wanglab/gogpt-training-data huggingface dataset:
Protein: Polyglutamine-binding protein 1 (Polyglutamine tract-binding protein 1) (A0A0S2Z4V5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic granule {ECO:0000256|ARBA:ARBA00004463}. Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
Interaction partners:
Sequence:
MPLPVALQTRLAKRGILKHLEPEPEEEIIAEDYDDDPVDYEATRLEGLPPSWYKVFDPSCGLPYYWNADTDLVSWLSPHDPNSVVTKSAKKLRSSNADAEEKLDRSHDKSDRGHDKSDRSHEKLDRGHDKSDRGHDKSDRDRERGYDKVDRERERDRERDRDRGYDKADREEGKERRHHRREELAPYPKSKKAVSRKDEELDPMDPSSYSDAPRGTWSTGLPKRNEAKTGADTTAAGPLFQQRPYPSPGAVLRANAEASRTKQQD
Protein: Heterochromatin protein 5, isoform A (LD43003p) (Q960N6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDIFDMVKAAPPPQTINPVDTKLSTPSPIPPDSPIDVNDLLESGNQLDENDLRMSRKSKNVEQCSIDLFDSETSFDHLDESLAKRKRKSVANSKPNKSRKSTVSASTPHNKRPKVSIDDDGEAIEEDQQSMVVVPTKTKAQQKMFSDQQSPNVKRKVRVLLRRLKQTEIDSAVESLANSSFINVPEIVNQSGTSGRSRHKKRKTSPKKQKSSTAQTNFHIKVPLQNGAKKRALNHSLRAHTPPPSLAKSSESTHSALKRSPKPKIKAKRLSSRGRNTDPDLVKRYGAHFFGCVVKVRRTRLPSAKWPDCKPPPIGDGVVRKVYPKKAVSFSEAVEILGSPGGPSRRSTFGSLSSRGAPKPTRLQRVDATGNVLEDIALTSTPLFSSSSGGSRERVRRRSCNGTPVVGRLKLRRLGRLSIDNSSSRSDGGGDNDDDDEEYIGRRMHLLN
Protein: Cyclin-dependent kinase inhibitor 3 (EC 3.1.3.16) (EC 3.1.3.48) (H7C0S3)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, perinuclear region {ECO:0000256|PIRNR:PIRNR037322}.
Interaction partners:
Sequence:
MKPPSSIQTSEFDSSDEEPIEDEQTPIHISWLSLSRVNCSQFLGLCALPGCKFKDVRRNVQKDTEELKSCGIQDIFVFCTRGELSKYRVPNLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELTTCLKNYRKTLIHCYGGLGRSCLAACLLLYLSDTISPEQAIDSLRDLRGSGAIQTIKQYNYLHEFRDKLAAHLSSRDSQSRSVSR
Protein: Gap junction protein (Q3S2N4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell junction, gap junction {ECO:0000256|ARBA:ARBA00004610}. Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU000630}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU000630}.
Interaction partners:
Sequence:
MADWSLLGSFLEEVQEHSTSVGKVWLTILFIFRILVLGTAAESSWGDEQEDFTCDTEQPGCENVCYDRAFPIAHIRFWVLQIVFVSTPSLIYMGHAMHIVRREEKKRKELDDEGAQRDGEKYPEDDKNKEDEGGGRRVRLKGALLQTYVLSILIRTVMEVIFIIIQYLIYGVFLSALYVCKAPPCPHPVNCYISRPTEKNVFIVFMLAVAAVSLLLSIVELYHLAWKQLRKYVHGYKASKQRPNTPSTMPALSPNPSTPNRACTPPPDFNQCLTSPPSSPTLQTHSLLHPTCPPFHDRLAHQQNSANMVTERHRGQDYLGVNFLSFSQTPTETPNSCASPSFLSSDFEDKRRFSKSSGTSSRMRPDDLAV
Protein: T. brucei spp.-specific protein (Q383Y8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MHLQINKYIYMYIYIYVCISVKVKMNKQKVWTRKSEMNDALHPALGVPVHHLVTRQKGKKQISFISHITSPTPSVYVFLLQAFPFLPIRMCAHPRTCAVTHLANLSYAPCGKIRKKELRPLFASSPPPSRQCYTLWRQRRRHGTTAATALQNNSNKTYKQKEE
Protein: 2-acylglycerol O-acyltransferase 3 (EC 2.3.1.20) (EC 2.3.1.22) (Acyl-CoA:monoacylglycerol acyltransferase 3) (MGAT3) (Diacylglycerol O-acyltransferase candidate 7) (hDC7) (Diacylglycerol acyltransferase 2-like protein 7) (Monoacylglycerol O-acyltransferase 3) (Q86VF5)
Organism: Homo sapiens (Human)
Function: Catalyzes the formation of diacylglycerol from 2-monoacylglycerol and fatty acyl-CoA. Also able to catalyze the terminal step in triacylglycerol synthesis by using diacylglycerol and fatty acyl-CoA as substrates. Has a preference toward palmitoyl-CoA and oleoyl-CoA. May be involved in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes. Also able to use 1-monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:27184406}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27184406}.
