wanglab/gogpt-training-data huggingface dataset:
Protein: DNA replication licensing factor MCM2 (EC 3.6.4.12) (C4LYY1)
Organism: Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM5
- DNA replication licensing factor MCM7
- ATPase AAA-type core domain-containing protein
- Cell division control protein 45 CDC45, putative
- Origin recognition complex subunit 1
- DNA helicase
- DNA replication licensing factor MCM6
- DNA replication complex GINS protein PSF2
Sequence:
MTDSADPHKDHPTTQKEAQSEEELNDSMIDQILQENDDNNKTHHDDETDEHQEDSLDVIPNDGIEEEELEDREYEKEIGIAKGVNELNETESSDDEGEDLFNPKLMDEDYERSEESEYDDPNLINNEIEHNEGVDEIEARRKADEEIDRRNALMRKVIDEEDSSIEEFNLLVEQQHRRRSEIEKLTMKQDTDIVIPQFGLNEEEVKERFKQREIEKMPIEQLQMMMSEAESKLQMYTKEHIKDAILKEDVHDLLVETLKNFLLYYTETETSKNVVYILSIRKMVSRNSGSLDVSFLHLAKSSKLLAQWIVLCPSSVIPIFSEAATQATLLLYPDYKDIRKQVNVRIVDYTTRIALRDLRHCHINTLIRVVGIVTRVTAIFPQLKAVKYICSVCQARLGPYFINKEMNKVPQLQVCTVCQSKGPFSIDVQNTIYQNYQKITIQEPPNSVSAGNVPRTKDVILLGDLIDKAQPGEEIDITGMYVHNYETGLNRNFGFPVFCTVIEANTIEKRSGDVISTTITHEEEQEIRRLANNPQIFQIIINSIAPAIYGHDASKAAIALALFGGEQRVLVDKGNHRTRGDINVLLLGDPGTAKSQLLKYSQKLAPRAVFTTGRGSTAVGLTAAVKKDSMNGEWALEGGALVLADEGVCLIDEFDKMDDQDRTSIHEAMEQQSISISKAGIVTSLKARCSVIAAANPKTGKYNPNKNLNQNVNLTEPIISRFDLIMIVRDVVDYEKDYKLAQFVVESHSINHPEASQKRESIAPIVNKTNIISHVLLKKYIAYARQNCHPKWSGTVGSQMIQQAYIEMRKCCDKYHTGQVTARQIEAINRLSEAHAKIHLRGVVTTEDVKIALKITLKSFISCQKTEQAKQLQQQFQNYLN
Protein: Superoxide dismutase (EC 1.15.1.1) (F5H4R2)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}.
Interaction partners:
Sequence:
MLPRVGGPGATSRERPWAASRGRLLLAEAHLTSRQLAPVLGYLGSRQKHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWTNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERGHLQ
Protein: Rac GTPase activating protein 1 (F8VVE5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSCPCFCPVALRMDTMMLNVRNLFEQLVRRVEILSEGNEVQFIQLAKDFEDFRKKWQRTDHELGKYKDLLMKAETERSALDVKLKHARNQVDVEIKRRQRAEADCEKLERQIQLIREMLMCDTSGSIQLSEEQKSALAFLNRGQPSSSNAGNKRLSTIDESGSILSDISFDKTDESL
Protein: Galactokinase (AFU_orthologue AFUA_3G10300) (Q5B3C3)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- UDP-glucose 4-epimerase
- Galactose-1-phosphate uridylyltransferase
- Aldose 1-epimerase, putative
- UDP-glucose 4-epimerase
- UDP-glucose 4-epimerase
- Uncharacterized protein
- NAD-dependent epimerase/dehydratase domain-containing protein
- Phosphoglucomutase
- Multifunctional tryptophan biosynthesis protein
- UTP--glucose-1-phosphate uridylyltransferase
Sequence:
MATPQELVPRTESIAEVYATDNASATTASPEHVKRFNNLVSHFHKQYNHSPDFVARSPGRVNIIGEHIDYNLYDVLPTAVSVDVIIAVKVVPTESSESAVKIANVLPDKFPTREFSVPKDSDVEIDPKKHEWVNYFKAGLVGALKVLRKGAADGSFAPASMEVLVDGNVPPGGGISSSAAFVCSSALAVMKANNHDVSKQDLLDLAVVSERAVGVYSGGMDQAASIFSRRGYLLYTQFFPNFSVQHVAIPKAAEEITFLMAQSFVTSNKAETAPRHYNLRVAECTLASVVLAKANGLTLPKDNSSLGYSLRTFHNELMRKEGRLGDPLEYQIDSVIQATLDILTQEQGYTREEIAQLLSISVPELETTYLSSFPVQAERFLLRQRALHCFKEARRVLDFKACLANASTLDDKRIHYLGQLLNESQDSCRDVYECSAPQVDEICNIARKAGTWGSRLTGAGWGGCTVHMLPQSKVEAVTKALTEEYYLKYFPDISEEKLKEAMVISKPSNGSFLITGAAISQVDV
