wanglab/gogpt-training-data huggingface dataset:
Protein: Sporulation-specific protein 1 (EC 2.7.11.1) (P08458)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Serine/threonine protein kinase required for spore wall development.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein HYM1
- Factor arrest protein 8
- Sporulation-specific protein 2
- Serine/threonine-protein phosphatase PP2A-1 catalytic subunit
- Factor arrest protein 11
- Uncharacterized protein YFL012W
- Protein SHC1
Sequence:
MESKEISIRSRTPPSKLYSIQSCIGRGNFGDVYKAVDRVTQEIVAIKVVNLEHSDEDIELLAQEIFFLAELKSPLITNYIATMLEDVSMWIVMEYCGGGSCSDLLKRSYVNGLPEEKVSFIIHEVTLGLKYLHEQRKIHRDIKAANILLNEEGMVKLGDFGVSGHIRSTLKRDTFVGTPYWMAPEVVCCEVDGYNEKADIWSLGITTYELLKGLPPLSKYDPMKVMTNLPKRKPPKLQGPFSDAAKDFVAGCLVKTPADRPSAYNLLSFEFVKNITITNLKSDVDLIKQKKVQERYTKVPKYPLQNRLYKNSNTVRGKEFWNFESTRLSTTQISKEELSPITQDSPTSSLNMESPYLLHGQTVTPITNPSSSSFRKCTQPVFELDSGMDIDSGCPNAQAETEIVPLSNHNKKHKKNDIQALKIEKFDYLKNIVSHILNRMYDRARDDETRKYVNEMLKQFIKTEANVPGFNEVFIEEISLRIEAIKKGFV
Protein: Ras-related protein Rab-12 (EC 3.6.5.2) (Q6IQ22)
Organism: Homo sapiens (Human)
Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab may play a role in protein transport from recycling endosomes to lysosomes regulating, for instance, the degradation of the transferrin receptor. Involved in autophagy (By similarity).
Subcellular location: Recycling endosome membrane {ECO:0000250|UniProtKB:P35283}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lysosome membrane {ECO:0000250|UniProtKB:P35283}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P51152}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:P35283}.
Interaction partners:
- Rab GDP dissociation inhibitor alpha
- DENN domain-containing protein 3
- RILP-like protein 1
- Rab GDP dissociation inhibitor beta
- RILP-like protein 2
- Rab proteins geranylgeranyltransferase component A 1
Sequence:
MDPGAALQRRAGGGGGLGAGSPALSGGQGRRRKQPPRPADFKLQVIIIGSRGVGKTSLMERFTDDTFCEACKSTVGVDFKIKTVELRGKKIRLQIWDTAGQERFNSITSAYYRSAKGIILVYDITKKETFDDLPKWMKMIDKYASEDAELLLVGNKLDCETDREITRQQGEKFAQQITGMRFCEASAKDNFNVDEIFLKLVDDILKKMPLDILRNELSNSILSLQPEPEIPPELPPPRPHVRCC
Protein: Myeloid cell nuclear differentiation antigen (P41218)
Organism: Homo sapiens (Human)
Function: May act as a transcriptional activator/repressor in the myeloid lineage. Plays a role in the granulocyte/monocyte cell-specific response to interferon. Stimulates the DNA binding of the transcriptional repressor protein YY1.
Subcellular location: Nucleus. Cytoplasm. Note=Uniformly distributed throughout the interphase cell nucleus. Associates with chromatin.
Interaction partners:
- TYRO protein tyrosine kinase-binding protein
- Toll-like receptor 8
- Tyrosine-protein kinase HCK
- Low affinity immunoglobulin gamma Fc region receptor III-A
- Aquaporin-9
- Neutrophil cytosol factor 2
- Transcription factor PU.1
- Leukocyte immunoglobulin-like receptor subfamily B member 2
- Tyrosine-protein kinase Fgr oncogene homolog)
- Leukocyte immunoglobulin-like receptor subfamily A member 1
Sequence:
MVNEYKKILLLKGFELMDDYHFTSIKSLLAYDLGLTTKMQEEYNRIKITDLMEKKFQGVACLDKLIELAKDMPSLKNLVNNLRKEKSKVAKKIKTQEKAPVKKINQEEVGLAAPAPTARNKLTSEARGRIPVAQKRKTPNKEKTEAKRNKVSQEQSKPPGPSGASTSAAVDHPPLPQTSSSTPSNTSFTPNQETQAQRQVDARRNVPQNDPVTVVVLKATAPFKYESPENGKSTMFHATVASKTQYFHVKVFDINLKEKFVRKKVITISDYSECKGVMEIKEASSVSDFNQNFEVPNRIIEIANKTPKISQLYKQASGTMVYGLFMLQKKSVHKKNTIYEIQDNTGSMDVVGSGKWHNIKCEKGDKLRLFCLQLRTVDRKLKLVCGSHSFIKVIKAKKNKEGPMNVN
Protein: Probable 6-phosphogluconolactonase 5 (6PGL5) (EC 3.1.1.31) (Q8LEV7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:24008768}.
