wanglab/gogpt-training-data huggingface dataset:
Protein: Sulfotransferase 1E1 (ST1E1) (EC 2.8.2.4) (EST-1) (Estrogen sulfotransferase) (Sulfotransferase, estrogen-preferring) (P49888)
Organism: Homo sapiens (Human)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of estradiol and estrone. Is a key enzyme in estrogen homeostasis, the sulfation of estrogens leads to their inactivation. Also sulfates dehydroepiandrosterone (DHEA), pregnenolone, (24S)-hydroxycholesterol and xenobiotic compounds like ethinylestradiol, equalenin, diethyl stilbesterol and 1-naphthol at significantly lower efficiency. Does not sulfonate cortisol, testosterone and dopamine. May play a role in gut microbiota-host metabolic interaction. O-sulfonates 4-ethylphenol (4-EP), a dietary tyrosine-derived metabolite produced by gut bacteria. The product 4-EPS crosses the blood-brain barrier and may negatively regulate oligodendrocyte maturation and myelination, affecting the functional connectivity of different brain regions associated with the limbic system.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:11006110}.
Interaction partners:
- Telomerase reverse transcriptase
- 17-beta-hydroxysteroid dehydrogenase type 1
- UDP-glucuronosyltransferase 1A6
- 17-beta-hydroxysteroid dehydrogenase type 2
- Aromatase
- UDP-glucuronosyltransferase 1A10
- UDP-glucuronosyltransferase 1A4
- UDP-glucuronosyltransferase 1A8
- UDP-glucuronosyltransferase 1A1
- UDP-glucuronosyltransferase 1A7
Sequence:
MNSELDYYEKFEEVHGILMYKDFVKYWDNVEAFQARPDDLVIATYPKSGTTWVSEIVYMIYKEGDVEKCKEDVIFNRIPFLECRKENLMNGVKQLDEMNSPRIVKTHLPPELLPASFWEKDCKIIYLCRNAKDVAVSFYYFFLMVAGHPNPGSFPEFVEKFMQGQVPYGSWYKHVKSWWEKGKSPRVLFLFYEDLKEDIRKEVIKLIHFLERKPSEELVDRIIHHTSFQEMKNNPSTNYTTLPDEIMNQKLSPFMRKGITGDWKNHFTVALNEKFDKHYEQQMKESTLKFRTEI
Protein: Thioredoxin domain-containing protein (Q582J3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Thioredoxin
Sequence:
MISLHLSSHSLMHVLLSFLLLCSGVVMGYYADVDYEVPSRVVQLTDATFDTIVMDPTKDVFVLYCVTWSRHCRSAVKLWADLSISQFKRPTADTFVAALIDAEAFPETAKRMGVKSYPTMLFYTRLEKATPLEYNGQGLLPLLDSFVFQNS
Protein: Spn43Ac (Q6V6U9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
RFSSELFKEIIKSQSQQNVVFSPFSVHALLALIYGASDGKTFRELQKAGEFSKNAMAVAQDFESVIKYKKHLEGADLTLATKVYYNRELGGVNHSYDEYAKFYFSAGTEAVDMQNAKDTAAKINAWVMDTTRNKIRDLVTPTDVDPQTQALLVNAVYFQGRWEHEFATMDTSPYDFQHTNGRISKVAMMFNDDVYGLAELPELGATALELAYKDSATSMLILLPNETTGLGKMLQQLSRPEFDLNRVAHRLRRQSVAVRLPKFQFEFEQDMTEPLKNLGVHQMFTPNSQVTKLMDQPVRVSKILQKAYINVGEAGTEASAASYAKFVPLSLPPKPTEFVANRPFVFAVRTPSSVLL
Protein: Dihydroorotase (Q9HT33)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Aspartate carbamoyltransferase catalytic subunit
- Carbamoyl phosphate synthase large chain
- Carbonate dehydratase
- Carbamoyl phosphate synthase small chain
- GTP cyclohydrolase FolE2
- Dihydroorotate dehydrogenase
- Dihydroorotase-like protein
- Dihydroorotase
- Orotidine 5'-phosphate decarboxylase
- N-acetylmuramoyl-L-alanine amidase AmiC
Sequence:
MQSLLIRNARMVNEGQVREGDLLVRHGRIERIAGCLENCGASREIDAAGRYLLPGMIDDQVHFREPGYPQKGSIASESRAAVAGGITSFMDMPNTRPATLSLEALAEKKRLAAAHSVANYGFHFGVSRDNLDTVAALDPREVAAVKVFMGASTGDMLVDDLPTLERLFASVPTLLLSHCEDTPRIEANLARWRQRFGERIPAAAHPRIRDAEACYRSTALAVELAQRHGTLLHVLHLSTARELALFEDKPLCQKRITAEVCVHHLLFDDSDYARLGHLLKCNPAIKSREDRDALRRALAGNRLDVIGTDHAPHAWAEKQQAYPQAPAGLPLVQHALPALLELVREGWLSLATLVAKTSHRVAELFAIADRGFLREGYWADLVLVSELEHPALASAMPLLSRCNWTPFRHRAFHHRIDTTIVSGQLAWHAGRLSDDCQGLPLRFSR
Protein: Cryptic beta-glucoside bgl operon antiterminator (P11989)
Organism: Escherichia coli (strain K12)
Function: Mediates the positive regulation of the beta-glucoside (bgl) operon by functioning as a transcriptional antiterminator. This is an RNA-binding protein that recognizes a specific sequence located just upstream of two termination sites within the operon.
