wanglab/gogpt-training-data huggingface dataset:
Protein: Keratin, type II cytoskeletal 72 (Cytokeratin-72) (CK-72) (Keratin-72) (K72) (Type II inner root sheath-specific keratin-K6irs2) (Type-II keratin Kb35) (Q14CN4)
Organism: Homo sapiens (Human)
Function: Has a role in hair formation. Specific component of keratin intermediate filaments in the inner root sheath (IRS) of the hair follicle (Probable).
Interaction partners:
- Keratin, type II cytoskeletal 73
Sequence:
MSRQLTHFPRGERLGFSGCSAVLSGGIGSSSASFRARVKGSASFGSKSLSCLGGSRSLALSAAARRGGGRLGGFVGTAFGSAGLGPKCPSVCPPGGIPQVTVNKSLLAPLNVEMDPEIQRVRAQEREQIKALNNKFASFIDKVRFLEQQNQVLETKWNLLQQLDLNNCRKNLEPIYEGYISNLQKQLEMLSGDGVRLDSELRNMQDLVEDYKKRYEVEINRRTAAENEFVVLKKDVDAAYMNKVELQAKVDSLTDEIKFFKCLYEGEITQIQSHISDTSIVLSMDNNRDLDLDSIIAEVRAQYEEIALKSKAEAETLYQTKIQELQVTAGQHGDDLKLTKAEISELNRLIQRIRSEIGNVKKQCADLETAIADAEQRGDCALKDARAKLDELEGALHQAKEELARMLREYQELVSLKLALDMEIATYRKLLESEECRMSGEYPNSVSISVISSTNAGAGGAGFSMGFGASSSYSYKTAAADVKTKGSCGSELKDPLAKTSGSSCATKKASR
Protein: Antigen-presenting glycoprotein CD1d1 (CD antigen CD1d.1) (P11609)
Organism: Mus musculus (Mouse)
Function: Antigen-presenting protein that binds self and non-self glycolipids and presents them to T-cell receptors on natural killer T-cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11754812}; Single-pass type I membrane protein {ECO:0000269|PubMed:11754812}. Endosome membrane {ECO:0000269|PubMed:11754812}. Lysosome membrane {ECO:0000269|PubMed:11754812}. Note=Subject to intracellular trafficking between the cell membrane, endosomes and lysosomes. {ECO:0000269|PubMed:11754812}.
Interaction partners:
- Beta-2-microglobulin
- T-cell surface glycoprotein CD4
- Tumor necrosis factor receptor superfamily member 5
- Interferon gamma
- Killer cell lectin-like receptor subfamily B member 1C
- CD83 antigen
- Interleukin-4
- T-lymphocyte activation antigen CD80
- CD40 ligand
- T-cell surface glycoprotein CD5
Sequence:
MRYLPWLLLWAFLQVWGQSEAQQKNYTFRCLQMSSFANRSWSRTDSVVWLGDLQTHRWSNDSATISFTKPWSQGKLSNQQWEKLQHMFQVYRVSFTRDIQELVKMMSPKEDYPIEIQLSAGCEMYPGNASESFLHVAFQGKYVVRFWGTSWQTVPGAPSWLDLPIKVLNADQGTSATVQMLLNDTCPLFVRGLLEAGKSDLEKQEKPVAWLSSVPSSADGHRQLVCHVSGFYPKPVWVMWMRGDQEQQGTHRGDFLPNADETWYLQATLDVEAGEEAGLACRVKHSSLGGQDIILYWDARQAPVGLIVFIVLIMLVVVGAVVYYIWRRRSAYQDIR
Protein: Gamma-glutamylputrescine synthetase PuuA (Gamma-Glu-Put synthetase) (EC 6.3.1.11) (Glutamate--putrescine ligase) (P78061)
Organism: Escherichia coli (strain K12)
Function: Involved in the breakdown of putrescine. Catalyzes the ATP-dependent gamma-glutamylation of putrescine, producing gamma-L-glutamylputrescine. Absolutely essential to utilize putrescine as both nitrogen and carbon sources and to decrease the toxicity of putrescine, which can lead to inhibition of cell growth and protein synthesis. In vitro is also able to use several diamines, and spermidine and spermine, instead of putrescine, but with a much lower activity, and cannot catalyze the gamma-glutamylation of ornithine or GABA.