Protein: Ubiquitin-like protein NEDD8 (Neddylin) (Q71UE8)
Organism: Rattus norvegicus (Rat)
Function: Ubiquitin-like protein which plays an important role in cell cycle control and embryogenesis via its conjugation to a limited number of cellular proteins, such as cullins or p53/TP53. Attachment of NEDD8 to cullins is critical for the recruitment of E2 to the cullin-RING-based E3 ubiquitin-protein ligase complex, thus facilitating polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins. Attachment of NEDD8 to p53/TP53 inhibits p53/TP53 transcriptional activity. Covalent attachment to its substrates requires prior activation by the E1 complex UBE1C-APPBP1 and linkage to the E2 enzyme UBE2M.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q15843}. Note=Mainly nuclear. {ECO:0000250|UniProtKB:Q15843}.
Interaction partners:
- Cullin-1
- NEDD8-conjugating enzyme UBC12
- NEDD8-activating enzyme E1 catalytic subunit
- Sentrin-specific protease 8
- E3 ubiquitin-protein ligase RBX1
- NEDD8-activating enzyme E1 regulatory subunit
- NEDD8-conjugating enzyme UBE2F
- Cullin-3
- Cullin 2
- Cullin-5
Sequence:
MLIKVKTLTGKEIEIDIEPTDKVERIKERVEEKEGIPPQQQRLIYSGKQMNDEKTAADYKILGGSVLHLVLALRGGGGLGQ
Protein: MB2k1 protein (MB2k2 protein) (P70679)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MAALWLLLLVLSLHCMGAGGFVAHVESTCVLDDAGTPQDFTYCVSFNKDLLACWDPDVGKIVPCEFGVLSRLAEIISMILNEQESLIQRLQNGLQDCATHTQPFWDVLTHRTRPPSVRVAQTAPFNTREPVMLACYVWGFYPADVTITWMKNGQLVPSHSNKEKTAQPNGDWTYQTVSYLALTPSYGDVYTCVVQHSGTSEPIRGDWTPGLSPIQTVKVSVSAATLGLGFIIFCVGFFRWRKSHSSSYTPLPGSTYPEGRH
Protein: Protein cordon-bleu (Q5NBX1)
Organism: Mus musculus (Mouse)
Function: Plays an important role in the reorganization of the actin cytoskeleton. Binds to and sequesters actin monomers (G actin). Nucleates actin polymerization by assembling three actin monomers in cross-filament orientation and thereby promotes growth of actin filaments at the barbed end. Can also mediate actin depolymerization at barbed ends and severing of actin filaments. Promotes formation of cell ruffles. Regulates neuron morphogenesis and increases branching of axons and dendrites. Regulates dendrite branching in Purkinje cells.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton. Cell projection, ruffle. Cytoplasm. Note=Recruited to the cell membrane via interaction with PACSIN1 (By similarity). Colocalizes with the actin cytoskeleton. Detected throughout the neuron cell body, as well as in axons and dendrites. {ECO:0000250}.