Interaction partners:
- 6-phosphogluconate dehydrogenase, decarboxylating 1, chloroplastic
- 6-phosphogluconate dehydrogenase, decarboxylating 2
- 6-phosphogluconate dehydrogenase, decarboxylating 3, chloroplastic
- Gluconokinase
- Glucose-6-phosphate 1-dehydrogenase 2, chloroplastic
- Glucose-6-phosphate 1-dehydrogenase 1, chloroplastic
- Inactive glucose-6-phosphate 1-dehydrogenase 4, chloroplastic
- Glucose-6-phosphate 1-dehydrogenase 5, cytoplasmic
- Glucose-6-phosphate 1-dehydrogenase 6, cytoplasmic
- Glucose-6-phosphate 1-dehydrogenase 3, chloroplastic
Sequence:
MAQRKMIVFPTKNELSEAMAEYTANLSAKFIKEKGLFTVVLSGGDLIDWLCKLVQPPYIDSIEWPKWHVFWVDERVCAWEDPDSNYKLAMEGFLSKVPIPDKNIYAIDKHLAADGNAEHCATLYEECLKNLVKEKIIPISKKTGYPEFDLQLLGMGPDGHMASLFPNHPQINEKQKWVTYITDSPKPPPKRITFTLPVINSTLYNLMAICDKAPAKSVAEIMKHNNLSLPSAHLSAQVENVWYLDQAAASEL
Protein: Ras-related protein RABH1d (AtRABH1d) (Q9SID8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Protein transport. Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER) (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Vacuolar protein-sorting-associated protein 33 homolog
- non-specific serine/threonine protein kinase
- Vacuolar protein sorting-associated protein 53 B
- Guanosine nucleotide diphosphate dissociation inhibitor At5g09550
- Guanosine nucleotide diphosphate dissociation inhibitor 1
- Guanosine nucleotide diphosphate dissociation inhibitor 2
- Dentin sialophosphoprotein
- Type I inositol polyphosphate 5-phosphatase 5
- Conserved oligomeric Golgi complex subunit 6
- Adenine nucleotide alpha hydrolases-like superfamily protein
Sequence:
MASVSPLAKYKLVFLGDQSVGKTSIITRFMYDKFDTTYQATIGIDFLSKTMYLEDRTVRLQLWDTAGQERFRSLIPSYIRDSSVAVVVYDVANRLSFLNTSKWIEEVRNERAGDVIIVLVGNKTDLVEKRQVSIEEGDSKGREYGVMFIETSAKAGFNIKPLFRKIAAALPGMESYSNTKNEDMVDVNLKPTSNSSQGDQQGGACSC
Protein: ADAMTS-like 5 (Q9CRC7)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MAIHPDPALHCLLVTLCSLKPRLFPLLPFLLWTLLSCDLRGAAQGPGEWTPWGSWSRCSSSCGRGVSVRRRQCVRLPGEELCWGDSHEYRVCQLPDCPPGTTPFRDLQCSLYNGHPVLDTQKTYQWVPFHGAPNVCDLNCLAEGHAFYHSFGRVLDGTPCTPGTQGLCVAGRCLSAGCDGILGSGTLEDRCGLCGGANDSCLFVQRVFRDAGDCPILTHHQRLRNTVERGVPLTSLAPGSQGSC
Protein: Exocyst complex component 8 (Exocyst complex 84 kDa subunit) (O54924)
Organism: Rattus norvegicus (Rat)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12954101}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12954101}. Cell projection, growth cone {ECO:0000269|PubMed:12954101}. Cell projection {ECO:0000269|PubMed:21658605}. Note=Binds lipids with phosphatidylinositol 3,4,5-trisphosphate groups (By similarity). Perinuclear in undifferentiated PC12 cells. Redistributes to growing neurites and growth cones during NGF-induced neuronal differentiation (PubMed:12954101). Localizes at the leading edge of migrating cells (PubMed:21658605). {ECO:0000250, ECO:0000269|PubMed:12954101, ECO:0000269|PubMed:21658605}.