Interaction partners:
- Gamma-glutamylputrescine oxidoreductase
- Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
- HTH-type transcriptional regulator PuuR
- Putrescine aminotransferase
- Polyamine aminopropyltransferase
- Spermidine N
- Agmatinase
- NADP/NAD-dependent aldehyde dehydrogenase PuuC
- Inducible ornithine decarboxylase
- Constitutive ornithine decarboxylase
Sequence:
METNIVEVENFVQQSEERRGSAFTQEVKRYLERYPNTQYVDVLLTDLNGCFRGKRIPVSSLKKLEKGCYFPASVFAMDILGNVVEEAGLGQEMGEPDRTCVPVLGSLTPSAADPEFIGQMLLTMVDEDGAPFDVEPRNVLNRLWQQLRQRGLFPVVAVELEFYLLDRQRDAEGYLQPPCAPGTDDRNTQSQVYSVDNLNHFADVLNDIDELAQLQLIPADGAVAEASPGQFEINLYHTDNVLEACDDALALKRLVRLMAEKHKMHATFMAKPYEEHAGSGMHIHISMQNNRGENVLSDAEGEDSPLLKKMLAGMIDLMPSSMALLAPNVNSYRRFQPGMYVPTQASWGHNNRTVALRIPCGDRHNHRVEYRVAGADANPYLVMAAIFAGILHGLDNELPLQEEVEGNGLEQEGLPFPIRQSDALGEFIENDHLRRYLGERFCHVYHACKNDELLQFERLITETEIEWMLKNA
Protein: Protein-methionine-sulfoxide reductase catalytic subunit MsrP (EC 1.8.5.-) (P76342)
Organism: Escherichia coli (strain K12)
Function: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide. Can catalyze the reduction of a variety of substrates in vitro, including dimethyl sulfoxide, trimethylamine N-oxide, phenylmethyl sulfoxide and L-methionine sulfoxide. Cannot reduce cyclic N-oxides. Shows no activity as sulfite oxidase.
Subcellular location: Periplasm {ECO:0000269|PubMed:16042411}. Note=Is attached to the inner membrane when interacting with the MsrQ subunit.
Interaction partners:
- Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ
- 5-hydroxyisourate hydrolase
- Biotin sulfoxide reductase
- Dimethyl sulfoxide reductase DmsA
- Peptide methionine sulfoxide reductase MsrB
- Free methionine-R-sulfoxide reductase
- Peptide methionine sulfoxide reductase MsrA
- Sensor histidine kinase HprS
- Probable dimethyl sulfoxide reductase chain YnfF
- Molybdopterin molybdenumtransferase
Sequence:
MKKNQFLKESDVTAESVFFMKRRQVLKALGISATALSLPHAAHADLLSWFKGNDRPPAPAGKALEFSKPAAWQNNLPLTPADKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPYVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYAAQVASLYRGLDLRENF
Protein: Enhancer of mRNA-decapping protein 3 (P39998)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Stimulates decapping of both stable and unstable mRNA during mRNA decay. Does not affect nonsense-mediated mRNA decay. Required for normal P-body assembly.
Subcellular location: Cytoplasm, P-body {ECO:0000269|PubMed:15020463}. Note=Is concentrated in several cytoplasmic foci called P bodies (or cytoplasmic processing bodies) which represent sites of mRNA decapping and 5' to 3' exonucleotidic decay.