Interaction partners:
- PTS system beta-glucoside-specific EIIBCA component
- 6-phospho-beta-glucosidase BglB
- PTS system arbutin-, cellobiose-, and salicin-specific EIIBC component
- 6-phospho-beta-glucosidase BglA
- Cryptic outer membrane porin BglH
- 6-phospho-beta-glucosidase AscB
- PTS system N,N'-diacetylchitobiose-specific EIIB component
- PTS system N-acetylmuramic acid-specific EIIBC component
- PTS system glucose-specific EIICB component
- PTS system N,N'-diacetylchitobiose-specific EIIC component
Sequence:
MNMQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRIISLAQERLGKLQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHLVSAQMSGNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQAWQCAERIAIFIGLQYQRKISPAEIMFLAINIERVRKEH
Protein: Nyctalopin (Q9GZU5)
Organism: Homo sapiens (Human)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Transient receptor potential cation channel subfamily M member 1
- Voltage-dependent L-type calcium channel subunit alpha-1F
- Metabotropic glutamate receptor 6
- Calcium-binding protein 4
- Probable G-protein coupled receptor 179
- Long-wave-sensitive opsin 1
- FERM domain-containing protein 7
- X-linked retinitis pigmentosa GTPase regulator
Sequence:
MLVLLLHAVVLGLPSAWAVGACARACPAACACSTVERGCSVRCDRAGLLRVPAELPCEAVSIDLDRNGLRFLGERAFGTLPSLRRLSLRHNNLSFITPGAFKGLPRLAELRLAHNGDLRYLHARTFAALSRLRRLDLAACRLFSVPERLLAELPALRELAAFDNLFRRVPGALRGLANLTHAHLERGRIEAVASSSLQGLRRLRSLSLQANRVRAVHAGAFGDCGVLEHLLLNDNLLAELPADAFRGLRRLRTLNLGGNALDRVARAWFADLAELELLYLDRNSIAFVEEGAFQNLSGLLALHLNGNRLTVLAWVAFQPGFFLGRLFLFRNPWCCDCRLEWLRDWMEGSGRVTDVPCASPGSVAGLDLSQVTFGRSSDGLCVDPEELNLTTSSPGPSPEPAATTVSRFSSLLSKLLAPRVPVEEAANTTGGLANASLSDSLSSRGVGGAGRQPWFLLASCLLPSVAQHVVFGLQMD
Protein: Probable PhiRv1 phage protein (O06608)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable PhiRv1 integrase
- Uncharacterized protein Rv1583c
- Possible PhiRv1 phage protein
Sequence:
MADIPYGTDYPDAPWIDRDGHVLIDDGGKPTQVHRGQARIAYRLAERYQDKLLHVAGIGWHSWDGRRWAADDRGEAKRAVLAELRQALSDSLNDKELRADVRKCESASGVAGVLDLAAALVPFAATVADLDSDPHLLNVANGTLDLHTLKLRPHAPADRITKICRGAYQSDTESPLWQAFLTRVLPDEGVRGFVQRLAGVGLLGTVREHVLAILIGVGANGKSVFDKAIRYALGDYACTAEPDLFMHRENAHPTGEMDLRGVRWVAVSESEKDRRLAESTIKRLTGGDTIRARKMRQDFVEFTPSHTPLLITNHLPRVPGDDTAIWRRIRVVPFEVVIPADEQDRELDARLQLEADSILSWAVAGWSDYQRIGLSQPDAVLAATSNYREDSDTIKRFIDDECVTSSPVLKATTTHLFEAWQRWRVQEGVPEISRKAFGQSLDTHGYPVTDKARDGRWRAGIAVRGADDFDD