Interaction partners:
- Diacylglycerol O-acyltransferase 1
- Phospholipid phosphatase 4
- Phospholipid phosphatase 5
- Monoglyceride lipase
- Acylglycerol kinase, mitochondrial
- 2-acylglycerol O-acyltransferase 2
- 2-acylglycerol O-acyltransferase 1
- Diacylglycerol O-acyltransferase 2
- Lipoprotein lipase
- Phosphatidate phosphatase LPIN3
Sequence:
MGVATTLQPPTTSKTLQKQHLEAVGAYQYVLTFLFMGPFFSLLVFVLLFTSLWPFSVFYLVWLYVDWDTPNQGGRRSEWIRNRAIWRQLRDYYPVKLVKTAELPPDRNYVLGAHPHGIMCTGFLCNFSTESNGFSQLFPGLRPWLAVLAGLFYLPVYRDYIMSFGLCPVSRQSLDFILSQPQLGQAVVIMVGGAHEALYSVPGEHCLTLQKRKGFVRLALRHGASLVPVYSFGENDIFRLKAFATGSWQHWCQLTFKKLMGFSPCIFWGRGLFSATSWGLLPFAVPITTVVGRPIPVPQRLHPTEEEVNHYHALYMTALEQLFEEHKESCGVPASTCLTFI
Protein: Basic helix-loop-helix (BHLH) family protein-like (Os01g0575200 protein) (cDNA clone:002-101-F10, full insert sequence) (Q8S0C6)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MDEVWCSLDSMPADIAAGIHQPPPPDLHDPSFWPAFADCAASFIAGGGGDNACFDELMAGGSSGDTRMVAMDDGDDGSGFLVGDAEAEHLMLSSSSPSSLSSGRSLSIDSAGSMSSFSLDAAAALAMSTLAVPHPYPPPVAHGMFASGDGGGGGGGAVDDHEDAIMRAMMAVISSASASPSSSGGSASSPTPFSRDSGAHHQPAGQPAMAAPQQPRGGNGGHVVVKSSSSSGGLAVPMDQKPGGGGRGRQQEEAAAASATNSSQLYHMMSERKRREKLNDSFHTLRSLLPPCSKKDKTTVLINAAKYLKSLETEITELEGTNTKLEKHIAGGGGAADAAMRARRAQQRAKVQISKAADSQSQQLVSLTVMVMVECDVVELVLHILECLRWMKEISVLSVYADTYSPQLLLKAIANIKLQIVGGDWNEASFHEAMTKAANDATISCAPLAITAAQ
Protein: General transcription factor IIF subunit 1 (Transcription factor 5 large chain) (TF5A) (Transcription initiation factor IIF subunit alpha) (TFIIF-alpha) (Q05913)
Organism: Drosophila melanogaster (Fruit fly)
Function: TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation.
Subcellular location: Nucleus {ECO:0000305|PubMed:8175788}.