Interaction partners:
- mRNA-decapping enzyme subunit 1
- m7GpppN-mRNA hydrolase
- 5'-3' exoribonuclease 1
- Protein SCD6
- ATP-dependent RNA helicase DHH1
- LSM1-LSM7 complex subunit LSM1
- Probable tubulin--tyrosine ligase PBY1
- LSM complex subunit LSM4
- Deadenylation-dependent mRNA-decapping factor PAT1
- LSM complex subunit LSM2
Sequence:
MSQFVGFGVQVELKDGKLIQGKIAKATSKGLTLNDVQFGDGGKSQAFKVRASRLKDLKVLTVASQSGKRKQQRQQQQQNDYNQNRGEHIDWQDDDVSKIKQQEDFDFQRNLGMFNKKDVFAQLKQNDDILPENRLQGHNRKQTQLQQNNYQNDELVIPDAKKDSWNKISSRNEQSTHQSQPQQDAQDDLVLEDDEHEYDVDDIDDPKYLPITQSLNITHLIHSATNSPSINDKTKGTVINDKDQVLAKLGQMIISQSRSNSTSLPAANKQTTIRSKNTKQNIPMATPVQLLEMESITSEFFSINSAGLLENFAVNASFFLKQKLGGRARLRLQNSNPEPLVVILASDSNRSGAKALALGRHLCQTGHIRVITLFTCSQNELQDSMVKKQTDIYKKCGGKIVNSVSSLESAMETLNSPVEIVIDAMQGYDCTLSDLAGTSEVIESRIKSMISWCNKQRGSTKVWSLDIPNGFDAGSGMPDIFFSDRIEATGIICSGWPLIAINNLIANLPSLEDAVLIDIGIPQGAYSQRTSLRKFQNCDLFVTDGSLLLDL
Protein: Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase) (P37869)
Organism: Bacillus subtilis (strain 168)
Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:21856851, ECO:0000269|PubMed:24642254}. Secreted {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:21856851, ECO:0000269|PubMed:24642254}. Cell surface {ECO:0000255|HAMAP-Rule:MF_00318}. Note=Present in the cytoplasm early in growth, as cells become stationary protein also accumulates in the medium; the N-terminus of the protein is not processed (PubMed:21856851, PubMed:24642254). An internal hydrophobic region is required for secretion, its replacement by another alpha-helix is not secreted (PubMed:21856851, PubMed:24642254). Also secreted in E.coli (PubMed:24642254). Fractions of enolase are present in both the cytoplasm and on the cell surface. The export of enolase possibly depends on the covalent binding to the substrate at Lys-339; once secreted, it remains attached to the cell surface (By similarity). {ECO:0000250|UniProtKB:P0A6P9, ECO:0000269|PubMed:21856851, ECO:0000269|PubMed:24642254}.
Interaction partners:
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- Triosephosphate isomerase
- Phosphoglycerate kinase
- Pyruvate kinase
- Glyceraldehyde-3-phosphate dehydrogenase 1
- Probable fructose-bisphosphate aldolase
- Glucose-6-phosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase 2
- ATP-dependent 6-phosphofructokinase
- Transketolase
Sequence:
MPYIVDVYAREVLDSRGNPTVEVEVYTETGAFGRALVPSGASTGEYEAVELRDGDKDRYLGKGVLTAVNNVNEIIAPELLGFDVTEQNAIDQLLIELDGTENKGKLGANAILGVSMACARAAADFLQIPLYQYLGGFNSKTLPVPMMNIVNGGEHADNNVDIQEFMIMPVGAPNFREALRMGAQIFHSLKSVLSAKGLNTAVGDEGGFAPNLGSNEEALQTIVEAIEKAGFKPGEEVKLAMDAASSEFYNKEDGKYHLSGEGVVKTSAEMVDWYEELVSKYPIISIEDGLDENDWEGHKLLTERLGKKVQLVGDDLFVTNTKKLSEGIKNGVGNSILIKVNQIGTLTETFDAIEMAKRAGYTAVISHRSGETEDSTIADIAVATNAGQIKTGAPSRTDRVAKYNQLLRIEDQLAETAQYHGINSFYNLNK
Protein: GTPase RhebL1 (EC 3.6.5.-) (Ras homolog enriched in brain like-1 c) (RhebL1c) (Ras homolog enriched in brain-like protein 1) (Rheb-like protein 1) (Rheb2) (Q8TAI7)
Organism: Homo sapiens (Human)
Function: Binds GTP and exhibits intrinsic GTPase activity. May activate NF-kappa-B-mediated gene transcription. Promotes signal transduction through MTOR, activates RPS6KB1, and is a downstream target of the small GTPase-activating proteins TSC1 and TSC2.