Protein: Plexus (Q9U8Q0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEKAKAYIKNELRGGSQQSEPATTPNPTSPASAPGTPQATRHSYPPVELMPSPGAAAHRSARTPGEQYHFGYQAHPAHHYHSGAKSTGRASAPPDNHHVPMTICFVCGGHGSFEPQPLRIRHNAERPSESYFPFLEGHEPPNGVPGVVPGQEYVWACMLCFRSLNEQWDAYERQKKPLLQRIYHMKRVDGKGYIGADVATQSEYAAQVLGLSAEHLTQNGLVDAHGDPYALARHYSPQQPSHHHHSTSRNASPSPNPIAAGGGGGEFYPRNSTPSSNHNRYLSRPQSRDMPVASPTSRPPSEPPAMKSAGYAQQKFKLSPAPPAGYQGQAPYHPAQYQQLQQQTAAYHLLQQQVNAGGGATESAHYKGNPYGALPSPGSGPLGPRAASTLEDDNATVLDLRNSSNSSAPPGPRHVGSTASSVSQPSQPQSEVGILDLSMPDKNSITEVCYVCGDEQRRGSLIELSTVKPRETGRPGPSVPYFPLFNEQHPRPARSRPKDPRGMIQACLPCYEDLMQQWNVHQASHKPESERSYLLRKRSTPAAERTTFVCYTCGTDTPSSQLRLVYCCPNAEREPYYPFIKTMKVYKNASPISPQGMVQVCSTCNEKHSGLAEGGPPPASSSIHSAVGGGSPSAGHSLESNSAMYSTSGAITGNSGAQFGGRNSPSEKSLANSDSMSNVRFRPYETNSNNSNSNTARDLKQIRRNDSRPNSPSSSQGAIENGHGQYPCSICKVLCPSNKMDWLSTSAEHMNSHAMHFPCLKANAVTNNNNNNNNTNNNNELNSNRVLACKDCKDYLASQWETMDAERVPLEHRRYNIPSPMLTSSSPNGSRHGAMSINTPPSTPSISSSTPASTSIYCYLCGLHSDLTLARVLYASKEGSRPYFPLLLKHNSLPNAEQLRNNSALVCTFCYHSMLNQWRKYEAQSPSVNPADRKYNWHDYNCHLCGITTYRKRVRALPVNEFPFVKHQKSDDGLLLENGEYAVVCLDCYESLRQQASQHDRFGVPISRRAYNWVPQPPPPEDSPESAVARLPCGERSDRIHINNALRPVPGKKTTSPKQYDKSKEVPPKAGQKRPATSPAPHIPVPHHLQTPPGGGAGGLPGSSVANSPIPSSAGGNALMNHALPNNHIGTPSPQQQHQHQQHQQQQQQQQHQAQQQAQQQAVAAAVQQQLAAGVGLPPGAIGAASASSRGSFAAALRTLAKQADIKEEDVGGDRSVPTSGAGGPPPSSSGPGSLNSVAGRVGSERPGEDRVSSNKKRSPPSPQPPEKIARLSHTPQTASLQPELLARSGFQPYRSDERLMHPAGAFPLEAYSHFAGLPGIPPAFLNPAGLPYTEQLYLEHRYQLFRAAGAHPSHPHAAALYPQMASPYSHLYSMMPGAALGISPAMHDRMKLEEEHRARLAREEEREREIQREKERELREQREKEQREKEQREKEQREREQREKEQREKEARERKLRDEERERERERQQLLTASHHYSNQLYSPLNRNLLGSMIPHLNMSLRGPPGALHGLPGMSHYHAAAANAQRQSPHGAMGLNLGMAGLPGVPPLGGHGPNLQHHLQQAAMGLAHPGAAGLTHPGFSAAALGLGAHPHSLNLSHPHMSPHHPASLAHQLPPHTSSAGGGGLSNSIPVTASSSLSASSPHTSLNLTSSVKLSADQVPTSTPSGGVSGSGMPPTTSSSHIPNMGHYYHHGHLAAMHAAAAAASGMTPTAAHQQQPLSLPSSPKITPPITPSSSANGGRAGGSPHAMRHHIAAAVAAAAQQSAMIDKAATPVTHEPTTLDLTGSNSNSSNQAPSNASSGQPTNHEVNGAESNGASQTESKEHLAIKEDGHKSSPPPVALEKKPATPNAAADKPIHPDSSPENSSRRSASPQSDANNSLPAVSVTAAASGKCKEETPKILDSDTTATTKTDIEEEKQRARLSVSPTPTAPKIMVASPDTVSTSGGVTSTTSGTTPPPVVSSSTSSAGKAPALTSDEVSTSAATSAAEPTR