Interaction partners:
- General transcription factor IIF subunit 2
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerase II subunit RPB9
- RNA polymerase II subunit A C-terminal domain phosphatase
- General transcription factor IIE subunit 1
- Transcription initiation factor IIB
- DNA-directed RNA polymerase II subunit RPB3
- Transcription initiation factor IIE subunit beta
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- General transcription factor IIH subunit 4
Sequence:
MSSASKSTPSAASGSSTSAAAAAAASVASGSASSSANVQEFKIRVPKMPKKHHVMRFNATLNVDFAQWRNVKLERENNMKEFRGMEEDQPKFGAGSEYNRDQREEARRKKFGIIARKYRPEAQPWILKVGGKTGKKFKGIREGGVGENAAFYVFTHAPDGAIEAYPLTEWYNFQPIQRYKSLSAEEAEQEFGRRKKVMNYFSLMLRKRLRGDEEEEQDPEEAKLIKAATKKSKELKITDMDEWIDSEDESDSEDEEDKKKKEQEDSDDGKAKGKGKKGADKKKKKRDVDDEAFEESDDGDEEGREMDYDTSSSEDEPDPEAKVDKDMKGVAEEDALRKLLTSDEEEDDEKKSDESDKEDADGEKKKKDKGKDEVSKDKKKKKPTKDDKKGKSNGSGDSSTDFSSDSTDSEDDLSNGPPKKKVVVKDKDKEKEKEKESAASSKVIASSSNANKSRSATPTLSTDASKRKMNSLPSDLTASDTSNSPTSTPAKRPKNEISTSLPTSFSGGKVEDYGITEEAVRRYLKRKPLTATELLTKFKNKKTPVSSDRLVETMTKILKKINPVKHTIQGKMYLWIK
Protein: Dipeptide and tripeptide permease A (P77304)
Organism: Escherichia coli (strain K12)
Function: Proton-dependent permease that transports di- and tripeptides as well as structurally related peptidomimetics such as aminocephalosporins into the cell. Has a clear preference for dipeptides and tripeptides composed of L-amino acids, and discriminates dipeptides on the basis of the position of charges within the substrate.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Prophage lysis protein S homolog EssQ
- Glutathione S-transferase GstA
Sequence:
MSTANQKPTESVSLNAFKQPKAFYLIFSIELWERFGYYGLQGIMAVYLVKQLGMSEADSITLFSSFSALVYGLVAIGGWLGDKVLGTKRVIMLGAIVLAIGYALVAWSGHDAGIVYMGMAAIAVGNGLFKANPSSLLSTCYEKNDPRLDGAFTMYYMSVNIGSFFSMIATPWLAAKYGWSVAFALSVVGLLITIVNFAFCQRWVKQYGSKPDFEPINYRNLLLTIIGVVALIAIATWLLHNQEVARMALGVVAFGIVVIFGKEAFAMKGAARRKMIVAFILMLEAIIFFVLYSQMPTSLNFFAIRNVEHSILGLAVEPEQYQALNPFWIIIGSPILAAIYNKMGDTLPMPTKFAIGMVMCSGAFLILPLGAKFASDAGIVSVSWLVASYGLQSIGELMISGLGLAMVAQLVPQRLMGFIMGSWFLTTAGANLIGGYVAGMMAVPDNVTDPLMSLEVYGRVFLQIGVATAVIAVLMLLTAPKLHRMTQDDAADKAAKAAVA
Protein: Uncharacterized protein orf160 (Q2F953)
Organism: Oryza sativa subsp. indica (Rice)
Interaction partners:
Sequence:
MSLPGTSSFIGEFLILVGAFQRNGKVRNFPYHYFRECEDFVTFLHFFLYTSGVALSAGELLFLDQNLPPVDEAPPSREILDLDLNAPLPDPEPEVEIVPGDDQHVPPIQEDNPITFHLQNDEQRESLEQMLHSVKERCIMKLRNELIVNKRSRKWGSTKF
Protein: Photosystem I P700 chlorophyll a apoprotein A1 (EC 1.97.1.12) (PSI-A) (PsaA) (P12154)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6.
Subcellular location: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein.
