wanglab/gogpt-training-data huggingface dataset:
Protein: Synaptobrevin homolog YKT6 (Q6FW27)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome M complete sequence
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome D complete sequence
- Golgi SNAP receptor complex member 1
- Protein transport protein SEC22
- Candida glabrata strain CBS138 chromosome J complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome I complete sequence
- Candida glabrata strain CBS138 chromosome I complete sequence
- Protein transport protein BOS1
Sequence:
MKIYYIGVFRSPAEQSSDEKALELTEVKDLSQFGFFERNSVGQFMTFFAETVATRTTAGQRQSVEEGNYIGHVYARSEGICGVLITDKDYPVRPAYTLLNKVLDEYLVAHPADQWKSITATNDSLKMAELSTYISKYQDPAQADAIMKVQQELDETKIVLHKTIENVLQRGEKLDNLVDKSESLTASSKMFYKQAKKTNSCCIIM
Protein: histidine kinase (EC 2.7.13.3) (Q8KLS0)
Organism: Cereibacter sphaeroides (Rhodobacter sphaeroides)
Interaction partners:
Sequence:
MSDAFDEMDEIWALYADDGAQALDAMEASLLALQAGEDAAAHVGPLFRAVHTFKGNSRVLGLSVVESRAHLCEDLIGLVRDAGVPMDGEIVEILLFASDTLRAMLEETAASRADVEGTGSEALMDQLRSKIARCSGAGAATAEVDAATAEERAATAEERAAATEAGAAPTETGAAATSAAEPSEAWGGSPETGAPAAAAEVLPVAGKAFPSVADILGLLDDSALPDTGEAAEVPLEAGGRPAGEGHAPAGPPPEAGPAEAPVPPAAEPARPAARLADDPVYRAIFRDMATAALTRFRAQIDAFATDPGATAQGARAEADGLCHAARQMGLDDWEAALAAFLSDSQGPERLAALVLELEALGDEPAPTPQVEEKPFFAAIAGPLAEIGRLGLRLVTGERPGPAERAAAADPLGQAALAQGYVRVAEAAQALAAAEGAEPFGTARLRLYEELAAVEALMPEAAAAAGVSPVGLLRRLCAAEAAETLAALDATLNAFRSAPLAETFGRFERLMRCVHHACAHHALDAAAQLAMSLVDLFGRAEAKGAVPDAMLVHIARGFIETIELAFEALAQGETPAMEVLDRLFEEAANVCFVSDGLVTAGAIERRLGLPADFHRVLSPESVRAAVEEMEKGQQFYIVRTDINSDDRTAEAFLDWLSGDQARSITNVTVFRGTETLFDFLISSRLGEADLIEALVRMDPSGRRLSLTQALRPRQDEPAPVEAPGEAPLAQGAAITPEMLETIGEISANQAMVQHLLTELAEADLAEATEALVRQAAGDWAAARGPVRALLEAHGARLQEIVQAGTQLTAQLAALQEETVTQRARPASTVLRPLRTFAETLARRRRREVCLTTSGDELALDLALLERLRGFLRGLVALRLDQDRGAPGTLHVSLWRDEERVTVLVQDDGAPEPDSPALADLAAEVGQAGGALRSVPLPGGGMRFHLGLPLSMVVLEGMVVGVDGMRYVLPVESIRTILQADAAAAMTISAAGGQRVLRLSETEIVAIHSLRGHPQEGHRERPWPASRRVYVVLGTGPRSVAIPVDELVGQQLVLLRPLRGVLARLTHLTGLALLAGGDVGMVLSANRICPPLPAEAG
Protein: Type 1 encapsulin shell protein EncA (Q1D6H4)
Organism: Myxococcus xanthus (strain DK1622)
Function: Shell component of a type 1, iron-storage encapsulin nanocompartment. Encapsulin nanocompartments are 32 nm in diameter with an iron- and phosphorus-rich core (4Fe:1P) about 24 nm in diameter. Upon expression in E.coli most particles are 32 nm, 20% are 18 nm. The core is filled with an average of 14 dense granules, 5-6 nm in diameter that are not evenly distributed. Each nanocompartment is estimated to hold 30,000-35,000 Fe atoms. The minor proteins EncB, EncC and EncD probably lie against the interior face of the nanocompartment (Probable).
Subcellular location: Encapsulin nanocompartment {ECO:0000269|PubMed:25024436, ECO:0000269|PubMed:31194509}.