Subcellular location: Endomembrane system {ECO:0000305|PubMed:16328882}; Lipid-anchor {ECO:0000305|PubMed:16006564}; Cytoplasmic side {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:16328882}.
Interaction partners:
- Tuberin
- Hamartin
- Serine/threonine-protein kinase mTOR
Sequence:
MPLVRYRKVVILGYRCVGKTSLAHQFVEGEFSEGYDPTVENTYSKIVTLGKDEFHLHLVDTAGQDEYSILPYSFIIGVHGYVLVYSVTSLHSFQVIESLYQKLHEGHGKTRVPVVLVGNKADLSPEREVQAVEGKKLAESWGATFMESSARENQLTQGIFTKVIQEIARVENSYGQERRCHLM
Protein: CASP8-associated protein 2 (FLICE-associated huge protein) (Q9UKL3)
Organism: Homo sapiens (Human)
Function: Participates in TNF-alpha-induced blockade of glucocorticoid receptor (GR) transactivation at the nuclear receptor coactivator level, upstream and independently of NF-kappa-B. Suppresses both NCOA2- and NCOA3-induced enhancement of GR transactivation. Involved in TNF-alpha-induced activation of NF-kappa-B via a TRAF2-dependent pathway. Acts as a downstream mediator for CASP8-induced activation of NF-kappa-B. Required for the activation of CASP8 in FAS-mediated apoptosis. Required for histone gene transcription and progression through S phase.
Subcellular location: Cytoplasm. Nucleus. Nucleus, PML body. Mitochondrion. Note=Exported from the nucleus to the mitochondria upon FAS activation.
Interaction partners:
- Caspase-8
- U7 snRNA-associated Sm-like protein LSm11
- Protein NPAT
- Cleavage and polyadenylation specificity factor subunit 3
Sequence:
MAADDDNGDGTSLFDVFSASPLKNNDEGSLDIYAGLDSAVSDSASKSCVPSRNCLDLYEEILTEEGTAKEATYNDLQVEYGKCQLQMKELMKKFKEIQTQNFSLINENQSLKKNISALIKTARVEINRKDEEISNLHQRLSEFPHFRNNHKTARTFDTVKTKDLKSRSPHLDDCSKTDHRAKSDVSKDVHHSTSLPNLEKEGKPHSDKRSTSHLPTSVEKHCTNGVWSRSHYQVGEGSSNEDSRRGRKDIRHSQFNRGTERVRKDLSTGCGDGEPRILEASQRLQGHPEKYGKGEPKTESKSSKFKSNSDSDYKGERINSSWEKETPGERSHSRVDSQSDKKLERQSERSQNINRKEVKSQDKEERKVDQKPKSVVKDQDHWRRSERASLPHSKNEITFSHNSSKYHLEERRGWEDCKRDKSVNSHSFQDGRCPSSLSNSRTHKNIDSKEVDAMHQWENTPLKAERHRTEDKRKREQESKEENRHIRNEKRVPTEHLQKTNKETKKTTTDLKKQNEPKTDKGEVLDNGVSEGADNKELAMKAESGPNETKNKDLKLSFMKKLNLTLSPAKKQPVSQDNQHKITDIPKSSGVCDSESSMQVKTVAYVPSISEHILGEAAVSEHTMGETKSTLLEPKVALLAVTEPRIGISETNKEDENSLLVRSVDNTMHCEEPICGTETSFPSPMEIQQTESLFPSTGMKQTINNGRAAAPVVMDVLQTDVSQNFGLELDTKRNDNSDYCGISEGMEMKVALSTTVSETTESILQPSIEEADILPIMLSEDNNPKFEPSVIVTPLVESKSCHLEPCLPKETLDSSLQQTELMDHRMATGETNSVYHDDDNSVLSIDLNHLRPIPEAISPLNSPVRPVAKVLRNESPPQVPVYNNSHKDVFLPNSAHSTSKSQSDLNKENQKPIYKSDKCTEADTCKNSPLDELEEGEIRSDSETSKPQESFEKNSKRRVSADVRKSKTIPRRGKSTVCLDKDSRKTHVRIHQTNNKWNKRPDKSSRSSKTEKKDKVMSTSSLEKIVPIIAVPSSEQEIMHMLRMIRKHVRKNYMKFKAKFSLIQFHRIIESAILSFTSLIKHLNLHKISKSVTTLQKNLCDIIESKLKQVKKNGIVDRLFEQQLPDMKKKLWKFVDDQLDYLFAKLKKILVCDSKSFGRDSDEGKLEKTSKQNAQYSNSQKRSVDNSNRELLKEKLSKSEDPVHYKSLVGCKKSEENYQDQNNSSINTVKHDIKKNFNICFDNIKNSQSEERSLEVHCPSTPKSEKNEGSSIEDAQTSQHATLKPERSFEILTEQQASSLTFNLVSDAQMGEIFKSLLQGSDLLDSSVNCTEKSEWELKTPEKQLLETLKCESIPACTTEELVSGVASPCPKMISDDNWSLLSSEKGPSLSSGLSLPVHPDVLDESCMFEVSTNLPLSKDNVCSVEKSKPCVSSILLEDLAVSLTVPSPLKSDGHLSFLKPDMSSSSTPEEVISAHFSEDALLEEEDASEQDIHLALESDNSSSKSSCSSSWTSRSVAPGFQYHPNLPMHAVIMEKSNDHFIVKIRRATPSTSSGLKQSMMPDELLTSLPRHGKEADEGPEKEYISCQNTVFKSVEELENSNKNVDGSKSTHEEQSSMIQTQVPDIYEFLKDASDKMGHSDEVADECFKLHQVWETKVPESIEELPSMEEISHSVGEHLPNTYVDLTKDPVTETKNLGEFIEVTVLHIDQLGCSGGNLNQSAQILDNSLQADTVGAFIDLTQDASSEAKSEGNHPALAVEDLGCGVIQVDEDNCKEEKAQVANRPLKCIVEETYIDLTTESPSSCEVKKDELKSEPGSNCDNSELPGTLHNSHKKRRNISDLNHPHKKQRKETDLTNKEKTKKPTQDSCENTEAHQKKASKKKAPPVTKDPSSLKATPGIKDSSAALATSTSLSAKNVIKKKGEIIILWTRNDDREILLECQKRGPSFKTFAYLAAKLDKNPNQVSERFQQLMKLFEKSKCR
Protein: Cadherin-16 (Kidney-specific cadherin) (Ksp-cadherin) (O75309)
Organism: Homo sapiens (Human)
Function: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MVPAWLWLLCVSVPQALPKAQPAELSVEVPENYGGNFPLYLTKLPLPREGAEGQIVLSGDSGKATEGPFAMDPDSGFLLVTRALDREEQAEYQLQVTLEMQDGHVLWGPQPVLVHVKDENDQVPHFSQAIYRARLSRGTRPGIPFLFLEASDRDEPGTANSDLRFHILSQAPAQPSPDMFQLEPRLGALALSPKGSTSLDHALERTYQLLVQVKDMGDQASGHQATATVEVSIIESTWVSLEPIHLAENLKVLYPHHMAQVHWSGGDVHYHLESHPPGPFEVNAEGNLYVTRELDREAQAEYLLQVRAQNSHGEDYAAPLELHVLVMDENDNVPICPPRDPTVSIPELSPPGTEVTRLSAEDADAPGSPNSHVVYQLLSPEPEDGVEGRAFQVDPTSGSVTLGVLPLRAGQNILLLVLAMDLAGAEGGFSSTCEVEVAVTDINDHAPEFITSQIGPISLPEDVEPGTLVAMLTAIDADLEPAFRLMDFAIERGDTEGTFGLDWEPDSGHVRLRLCKNLSYEAAPSHEVVVVVQSVAKLVGPGPGPGATATVTVLVERVMPPPKLDQESYEASVPISAPAGSFLLTIQPSDPISRTLRFSLVNDSEGWLCIEKFSGEVHTAQSLQGAQPGDTYTVLVEAQDTDEPRLSASAPLVIHFLKAPPAPALTLAPVPSQYLCTPRQDHGLIVSGPSKDPDLASGHGPYSFTLGPNPTVQRDWRLQTLNGSHAYLTLALHWVEPREHIIPVVVSHNAQMWQLLVRVIVCRCNVEGQCMRKVGRMKGMPTKLSAVGILVGTLVAIGIFLILIFTHWTMSRKKDPDQPADSVPLKATV
Protein: ShKT domain-containing protein (O44667)
Organism: Caenorhabditis elegans
Interaction partners:
- PHAryngeal gland Toxin-related
- Uncharacterized protein
- NADH dehydrogenase 1 alpha subcomplex subunit 12
- G_PROTEIN_RECEP_F1_2 domain-containing protein
- DUF1525 domain-containing protein
- ZP domain-containing protein
- LysM domain-containing protein
- Uncharacterized protein.