Interaction partners:
- Exocyst complex component 3
- Exocyst complex component 6
- Exocyst complex component 2
- Exocyst complex component 7
- Exocyst complex component 5
- Exocyst complex component 4
- Exocyst complex component 1
- Ras-related protein Ral-B
- Ras-related protein Ral-A
- Exocyst complex component
Sequence:
MSDSGASRLRRQLESGGFEARLYVKQLSQQSDGDRDLQEHRQRVQALAEETAQNLKRNVYQNYRQFIETAREISYLESEMYQLSHLLTEQKSSLESIPLALLPAAAAGASTGEDTAGAGPRERGAAQAGFLPGPAGVPREGPGTGEEGKQRTLTTLLEKVEGCRDLLETPGQYLVYNGDLVEYEADHMAQLQRVHGFLMNDCLLVATWLPQRRGMYRYNALYPLDRLAVVNVKDNPPMKDMFKLLMFPESRIFQAENAKIKREWLEVLEETKRALSDKRRREQEEAAALRAPPPVTSKGSNPFEDEAEEELATPEAEEEKVDLSMEWIQELPEDLDVCIAQRDFEGAVDLLDKLNHYLEDKPSPPSVKELRAKVDERVRQLTEVLVFELSPDRSLRGGPKATRRAVSQLIRLGQCTKACELFLRNRAAAVHTAIRQLRIEGATLLYIHKLCHVFFTSLLETAREFETDFAGTDSGCYSAFVVWARSAMGMFVDAFSKQVFDSKESLSTAAECVKVAKEHCQQLGEIGLDLTFIIHALLVKDIQGALLSYKEIIIEATKHRNSEEMWRRMNLMTPEALGKLKEEMRSCGVSNFEQYTGDDCWVNLSYTVVAFTKQTMGFLEEALKLYFPELHMVLLESLVEVILVAVQHVDYSLRCEQDPEKKTFIRQNASFLYDTVLPVVERRFEEGVGKPAKQLQDLRNASRLLRVNPESTTSVV
Protein: Sphingoid long-chain bases kinase 1 (AtLCBK1) (LCB kinase 1) (EC 2.7.-.-) (Sphingosine kinase 1) (Q9LRB0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the production of sphingolipid metabolites. Active on sphingosine, phytosphingosine (PHS, 4-hydroxysphinganine), D-erythro-dihydrosphingosine, D-erythro-sphingosine and trans-4, trans-8-sphingadienine, an LCB found exclusively in plants, but not on N-acetyl-dihydrosphingosine (C2-dihydroceramide) and D-threo-dihydrosphingosine.