Interaction partners:
- Photosystem I P700 chlorophyll a apoprotein A2
- Photosystem I iron-sulfur center
- Uncharacterized protein
- Photosystem I reaction center subunit II
- Photosystem I assembly protein Ycf3
- Photosystem I reaction center subunit III
- Uncharacterized protein
- Photosystem I reaction center subunit XI, chloroplastic
- Photosystem I reaction center subunit IX
- Photosystem I reaction center subunit VIII
Sequence:
MTISTPEREAKKVKIAVDRNPVETSFEKWAKPGHFSRTLSKGPNTTTWIWNLHADAHDFDSHTSDLEEISRKVFSAHFGQLGIIFIWLSGMYFHGARFSNYEAWLSDPTHIKPSAQVVWPIVGQEILNGDVGGGFQGIQITSGFFQLWRASGITSELQLYTTAIGGLVMAAAMFFAGWFHYHKAAPKLEWFQNVESMLNHHLGGLLGLGSLAWAGHQIHVSLPVNKLLDAGVDPKEIPLPHDLLLNRAIMADLYPSFAKGIAPFFTLNWSEYSDFLTFKGGLNPVTGGLWLSDTAHHHVAIAVLFLVAGHMYRTNWGIGHSMKEILEAHRGPFTGEGHVGLYEILTTSWHAQLAINLALFGSLSIIVAHHMYAMPPYPYLATDYGTQLSLFTHHTWIGGFCIVGAGAHAAIFMVRDYDPTNNYNNLLDRVIRHRDAIISHLNWVCIFLGFHSFGLYIHNDTMSALGRPQDMFSDTAIQLQPVFAQWIQNTHFLAPQLTAPNALAATSLTWGGDLVAVGGKVAMMPISLGTSDFMVHHIHAFTIHVTVLILLKGVLFARSSRLIPDKANLGFRFPCDGPGRGGTCQVSAWDHVFLGLFWMYNSLSIVIFHFSWKMQSDVWGTVTASGVSHITGGNFAQSANTINGWLRDFLWAQSSQVIQSYGSALSAYGLIFLGAHFVWAFSLMFLFSGRGYWQELIESIVWAHNKLKVAPAIQPRALSITQGRAVGVAHYLLGGIATTWSFFLARIISVG
Protein: Solute carrier family 15 member 1 (Intestinal H(+)/peptide cotransporter) (Oligopeptide transporter, small intestine isoform) (Peptide transporter 1) (Proton-coupled dipeptide cotransporter) (Q9JIP7)
Organism: Mus musculus (Mouse)
Function: Proton-coupled amino-acid transporter that transports oligopeptides of 2 to 4 amino acids with a preference for dipeptides. Primarily responsible for the absorption of dietary di- and tripeptides from the small intestinal lumen (By similarity).
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:P46059}; Multi-pass membrane protein {ECO:0000255}. Note=Localized to the apical membrane of enterocytes. {ECO:0000250|UniProtKB:P46059}.
Interaction partners:
- Sodium/glucose cotransporter 1
- Solute carrier family 22 member 6
- ATP-binding cassette sub-family C member 2
- Solute carrier family 2, facilitated glucose transporter member 2
Sequence:
MGMSKSRGCFGYPLSIFFIVVNEFCERFSYYGMRALLVLYFRNFLGWDDNLSTAIYHTFVALCYLTPILGALIADSWLGKFKTIVSLSIVYTIGQAVISVSSINDLTDHDHNGSPDSLPVHVALSMVGLALIALGTGGIKPCVSAFGGDQFEEGQEKQRNRFFSIFYLAINGGSLLSTIITPILRVQQCGIHSQQACYPLAFGVPAALMAVALIVFVLGSGMYKKFQPQGNIMGKVAKCIGFAIKNRFRHRSKAYPKREHWLDWAKEKYDERLISQIKMVTKVMFLYIPLPMFWALFDQQGSRWTLQATTMNGKIGAIEIQPDQMQTVNAILIVIMVPIVDAVVYPLIAKCGFNFTSLKKMTVGMFLASMAFVVAAIVQVEIDKTLPVFPGGNQVQIKVLNIGNNNMTVHFPGNSVTLAQMSQTDTFMTFDIDKLTSINISSSGSPGVTTVAHDFEQGHRHTLLVWNPSQYRVVKDGLNQKPEKGENGIRFVNTLNEMVTIKMSGKVYENVTSHNASGYQFFPSGEKQYTINTTAVAPTCLTDFKSSNLDFGSAYTYVIRRASDGCLEVKEFEDIPPNTVNMALQIPQYFLLTCGEVVFSVTGLEFSYSQAPSNMKSVLQAGWLLTVAVGNIIVLIVAGAGHFPKQWAEYILFASLLLVVCVIFAIMARFYTYINPAEIEAQFDEDEKKKGIGKENPYSSLEPVSQTNM
Protein: Variant surface glycoprotein (VSG), putative (Q4GZE7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MLKTIIGTIVLLIPQPALSNSAADENRGPFTALCTLVNLAKQPPAQLQAPADIAATLETIAAINMTVADSTFMDKVDVNKDYATADQPFRDARPGWEKNYALFSKAKRKATGDEKAKFASWAAKKGIPNLKQQVIKLAEAAQKIGADAEAAASRLATGKVEELLNKALYGTAAPTDTSYKLATDTADNRAKLCSQKGGKGKSIPGKSLVHDLICLCARGPNSDASQGKACCGDCDGNLATEVAVNSDAKTQIDALTKACSKLGSPTELTRATLTGAVAALANQLQHKTATQSSENNVLGTMHSDGSAGCTGNAASNGGKCVVYKDGLTSSGDNAVQWLKHLQEAISEEARRHAASQKLQTLATQIKLLNITLAALEHGTTAQEHVAAEDKPKAADSTDKNKECNKAKDDKEKCNELKEKGCVFNETGEANKKCQFNETKASKNGVPVTQTQTAGSTEATAVNCGQHNEKTKCEEENKGKSSPVCGWRKGKEGEPEQDKEMCRSSSFLLNNKFALSMVSAAFMALLF
Protein: ATP-dependent DNA helicase RecG (EC 5.6.2.4) (DNA branch migration protein RecG) (Probable DNA 3'-5' helicase RecG) (P24230)
Organism: Escherichia coli (strain K12)
Function: Plays a critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA). Has a role in constitutive stable DNA replication (cSDR) and R-loop formation. Is genetically synergistic to RadA and RuvABC.