Interaction partners:
- Encapsulin nanocompartment cargo protein EncB
- Encapsulin nanocompartment cargo protein EncC
- Encapsulin nanocompartment cargo protein EncD
- M23 peptidase domain protein
- Sigma-54 dependent DNA-binding response regulator
- Porin
Sequence:
MPDFLGHAENPLREEEWARLNETVIQVARRSLVGRRILDIYGPLGAGVQTVPYDEFQGVSPGAVDIVGEQETAMVFTDARKFKTIPIIYKDFLLHWRDIEAARTHNMPLDVSAAAGAAALCAQQEDELIFYGDARLGYEGLMTANGRLTVPLGDWTSPGGGFQAIVEATRKLNEQGHFGPYAVVLSPRLYSQLHRIYEKTGVLEIETIRQLASDGVYQSNRLRGESGVVVSTGRENMDLAVSMDMVAAYLGASRMNHPFRVLEALLLRIKHPDAICTLEGAGATERR
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (F1M9C3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Dual specificity mitogen-activated protein kinase kinase 1
- RAF proto-oncogene serine/threonine-protein kinase
- 14-3-3 protein beta/alpha
- GTPase NRas
- GTPase KRas
- Protein sprouty homolog 2
- GTPase HRas
- Ras GTPase-activating-like protein IQGAP1
- 14-3-3 protein zeta/delta
- Dual specificity mitogen-activated protein kinase kinase 2
Sequence:
MVSLCNFDCHLEPRLSLGWNSICRLSRPQTHTVWNIKQMIKLTQEHIEALLDKFGGEHNPPSIYLEAYEEYTSKLDALQQREQQLLESLVFQTPTDVSRNNPKSPQKPIVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVLENVPLTTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNYDQLDLLFVSKFFEHHPVPQEEAFSAETTLPSGCSSAPPSDSIGPQILTSPSPSKSIPIPQPFRPADEDHRNQFGQRDRSSSAPNVHINTIEPVNIDDLIRDQGFRGDGGSTTGLSATPPASLPGSLTNVKALQKSPGPQRERKSSSSSSSTEDRSRMKTLGRRDSSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDMKMRSVFSFTYYTSDIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSLPKIHRSASEPSLNRAGFQTEDFSLYACASPKTPIQAGGYGGFK
Protein: Fiery mountain, isoform D (M9PEH8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Serine/threonine-protein phosphatase 6 catalytic subunit
Sequence:
MFWDKGYAPSANIEALLEKENSTLEEFLDEEDILQECKTQKKNLVNYFTRPEVIRRLVELITTEPSEDVPMSKRFRYANMSCEILTLGLPSLDEKLLNDAETLQLLYSYLEKEPPLNPLLSSFFSKTFSMLFTKKPEQDWFLYQHMCLQLLEYIKSQKTFLDFICKHFDTPVIPDLIMQMMKDIEGGRLKRNLFEWLTEDKIVERLIAILRNPQETDKHANVADFFCDLINQGRLMRQTEQENDSFEPAFDGSNPILKTIEFADTIEALLNVILEPNAQESAILSGISVVLTLIKPITFTDEPNSDRQRLLQKREREIHQEVQETVITVMAPRLQEFVHILKNPPAKPTLETTAAVLTPPFGKTRLQVCRVFTALLETKHETIQQAICATEYFSLLLDFFKQYCWNNFLHTEMEKALYVVFYNELSNNNTASTEVTDYFTADCLINAFLKVGTEESEVEMKNALNDAKRAEGGKDEEGGDIEIEVAAAQEVAAQTPDERQTAAEENQEHEEHMSQVEAAAEATASEDAEPKAQDNEVKNSEVDGESPTDQQESEATLNDLDKTKTVPSPPPSEMQSHLIVNCHLISKLVDLWQHNAQAQSAEKGRRLGYMGHLIKILRHITNCISESEHIGDLITSSLSDEDEVKLWQSLIDAETGEFSLAVKQQTKLLADCNPHEENQYNDGSNDYTGEINAWNVGNLPYREVDCSELNNTLQDIFFAIDQNRFQFGRNIDDEDDDDDEHGDHSGGGDGHGHGMFTKNSNTLNNLADPWDIQFAVLSSAPTQVNTGTANWGTDFNSDNFADFDAHFSTFGSDLGMPISAPPGEEEEEDSSPAPESATQVNPEEERQPAESIGLAVGKGVQDNLACTDDQQAEYDNNANVEKAISDKLAESSVVETAAIVTRLQSVLLDGEDDYEDDEGMWTKPLGADRPSETEQITPISNGPDSKVNELGLPFSNHANDISSNNVDGHEANITTEQQKLAAAAKTNNVEIATTTT