Interaction partners:
- Enhanced disease resistance-like protein
- At5g19590
- Uncharacterized protein
- Sphingosine-1-phosphate lyase
- Alkaline ceramidase
- Long chain base biosynthesis protein 1
- Long chain base biosynthesis protein 2a
- Neutral ceramidase 1
- Long chain base biosynthesis protein 2b
- serine C-palmitoyltransferase
Sequence:
MQKSGVNRNPSLKVAIPQAQQSLRRLGFCSQIATGGSQQSSPIVFPEKRNKKVKASSRRGEVTNDPQVKPKPDEHRIDIGGGDEKSDLLGSLVYAGKLVLDKRKSASGKDATEIQQPAATDISIKKAVDAKLTSSALVWGSDMLQLNDVVSVTYNVGLRHFTVHAYPIGKGSCGLSCFTKPKRSRKDFRFVAPTVEEAVQWVASFGDQQCFINCLPHPLVAKKQASSELFSVPIDTPPELVFRCKSAPKMLVILNPRSGHGRSIKVFHNVVEPIFKLAGIKMEVVKTTKAGHARELASTVDINLCSDGIICVGGDGIINEVLNGLLTRSNPKEGVSIPIGIVPAGSDNSLVWTVLGVRDPISAALSIVKGGLTATDVFAVEWIHTGIIHFGMTVSYYGFVSDVLELSEKYQKRFGPLRYFVAGFLKFMCLPKYSYEVEYLPAQKEDAEGKIRLEKEAVDMQDLYTDVMRRSSREGFPRASSLSSIDSIMTPSVGELDTCSSTHASTEPSEYVRGIDPKMKRLSSGRRDVTAEPEVIHPQAQSTTPNWPRTRSKSRMDKGWMGLTSVQDPPTRCSWGNTGGQDREDISSTVSDPGPIWDAGPKWDTEPSAWDVENSIELPGPPEDIETGLRKQSITPIFEDKWVSRKGHFLGIMVCNHACRTVQSSQVVAPNSEHDDGTMDMLLVHGCGRLRLLRFFILLQTGRHLSLPYVECVKVKSVKIKAGKNTHDSCGIDGELFALHGEVISTMLPEQCRLIGNAPGRHS
Protein: Tripartite terminase subunit 2 (P10217)
Organism: Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Function: Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM1 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04015, ECO:0000269|PubMed:18559942}. Note=Found associated with the external surface of the viral capsid during assembly and DNA packaging, but seems absent in extracellular mature virions. {ECO:0000255|HAMAP-Rule:MF_04015}.
Interaction partners:
Sequence:
MAGREGRTRQRTLRDTIPDCALRSQTLESLDARYVSRDGAHDAAVWFEDMTPAELEVVFPTTDAKLNYLSRTQRLASLLTYAGPIKAPDDAAAPQTPDTACVHGELLAAKRERFAAVINRFLDLHQILRG
Protein: 40S ribosomal protein S3 (H0YEU2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XFVADGIFKAELNEFLTRELAEDGYSGVEVRVTPTRTEIIILATRACYGVLRFIMESGAKGCEVVVSGKLRGQRAKSMKFVDGLMIHSGDPVNYYVDTAVRHVLLRQGVLGIKVKIMLPWDPTGKIGPKKPLPDHVSIVEPKDEILPTTPISEQKGGKPEPPAMPQPVPTA
Protein: F-box protein SNE (Protein SNEEZY) (Sleepy protein 2) (Q9LUB6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential component of a SCF-type E3 ligase complex that positively regulates the gibberellin signaling pathway. Upon gibberellin treatment, such complex probably mediates the ubiquitination and subsequent degradation of DELLA proteins (GAI, RGA and RGL2), some repressors of the gibberellin pathway, leading to activate the pathway. Can partially complement the absence of GID2/SLY1.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DELLA protein RGA
- DELLA protein GAI
- DELLA protein RGL2
- Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY
- DELLA protein RGL1
Sequence:
MSSEKRVGMVEKSNNKRQRVNQVPVFSINDHHDVLVEILRRLDGSSLCSAACVCRLWSAVARNDSIWEELCFRQVSPRPSLSLRSVVSALGGYRCLYFLCIRPVLARLPKLLWTRDQLQLSLSLYCVHYYERLYVGAWLGDAPPSSLIFLRKPVNVV
Protein: Ribonuclease (EC 3.1.26.4) (Q38BC8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Ribonuclease H2 subunit B wHTH domain-containing protein
- Proliferating cell nuclear antigen
- Bifunctional dihydrofolate reductase-thymidylate synthase
- DNA primase
- ribonuclease H
- DNA helicase
Sequence:
MLGVRACFSHSPALLFGAFRPTMPCKNSADRGSHERKTPWDALRELRVPPRTTVDSVATLDSTLDMVGYQLFRDGLLSPPPLSFLQRRQQQLQFPKHLTPEMRRLEKEKEQLMARMRKNGVVIRRSIKETFLTIGCDEAGRGPLAGPVVGAAVCRIPRSSFNNDLKALYDADEEFQIFDSKSVSETQRKVVYNNITGYHNLFSLVEDQDFVVHHAGGDSVPDNVLKKRLPSHTKLGKLPFKKLLSMQTPYLISYHGSNVSGNYLYFWAIGIANHTYIDTVNIYSASMNTMHRCCLGVWDALNDARFSYHVAPRPKNCSIAQYLFSRFCITAANDDRRRYEVPDQIDLVEGATDFFDAEPVQPPLVLVDGHTAPYETVSVFTDVQTGGCVQPIIEGDKRSLTIAAASCLAKVSRDEIMDYLDPLYPKYHFAENKGYPVDHHMRAVKKHGLSSIHRRSYRPCAEALARQARRKMKDSHS
Protein: Microspherule protein 1 (58 kDa microspherule protein) (Cell cycle-regulated factor p78) (INO80 complex subunit J) (MCRS2) (Q96EZ8)
Organism: Homo sapiens (Human)
Function: Modulates the transcription repressor activity of DAXX by recruiting it to the nucleolus. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. Putative regulatory component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. May also be an inhibitor of TERT telomerase activity. Binds to G-quadruplex structures in mRNA. Binds to RNA homomer poly(G) and poly(U).