Interaction partners:
- Drebrin-like protein
- Junction-mediating and -regulatory protein
Sequence:
MDAPRALAAKPPTGRKMKARAPPPPGKPAAQNVHSEQKLPHDATLGSQQSLVYMKEALQNSTLDITVVLPSGLEKQSVVSGSHAMMDLLVELCLQNHLNPSHHVLEIWSSETQQPLSFKPNTLIGSLNVHTVLLKEKVPEERVKPGLTKAPEKSVRLVVNYLRTQKAVVRVSPEVPLQNILPVICAKCEVNPEHVILLRDNVAGEELELSKSLNELGIKELYAWDNRREMFRKSSLGNDETDKEKKKFLGFFKANKRSNSKAEHLGLSGADSDEDPAKSASGGDLNGCVTTPNSPSLHSRSLTLGPSLSLGNISGVSMKSDMKKRRAPPPPSPKLLGQDKVSEKASLSSQADLQKKKRRAPAPPPPQQPPPSPVVPNRKEDKEENRKSTVGVGRQVPQKPPRGTARGPPQLVLPPPPPYPPPDTDVTEPVTFPGEGAGSETSELRPKLSLPLGPGSHCSMGGVSQVPAESEETASEDTTEDSGVMSSPSDAISLDSQQDSMRSKDKWSTDQEDGSDQDLAGTPELGPQKSPSWGKSGSGSSILRTEKATMPTNDDEDLFITGHLHQTLAELDEDLEGMEENYETDTSSLTNSVNGVSNHSLQEAIIPDSGVDDIPVTFIGEVSDEPFDSGLFSSRCNNATTFNTGSIASQRSHLSPSQTEHSQPFVRTSRKEPDPSPPSQDNRKRNQPTLANTSENENPVETDPTVTSLVSKLLIDDPKAKDKGKVHGSSHSEKTQAGHGINSLRVNPRDGKDESSNSAPPPWSHHGQALGGSYGLKYGLTTYKIVPPKSEMRCYDRDVSLSTGAIKIDELGNLVSPHMNGSRTISPPSAVVETDTPPIGKVKEFWRRNSMEKYLNGPAECTIKRAPSTTITATPEKPQQDNGMKAAFTVTTPQQQPASQEYGAHLEEERSRPQSAVSCSVKVPASNPTDITFLKPQRRTSSQYVASAIAKKMGPPKVHADVVRPHKATTEQCHEEAKLARSPPTRKDDAAPNLHSEARQHEHGTNQSSVCLPSNPGVQLPAGGHPKVEVNSTYGKSSTQDYPAAVHRNSYFLPGRSSHRDRVSVGQSCGFNEKQTTSNQKANSTSNFSQALDKAHPPPLLLAEARDSGRILMNGSARTPGNCEPPHSPKESTLTSYIILQTEEKPSSLSTDGQDADDTLPSSIFGPKKKFKPVIQRPLPKDVSLHSALMEAIHSSGGREKLRKTAEQTSEGRPKKPSYVEAESERSALLAAIRGHSGTLSLRKVSSLASEELQSFRNAALGAPGLDKPQQEDLGLPPPPALPPPPAPAPQAPSASVTVSRFSTGTPSNSVNARQALMDAIRSGTGAARLRKVPLLV
Protein: Poly [ADP-ribose] polymerase 2 (EC 2.4.2.30) (Poly ADP-ribose metabolism enzyme 2) (Protein poly-ADP-ribosyltransferase parp-2) (EC 2.4.2.-) (Q09525)
Organism: Caenorhabditis elegans
Function: Poly[ADP-ribose] polymerase modifies various nuclear proteins by poly(ADP-ribosyl)ation, a post-translational modification synthesized after DNA damage that appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks and programmed cell death.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9UGN5}.
Interaction partners:
- Poly [ADP-ribose] polymerase 1
- Poly
- Poly
- Probable tyrosyl-DNA phosphodiesterase
- Flap endonuclease 1
- Zinc finger, CCHC-type
- Ku domain-containing protein
- DNA ligase IV
- Uracil-DNA glycosylase
- DNA ligase 1
Sequence:
MSIINDENGRGYKVHLCKTNIAQNNNKFYDMELLDEGGDFIVKLINGRIGYRGVTQLKDFDDLDRAKKFFESKFYEKTHLHWEERDDEPVPNKYAVVELATNARQTEKEVKKEEPEPEPKVDEKNTRGRKKRGIVKEKKEIKKEEEPVEEVNEKLKELMKCICDEDVHLGLLKQLKFNEAFGRPIDCLSLAQLTTGYEILSKIEESIGGKSARRSTRGRPRVADRVLAVKSDGPSLHDINKYYSLIPHSFGFCVPPKIDSHAKIQAERELLDALKGSIEASLELKDLKKTASSKDIYQRLYERLPCHLEPVSEEIAGKIGDCLAMRGPTHCYKLSLIDAFELKDPNEIPTEAPVEVQEVPKKRGRKSTKTAAPTVPPPTTKRLLWHGTRVTNVFSILMNGLQFPVGDRCGLMFGNGVYFANVPTKSANYCCPEASKRVFMLLCEVETANPLVLYESEIDADEKMEKAKKTSVYAAGKHTPRDTVEINGIPAFKSNLETIEEETRLLYDEYVMFNKEHFKIKYVVEVKVDRLTAKEMMA