Interaction partners:
- tRNA
- DNA helicase II
- Holliday junction branch migration complex subunit RuvA
- ATP-dependent DNA helicase RecQ
- Holliday junction branch migration complex subunit RuvB
- DNA replication and repair protein RecF
- DNA-directed RNA polymerase subunit omega
- Replicative DNA helicase DnaB
- Bifunctional
- Single-stranded-DNA-specific exonuclease RecJ
Sequence:
MKGRLLDAVPLSSLTGVGAALSNKLAKINLHTVQDLLLHLPLRYEDRTHLYPIGELLPGVYATVEGEVLNCNISFGGRRMMTCQISDGSGILTMRFFNFSAAMKNSLAAGRRVLAYGEAKRGKYGAEMIHPEYRVQGDLSTPELQETLTPVYPTTEGVKQATLRKLTDQALDLLDTCAIEELLPPELSQGMMTLPEALRTLHRPPPTLQLSDLETGQHPAQRRLILEELLAHNLSMLALRAGAQRFHAQPLSANDTLKNKLLAALPFKPTGAQARVVAEIERDMALDVPMMRLVQGDVGSGKTLVAALAALRAIAHGKQVALMAPTELLAEQHANNFRNWFAPLGIEVGWLAGKQKGKARLAQQEAIASGQVQMIVGTHAIFQEQVQFNGLALVIIDEQHRFGVHQRLALWEKGQQQGFHPHQLIMTATPIPRTLAMTAYADLDTSVIDELPPGRTPVTTVAIPDTRRTDIIDRVHHACITEGRQAYWVCTLIEESELLEAQAAEATWEELKLALPELNVGLVHGRMKPAEKQAVMASFKQGELHLLVATTVIEVGVDVPNASLMIIENPERLGLAQLHQLRGRVGRGAVASHCVLLYKTPLSKTAQIRLQVLRDSNDGFVIAQKDLEIRGPGELLGTRQTGNAEFKVADLLRDQAMIPEVQRLARHIHERYPQQAKALIERWMPETERYSNA
Protein: Anaphase-promoting complex subunit 4-like WD40 domain-containing protein (Q385K9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKILHTRAAAEPILLATTCHNMNLLAVVTKSLVVVYRSTTLTVVTQFALSIPADETSVCACWSPSGRLLVIGLQNGEAFLLDVESGDLVRRFVPRSDAECSSIMVEDISGGTAPAPAAGDADNDGDDEGVGKSYDPLRQPPVLFTSMKGAIMACTWTTVASQVSSTNRHQERCLPLRTTVLSPILDELEREDETPVLILLDQEGGLSFLPGGMREVCFVPARLPVNLTPNLACVDTFVVCKPSTAAGKEGDSGGLALKHLDCATGDSSKRDADNAVAAHVAYLVVRRSLSKEHPHVIRFDLSPIIASATRRDVVSVCCIAEYCRMGRDCFLYSLRRWTNLICTVHNDMFLPKNAMLLRDSLVEEIAHPQEKEVMKYFNAVNLATLVNDAEELSQQLKQLILQISNVAYRCYDIALHISEAHCADRQRQRLLLSVIGNLRLRCSNLMREMRHGAEREKELLQWVIQRAALLTNATPPATDVLLLNEPLRARWHSMLLRTLHRIGHGESAVTSLVDEKGMRNEVDLAQIVKSCMPRHYEVTGYDLPLVCQQSDPVHIRQCEILISDKTSFAVDGVMLRTVALTREEPFQPLTAFFVLERQPGAGSVFRQVQEWVSVETQQLQLTVDTASFLWSAVVDEESHCVVLWEQKVTSQTPSAALTGAAANTWAEQTLVLALTDENGALELHNEGVDESVDETGGNATETSAQGAKYAVLEVKGISTKHLRVSVSQVRGFGVLYAKERFVVVDFYRG
Protein: Ras-related protein Rab-22A (Rab-22) (Q9UL26)
Organism: Homo sapiens (Human)
Function: Plays a role in endocytosis and intracellular protein transport. Mediates trafficking of TF from early endosomes to recycling endosomes. Required for NGF-mediated endocytosis of NTRK1, and subsequent neurite outgrowth. Binds GTP and GDP and has low GTPase activity. Alternates between a GTP-bound active form and a GDP-bound inactive form.