Subcellular location: Nucleus {ECO:0000269|PubMed:15044100, ECO:0000269|PubMed:16571602, ECO:0000269|PubMed:18922472, ECO:0000269|PubMed:20018852}. Nucleus, nucleolus {ECO:0000269|PubMed:16571602, ECO:0000269|PubMed:9654073}. Cytoplasm {ECO:0000269|PubMed:16571602}. Note=In microspherules in the nucleolus. {ECO:0000269|PubMed:9654073}.
Interaction partners:
- KAT8 regulatory NSL complex subunit 3
- KAT8 regulatory NSL complex subunit 2
- PHD finger protein 20
- KAT8 regulatory NSL complex subunit 1
- WD repeat-containing protein 5
- UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
- Chromatin-remodeling ATPase INO80
- INO80 complex subunit E
- Histone acetyltransferase KAT8
- Host cell factor 1
Sequence:
MDKDSQGLLDSSLMASGTASRSEDEESLAGQKRASSQALGTIPKRRSSSRFIKRKKFDDELVESSLAKSSTRAKGASGVEPGRCSGSEPSSSEKKKVSKAPSTPVPPSPAPAPGLTKRVKKSKQPLQVTKDLGRWKPADDLLLINAVLQTNDLTSVHLGVKFSCRFTLREVQERWYALLYDPVISKLACQAMRQLHPEAIAAIQSKALFSKAEEQLLSKVGSTSQPTLETFQDLLHRHPDAFYLARTAKALQAHWQLMKQYYLLEDQTVQPLPKGDQVLNFSDAEDLIDDSKLKDMRDEVLEHELMVADRRQKREIRQLEQELHKWQVLVDSITGMSSPDFDNQTLAVLRGRMVRYLMRSREITLGRATKDNQIDVDLSLEGPAWKISRKQGVIKLKNNGDFFIANEGRRPIYIDGRPVLCGSKWRLSNNSVVEIASLRFVFLINQDLIALIRAEAAKITPQ
Protein: Orthopedia homeobox a (F6NUE7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MLSHADLLDARLGMKDAAAELLGHREALKCRLGGGGTDPVHPGDLAPVSDAVEGATLLPGDDINSAGSNPPGVAVNSKDQEKQQQQQQNPTQSSSQQSQKQKRHRTRFTPAQLNELERSFAKTHYPDIFMREELALRIGLTESRVQVWFQNRRAKWKKRKKTTNVFRAPGTLLPTHHGLPQFPSAAAAAAAMGDSLCSFHANDTRWAAAGMPGVSQLQLPPALGRQQAMAQSLSQCSLGAGPPPNSMSLSNMSSNGSGLQSHLYQPTFPGMVPASLSGPTNVTGSPQLCSSPDTDVWRGTSIASLRRKALEHTVSMSFT
Protein: G-protein coupled estrogen receptor 1 (G protein-coupled estrogen receptor 1) (G-protein coupled receptor 30) (B0F9W3)
Organism: Micropogonias undulatus (Atlantic croaker)
Function: Membrane G-protein coupled estrogen receptor that binds to 17-beta-estradiol (E2) with high affinity, leading to rapid and transient activation of numerous intracellular signaling pathways. Plays a role in the embryonic development of sensory and motor neurons. May induce apoptosis and reduce proliferation of brain cells. Involved in maintenance of meiotic arrest in oocytes.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:18420744}; Multi-pass membrane protein {ECO:0000269|PubMed:18420744}. Basolateral cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, axon {ECO:0000250}. Postsynaptic density {ECO:0000250}. Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Colocalized with cadherin at the plasma membrane.