Protein: TIAM Rac1 associated GEF 1 (A0A8I6AC12)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGNAESQNVDHEFYGEKHASLGRKHTSRSLRLSHKTRRTRHASSGKAIHRNSEVSTRSSSTPSIPQSLAENGLEPFSQEGALDDFGDPIWVDRVDMGLRPVSYTDSSVTPSVDGSIVLTAASVQSMPDSEESRLYGDDAAYLAEGGRRQRPYTSNGPTFMETASFKKKRSKSADIWREDSLEFSLSDLSQEHLTSNEEILGSAEEKDCEEARGMETGASPRQLSTCQRANSLGDLYAQKNSGVKANGGPRNRFSSYCRNLVSDIPDLAKHKMPPAAVETPTYSNYNTLPCRKSHCLSEGATNPQISLSKSMQGRRAKTTQDVNTGEGSEFADSGIEGATTDTDLLSRRSNATNSSYSPPTGRAFVGSDSGSSSTGDAARQGVYENFRRELEMSTTNSESLEEAGSAHSDEQSSGTLSSPGQSDILLTAAQGTVRKAGALAVKNFLVHKKNKKVESATRRKWKHYWVSLKGCTLFFYESDGRSGIDHNSVPKHAVWVENSIVQAVPEHPKKDFVFCLSNSLGDAFLFQTTSQTELENWITAIHSACAAAVARHHHKEDTLRLLKSEIKKLEQKIDMDEKMKKMGEMQLSSVTDAKKKKTILDQIFVWEQNLEQFQMDLFRFRCYLASLQGGELPNPKRLLGFASRPTKVAMGRLGIFSVSSFHALVAARTGEIGVRRRTQAMSRSASKRRSRFSSLWGLDTTSKKKQGRPTINQVFGEGTDAVKRSLEGIFDDSVPDGKREKEVVLPSVHQHNPDCDIWVHEYFTPSWFCLPNNQPALTVVRPGDTARDTLELICKAHQLDHSAHYLRLKFLMENKMQFYVPQPEEDIYELLYKEIEICPKVTQNIHIEKSDAAADNYGFLLSSVDEDGVRRLYVNSVKETGLASKKGLKAGDEILQINNRAAGTLNSSMLKDFLSQPSLGLLVRTYPEPEGGVELLENPPHRVDGPVDLGESPLTFLTSNPGHSLSSEQGSSAETAPEEGEGPDLESSDETDHSSKSTEQVTAFCRSLHEMSPSDSSPSPQDATSPQLATTRQLSDADKLRKVICELLETERTYVKDLNCLMERYLKPLQKETFLTQDELDVLFGNLTEMVEFQVEFLKTLEDGVRLVPDLEKLEKVDQFKKVLFSLGGSFLYYADRFKLYSAFCASHTKVPKVLVKAKTDTAFKAFLDAQNPRQQHSSTLESYLIKPIQRVLKYPLLLRELFALTDAESEEHYHLDVAIKTMNKVASHINEMQKIHEEFGAVFDQLIAEQTGEKKEVADLSMGDLLLHTSVIWLNPPASLGKWKKEPELAAFVFKTAVVLVYKDGSKQKKKLVGSHRLSIYEEWDPFRFRHMIPTEALQVRALPSADAEANAVCEIVHVKSESEGRPERVFHLCCSSPESRKDFLKSVHSILRDKHRRQLLKTESLPSAQQYVPFGGKRLCALKGARPAMSRAVSAPSKSLGRRRRRLARNRFTIDSDAISASSPEKEPQQPPGGGDTDRWVEEQFDLAQYEEQDDIKETDILSDDDEFCESAKGASVDIDLQEQLQAASISQRARGRKTLDSHASRMTQLKKQAALSGINGGLESASEEVIWVRREDFAPSRKLNTEI
Protein: Uncharacterized protein C645.12c (Q9Y7V1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MSSARELLRKVKQERLGQKRGLKASSQELKRQKTRDHKSFENLGRDQSRELAVSDFNEKQSTEPPKDTRAVSALPENFFDESIAKNKELIEEEWNDFQNEIGIIEENAVEQEITLQQQQLLAEKDEENEIADNDLEPEVYDILYEEESKLGESRDLIRRLKQKRFETKKNNFSVKESSNLSNNDSDASLDEDTLLWGL
Protein: Probable acetyl-/propionyl-coenzyme A carboxylase alpha chain (Alpha subunit) AccA2: biotin carboxylase + biotin carboxyl carrier protein (BCCP) (P71538)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable biotin-dependent acyl-coenzyme A carboxylase beta2 subunit
- Probable biotin-dependent acyl-coenzyme A carboxylase beta3 subunit
- Biotin-dependent acetyl-/propionyl-coenzyme A carboxylase beta6 subunit