Protein: Matrix metalloproteinase 1, isoform H (EC 3.4.24.-) (A0A0B4JDA7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTNCQSSVFIVVGTLFSIMAAAQSAPVSTTTQAEIYLSQFGYLPASARNPASSGLHDQRTWVSAIEEFQSFAGLNITGELDAETMKLMSLPRCGVRDRVGTGDSRSKRYALQGSRWRVKNLTYKISKYPKRLKRVDVDAEIGRAFAVWSEDTDLTFTRKTSGPVHIEIKFVESEHGDGDAFDGQGGTLAHAFFPVFGGDAHFDDAELWTIGSPRGTNLFQVAAHEFGHSLGLSHSDQSSALMAPFYRGFEPVFKLDEDDKAAIQSLYGRKTNQLRPTNVYPATTQRPYSPPKVPLDDSICKDSKVDTLFNSAQGETYAFKGDKYYKLTTDSVEEGYPQLISKGWPGLPGNIDAAFTYKNGKTYFFKGTQYWRYQGRQMDGVYPKEISEGFTGIPDHLDAAMVWGGNGKIYFFKGSKFWRFDPAKRPPVKASYPKPISNWEGVPNNLDAALKYTNGYTYFFKGDKYYRFHDARFAVDSATPPFPRPTAHWWFGCKNTPSSTAVGDHQSNDEPIVPEVAERTGNGAMSQSKLTSSSAVSTVITTILMCLVSKLIVS
Protein: Rifin (Q8I082)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKVHYINILLFELPLNILIYNQRNHNSTTPHHPPNTRLLCECEWYAPSNYDNDPQMKAVMQDFDRQTSQRFEEYNERLLENKQKCKEQCDKEIQKIILKDKLEKELAEKFVTLQTDIQSDAIPTCVCEKSVADKVEKTCLKCGGVLGGGVTPAWGLLSGIVYTGWKAAALAAAKELAEKAGAAEGASQGAAAGAVEVIKSIKTTFGIESLGVNPLQSLFNAENYMNAKFISESIHSEFISSGCGAILKPPNKPICTSVYKGIEATSRGKGVKPIEFIGKKVETMVSQAKDVAEATKAQVTSETTATLTDLKTGVVQTTYMGYQTVIIASIVAILLIVLVMIIIYLILRYRRKKKMKKKLQYIKLLEE
Protein: GRIP and coiled-coil domain containing 2 (B8ZZW2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MMLIQKAKSRCTELEKEIEELRSKPVTEGTGDIIKALTERLDALLLEKAETEQQCLSLKKENIKMKQEVEDSVTKMGDAHKELEQSHINYVKEIENLKNELMAVRSKYSEDKANLQKQLEEAMNTQLELSEQLKFQNNSEDNVKKLQEEIEKIRPGFEEQILYLQKQLDATTDEKKETVTQLQNIIEANSQHYQKNINSLQEELLQLKAIHQEEVKELMCQIEASAKEHEAEINKLNELKENLVKQCEASEKNIQKKYECELENLRKATSNANQDNQICSILLQENTFVEQVVNEKVKHLEDTLKELESQHSILKDEVTYMNNLKLKLEMDAQHIKDEFFHEREDLEFKINELLLAKEEQGCVIEKLKSELAGLNKQFCYTVEQHNREVQSLKEQHQKEISELNETFLSDSEKEKLTLMFEIQGLKEQCENLQQEKQEAILNYESLREIMEILQTELGESAGKISQEFESMKQQQASDVHELQQKLRTAFTEKDALLETVNRLQGENEKLLSQQELVPELENTIKNLQEKNGVYLLSLSQRDTMLKELEGKINSLTEEKDDFINKLKNSHEEMDNFHKKCEREERLILELGKKVEQTIQYNSELEQKVNELTGGLEETLKEKDQNDQKLEKLMVQMKVLSEDKEVLSAEVKSLYEENNKLSSEKKQLSRDLEVFLSQKEDVILKEHITQLEKKLQLMVEEQDNLNKLLENEQVQKLFVKTQLYGFLKEMGSEVSEDSEEKDVVNVLQAVGESLAKINEEKCNLAFQRDEKVLELEKEIKCLQEESVVQCEELKSLLRDYEQEKVLLRKELEEIQSEKEALQSDLLEMKNANEKTRLENQNLLIQVEEVSQTCSKSEIHNEKEKCFIKEHENLKPLLEQKELRDRRAELILLKDSLAKSPSVKNDPLSSVKELEEKI
Protein: Calcium and integrin-binding family member 2 (Q9W2Q5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9Z309}.