Interaction partners:
Sequence:
MEEQTTSLVWIYVNSTEQLNTSYEYNTTYLIEDSDKYQSYVIGLFLSCLYTILLFPIGFIGNILILVVNLNHRGKMAIPDLYFVNLAVADLILVADSLIEVFNLNEKYYDYAVLCTFMSLFLQVNMYSSIFFLTWMSFDRYIALANSMSSSPLRTMQHAKLSCGLIWMASILATLLPFTIVQTQHRGEVHFCFANVFEIQWLEVTIGFLVPFSIIGLCYSLIGRILMRSQKHRGLWPRRQKALRMIVVVVLVFFICWLPENVFISIQLLQGTADPSQRTATTLRHDYPLTGHIVNLAAFSNSCLNPIIYSFLGETFRDKLRLFIKQKASWSVVNRFCHHGLDLHLPVRSEVSEV
Protein: Flavin-containing monooxygenase 1 (EC 1.14.13.148) (EC 1.14.13.8) (Dimethylaniline monooxygenase [N-oxide-forming] 1) (Dimethylaniline oxidase 1) (Fetal hepatic flavin-containing monooxygenase 1) (FMO 1) (Trimethylamine monooxygenase) (Q01740)
Organism: Homo sapiens (Human)
Function: Broad spectrum monooxygenase that catalyzes the oxygenation of a wide variety of nitrogen- and sulfur-containing compounds including xenobiotics. Catalyzes the S-oxygenation of hypotaurine to produce taurine, an organic osmolyte involved in cell volume regulation as well as a variety of cytoprotective and developmental processes. In vitro, catalyzes the N-oxygenation of trimethylamine (TMA) to produce trimethylamine N-oxide (TMAO) and could therefore participate to the detoxification of this compound that is generated by the action of gut microbiota from dietary precursors such as choline, choline containing compounds, betaine or L-carnitine (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P36365}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome P450 3A4)
- Cytochrome P450 2D6
- Cytochrome P450 2C9
Sequence:
MAKRVAIVGAGVSGLASIKCCLEEGLEPTCFERSDDLGGLWRFTEHVEEGRASLYKSVVSNSCKEMSCYSDFPFPEDYPNYVPNSQFLEYLKMYANHFDLLKHIQFKTKVCSVTKCSDSAVSGQWEVVTMHEEKQESAIFDAVMVCTGFLTNPYLPLDSFPGINAFKGQYFHSRQYKHPDIFKDKRVLVIGMGNSGTDIAVEASHLAEKVFLSTTGGGWVISRIFDSGYPWDMVFMTRFQNMLRNSLPTPIVTWLMERKINNWLNHANYGLIPEDRTQLKEFVLNDELPGRIITGKVFIRPSIKEVKENSVIFNNTSKEEPIDIIVFATGYTFAFPFLDESVVKVEDGQASLYKYIFPAHLQKPTLAIIGLIKPLGSMIPTGETQARWAVRVLKGVNKLPPPSVMIEEINARKENKPSWFGLCYCKALQSDYITYIDELLTYINAKPNLFSMLLTDPHLALTVFFGPCSPYQFRLTGPGKWEGARNAIMTQWDRTFKVIKARVVQESPSPFESFLKVFSFLALLVAIFLIFL
Protein: Secretory 16, isoform I (X2JEM2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
- Protein SEC13 homolog
- Protein transport protein SEC23
- Protein transport protein Sec31A
- Secretory 24AB, isoform A
- Secretory 24CD, isoform C