- Biotin-dependent acetyl-/propionyl-coenzyme A carboxylase beta5 subunit
- Acyl-CoA dehydrogenase FadE12
- Exopolyphosphatase
- Probable acyl-CoA dehydrogenase FadE13
- Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase beta1 subunit
- Probable enoyl-CoA hydratase EchA7
- Probable fatty acid synthase Fas
Sequence:
MGITRVLVANRGEIARRVFATCRRLGLGTVAVYTDPDAAAPHVAEADARVRLPQTTDYLNAEAIIAAAQAAGADAVHPGYGFLSENAEFAAAVQEAGLTWVGPPVDAVRAMGSKIESKKLMAAAGVPVLEELDPDAVTTAQLPVLVKASAGGGGRGMRVVHELSALPAEVEAARREAQSAFGDPTVFCERYLPTGHHVEVQVMADTHGTVWAVGERECSIQRRHQKIIEEAPSPLVERVPGMRAKLFDAARLAASAIGYTGAGTVEFLADDSPGREGEFYFLEMNTRLQVEHPVTEETTGLDLVELQLMIADCGRLDTEPPPAQGYSIEARLYAEDPAHGWQPQAGVMHTIEVPGVRAQFDSLGQRTGIRLDSGIVDGSTVSIHYDPMLAKVVSYGATRRQAALVLADALVRARLHGLRTNRELLVNVLRHPAFLDGATDTGFFDTHGMAELSTPLADTATLRLSAIAAALADAEHNRASAGVFSSIPSGWRNLASGYQVKTYRDDADTEHRVEYRFTRTGLALPGDPVVQLVSADVDQVVLAQDGVAHGFTVARHGPDVYVDSARGPVHLVALSRFPEPSSAVEQGSLVAPMPGNVIRIGAEVGDTVTAGQPLIWLEAMKMEHTIAAPADGVLTHVSVNTGQQVEVGAILARVEAPQNGPAEGDSP
Protein: Nuclear transcription factor Y subunit beta (CAAT box DNA-binding protein subunit B) (Nuclear transcription factor Y subunit B) (F8VSL3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNLMDGDSSTTDASQLGISADYIGGSHYVIQPHDDTEDSMNDHEDTNGSKESFREQDIYLPIANVARIMKNAIPQTGKIAKDAKECVQECVSEFISFITSEASERCHQEKRKTINGEDILFAMSTLGFDSYVEPLKLYLQKFREAMKGEKGIGGAVTATDGLSEELTEEAFTNQLPAGLITTDGQQQNVMVYTTSYQQISGVQQIQFS
Protein: Uncharacterized protein (Q38BS2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Trans-sialidase
- Ribosomal protein S23 mitochondrial conserved domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Rhodanese domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MRCSCAFLDKSVFAAKRRVIVPIHPTPNFPAHFIKSAFTTDPLKEKQKARFSSGGEAMREVQDIPKNLEGERSRRDLASRGDTEFQALVEFIEGASYDQLISGRRFKKVYDVLSENDDMFIWLCHTAMSVLNPGDMRSRLIYNHLRILAESVASGEMTQRTAFRFFESAVRSPAYREIAKRQLEGGAATRLAGISAAADVMRRMGLTRRPMSSYFELYQRIVERSEAMTPWGFPPLFQFEERLSLEPRLKFFSRASQQSLERRRRGHVMTPHTALHGRRIFWIPPTWNRAGRFLGPHVTLYPGMTPD
Protein: GEM-like protein 5 (Q9LYV6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- RING-H2 finger protein ATL11
- HVA22-like protein b
- Probable pectate lyase 18
- Putative defensin-like protein 72
Sequence:
MTGSQEDQPKIIIDQEQPKTLETEHQPEPSSSSPDQKKWGTHVMGAPAAPVAHPDNQQAAAWVAGDNQQTQYQPYVIYSPVEHPTTNNPLEPVIGMFHTWSRKAETVARNLWHNLKTGPSMSETAWGKVNLTAKAITKGGFESLFRQIFGTEPNETLKKTFACYLSTTTGPVAGTVYLSNARVAFCSDRPLYFTAPSGQESWSYYRVVVPLANVATVNPVVVKETPPEKYIQLTTVDGHDFWFMGFVNYEKATHHLLTSVSDFQTAHGSVSG
Protein: Prostaglandin E2 receptor EP4 subtype (PGE receptor EP4 subtype) (PGE2 receptor EP4 subtype) (Prostanoid EP4 receptor) (P43114)