Interaction partners:
- Myosin-VIIa
- Dyschronic, isoform G
- Serine/threonine-protein phosphatase 2B catalytic subunit 2
- Serine/threonine-protein phosphatase 2B catalytic subunit 1
- Myosin 28B1, isoform B
- Serine/threonine-protein phosphatase 4 regulatory subunit 2
- Serine/threonine-protein phosphatase PP2A
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Serine/threonine-protein phosphatase 2B catalytic subunit 3
- Serine/threonine-protein phosphatase
Sequence:
MGNKVVTFTEQELDDYQDCTFFTRKEILRVHKRFRELRPDLVPRQMTEGQASSVKVPCECIEKMPELRENPFRRRICEAFSRDGQGNLSFEDFLDALSVFSEQAPRDIKVFYAFKIYDFDQDGFIGHADLMSCLTTMTKNELSPEEHQQIADKVIEEADVDGDGKLSILEFEHVILRAPDFLSTFHIRI
Protein: Colipase (G1MPW1)
Organism: Meleagris gallopavo (Wild turkey)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MVLTLRLLLATLLIALALGAPSERGLIFNLDTGELCVQSAQCKSGCCQRDSGLSLARCSLKAAETQDCSRKSLYGVYYKCPCESGLSCDADWSIVGSITNTDYGVCYDKRDPTTSR
Protein: ADP/ATP translocase (ADP,ATP carrier protein) (Q57VM4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU368008}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU368008}.
Interaction partners:
Sequence:
MVGGDGEEPGLQRQAKRALGDPLPLDNEMESEAPNDFSNDPSDNISVQSLQVACVQKCCLCTIVAPLDRIKFVMQCQKELQRTGVLDRTFRSSWHCFRCIHSIEGIRSFWRGNLVQVGSLLPVTAAHMLLGGPMQMWVYNNFPRGFPFGHSAATYASILCGALAVSAVSYPLEFARFRLAVDLRRSPCDLYDYRHSLAFFAQSVFSEAPHLLYAGFGLYVTGSIIYGVMYTGLTQQVLSRLPSEPGGYTATVVQVGAGVGVSAVSTLGLHPLDTMRRRMMIAVTMDGLRYASARHCFHHILSTEGIAGFYRGAAFTMVRMVYISSLYMWFLPAA
Protein: Charged multivesicular body protein 3 (Chromatin-modifying protein 3) (Neuroendocrine differentiation factor) (Vacuolar protein sorting-associated protein 24) (hVps24) (Q9Y3E7)
Organism: Homo sapiens (Human)
Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Selectively binds to phosphatidylinositol 3,5-bisphosphate PtdIns(3,5)P2 and PtdIns(3,4)P2 in preference to other phosphoinositides tested. Involved in late stages of cytokinesis. Plays a role in endosomal sorting/trafficking of EGF receptor. Isoform 2 prevents stress-mediated cell death and accumulation of reactive oxygen species when expressed in yeast cells.
Subcellular location: Cytoplasm, cytosol. Membrane; Lipid-anchor. Endosome. Late endosome membrane {ECO:0000305}. Note=Localizes to the midbody of dividing cells.