- small monomeric GTPase
- FI09914p
- Syntaxin-5
- Transport and Golgi organization protein 1
- Ergic53, isoform A
Sequence:
MLHNNAPWLPPHQQQQQQAPQQHPTPQQQHAMPQQQQTLPAQQQQQQVYASQMFQQHQPNYWPEDQHQQQQQPQSLNYNNYFPGQQQQHPMQQQQLPPQQQLPPQQQQPTQQQHTIQQQLYYPTQQQPQVPAPAEPALDSFDNNNSGGGGGGGRSDGWGDWGDWNDNSNNNNSNGTDGLLEPTGQLLEDSFNVQSSQGSWQAFATSNNVNNNGELPPPANPQSTSLQQQPLNQQSIPLLHQQPQSPPELGQEPELDAIVPPQAFQNQPPTAAPPPTSLTSFSAQMTAVGSPIYAVGASSAHSAGVGASPAPPTGVVAPPAHLAGIGAPPAHLAGVGASPAPSALVGASPAPIIGVGAPPVGAPPVGAPPADATTIAPPAALPPSIVPSSGSNPFKRSTGLNKRVNIMADPAAGAPSPPAPAAAIAPVAPVAPIPPPADQLFGMPAEAHGEGFNLIAAPPVEASLGTPLSAPIPAPIPVPNASLYASPAVPQAFAHLEPDNQEVLSAPNDERAQYLQTSHLSEQLGEGEADQDAGLLPPPGLSRLVLGQPELDSQQQRQVTGATEQPPLNVAQAAALHMQERRADGEDTSDGEQQVRNIQTPPRRVVTGVETNAPSLREQREVVLDGENLEDREAIPPPTLAELPTTSVHHNILPDEAEQLHHNNPPQAMTPLNAQQPHQQQSTLQQQHQQHSTTQQEKKRAAVGRRTTASLDLESDESDEFLQSERERDRERERRDLMEERHSRGRSHSHYPYEGETEDSVRGAAHHETKSLRETHHKRNHDSARSRRHQDPKVERERERDRERDRTWRRRSNKYHSGGEDPDRSYDHSRRYNNSNYEGESDNPEYNHMGDAELDGSGGRSSKTSRHRRSAAEEDFDDYERERNRSRRSTKPQSSAEKSRSSGGRRNYENSGRSARADDGRRRYQDQRNPGAQYPVSATGYVPYGMYEQMSRNPQVYADMYAKFYGQMINSMNAAVSAAASKGGVPAGAGVIPGLMPSAVPVSAAQLVAATSGGSVSGSSEAAMLRERERYTHAYITQANEFHRHQYKELIYQQQQQQQQQQQQQQQREDHLNSSFSVAEDNASFYGSHGGGSIYNQYQSYPLSSARSLSNLNGDGRNSRCGPYYAGSECGLDIRAAADAAPSTYGGVAGTAGPVTNTAVARPPRRRTPLQFSRPHLVASYAMSLLLKVKPKYAGRGRLRNDVEVAPPRIRDGTSSLLRMYPGPLQGRKLHKDKIISFCKEQIRLGPTKGCTALYATQKKPQGSVTKYRASHALMWHLLILLLRQNGYIADTDVGDLLLENQQEYPYDPSEFEAENEPDADAEQDAAAPADKTVDSDLDSESAAGVTPAEPLAAGAATSSINGADAANAATPLSEQAATDKFRSYVLRGNVEEALQWATDNGLWTHAFFLALYEDRYALTDVAQKFLNRAIKANDPLQTLYQMKSCHTPACVSQLRDEQWGDWRSHLSILVTNKSRQPEYDRSSVVALGDTLFQRGDIYAAHFCYLVAQEEFGRYDSSATELTTLTANVPRLILLGSSHYKHFNEFASNEAIIMTEIYEYARSLFDPKFSIAHFQHYKFLLATRILDYGQHFRCTNYLEQIARHIELKPESYDSNFIQRVCGLAERLRYHDPILINRVSFASPPNATSKDSAAAEEKAWLRQLRSLAYVQPQQEQLQQLQQNQQVQQEQNDIDQQFAEVNKQFRELNMQYESNSNMENTLQPQLPPVDQQPPQQQQQVLSESYQQPTQQYYEPPPQAPTESDPYGQGQPSYYDPNAGQLHYDPNAAQHQYDQQQPQPQPTPSYGQIEPGTEAYQPGQATADPAAVPSGYGYDYWSGTQQPPYGDEPNENQAALKDEEEEDEEQDEQQILQYAKQQILQQTKQQQLQQEQHTRSNGAASINNRFKSNALKQERSSGSLRKRQEASRTATIAAAAAAIAQITPATVAAAATPPAASAKAFNLNDVSSFSSTNKRHQATSSSNNRSSSNQAAAAAAATKAAAIATVPAAPNQLLSCRKSNSQNSPYLATPKTLTTPTRFIAAKAATVTATPTAPATSTTTSTTIGARGSSTKRVYFNLPSTIAESEQEFEHELDYDEEMEEENSMALAQAKPNVHLARKPHIVFNGTYPIDMPLTQGQSQLKSNSYDPEANADRGDLQRYRNYMLHDYVIDEDAEGEEQAEEEGEEDEYGDGDEDLFPYADDDESFDDGDYYTHQLLNKYGIIPSGEKQRVERTPASVEAATSAAQPQHVWSMKELIANPAIPLNYKKMCSEVEQSLSRFENYLDSKKEQQVPPGAAVRTFDIDAPTRRGHRSSTSTNAGLDLRSKKKL