Organism: Rattus norvegicus (Rat)
Function: Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(s) proteins that stimulate adenylate cyclase. Has a relaxing effect on smooth muscle. May play an important role in regulating renal hemodynamics, intestinal epithelial transport, adrenal aldosterone secretion, and uterine function.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Prostaglandin E2 receptor EP2 subtype
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Neuroendocrine secretory protein 55
- Prostaglandin E synthase
- Guanine nucleotide-binding protein G
- Beta-arrestin-1
Sequence:
MSIPGVNASFSSTPERLNSPVTIPAVMFIFGVVGNLVAIVVLCKSRKEQKETTFYTLVCGLAVTDLLGTLLVSPVTIATYMKGQWPGDQALCDYSTFILLFFGLSGLSIICAMSIERYLAINHAYFYSHYVDKRLAGLTLFAVYASNVLFCALPNMGLGRSERQYPGTWCFIDWTTNVTAYAAFSYMYAGFSSFLILATVLCNVLVCGALLRMLRQFMRRTSLGTEQHHAAAAAAVASVACRGHAAASPALQRLSDFRRRRSFRRIAGAEIQMVILLIATSLVVLICSIPLVVRVFINQLYQPSVVKDISRNPDLQAIRIASVNPILDPWIYILLRKTVLSKAIEKIKCLFCRIGGSGRDGSAQHCSESRRTSSAMSGHSRSFLSRELREISSTSHTLLYLPDLTESSLGGKNLLPGTHGMGLTQADTTSLRTLRISETSDSSQGQDSESVLLVDEVSGSQREEPASKGNSLQVTFPSETLKLSEKCI
Protein: Nuclear factor 1 (A0A1B0GWI9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU000690}.
Interaction partners:
Sequence:
XAMDEFHPFIEALLPHVRAIAYTWFNLQARKRKYFKKHEKRMSKDEERAVKDELLSEKPEIKQKWASRLLAKLRKDIRQEYREDFVLTVTGKKHPCCVLSNPDQKGKIRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLMKSPHCTNPALCVQPHHITVSVKELDLFLAYYVQEQDSGQSGSPSHNDPAKNPPGYLEDSFVKSGVFNVSELVRVSRTPITQGTGVNFPIGEIPSQPYYHDMNSGVNLQRSLSSPPSSKRPKTISIDENMEPSPTGDFYPSPSSPAAGSRTWHERDQDMSSPTTMKKPEKPLFSSASPQDSSPRLSTFPQHHHPGIPGVAHSVISTRTPPPPSPLPFPTQAILPPAPSSYFSHPTIRYPPHLNPQDTLKNYVPSYDPSSPQTSQLRICDWTMNQNGRHLYPSTSEDTLGITWQSPGTWASLVPFQVSNRTPILPANVQNYGLNIIGEPFLQAETSN
Protein: Glutathione hydrolase light chain 2 (Gamma-glutamyltransferase light chain 2) (Gamma-glutamyltransferase-like protein 4) (Q14390)
Organism: Homo sapiens (Human)
Interaction partners:
- Glutathione hydrolase 6
Sequence:
MTSEFFAAQLRAQISDDTTHPISYYKPEFYTPVDGGTAHLSVVAEDGSAVSATSTINLYFGSKVRSPVSEILFNDEMDDFSSPNITNEFGVPPSPANFIQPGKQPLSSMCPTIMVGQDGQPPSHADHTPMPQAIIYNLWFGYDVKRAVEEPRLHNQLLPNVTTVERNIDQAVTAALETRHHHTQIASTFIAVVQAIVRTAGGWAAASDSRKGGEPAGY
Protein: Probable sugar phosphate/phosphate translocator At2g25520 (Q9SKJ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Transmembrane protein
- Histone-lysine N-methyltransferase SETD1B-like protein
- Protein NUCLEAR FUSION DEFECTIVE 4
- Serine/threonine-protein kinase PCRK2
- Metal tolerance protein C1
- Major facilitator superfamily protein
- Thioredoxin H1
Sequence:
MGKGRALSDGVIKKIILSYTYVAIWIFLSFTVIVYNKYILDKKMYNWPFPITLTMIHMGFCSSLAVILIKVFKVVEPVSMSRETYLRSVVPIGALYSLSLWLSNSAYIYLSVSFIQMLKALMPVAVYSIGVLLKKETFKSQTMTNMLSISFGVAIAAYGEAKFDGWGVFLQLGAVAFEATRLVLIQILLTSKGINLNPITSLYYVAPCCLVFLSVPWIFVEFPVLRDTSSFHFDFVIFGTNSVCAFALNLAVFLLVGKTSALTMNVAGVVKDWLLIAFSWSVIKDTVTPINLFGYGLAFLGVGYYNHCKLQALKAKDAQKKVQASDDEAGKLLEERESEAKRNETQD
Protein: SRP-independent targeting protein 1 (Q04007)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions in the SND pathway, a SRP (signal recognition particle) and GET (guided entry of tail-anchored proteins) independent pathway for targeting a broad range of substrate proteins to the endoplasmic reticulum. SND functions in parallel to GET in targeting proteins with downstream hydrophobic motifs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:27905431}.
Interaction partners:
- SRP-independent targeting protein 2
- Protein phosphatase 2C homolog 4
- SRP-independent targeting protein 3
- Uncharacterized protein YMR265C
Sequence:
MDTVGTDAAAASINERRFAQSTSPKVSVKSQDSLFLITYSNMQQTVVQASLADRYPSLKKLNILLYIDIPTIDYYNDEMTHNKLSRLNKRFKLHRLRNSIAQSFSNTSTAEDNDKFWEELKSLISSRSTPENKFDLNVLVSSSGSLRYVETIRFLVEKLFNSFKDLYVQKKLNLCFQINVSPTSLKWFSTFLNAELLNLKIINWQNIGSFTKTIQNSKSLPFKEYYTKLNEKFTGSNQSNGSMQDQTVLDSIVIVTNSTGVKALLTLLSDHPLTSLISQESIKALHEYSDAVNEDKGDDQSNTSLKRNSSSLLNFQNSVLTSNKDKSVRIRSLSINRKSNRAHMFKTNESITTIPSTSINNLIGQESNLRKQPSGTALHLQSHLHPHSRSQSYSSSNMSRSPSPFPYGKTPSNDELVYDELNNQINEVQDRAKNEEIVLYNNNNYDDYTKERGEQEQDRTSYADEYGFNYDDEEGGNEDNYDDDEDDDDDDDDDDESDDEGLSFYAPSILSRSGSSTDVLSSGIDSMAKNSKETRGRFRSLSLMDPALQKPFNQKFPNSQQPDSAGASSPKRSTSSNHFTNVYVHDGDFDGTDTINNKKNLSSATLIKRKSLMNRNLAPSISNGLIPPEFISRISTPSTSASSSNSSLNDMSTVSNAFSKLLNDTSKKQKFLNSPIPQHTQQASPLLMRNNSNSNLLFEKNLINKSFEELRRQPSVNLFSTLMNGNMEKNGLALNFKSRTPTDALMANSIKNSNNSSHRLLNLEEEDQIMSGSLPKEREDDNDSTNSTIVPNHPDNDNYNDNDNDNNTGINSNNFNLNLYDDNDSAGFTDVTTEGVKYSNSNSTVTKPVYKKAVTLDLYGEDDMDNMGGWVLGGNAR
Protein: Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial (EC 1.14.13.-) (2-methoxy-6-polyprenolphenol 4-hydroxylase) (EC 1.14.15.-) (O01884)
Organism: Caenorhabditis elegans
Function: FAD-dependent monooxygenase required for the C5-ring hydroxylation during ubiquinone biosynthesis. Catalyzes the hydroxylation of 3-polyprenyl-4-hydroxybenzoic acid to 3-polyprenyl-4,5-dihydroxybenzoic acid. The electrons required for the hydroxylation reaction may be funneled indirectly from NADPH via a ferredoxin/ferredoxin reductase system to COQ6.
Subcellular location: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03193}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03193}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03193}.