Protein: Proteinase-activated receptor 3 (PAR-3) (Coagulation factor II receptor-like 2) (Thrombin receptor-like 2) (Q920E1)
Organism: Rattus norvegicus (Rat)
Function: Receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Proteinase-activated receptor 4
- Prothrombin
Sequence:
MEMKVLILVGVRLLFLPTTVCQSGMKHVSDNSALTAESFNGNEHSFEEFPLSDIEGWTGATTTIKAKCPEESITTLHVNNATMGYLRSSLSTKVIPAIYILVFVIGVPANIVTLWKLSSRTKSICLVIFHTNLAIADLLFCVTLPFKIAYHLNGNDWVFGEVMCRVTTVAFYGNMYCAILILTCMGINRYLATVHPFTYRKLPKRNFTLLMCGVVWVMVVLYMLPLAILKQEYHLVQPGITTCHDVHDTCESPLPFQFYYFVSLAFFGFLIPFVVSVFCYTTLIHKLNAQDRKWLRYIKAVLLILVIFTICFAPTNIILIIHHANYYYSNTDSLYFMYLIALCLGSLNSCLDPFLYFIMSKIVDQLTS
Protein: Evasin P1229 (A0A0K8R4R9)
Organism: Ixodes ricinus (Common tick) (Acarus ricinus)
Function: Salivary chemokine-binding protein which binds to host chemokines CXCL1 and CXCL8.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MEVRTFAFLQIVVFVALGIQLFAAVTDAADADDEFFTVDYCGMNCTLQQDGSWTPCTQKNAECKCYHESGSSVGLCLSTAYTDFNQFGDPNNSDLDAATPRHPDASSR
Protein: Uncharacterized protein (Q57V68)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Nucleoporin
- Nucleoporin
Sequence:
MRERPRITVRLCAKKDSFTPTSSHRFGDHSAMSRHGVSTGTVVLRNGEEVDHQKNMSNIARVSGSLAWCMTRLGGLAKGVMRAVLGVTTVGGADASRCGPTPDSVASSHAPPSQTNSPVPPITNNVTTAANTMHMQSHRSGVAAVARAECNPVVVRPGEFAGNAHQRGSQMIEPETGPYTHHYQYNFYYAAPSNNLPTVDPLLLARFNEPRYTIRPSRPSYRSTILAPRPTPEKRRRDQGDADASSTMRQDLLRRVTFEAEGLGGGTDRGTNRDGEKAAHVAGPTSGTTRTPSNPFSSGASAGNASASGEKNNAPRNPFSFGASAGSAAASGEKDNAPRNPFSFGASAGNASASGEKDNAPRNPFSFGASAGNASASGEKDNAPRNPFSFGASAGSAAASSGIGAVTSKTASSGGFFKSGPSAVPFDDEGFADNAGGDDEDGSPSPTAGSTSGVTRTPSNPFSSGASAGNASASGEKDNAPRNPFSFGASAGNASASGEKDNAPRNPFSFGASAGSAAASSGIGAVTSKTASSGGFFKSGPSAVPFDDEGFADNAGGDDEDGSPSPTAGSTSGVTRTPSNPFSFGASAGNASASGEKDNAPRNPFSFGASAGSAAASSGIGAVTSKTASSGGFFKSGPSAVPFDDEGFADNAGGDDEDGSPSPTAGSTSGVTRTPSNPFSFGASAGNASASGEKNNAPRNPFSFGASAGNASASGEKNNAPRNPFSFGASAGNASASGEKNNAPRNPFSFGASAGNASASGEKDNAPRNPFSFGASAGNASASGEKDNAPRNPFSFGASAGSAAASSGIGAVTSKTASSGGFFKSGPSAVPFDDEGFADNAGGDDEDGSPSPTAGSTSGVTRTPSNPFSFGASAGNASASGEKDNAPRNPFSFGASAGNASASGEKDNAPRNPFSFGASAGNASASGEKDNAPRNPFSFGASAGNASASGEKDNAPRNPFSFGASAGNASASGEKNNAPRNPFSFGASSGNA
Protein: Gamma-aminobutyric acid receptor subunit epsilon (GABA(A) receptor subunit epsilon) (GABAAR subunit epsilon) (Q9ES14)
Organism: Rattus norvegicus (Rat)
Function: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.