Protein: Putative uncharacterized protein BUD19 (O94143)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Putative uncharacterized protein YGR160W
Sequence:
MTKSLKHKYVLRLDVHLGSSPVSSLSVVTDSVVGSQSDPLWQWSVLLLSLSHFLLDSERLLSLIKRETYRAHTKCTIVKNVSNNVQTHQYDAFTDPRQYHLT
Protein: Protein O-mannosyl-transferase TMTC3 (EC 2.4.1.109) (Protein SMILE) (Transmembrane O-mannosyltransferase targeting cadherins 3) (Transmembrane and tetratricopeptide repeat-containing 3) (Q6ZXV5)
Organism: Homo sapiens (Human)
Function: Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. The 4 members of the TMTC family are O-mannosyl-transferases dedicated primarily to the cadherin superfamily, each member seems to have a distinct role in decorating the cadherin domains with O-linked mannose glycans at specific regions. Also acts as O-mannosyl-transferase on other proteins such as PDIA3. Involved in the positive regulation of proteasomal protein degradation in the endoplasmic reticulum (ER), and the control of ER stress response.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:21603654}. Note=In odontoblast cultures, it colocalizes with PDIA3 in the endoplasmic reticulum. {ECO:0000269|PubMed:21603654}.
Interaction partners:
Sequence:
MANINLKEITLIVGVVTACYWNSLFCGFVFDDVSAILDNKDLHPSTPLKTLFQNDFWGTPMSEERSHKSYRPLTVLTFRLNYLLSELKPMSYHLLNMIFHAVVSVIFLKVCKLFLDNKSSVIASLLFAVHPIHTEAVTGVVGRAELLSSIFFLAAFLSYTRSKGPDNSIIWTPIALTVFLVAVATLCKEQGITVVGICCVYEVFIAQGYTLPLLCTTAGQFLRGKGSIPFSMLQTLVKLIVLMFSTLLLVVIRVQVIQSQLPVFTRFDNPAAVSPTPTRQLTFNYLLPVNAWLLLNPSELCCDWTMGTIPLIESLLDIRNLATFTFFCFLGMLGVFSIRYSGDSSKTVLMALCLMALPFIPASNLFFPVGFVVAERVLYVPSMGFCILVAHGWQKISTKSVFKKLSWICLSMVILTHSLKTFHRNWDWESEYTLFMSALKVNKNNAKLWNNVGHALENEKNFERALKYFLQATHVQPDDIGAHMNVGRTYKNLNRTKEAEESYMMAKSLMPQIIPGKKYAARIAPNHLNVYINLANLIRANESRLEEADQLYRQAISMRPDFKQAYISRGELLLKMNKPLKAKEAYLKALELDRNNADLWYNLAIVHIELKEPNEALKKNFNRALELNPKHKLALFNSAIVMQESGEVKLRPEARKRLLSYINEEPLDANGYFNLGMLAMDDKKDNEAEIWMKKAIKLQADFRSALFNLALLYSQTAKELKALPILEELLRYYPDHIKGLILKGDILMNQKKDILGAKKCFERILEMDPSNVQGKHNLCVVYFEEKDLLKAERCLLETLALAPHEEYIQRHLNIVRDKISSSSFIEPIFPTSKISSVEGKKIPTESVKEIRGESRQTQIVKTSDNKSQSKSNKQLGKNGDEETPHKTTKDIKEIEKKRVAALKRLEEIERILNGE