Subcellular location: Endosome membrane {ECO:0000250|UniProtKB:P51154}; Lipid-anchor {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P51154}; Lipid-anchor {ECO:0000305}. Early endosome {ECO:0000269|PubMed:16537905}. Late endosome {ECO:0000250|UniProtKB:P51154}. Cell projection, ruffle {ECO:0000269|PubMed:21419809}. Cytoplasmic vesicle {ECO:0000269|PubMed:21419809}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle, phagosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Recruited to phagosomes containing S.aureus or M.tuberculosis. {ECO:0000269|PubMed:21255211}.
Interaction partners:
- Ras-related protein Rab-31
- Rabenosyn-5
- Rab5 GDP/GTP exchange factor
- Rab GDP dissociation inhibitor alpha
- RAD51-associated protein 1
- TBC1 domain family member 10B
- Early endosome antigen 1
- DCC-interacting protein 13-beta
- TBC1 domain family member 10A
- Rab GTPase-binding effector protein 1
Sequence:
MALRELKVCLLGDTGVGKSSIVWRFVEDSFDPNINPTIGASFMTKTVQYQNELHKFLIWDTAGQERFRALAPMYYRGSAAAIIVYDITKEETFSTLKNWVKELRQHGPPNIVVAIAGNKCDLIDVREVMERDAKDYADSIHAIFVETSAKNAININELFIEISRRIPSTDANLPSGGKGFKLRRQPSEPKRSCC
Protein: Guanine nucleotide-binding protein alpha-2 subunit (GP2-alpha) (P10823)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Alpha subunit of the heterotrimeric guanine nucleotide-binding protein (G protein) involved in glucose-induced cAMP signaling. Binds to its cognate transmembrane receptor GPR1, which senses extracellular carbon sources, and activates cAMP-PKA signaling and governs diploid pseudohyphal differentiation and haploid invasive growth. The G protein beta-mimic proteins GPB1 and GPB2 inhibit GPA2-GPR1 coupling, probably to reduce signaling in the absence of glucose.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16030250}; Lipid-anchor {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16030250}; Cytoplasmic side {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16030250}.
Interaction partners:
- G protein-coupled receptor GPR1
- Regulator of G-protein signaling 2
- Adenylate cyclase
- Ras-like protein 2
- Guanine nucleotide-binding protein subunit beta
- Protein SST2
- Guanine nucleotide-binding protein subunit beta 1
- Guanine nucleotide-binding protein subunit beta 2
- Low glucose sensor SNF3
- Ras-like protein 1
Sequence:
MGLCASSEKNGSTPDTQTASAGSDNVGKAKVPPKQEPQKTVRTVNTANQQEKQQQRQQQPSPHNVKDRKEQNGSINNAISPTATANTSGSQQINIDSALRDRSSNVAAQPSLSDASSGSNDKELKVLLLGAGESGKSTVLQQLKILHQNGFSEQEIKEYIPLIYQNLLEIGRNLIQARTRFNVNLEPECELTQQDLSRTMSYEMPNNYTGQFPEDIAGVISTLWALPSTQDLVNGPNASKFYLMDSTPYFMENFTRITSPNYRPTQQDILRSRQMTSGIFDTVIDMGSDIKMHIYDVGGQRSERKKWIHCFDNVTLVIFCVSLSEYDQTLMEDKNQNRFQESLVLFDNIVNSRWFARTSVVLFLNKIDLFAEKLSKVPMENYFPDYTGGSDINKAAKYILWRFVQLNRANLSIYPHVTQATDTSNIRLVFAAIKETILENTLKDSGVLQ
Protein: DNA-directed RNA polymerase III subunit rpc8 (RNA polymerase III subunit C8) (RNA polymerase III subunit C25) (O94285)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- Probable DNA-directed RNA polymerase III subunit rpc6
- DNA-directed RNA polymerase III subunit rpc9
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase III subunit rpc3
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- DNA-directed RNA polymerases I and III subunit RPAC2
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
Sequence:
MFLLSRFSDIISIHPSNFWKPTKEALAEEIHKKYANKVIQNIGLAICVYDFLKIGEGIIKYGDGSSYMNVVFRLIIFRPFRGEVMLGKIKSCSEEGIRVTISFFDDIFIPKDMLFDPCVFRPDERAWVWKIEGEDGSEGTELYFDIDEEIRFQIESEDFVDISPKRNKNATAITGTEALESVSPYTLIASCSRDGLGIPAWWK
Protein: Exonuclease 1 (EC 3.1.-.-) (Q5T398)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU910737}.