Interaction partners:
- Charged multivesicular body protein 4a
- Charged multivesicular body protein 6
- Charged multivesicular body protein 2a
- Charged multivesicular body protein 1b
- Charged multivesicular body protein 4b
- STAM-binding protein
- Charged multivesicular body protein 1a
- Charged multivesicular body protein 5
- Charged multivesicular body protein 2b
- Vacuolar protein-sorting-associated protein 25
Sequence:
MGLFGKTQEKPPKELVNEWSLKIRKEMRVVDRQIRDIQREEEKVKRSVKDAAKKGQKDVCIVLAKEMIRSRKAVSKLYASKAHMNSVLMGMKNQLAVLRVAGSLQKSTEVMKAMQSLVKIPEIQATMRELSKEMMKAGIIEEMLEDTFESMDDQEEMEEEAEMEIDRILFEITAGALGKAPSKVTDALPEPEPPGAMAASEDEEEEEEALEAMQSRLATLRS
Protein: Inositol monophosphatase 1 (IMP 1) (IMPase 1) (EC 3.1.3.25) (D-galactose 1-phosphate phosphatase) (EC 3.1.3.94) (Inositol-1(or 4)-monophosphatase 1) (Lithium-sensitive myo-inositol monophosphatase A1) (O55023)
Organism: Mus musculus (Mouse)
Function: Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides and has been implicated as the pharmacological target for lithium action in brain. Has broad substrate specificity and can use myo-inositol monophosphates, myo-inositol 1,3-diphosphate, myo-inositol 1,4-diphosphate, scyllo-inositol-phosphate, D-galactose 1-phosphate, glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P29218}.
Interaction partners:
- Inositol-3-phosphate synthase 1
- Inositol monophosphatase 2
- Inositol oxygenase
- Inositol polyphosphate 1-phosphatase
- Golgi-resident adenosine 3',5'-bisphosphate 3'-phosphatase
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Inositol polyphosphate-4-phosphatase type I A
- Myotubularin
- Type II inositol 3,4-bisphosphate 4-phosphatase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1
Sequence:
MADPWQECMDYAVILARQAGEMIREALKNEMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPCHSFIGEESVAAGEKTVFTESPTWFIDPIDGTTNFVHRFPFVAVSIGFLVNKEMEFGIVYSCVEDKMYTGRKGKGAFCNGQKLQVSQQEDITKSLLVTELGSSRKPETLRIVLSNMEKLCSIPIHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVTEAGGVLMDVTGGPFDLMSRRIIAANSITLAKRIAKEIEIIPLQRDDES
Protein: Trehalose monomycolate transport factor A (TMM transport factor A) (A0QQF4)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Required for MmpL3-dependent trehalose monomycolate (TMM) transport to the cell wall. Required for growth and cell elongation.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:31239378}; Single-pass membrane protein {ECO:0000255}. Cell septum {ECO:0000269|PubMed:31239378}. Cell tip {ECO:0000269|PubMed:31239378}. Note=Colocalizes with MmpL3 to the cell poles and septa. Trehalose monomycolate (TMM) synthesis is not required for localization to the poles or septa. {ECO:0000269|PubMed:31239378}.