Interaction partners:
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Ubiquinone biosynthesis protein coq-4, mitochondrial
- Atypical kinase coq-8, mitochondrial
- All trans-polyprenyl-diphosphate synthase PDSS1
- Kynureninase
- 2Fe-2S ferredoxin-type domain-containing protein
- Phytoene synthase
- Cholesterol 7-desaturase
Sequence:
MKLPGGTIICARNASSYYDTVIVGGGMVGNAMACSLGANKSFQSKSVLLLDAGRSPSLASFKPGAPFNNRVVATSPTSIDTFKKLGVWDQINSHRTKKVNRLFVFDSCSTSEIEFERGQQEEVAFIIENDLIVGSLYEKLAEYKNVDVKTGAKVEDCSIPNALENMATIKLENGDVIETSLLIGADGVNSKVRHASNLDYTTFNYNQHGLVAIVNIETANGKNETAWQRFTTLGPVALLPLSDTVSGLTWSTSPEEAQRLKQLPSDQFVDELNSALFSQNNQIPLVNQTIFALNRMNPFRTETFGRKAEGTTPPHVITVQDKSRASFPLGFGNAHSYITTRCALIGDAAHRMHPLAGQGVNLGWSDVQILDKVLGDAVREGADIGSITYLREYDSAAQKHNLPVMVSVDLLNRLYRTDAPAIVAARAFGLNAFNSLGPVKNFLMNYLSAHR
Protein: Soluble guanylate cyclase gcy-33 (EC 4.6.1.2) (P90895)
Organism: Caenorhabditis elegans
Function: Synthesizes cyclic GMP (cGMP) from GTP (By similarity). May be involved in sensitivity to quinine by regulating egl-4 activity through the production of cGMP.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Inosine triphosphate pyrophosphatase
- Bis
- FMRF-Like Peptide
- Cyclic nucleotide-binding domain-containing protein
- Soluble guanylate cyclase gcy-31
- GTP cyclohydrolase 1
- Cyclic nucleotide-gated channel
- Probable 3',5'-cyclic phosphodiesterase pde-5
- Probable 3',5'-cyclic phosphodiesterase pde-2
- FMRFamide-like neuropeptides 19
Sequence:
MYGLVIEGVRFMIQENWGPQVLLQVQKLTSLSEKSVSTHDQYSEHVVPQMFKAIHEITGTPYEQIGVLAGRFFVQFLIRNGYGDLMNVMGRRFSDFIKGLDNIHEYFRFSYPKLRAPSFYCKSESEDGLILHYRSRRTGYLSYVIGQLVELARVFYQLDIGIQVLKKKEKGRFTFVVLKISFDNVGLGQDLKLKERVKNLNEYLPVDTKSFLQMFPFHIAFNKKLEILMAGQGLLNLMPNIQGLLMTDVFDLQRPCIKFTAEGIMVHQNCVFQIESLHPVVKQTEENITVQINDITEDKVSLEKKTVMDNEYESLPYVTLRGPITVLKSSETFLLLATCVVDTLDTMFKMGLYLNDFGESDCNREIIMATIQKSDTLKTMLENEKRRSEVLTEMTREISEAKKTARTLLTQMMPYEVAQTMMRSGSVDHCEAFECVSIGFIRVCDFSKISLFIEAFEVVNLLNTIYSHLDSIVDTHGVYKVETIGESYMISAGCPYRDDYDAEMVSDCCLEMVSHIKSFEYQSHDAVKKVLIKCGIFTGPVVGGVVGVRTPRYCLFGDTVNTASRMESSNQTPMTIQIGQRTKDRVEKQASGAFRIKPKGNVFVKGKGDMRVYEIEKKKGRARYKKSDPLRKKMVAEKKEAEELLDEDNEGHRSSALSRMSLGESIDSSSSRRGSLSGSQLELNKTIAQTIELTSKASAALDLNMQDENNRPPTWSASHSQDIRKPRKTESKITLNSRLSSSDLAVSRVETSKDSDGETPRPTSSELKEVNRIREEALAQEKEEERTTKEENQKIEEVGEDHVSEATSLLDSEVSHGDNNISFSQMPSDSIPHEDRTSLPSATPSEIGDAISKKKLEKEDSNSSMSSLDERTTVSAKPTTTRRLLNQKDLEKEKKRSSMAGSSVTSSSAHSHSIRSKKDTRDKSRCKCEDIRADNKLKTKVCSIM