Interaction partners:
Sequence:
MGIQGLLQFIKEASEPIHVRKYKGQVVAVDTYCWLHKGAIACAEKLAKGEPTDRRRQANLLKGKQLLREGKVSEARECFTRSINITHAMAHKAARSQGVDCLVAPYEADAQLAYLNKAGIVQAIITEDSDLLAFGCKKVILKMDQFGNGLEIDQARLGMCRQLGDV
Protein: Meiotically up-regulated gene 87 protein (O94418)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Nucleus envelope {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Nucleoporin nup186
- Nucleoporin nup184
- Probable nucleoporin C890.06
- Nucleoporin nup44
- Nucleoporin nsp1
- Nucleoporin nup189
- Nucleoporin nup45
- Nucleoporin nup107
- Nucleoporin nup85
- Nucleoporin seh1
Sequence:
MTVASDDSPKEARGIPFLDQKSRKLANELLEPCLPFIQFNLGEIEQRAKHYLNTVPTSKDGNTKAHYLLAGSGINAEQTWKKIESLSLQVRPPTTLELSFTDVDMFLKYHREKNVLNSLEALVQNTQIAFDQYLEEEWRSKAAKSRPSFDNILLENKKRVSFYPFSVQRSQKFASTLKMCLEEEALHGFQSKLVSSFCEVAREFAHDTKSLLLYESWKLLSSVILDKDSVTVFGNKGIISKAFDIETEDGSVNSRFYQRISDCSRKFLEAQFFEVLNKEIAKTPQAALVGGVPSIRNKIRAYLNIRLLRNGVWINPDLEIIQDVPIWAFIFYLLRCGFLKEAVDFTEENRDLFEKVAEKFPFYINAYAKAPNGILPRQLRSQLFSEFNQTIRLQESSDPYKYAVYKIIGRCDLSKTSCPSICSVTEDYIWFQLILSREFTEKSVSAHEFFSLEDVQHILLSYGSDYFTNNGSNPVMYFFLLMLCGLYERAINFLYPYFPTDAVHFAITCAYYGLLRTAPSSSVVSNEPGKIQSMLVETKSGKPSLEFDRLLIDYTQTCQELSPVMSACYLIPMCKIDKYISMCHKSLCSLVLSTRDYVNLLGDIRGDGERTPSFLENHRSLIGLSSVKEYLSKITLTAAKQADDQGLLSDAILLYHLAEDYDAAVTVINRRLGSALLRFLDQFVFPDKLISLTKSMMDVYNRNPSLYAKVDYKNRETTNLLLLTVEAFNAYTNKDYEQALSSLQQLEILPLDPLDSDCETFVVRKLAKEFRFLNENLLQNVPGIVLIAMNSLKELYAKQKSSSFGNDAISVDKLRLYRQKARRIVMYSFLIEYRMPSQILEQLNRCEIEMT
Protein: Heliorhodopsin HeR (A0A151EDA9)
Organism: Thermoplasmatales archaeon SG8-52-1
Interaction partners:
Sequence:
MTENEEINFRKFRIFNGIMGVIHLIQVFLVLYLSNNFSLPITVNKPVYNEITNSISPVAETLFSIEIGPLVAMFLFISATAHILIATVLYYRYVQNLKNHMNPYRWFEYSISASFMIVIIAMLTTIYDLGTLLALFTLTAVMNLMGLMMELHNQTTQNTNWTSYIIGCIAGFVPWIVIFIPLISAESVPDFVIYIFISIAIFFNCFAINMYLQYKKIGKWKNYLHGEKVYIILSLVAKSALAWQVFAGTLRPM
Protein: CKLF-like MARVEL transmembrane domain-containing protein 4 (Chemokine-like factor superfamily member 4) (Q8IZR5)
Organism: Homo sapiens (Human)
Function: Acts as a backup for CMTM6 to regulate plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity. May protect PD-L1/CD274 from being polyubiquitinated and targeted for degradation.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- CKLF-like MARVEL transmembrane domain-containing protein 1