Subcellular location: Cell membrane; Multi-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Inactive phospholipase C-like protein 1
- Huntingtin-associated protein 1
- Vesicle-fusing ATPase
- Trafficking kinesin-binding protein 2
- Gamma-aminobutyric acid type B receptor subunit 2
- Gamma-aminobutyric acid receptor subunit beta-1
- Gamma-aminobutyric acid receptor subunit beta-2
- Gamma-aminobutyric acid type B receptor subunit 1
- Gamma-aminobutyric acid receptor-associated protein
- Gamma-aminobutyric acid receptor subunit theta
Sequence:
MLPKVLLMLLNMFLALQWRVGPHIKLENKPPAQDKVVFGPQPQPSGKKLPARETELTADHTTERPRGKLTRASQILNTILSNYDHKLRPSIGEKPTVVTVKVFVNSLGPISILDMEYSIDIIFYQTWYDERLRYNDTFETLILHGNVVSQLWIPDTFFRNSKRTQEYDITIPNQMALIHKDGKVLYTVRMTIDARCSLHMLNFPMDSHSCPLSFSSFSYDEHEMIYKWENFKLKIDAKNTWKLLEFDFTGVNNKTEIISTPVGDFMVMTFFFNVSRRFGFIVFQNYIPSSVTTMLSWVSFWIKIEAAAARASVGVSSVLTMATLGTFSRKNFPRVSYLTALDFYIAICFVLCFCTLLEFTVLNFLTYNNIERQASPKFYQFPTNSRANARTRARARTRARARARARQQQEVFVCEIVTYEENAEEGYQWSPRSRRPQCPWRRCGRSYVCFRVLRKYFCMVPGCEGNNWQRGRICIHVYRLDNYSRVLFPITFFFFNVVYWVICLNL
Protein: Phosphatidylinositol transfer protein beta isoform (F1QRW4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004586}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004394}.
Interaction partners:
- Membrane-associated phosphatidylinositol transfer protein 3
- PITP-less RdgB-like protein.
- Pecanex 1.
- Small G protein-signaling modulator 2.
- Golgi phosphoprotein 3-like.
- Golgin subfamily A member 1
- Myosin XVIIIAb
- Arachidonate 12-lipoxygenase
- Signal-induced proliferation-associated 1-like 1
- SET domain-containing 4.
Sequence:
MVLIKEYRVVLPCSVEEYQVGQLFSVAEASKNETGGGEGIEVLKNEPYEKEGEKGQYTHKIYHLKSKVPGFVKMIAPEGALVFHEKAWNAYPYCRTIVTNEYMKDDFMIKIETWHKPDTGALENVHDLDPITWKTVEVVHIDIADRSQVEPGDYKPEEDPEIFHSEKTGRGPLGPDWKKELLAKPDSPRMCAYKLVTVKFKWWGLQTKIENFIHKQEKRIFTNFHRQLFCWIDNWVELTMEDIRRMEEETQRELEELRKTGQVRGTSAAHEQ
Protein: Short-chain dehydrogenase, putative (Q57YP3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPFQLSRRLVVASVRQIRVRIPCSRCYCLYESCRSYRQTPSLFPPRKISQAKQKPLFPGMYRTVRLFDGEHTYHYGRHTYTIMRESLTFAIIPLGCVAAYAATYFDPFAAVPLELQGAYLVFLLIGSRLYARGRSCRTVKDLTGRHVVVTGGTSGIGKETAARLAAAGADVTVLARSSSHAEAAITYIRRSAHCEGQVVQFTPLDLSDFLAVRDYCRRLRHTNTRLDILVNCAGVMHQRQVMSRCGDDEQLAVNLLGPYLLTEGLLPLIAESGGRIVNVSCSAHVAVRGNIVQTYLSGRGVWSPRVRGKFDGLEQYGLTKLGCIYHAQELASRSYHSTTKGNASFCPTDTSHPSLGSSAINKGSNLNLYHYKHNSGNRASNNNDSGDGGGDDEAGAPNYTTCVAVPGGVVTGIYRYVPLAATFRWFRWIYLLFMRSAREGSQTVVDCCLRDDIVNGGYYQNCRYAPSGLSAAACNIEERKNVLTWVRRKMQPYMQWDR
Protein: Probable secreted beta-glucosidase UTH1 (EC 3.2.1.-) (Youth protein 1) (P36135)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in aging, oxidative stress response, and in the regulation of mitochondrial biogenesis. Inactivation of UTH1 increases life span, leads to higher resistance to heat stress and against hydrogen peroxide, and increases sensitivity to the superoxide radical-generating drug paraquat and to copper. Also required for the selective autophagic degradation of mitochondria (mitophagy) in response to nitrogen starvation. Involved in the remodeling of the cell wall during the various phases of yeast culture development and under various environmental conditions and plays a role in septation. Involved in cell sensitivity to boric acid.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:11958935}; Peripheral membrane protein {ECO:0000269|PubMed:11958935}. Secreted, cell wall {ECO:0000269|PubMed:11958935}. Note=Non-covalently bound to the cell wall (PubMed:11958935).