Interaction partners:
- Cysteine desulfurase family protein
- Seven-bladed beta-propeller protein MSMEG_5308
- Dihydroorotate dehydrogenase
- O-acyltransferase WSD1 C-terminal domain-containing protein
- Orotidine 5'-phosphate decarboxylase
- Spou rRNA methylase family protein
- Aspartate carbamoyltransferase catalytic subunit
- Carbamoyl phosphate synthase large chain
- Glycosyl hydrolase family protein 76
- Uncharacterized protein
Sequence:
MVPLWFTLSALCFVGAAVLLYVDIDRRRGLGRRRKSWAKSHGFDYEYESEDLLKRWKRGVMSTVGDVTAKNVVLGQIRGEAVFIFDIEEVATVIALHRKVGTNVVVDLRLKGLKEPRENDIWLLGAIGPRMVYSTNLDAARRACDRRMVTFAHTAPDCAEIMWNEQNWTLVAMPVTSNRAQWDEGLRTVRQFNDLLRVLPPVPQNGSQAALPRRGGSPSRPLAPTPAGRRELPPGRADVPPARGDVSRFAPRPEAGRSDAFRRPPPARNGREASHFQR
Protein: ER membrane protein complex subunit 5 (Killer toxin-resistance protein 27) (P40540)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- ER membrane protein complex subunit 1
- ER membrane protein complex subunit 3
- ER membrane protein complex subunit 2
- ER membrane protein complex subunit 4
- ER membrane protein complex subunit 6
- Endoplasmic reticulum membrane protein complex subunit 10
- Protein SOP4
- GPI mannosyltransferase 2
Sequence:
MSFVSKLLYTVSALVLFHSGFSSYEFHHLLKLNSLNNAQGAISKLPKDIMYETYAGLILFVLAVFTSFEKLQYLPIESNDGKIISQGNYLKEIALNKATNVDNLIGSNPNGEIIFTPSFVDVHMKRKICREWASNTVKKEK
Protein: APC regulator of WNT signaling pathway (A0A2Q2SV78)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MYASLGSGPVAPLPASVPPSVLGSWSTGGSRSCVRQETKSPGGARTSGHWASVWQEVLKQLQGSIEDEAMASSGQIDLLERLKELNLDSSNFPGVKLRSKMSLRSYGSREGSVSSRSGECSPVPMGSFPRRGFVNGSRESTGYLEELEKERSLLLADLDKEEKEKDWYYAQLQNLTKRIDSLPLTENFSLQTDMTRRQLEYEARQIRVAMEEQLGTCQDMEKRAQRSSQNKHETGSHDAERQNEGQGVGEINMATSGNGQGSTTRMDHETASVLSSSSTHSAPRRLTSHLGTKVEMVYSLLSMLGTHDKDDMSRTLLAMSSSQDSCISMRQSGCLPLLIQLLHGNDKDSVLLGNSRGSKEARARASAALHNIIHSQPDDKRGRREIRVLHLLEQIRAYCETCWEWQEAHEPGMDQDKNPMPAPVEHQICPAVCVLMKLSFDEEHRHAMNELGGLQAIAELLQVDCEMYGLTNDHYSITLRRYAGMALTNLTFGDVANKATLCSMKGCMRALVAQLKSESEDLQQVIASVLRNLSWRADVNSKKTLREVGSVKALMECALEVKKESTLKSVLSALWNLSAHCTENKADICAVDGALAFLVGTLTYRSQTNTLAIIESGGGILRNVSSLIATNEDHRQILRENNCLQTLLQHLKSHSLTIVSNACGTLWNLSARNPKDQEALWDMGAVSMLKNLIHSKHKMIAMGSAAALRNLMANRPAKYKDANIMSPGSSLPSLHVRKQKALEAELDAQHLSETFDNIDNLSPKASHRSKQRHKQSLYGDYVFDTNRHDDNRSDNFNTGNMTVLSPYLNTTVLPSSSSSRGSLDSSRSEKDRSLERERGIGLGNYHPATENPGTSSKRGLQISTTAAQIAKVMEEVSAIHTSQEDRSSGSTTELHCVTDERNALRRSSAAHTHSNTYNFTKSENSNRTCSMPYAKLEYKRSSNDSLNSVSSSDGYGKRGQMKPSIESYSEDDESKFCSYGQYPADLAHKIHSANHMDDNDGELDTPINYSLKYSDEQLNSGRQSPSQNERWARPKHIIEDEIKQSEQRQSRNQSTTYPVYTESTDDKHLKFQPHFGQQECVSPYRSRGANGSETNRVGSNHGINQNVSQSLCQEDDYEDDKPTNYSERYSEEEQH