- CKLF-like MARVEL transmembrane domain-containing protein 3
- Chemokine-like factor
- CKLF-like MARVEL transmembrane domain-containing protein 2
- CKLF-like MARVEL transmembrane domain-containing protein 5
- Programmed cell death 1 ligand 1
Sequence:
MRSGEELDGFEGEASSTSMISGASSPYQPTTEPVSQRRGLAGLRCDPDYLRGALGRLKVAQVILALIAFICIETIMACSPCEGLYFFEFVSCSAFVVTGVLLIMFSLNLHMRIPQINWNLTDLVNTGLSAFLFFIASIVLAALNHRAGAEIAAVIFGFLATAAYAVNTFLAVQKWRVSVRQQSTNDYIRARTESRDVDSRPEIQRLDTFSYSTNVTVRKKSPTNLLSLNHWQLA
Protein: Thioredoxin domain-containing protein (Q38BK3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVGASSKRPREHETAVEPILAGSFSGGNVSKKSFNGTVVAETDNKSLGVTATLLRDVDFNSQSSMKRSVSNNSNMVGSQNDDSNDECEGEVCELFKSPAQLGGKLQVGVDSRPDVPVSNGQKTLLHAECTNSTASVDGAITTLHTLQQLKELFHTPPVQLEAQAKAPLLQLCAGETVFVVLHSNKEEIEGMLGNVTKKLSACRIFCLDLSALPLAERSGAGAQITPNSASVDRVGDVILQRVTKILDLNSLLNGTPSAEGPSQSLSIKHSSAGAQVEFENVASSAQSSAKDEICHHELTLPSMVMWRVAGGPVDEYGDITAMGSYEAIQSEVGSVPPYGKPLVVKELQTVDQLHSLSLLAPVYTVEHLLRKIGETVLFPPGNDTPSGTHTFIYMGASWCPPCMRVVASLPTMMKEGFPHSFACVVKADMDFAEPLYKFFGVEIIPTFILLNNDVLKGAGDWSAFLKGSGKCMGTCLEQLREGLRRSKMGQIQNSKVPLIQSFIDNHTKGLSFDEEF
Protein: Importin subunit alpha-1 (J3KS65)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSTNENANTPAARLHRFKNKGKDSTEMRRRRIEVNVELRKAKKDDQMLKRRNVSSFPDDATSPLQENRNNQGTVNWSVDDIVKGINSSNVENQLQATQAARKLLSREKQPPIDNIIRAGLIPKFVSFLGRTDCSPIQFESAWA
Protein: V-FLIP (Q1XBR6)
Organism: Bovine herpesvirus 4 (BoHV-4) (Movar virus)
Interaction partners:
Sequence:
MVTRDVLLAIETHLNQNEKTFVMYFLLDPYIPKECKDFLPTLENLHSKRKIRYPILIELMYILQRFDLLRSIFLLDHRFVKDQITSSHWKYISPYKQLIFSIGQNIDDEDLISIKFISMNYIGKSPSKIKNYLDWVRALEKVDMVGPDNLDLFETFFKQIHRMDIVKMIKNYRTRETLQITL
Protein: Cysteine protease (EC 3.4.22.-) (K7ESM7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU363115}.
Interaction partners:
Sequence:
XLPRDWTWAEGMGLGPPELSGSASPSRYHGPARWMPPRWAQGAPELEQERRHRQIVSWFADHPRAPFGLHRLVELGQSSGKKAGDWKAVESCSDVTRLVVYVSQDCTVYKADVARLVARPDPTAEWKSVVILVPVRLGGETLNPVYVPCVKELLRCELCLGIMGGKPRHSLYFIGYQDDFLLYLDPHYCQPTVDVSQADFPLE