Interaction partners:
- Autophagy-related protein 32
- Probable secreted beta-glucosidase SIM1
- Probable circularly permuted 1,3-beta-glucanase TOS1
- [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 2, mitochondrial
Sequence:
MKLSALLALSASTAVLAAPAVHHSDNHHHNDKRAVVTVTQYVNADGAVVIPAATTATSAAADGKVESVAAATTTLSSTAAAATTSAAASSSSSSSSSSSSSSSVGSGDFEDGTISCSDFPSGQGAVSLDWLGLGGWASIMDMNGNTATSCQDGYYCSYACSPGYAKTQWPSEQPSDGRSVGGLYCKNGKLYRSNTDTNSLCVEGQGSAQAVNKVSGSIAICGTDYPGSENMVVPTVVGAGSSQPINVIKEDSYYQWQGKKTSAQYYVNNAGVSVEDGCIWGTEGSGVGNWAPVVLGAGYTDGITYLSIIPNPNNKEAPNFNIKIVATDGSTVNGACSYENGVYSGSGSDGCTVSVTSGSANFVFY
Protein: D-galactonate dehydratase family member Ent638_0932 (A4W7D6)
Organism: Enterobacter sp. (strain 638)
Function: Has no detectable activity with D-mannonate and with a panel of 70 other acid sugars (in vitro), in spite of the conservation of the residues that are expected to be important for catalytic activity and cofactor binding. May have evolved a divergent function.
Interaction partners:
- Mannonate dehydratase
- Fructuronate reductase
- D-galactonate dehydratase family member Ent638_1932
- TIGRFAM: 2-deoxy-D-gluconate 3-dehydrogenase
- TIGRFAM: 2-deoxy-D-gluconate 3-dehydrogenase
- PFAM: D-galactarate dehydratase/Altronate hydrolase domain protein
- PFAM: PfkB domain protein
- 2-keto-3-deoxygluconate kinase
- 6-phosphogluconate dehydrogenase
- Ribose 5-phosphate isomerase
Sequence:
MTPVIIKNIECFITRPDRHNLVTVRVTTEQGITGHGCATFQQRPLAVKTLVDEYLQPLMIGRDANNIEDLWQMMNVNAYWRNGPLMNNAISGVDMALWDIKGQLAGMPLYQLFGGKSRDAIPAYSHASGETLEALFASVDALIAQGYRHIRCQLGFYGGTPSALHAPDNPTPGAWFDQQEYMSNTVEMFHALREKYGWKLHILHDVHERLFPQQAVQLAKQLEPFQPYFIEDILPPQQSAWLEQVRQQSCVPLALGELFNNPAEWHDLIVNRRIDFIRCHVSQIGGITPALKLAHLCQAFGVRLAWHGPGDMTPIGVAVNTHLNIHLHNAAIQEFIPRSATTNDVFPGAPEVKEGFVYPPVQPGIGVGFNEALALAHPVLYRPHEWTQSRLPDGTIHTP
Protein: Single stranded DNA binding protein 4 (Q3U4B1)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- LIM domain-binding protein 1
- LIM domain-binding protein 2
Sequence:
MYGKASKGCAPSDGQAREKLALYVYEYLLHVGAQKSAQTFLSEIRWEKNITLGEPPGFLHSWWCVFWDLYCAAPDRREACEHSSEAKVFQDYSAAAAPSPVMGAMTPNDAMAAGPVAPGFFQPFMSPRFPGGARPILRMPGQPPVGLPGSQPLIPAAMDPSPRVQGHPSLGGPMQRVTPPRGMASVGPQGYGTGMRPPPNSLATSQVLPSMNMGPGVRGPWASPSGNSIPYSSSSPGSYSGPAGGGGAPGTPIMPSPGDSTNSSENMYTIMNPIGPGAGRANFPLGPSPEGPMASMSTMEPHHVNGSLGSGDMDGLPKNSPGAVGGLSNAPGTPRDDGEMAAAGTFLHPFPSESYSPGMTMSV
Protein: FI03373p (Multicopper oxidase 1, isoform A) (Multicopper oxidase 1, isoform B (EC 1.-.-.-, EC 1.10.3.3, EC 1.16.3.1)) (Multicopper oxidase 1, isoform C) (Q9VLC3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein Malvolio
Sequence:
MSVSHNYDQMSQPTNTTTTQTKASKRPSRFNSKMPVVNSRLAELARITVLLTALLVSYASGLQTVGESADDNTICLYREYNTTYRKEIGAVWFASKDPCLVYSCAAGVAKDPQAHIVATQVDCNEFYCEVGSELRSVEGSCCGECVRTHCQHNHTLYAVGESWHNDADCTLIECGRLDNGQIVMNTYKRNCPALTEDCPASRLEERNCCPYCRPLQTARIEELQDNVAESTDDIWTAEWYRNHPCNRDCQVGAEPMTCRYKFVVEWYQTFSKACYDCPRNLTDCSRPHCVMGDGLERSITVVNRMMPGPAIEVCEGDEIVVDVKNHLLGESTSIHWHGLHQKKTPYMDGVPHITQCPITPHATFRYSFPADLSGTHFWHSHTGMQRGDGVFGALIIRKPKTAEPHGGLYDFDLSEHVMIVQDWIHDTGASIFSYHHHSRGDNKPHNLLVNGKGRYYNRIWAEAKQAHRRAEERTTQPVEPLPKSQVDFVQTLPRQARLAKTNTTKLFPVNSRQKRGNLNEIPLELVPHQIYTVRRGFRYRFRIINAEYLNCPIVVSIDGHNLTAINSDGFDIEAMDVGSIVTYSGERFDFVLNANLEVGNYWIRLKGLMDCSEVFTSAFQVAILRYEGAPDEEPTAELSYGHKAEGIELNVMNRGPGYPDTKTVAEMRALPIYDHVSGIDHDTLKPEADYKFFIYYDFYTKNNPDFHDKDLYAMDMEMTQQNRLYTPQLNHITLNFPSLALLPSRSQLKDSDFCNETSLMDQGIDCRQEFCKCHHVLQVPLGAVVEMIIVDEGFQYYANHPFHLHGNAFRVMGLERLGENVTVEMIKQLDQFNLLKRNLDNPPVKDTVTIPDGGYTIIRFEASNPGYWLFHCHIEFHAEIGMALVFKVGNDDQMVPVPENFPTCGDYNPDLRSDGGTTEDSGSSKPITATPPNTGGGGSGLEPTWITLMISSMLVKLYR
Protein: GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-undecaprenol alpha-1,4-N-acetyl-D-galactosaminyltransferase (EC 2.4.1.292) (Protein glycosylation H) (Q0P9C5)
Organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Function: Processive glycosyltransferase that is part of the biosynthetic pathway of the lipid-linked oligosaccharide (LLO) that serves as the glycan donor in bacterial protein N-glycosylation. Catalyzes the transfer of exactly three alpha-(1->4)-N-acetylgalactosamine (GalNAc) units to the growing LLO precursor, GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-undecaprenyl. Cannot accept UDP-GlcNAc as substrate.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:29386647}; Peripheral membrane protein {ECO:0000305|PubMed:29386647}.
Interaction partners:
- GalNAc
- Undecaprenyl phosphate N,N'-diacetylbacillosamine 1-phosphate transferase
- Protein glycosylation K
- Undecaprenyl-diphosphooligosaccharide--protein glycotransferase
- UDP-N-acetylbacillosamine N-acetyltransferase
- Two-domain glucosyltransferase
- N,N'-diacetylbacillosaminyl-diphospho-undecaprenol alpha-1,3-N-acetylgalactosaminyltransferase
- N-acetylgalactosamine-N,N'-diacetylbacillosaminyl-diphospho-undecaprenol 4-alpha-N-acetylgalactosaminyltransferase
- UDP-glucose 4-epimerase
- UDP-N-acetyl-alpha-D-glucosamine C6 dehydratase
Sequence:
MMKISFIIATLNSGGAERALVTLANALCKEHEVSIIKFHAGESFYKLENEVKVTSLEQFRFDTLYHKIASRFKKFFALRKALKESKSDVFISFLDTTNIACIAAKIGLKTPLIISEHSNEAYLKPKIWRFLRRVSYPFCDALSVLGSSDKVYYERFVKRVKLLLNPCHFSDEISFDSSFEKENLVLFIGRLDHNKNPVMFLKAIAHLDKNLQENYKFVIAGDGQLRQELEYKVKSLGIKVDFLGRVENVKALYEKAKVLCLCSFVEGLPTVLIESLYFEVCRISSSYYNGAKDLIKDNHDGLLVGCDDEIALAKKLELVLNDENFRKELVNNAKQRCKDFEISHIKEEWLKLIAEVKNA
Protein: Apolipoprotein A-I (Apo-AI) (ApoA-I) (Apolipoprotein A1) [Cleaved into: Proapolipoprotein A-I (ProapoA-I)] (P08250)
Organism: Gallus gallus (Chicken)
Function: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT).