Protein: Spectrin beta chain (A0A8I6AWM3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MTSATEFENVGNQPPYSRINARWDAPDDELDNDSSSARLFERSRIKALADEREVVQKKTFTKWVNSHLARVSCRISDLYKDLRDGRMLIKLLEVLSGEMLPRPTKGKMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLVLGLIWTIILRFQIQDIVVQTQEGRETRSAKDALLLWCQMKTAGYPQVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFDVAERQLGIIPLLDPEDVFTENPDEKSIITYVVAFYHYFSKMKVLAVEGKRVGKVIDHAIETEKMIEKYSGLASDLLTWIEQTISVLNSRKFANSLSGVQQQLQAFSTYRTVEKPPKFQEKGNLEVLLFTIQSRMRANNQKVYTPHDGKLVSDINRAWESLEEAEYQRELALRSELIRQEKLEQLARRFDRKAAMRETWLNENQRLVTQDNFGYDLAAVEAAKKKHEAIETDTAAYEERVKALEDLAQELEKENYHDQKRISARKNNILRLWSYLQELLRSRRQRLEATLALQKLFQDMLHSIDWMDEIKAHILSAEFGKHLLEVEDLLQKHKLMEADIAIQGDKVKTITAATLQFTEGKGYQPCDPQVIQDRVSHLEQCFSELSNMAAGRKAQLEQSKRLWKFFWEMDEAESWIKEKEQIYSSLDYGKDLTSVLILQRKHKAFEDELRGLDAHLKQIFQEAEDMVAQKQFGHPQIETRVKEVSAQWDHLKELAAFRKKDLQDAENFFQFQGDADDLKAWLQDAHRLLSGEDVGQDEGATRALGKKHKEFLEELEESRGVMEHLENQAQGFPEEFRDSPDVTNRLQALRKLYQQVMAQAELRGHKLQEALDLYTVFGESDACELWMTEKGKWLDQMDIPNTLEDLEVVQHRFDILDQEMKTLMAQIDGVNLAANNLVESGHPRSGEVKQYQDRLNKRWQAFQAVVSEQREAVDSALRVNNYCVDCEETSKWIVDKTKVVESTKDLGQDLAGVIAIQRKLSGLERDVLAIRDRVSALERESQYLMESHPDQKEDIGQRQADVEKMWKGLQDALQGQELSLGEASKLQAFLQDLDDFKAWLSMAQKAVASEDMPESLPEAEQLLQQHAAIKEEIDAHKDDYHRVKASGEKVIEGQTDPDYQLLGQRLEGLDTDWDALWRMWESRGNTLTQCLGFQEFQKDAKQAEAILSNQEYTLAHLEPPDSLAAAEAGIRKFEDFLVSMENNRDKVLSPVDSGNMLVSEGNLYSNKIKEKVQLIEDRHMKNNEKAQEVTALLKDNLELQNFLQNCKELTLWINDKLLTSPDISYDEARNLHNKWMKHQAFMAELASHQGWLENIVAEGRQLMAEKPQFTDVVSERLEALHKLWDELQTTTKAKTEQLSAARSSDLRLQTHADLSKWISAMEDQLRSDDLGKDLTTVNRMLVKLKRVEEQVNLRKEELEELFAEAPPLGAEAGDTDMSIEKRFLDLLEPLGRRKKQLELSKAKLQISRDLEDETLWVEERLPLAQSADYGTNLQTVQLFMKKNQTLQNEILGHAPRVEDVLHRGQELVKAAEIDCQDIEERLGHLQSSWDTLREAAAGRLQRLREAHEAQQYYLDAGEAEAWISEQELYVFSDEPPKDEEGAIVMLKRHLRQQRTVEEYGRNIKQLAGRAQSLLSAGHPEGEQIIRLQGQVDKQYAGLKDMAEERRRKLENMYHLFQLKREADDLEQWITEKEMVASSQEMGQDFDHVTMLRDKFRDFARETGAIGQERVDNVNSIIERLIDAGHSEAATIAEWKDGLNDMWADLLELIDTRMQLLAASYDLHRYFYTGTEILGLIDEKHRELPEDVGLDASTAESFHRVHTAFERELHLLGVQVQQFQDVATRLQTAYAGEKADAIQSKEQEVSAAWQALLDACAGRRAQLVDTADKFRFFSMVRDLLSWMESIIRQIETQERPRDVSSVELLLKYHQGIKAEINTRAKNFSTCLELGESLLQRQHQASDEIREKLQQVISRRQEMNDKWEARSDRLHMLLEVCQFSRDASVAEAWLIAQEPYLASRDFGHTVDSVEKLIKRHEAFEKSTASWAERFAALEKPTTLELKERQTPDRPTEEPGPQEEEGETAGEAPQVHHAATERTSPGEERGPWPQDLQPPPLPGHHKDEQEKSVGDERPATEPLFKVLDTPLSEGDEPTTLPAQRDLGHTVQMEGYLGRKHDLEGPNKKASNRSWNNLYCVLRNSQLTFYKDAKNLALGVPYHGEEPLALRHAICEIAVNYKKKKHVFKLRLSNGSEWLFHGKDEEEMLLWLQGMSTAINESQSIRVKAQSLPLPSLAGPDASVGKKDKEKRFSFFPKKK