- PAW domain-containing protein
- Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase pps-1
Sequence:
MYSHGIAAFLLVLVSQASAEIKLGCKSDPMPDANGKCPPGTTMITAGGCCPDNDVYIISDTTTTMAPTTPSPGSCCDKINPKTGVSDCPGMKNYCNYGPYIDIMKDQCPKTCGYCGSGSATTPGICRDKLNPTTGVSDCPARRNLCNNGIYHDVMKDQCPKTCGYCK
Protein: Nuclear transcription factor Y subunit C-2 (AtNF-YC-2) (Transcriptional activator HAP5B) (Q8LCG7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters.
Subcellular location: Nucleus {ECO:0000269|PubMed:24728648}. Cytoplasm {ECO:0000269|PubMed:24728648}.
Interaction partners:
- Nuclear transcription factor Y subunit A-4
- Nuclear transcription factor Y subunit B-3
- Nuclear transcription factor Y subunit B-6
- Nuclear transcription factor Y subunit B-2
- Nuclear transcription factor Y subunit A-1
- Nuclear transcription factor Y subunit B-1
- Nuclear transcription factor Y subunit B-10
- Nuclear transcription factor Y subunit B-9
- Nuclear transcription factor Y subunit B-7
- Nuclear transcription factor Y subunit B-5
Sequence:
MEQSEEGQQQQQQGVMDYVPPHAYQSGPVNAASHMAFQQAHHFHHHHQQQQQQQLQMFWANQMQEIEHTTDFKNHTLPLARIKKIMKADEDVRMISAEAPVIFAKACEMFILELTLRAWIHTEENKRRTLQKNDIAAAISRTDVFDFLVDIIPRDELKEEGLGVTKGTIPSVVGSPPYYYLQQQGMMQHWPQEQHPDES
Protein: Dolichyl-phosphate-mannose--protein mannosyltransferase 4 (EC 2.4.1.109) (P46971)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Forms a homodimeric complex to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. Specifically acts on secretory proteins with an ER-luminally oriented Ser/Thr-rich region flanked by a membrane anchor such as FUS1, AXL2, GAS1, KEX2, MID2, WSC1, WSC2, OPY2, PRM5, RAX2, or YNL176.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P33775}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Dolichyl-phosphate-mannose--protein mannosyltransferase 2
- Dolichyl-phosphate-mannose--protein mannosyltransferase 1
- Dolichyl-phosphate-mannose--protein mannosyltransferase 3
- Mitochondrial oxaloacetate transport protein
- Dolichyl-phosphate-mannose--protein mannosyltransferase 5
- UDP-N-acetylglucosamine transporter YEA4
- Mannan polymerase I complex VAN1 subunit
- Probable alpha-1,6-mannosyltransferase MNN11
- Probable alpha-1,6-mannosyltransferase MNN10
- Mannan polymerase complexes subunit MNN9
Sequence:
MSVPKKRNHGKLPPSTKDVDDPSLKYTKAAPKCEQVAEHWLLQPLPEPESRYSFWVTIVTLLAFAARFYKIWYPKEVVFDEVHFGKFASYYLERSYFFDVHPPFAKMMIAFIGWLCGYDGSFKFDEIGYSYETHPAPYIAYRSFNAILGTLTVPIMFNTLKELNFRAITCAFASLLVAIDTAHVTETRLILLDAILIISIAATMYCYVRFYKCQLRQPFTWSWYIWLHATGLSLSFVISTKYVGVMTYSAIGFAAVVNLWQLLDIKAGLSLRQFMRHFSKRLNGLVLIPFVIYLFWFWVHFTVLNTSGPGDAFMSAEFQETLKDSPLSVDSKTVNYFDIITIKHQDTDAFLHSHLARYPQRYEDGRISSAGQQVTGYTHPDFNNQWEVLPPHGSDVGKGQAVLLNQHIRLRHVATDTYLLAHDVASPFYPTNEEITTVTLEEGDGELYPETLFAFQPLKKSDEGHVLKSKTVSFRLFHVDTSVALWTHNDELLPDWGFQQQEINGNKKVIDPSNNWVVDEIVNLDEVRKVYIPKVVKPLPFLKKWIETQKSMFEHNNKLSSEHPFASEPYSWPGSLSGVSFWTNGDEKKQIYFIGNIIGWWFQVISLAVFVGIIVADLITRHRGYYALNKMTREKLYGPLMFFFVSWCCHYFPFFLMARQKFLHHYLPAHLIACLFSGALWEVIFSDCKSLDLEKDEDISGASYERNPKVYVKPYTVFLVCVSCAVAWFFVYFSPLVYGDVSLSPSEVVSREWFDIELNFSK
Protein: Ammonium transporter (Q8TFN8)
Organism: Emericella nidulans (Aspergillus nidulans)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU362002}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362002}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSTYPVAYNGTGVNGGDSLREDLNIYYSSGDIAWVITSTALVLLMIPGVGFFYSGLARRKSALSLIWLSLMSIGVVSFQWFFWGYSLAFSHTAGKYIGNLDNFGFKGVLGAPSVGSTKVPDLLFAVFQGMFAAITVALAVGAVAERGRMLPCMVFVFIWSTIIYDPVACWTWNASGWVFQLGGLDFAGGTPVHIVSGTTALAYSLMLGKRRGHGTHELNYRPHNVTHVVIGTVFLWVGWFGFNAGSALSANLRAVMAAVVTNLAASVGGVTWCLLDYRLERKWSTVGFCSGVISGLVAITPGSGFVTPWAAFIFGVVGAAACNFATKVKYLIRVDDALDIFAVHGIGGLVGNLLTGLFAADYIAHLDGSTEIDGGWINHNYIQLGYQLADSVTGMAYSFFGSCIILFIINMIPGLSLRVPEEDEVLGIDDAEIGEFAYDYVELTRDVINGTTEPMDGASKRSTTPTGPVEPSPAELKA
Protein: Forkhead box protein L2 (Q8MIP2)
Organism: Capra hircus (Goat)
Function: Transcriptional regulator. Critical factor essential for ovary differentiation and maintenance, and repression of the genetic program for somatic testis determination (By similarity). Prevents trans-differentiation of ovary to testis through transcriptional repression of the Sertoli cell-promoting gene SOX9 (By similarity). Has apoptotic activity in ovarian cells (By similarity). Suppresses ESR1-mediated transcription of PTGS2/COX2 stimulated by tamoxifen (By similarity). Activates SIRT1 transcription under cellular stress conditions (By similarity). Activates transcription of OSR2 (By similarity). Is a transcriptional repressor of STAR (By similarity). Participates in SMAD3-dependent transcription of FST via the intronic SMAD-binding element (By similarity). Is a regulator of CYP19 expression.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}.