Subcellular location: Secreted.
Interaction partners:
- Apolipoprotein B
- Phosphatidylcholine-sterol acyltransferase
- Uncharacterized protein.
- Cholesteryl ester transfer protein
- Phospholipid transfer protein
- Scavenger receptor class B member 1
- Apovitellenin-1
- Uncharacterized protein.
- Albumin
- Uncharacterized protein
Sequence:
MRGVLVTLAVLFLTGTQARSFWQHDEPQTPLDRIRDMVDVYLETVKASGKDAIAQFESSAVGKQLDLKLADNLDTLSAAAAKLREDMAPYYKEVREMWLKDTEALRAELTKDLEEVKEKIRPFLDQFSAKWTEELEQYRQRLTPVAQELKELTKQKVELMQAKLTPVAEEARDRLRGHVEELRKNLAPYSDELRQKLSQKLEEIREKGIPQASEYQAKVMEQLSNLREKMTPLVQEFRERLTPYAENLKNRLISFLDELQKSVA
Protein: Histone H2A (P08844)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Histone H2B
- Histone H4.1
- FACT complex subunit spt16
- RNA polymerase I specific transcription initiation factor Rrn7, putative
- Histone H4.2
- Histone H2A.Z
- Histone H3
- Histone H3
- Histone-lysine N-methyltransferase, H3 lysine-36 specific
- FACT complex subunit pob3
Sequence:
MTGGKSGGKASGSKNAQSRSSKAGLAFPVGRVHRLLRKGNYAQRVGAGAPVYLAAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGHVTIAQGGVLPNIHQNLLPKKTPKAGKGSQEL
Protein: DNA-directed DNA polymerase (EC 2.7.7.7) (Q385L3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSRGWYENILACCCNKVFLASCVATSFFPFLFLWQECPSPYVVLLSVRTDMKNLSIFSARRDDSLSAFFWTDSLIKSCGNIGSSGIHASVTSKQKKSPAASTDRKRRRSTEFSTETLLIAETPVTTASKNTVLTPSASRALSPPVASGPSCAEISVRGFDDALSVSEDLFEGRLGPAVVDVELGENTSLMNDASAFSAALAEIDRGSASDVQKLNSSIKVMLLVGGEAYYVFTPRDTFSITFLAKLLASENVTKVLLNGRPLYQLLFRFLGTDRIDVRNLVDLSVWVQVIERVRGPIHAGIKCANPKEAMMKLPESVRAQIQTRVNNSMVVLRHGGSLPADGPLRQGGGGQNMLEMPPLPSIGSISDSQMEDRLCSSMALHEYYESFVKSVDDDNPKVSSVCSLPAVCRLETSVAFLCEVMTYHGMFVRKTAFELMTKDLEDQIEKISDYGKTLLDASPCSKYSGGCFSVREATAEVMVDCLRDTYGYNLSVNGSFDKQLQKLYRGAGKGNESGRKLAHVWLAIRERTDFMRTLRSNVENMNMLDRIVDVATQVASNEEDEGANDCSGSGGSSVGSTKKAVCYSVHPHWAVHHTSTGRLYCSRPNLQTVPKTAQKCTYVSPLTSDYGLLFTNPEWTMRHLYGPAPGCVLLSFDFNQMELRVLAHLSGDELLIKHLSSEYDVLSAMTRHITGLSDDEQVPPHLRETVKVVVYGLFYGMGLATMKERVKILMDSAHSVPSSQRKFTADTLLRAFHQRYPAAGKFLTRARIRAFHEARCVTLTGINDLSSEKDGNRRRQHSIARILQGSSSTLFQSAMVKVHERRHDIVPNLPAAPFALVLCIHDELIYSVVEGYVDVVARKIKGIMVEQAQVFSLRVPLRVSVKVGKTFGSLEKLDVP
Protein: Ras-related protein Rab-5C (EC 3.6.5.2) (P51147)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Protein transport. Probably involved in vesicular traffic.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P20339}; Lipid-anchor {ECO:0000250|UniProtKB:P20339}; Cytoplasmic side {ECO:0000250|UniProtKB:P20339}. Early endosome membrane {ECO:0000250|UniProtKB:P20339}; Lipid-anchor {ECO:0000250|UniProtKB:P20339}. Melanosome {ECO:0000250|UniProtKB:P51148}.
