor type-2A
- Bone morphogenetic protein 4
- Activin receptor type-1C
- Bone morphogenetic protein 6
Sequence:
MTAPWAALALLWGSLCAGSGRGEAETRECIYYNANWELERTNQSGLERCEGEQDKRLHCYASWRNSSGTIELVKKGCWLDDFNCYDRQECVATEENPQVYFCCCEGNFCNERFTHLPEPGGPEVTYEPPPTAPTLLTVLAYSLLPIGGLSLIVLLAFWMYRHRKPPYGHVDIHEVRQCQRWAGRRDGCADSFKPLPFQDPGPPPPSPLVGLKPLQLLEIKARGRFGCVWKAQLMNDFVAVKIFPLQDKQSWQSEREIFSTPGMKHENLLQFIAAEKRGSNLEVELWLITAFHDKGSLTDYLKGNIITWNELCHVAETMSRGLSYLHEDVPWCRGEGHKPSIAHRDFKSKNVLLKSDLTAVLADFGLAVRFEPGKPPGDTHGQVGTRRYMAPEVLEGAINFQRDAFLRIDMYAMGLVLWELVSRCKAADGPVDEYMLPFEEEIGQHPSLEELQEVVVHKKMRPTIKDHWLKHPGLAQLCVTIEECWDHDAEARLSAGCVEERVSLIRRSVNGTTSDCLVSLVTSVTNVDLLPKESSI