Interaction partners:
Sequence:
MMASYPEPEDASGALLAPETGRAAKEPEAPAPPSPGKGGGGGAGAAPEKPDPAQKPPYSYVALIAMAIRESAEKRLTLSGIYQYIIAKFPFYEKNKKGWQNSIRHNLSLNECFIKVPREGGGERKGNYWTLDPACEDMFEKGNYRRRRRMKRPFRPPPAHFQPGKGLFGAGGAAGGCGVAGAGADGYGYLAPPKYLQSGFLNNSWPLPQPPSPMPYASCQMAAAAAAAAAAAAAAGPGSPGAAAVVKGLAGPAASYGPYSRVQSMALPPGVVNSYNGLGGPPAAPPPPPHPHSHPHAHHLHAAAAPPPAPPHHGAAAPPPGQLSPASPATAAPPAPAPTNAPGLQFACARQPELAMMHCSYWDHDSKTGALHSRLDL
Protein: Thyroid hormone receptor alpha-A (zTRalpha-A) (Nuclear receptor subfamily 1 group A member 1-A) (Thyroid hormone receptor alpha-1) (TRalpha-1) (Q98867)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: High affinity receptor for triiodothyronine (By similarity). In the absence of thyroid hormone during late blastula stage development, acts as a transcriptional repressor. Whereas in the presence of thyroid hormone, can act as an activator of transcription. In addition, represses retinoic acid (RA)-signaling during blastula and gastrula stages of development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:9447705}.
Interaction partners:
- Thyroid hormone receptor alpha b
- Iodothyronine deiodinase
- Pro-thyrotropin-releasing hormone
- Thyroid-stimulating hormone subunit beta a.
- Iodothyronine deiodinase
- Solute carrier organic anion transporter family member
- Thyroglobulin.
- UDP-glucuronosyltransferase
- Monocarboxylate transporter 10
- Nuclear receptor corepressor 1.
Sequence:
MENTEQEHNLPEGDETQWPNGVKRKRKNSQCSMNSTSDKSISVPGYVPSYLEKDEPCVVCGDKATGYHYRCITCEGCKGFFRRTIQKNLHPSYSCKYDSCCIIDKITRNQCQLCRFRKCISVGMAMDLVLDDSKRVAKRRLIEENREKRKKEEIVKTLHNRPEPTVSEWELIRMVTEAHRHTNAQGPHWKQKRKFLPEDIGQSPAPTSDNDKVDLEAFSEFTKIITPAITRVVDFAKKLPMFSELPCEDQIILLKGCCMEIMSLRAAVRYDPESETLTLSGEMAVSREQLKNGGLGVVSDAIFDLGKSLSQFNLDDSEVALLQAVLLMSSDRSGLTCVEKIEKCQEMYLLAFEHYINHRKHNISHFWPKLLMKVTNLRMIGACHASRFLHMKVECPTELFPPLFLEVFEDQEGSTGVAAQEDGSCLR
Protein: Charged multivesicular body protein 2b (CHMP2.5) (Chromatin-modifying protein 2b) (CHMP2b) (Vacuolar protein sorting-associated protein 2-2) (Vps2-2) (hVps2-2) (Q9UQN3)
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.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16041373}. Late endosome membrane {ECO:0000305|PubMed:16041373}; Peripheral membrane protein {ECO:0000305|PubMed:16041373}.
Interaction partners:
- Vacuolar protein sorting-associated protein 4B
- Charged multivesicular body protein 3
- Charged multivesicular body protein 1a
- Charged multivesicular body protein 1b
- Charged multivesicular body protein 4a
- Charged multivesicular body protein 4b
- Charged multivesicular body protein 2a
- Vacuolar protein sorting-associated protein 4A
- Charged multivesicular body protein 6
- Charged multivesicular body protein 7
Sequence:
MASLFKKKTVDDVIKEQNRELRGTQRAIIRDRAALEKQEKQLELEIKKMAKIGNKEACKVLAKQLVHLRKQKTRTFAVSSKVTSMSTQTKVMNSQMKMAGAMSTTAKTMQAVNKKMDPQKTLQTMQNFQKENMKMEMTEEMINDTLDDIFDGSDDEEESQDIVNQVLDEIGIEISGKMAKAPSAARSLPSASTSKATISDEEIERQLKALGVD
Protein: RCG36947 (Rap2A-like protein) (Q78P65)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
Sequence:
MREYKVVVLGSGGVGKSALTVQFVTGTFIEKYDPTIEDFYRKEIEVDSSPSVLEILDTAGTEQFASMRDLYIKNGQGFILVYSLVNQQSFQDIKPMRDQIIRVKR