Interaction partners:
- Phosphatidylinositol 3-kinase catalytic subunit type 3.
- RAB guanine nucleotide exchange factor 1.
- RAB5B, member RAS oncogene family.
- Ras and Rab interactor 1.
- Ras-related protein Rab-5A
- Early endosome antigen 1.
- Adaptor protein, phosphotyrosine interacting with PH domain and leucine zipper 2.
- Adaptor protein, phosphotyrosine interacting with PH domain and leucine zipper 1.
- Ankyrin repeat and FYVE domain containing 1.
- Rabaptin, RAB GTPase binding effector protein 1.
Sequence:
MAGRGGAARPNGPAAGNKICQFKLVLLGESAVGKSSLVLRFVKGQFHEYQESTIGAAFLTQTVCLDDTTVKFEIWDTAGQERYHSLAPMYYRGAQAAIVVYDITNTDTFARAKNWVKELQRQASPNIVIALAGNKADLASKRAVEFQEAQAYADDNSLLFMETSAKTAMNVNEIFMAIAKKLPKNEPQNAAGAPSRNRGVDLQENSPASRSQCCSN
Protein: Probable glutamine synthetase GlnA3 (Glutamine synthase) (GS-I) (O07752)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Amidohydrolase-related domain-containing protein
- Glutamate synthase large chain
- NAD-specific glutamate dehydrogenase
- assimilatory sulfite reductase
- Glutamine--fructose-6-phosphate aminotransferase
- Glutamate synthase small chain
- Carbamoyl phosphate synthase large chain
- Bifunctional uridylyltransferase/uridylyl-removing enzyme
- Carbamoyl phosphate synthase small chain
- Amidophosphoribosyltransferase
Sequence:
MTATPLAAAAIAQLEAEGVDTVIGTVVNPAGLTQAKTVPIRRTNTFANPGLGASPVWHTFCIDQCSIAFTADISVVGDQRLRIDLSALRIIGDGLAWAPAGFFEQDGTPVPACSRGTLSRIEAALADAGIDAVIGHEVEFLLVDADGQRLPSTLWAQYGVAGVLEHEAFVRDVNAAATAAGIAIEQFHPEYGANQFEISLAPQPPVAAADQLVLTRLIIGRTARRHGLRVSLSPAPFAGSIGSGAHQHFSLTMSEGMLFSGGTGAAGMTSAGEAAVAGVLRGLPDAQGILCGSIVSGLRMRPGNWAGIYACWGTENREAAVRFVKGGAGSAYGGNVEVKVVDPSANPYLASAAILGLALDGMKTKAVLPSETTVDPTQLSDVDRDRAGILRLAADQADAIAVLDSSKLLRCILGDPVVDAVVAVRQLEHERYGDLDPAQLADKFRMAWSV
Protein: Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2 (EC 2.4.1.135) (Beta-1,3-glucuronyltransferase 2) (GlcAT-D) (UDP-glucuronosyltransferase S) (GlcAT-S) (Glucuronosyltransferase S) (Q9NPZ5)
Organism: Homo sapiens (Human)
Function: Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on both glycolipids and glycoproteins.
Subcellular location: Golgi apparatus membrane; Single-pass type II membrane protein.
Interaction partners:
- Carbohydrate sulfotransferase 10
- Beta-1,4-galactosyltransferase 1
- Beta-1,4-galactosyltransferase 2
- Beta-1,4-galactosyltransferase 3
- UDP-glucuronosyltransferase 2B7
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1
- UDP-galactose translocator
- Cytochrome P450 2E1
- Cytochrome P450 1A2
- UDP-glucuronosyltransferase 1A6
Sequence:
MKSALFTRFFILLPWILIVIIMLDVDTRRPVPPLTPRPYFSPYAVGRGGARLPLRRGGPAHGTQKRNQSRPQPQPEPQLPTIYAITPTYSRPVQKAELTRLANTFRQVAQLHWILVEDAAARSELVSRFLARAGLPSTHLHVPTPRRYKRPGLPRATEQRNAGLAWLRQRHQHQRAQPGVLFFADDDNTYSLELFQEMRTTRKVSVWPVGLVGGRRYERPLVENGKVVGWYTGWRADRPFAIDMAGFAVSLQVILSNPKAVFKRRGSQPGMQESDFLKQITTVEELEPKANNCTKVLVWHTRTEKVNLANEPKYHLDTVKIEV