wanglab/gogpt-training-data huggingface dataset:
Protein: E3 ubiquitin-protein ligase AMFR (EC 2.3.2.36) (Autocrine motility factor receptor) (AMF receptor) (RING finger protein 45) (gp78) (Q9UKV5)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that mediates the polyubiquitination of lysine and cysteine residues on target proteins, such as CD3D, CYP3A4, CFTR, INSIG1, SOAT2/ACAT2 and APOB for proteasomal degradation. Component of a VCP/p97-AMFR/gp78 complex that participates in the final step of endoplasmic reticulum-associated degradation (ERAD). The VCP/p97-AMFR/gp78 complex is involved in the sterol-accelerated ERAD degradation of HMGCR through binding to the HMGCR-INSIG1 complex at the ER membrane. In addition, interaction of AMFR with AUP1 facilitates interaction of AMFR with ubiquitin-conjugating enzyme UBE2G2 and ubiquitin ligase RNF139, leading to sterol-induced HMGCR ubiquitination. The ubiquitinated HMGCR is then released from the ER into the cytosol for subsequent destruction. In addition to ubiquitination on lysine residues, catalyzes ubiquitination on cysteine residues: together with INSIG1, mediates polyubiquitination of SOAT2/ACAT2 at 'Cys-277', leading to its degradation when the lipid levels are low. Catalyzes ubiquitination and subsequent degradation of INSIG1 when cells are depleted of sterols. Mediates polyubiquitination of INSIG2 at 'Cys-215' in some tissues, leading to its degradation. Also regulates ERAD through the ubiquitination of UBL4A a component of the BAG6/BAT3 complex. Also acts as a scaffold protein to assemble a complex that couples ubiquitination, retranslocation and deglycosylation. Mediates tumor invasion and metastasis as a receptor for the GPI/autocrine motility factor. In association with LMBR1L and UBAC2, negatively regulates the canonical Wnt signaling pathway in the lymphocytes by promoting the ubiquitin-mediated degradation of CTNNB1 and Wnt receptors FZD6 and LRP6.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11724934, ECO:0000269|PubMed:22728137, ECO:0000269|PubMed:36593296}; Multi-pass membrane protein {ECO:0000269|PubMed:11724934}. Note=Palmitoylation promotes localization to the peripheral endoplasmic reticulum. {ECO:0000269|PubMed:22728137}.
Interaction partners:
- Transitional endoplasmic reticulum ATPase
- Ubiquitin-conjugating enzyme E2 G2
- Derlin-1
- Insulin-induced gene 1 protein
- Polyubiquitin-C
- Derlin-2
- Glucose-6-phosphate isomerase
- FAS-associated factor 2
- Protein OS-9
- Protein sel-1 homolog 1
Sequence:
MPLLFLERFPWPSLRTYTGLSGLALLGTIISAYRALSQPEAGPGEPDQLTASLQPEPPAPARPSAGGPRARDVAQYLLSDSLFVWVLVNTACCVLMLVAKLIQCIVFGPLRVSERQHLKDKFWNFIFYKFIFIFGVLNVQTVEEVVMWCLWFAGLVFLHLMVQLCKDRFEYLSFSPTTPMSSHGRVLSLLVAMLLSCCGLAAVCSITGYTHGMHTLAFMAAESLLVTVRTAHVILRYVIHLWDLNHEGTWEGKGTYVYYTDFVMELTLLSLDLMHHIHMLLFGNIWLSMASLVIFMQLRYLFHEVQRRIRRHKNYLRVVGNMEARFAVATPEELAVNNDDCAICWDSMQAARKLPCGHLFHNSCLRSWLEQDTSCPTCRMSLNIADNNRVREEHQGENLDENLVPVAAAEGRPRLNQHNHFFHFDGSRIASWLPSFSVEVMHTTNILGITQASNSQLNAMAHQIQEMFPQVPYHLVLQDLQLTRSVEITTDNILEGRIQVPFPTQRSDSIRPALNSPVERPSSDQEEGETSAQTERVPLDLSPRLEETLDFGEVEVEPSEVEDFEARGSRFSKSADERQRMLVQRKDELLQQARKRFLNKSSEDDAASESFLPSEGASSDPVTLRRRMLAAAAERRLQKQQTS
Protein: Polymerase acidic protein (EC 3.1.-.-) (RNA-directed RNA polymerase subunit P2) (P03433)
Organism: Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)
Function: Plays an essential role in viral RNA transcription and replication by forming the heterotrimeric polymerase complex together with PB1 and PB2 subunits. The complex transcribes viral mRNAs by using a unique mechanism called cap-snatching. It consists in the hijacking and cleavage of host capped pre-mRNAs. These short capped RNAs are then used as primers for viral mRNAs. The PB2 subunit is responsible for the binding of the 5' cap of cellular pre-mRNAs which are subsequently cleaved after 10-13 nucleotides by the PA subunit that carries the endonuclease activity.
Subcellular location: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04063}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04063}. Note=PB1 and PA are transported in the host nucleus as a complex. {ECO:0000255|HAMAP-Rule:MF_04063, ECO:0000269|PubMed:15308710, ECO:0000269|PubMed:22001919, ECO:0000269|PubMed:8113737}.
Interaction partners:
Sequence:
MEDFVRQCFNPMIVELAEKTMKEYGEDLKIETNKFAAICTHLEVCFMYSDFHFINEQGESIIVELGDPNALLKHRFEIIEGRDRTMAWTVVNSICNTTGAEKPKFLPDLYDYKENRFIEIGVTRREVHIYYLEKANKIKSEKTHIHIFSFTGEEMATKADYTLDEESRARIKTRLFTIRQEMASRGLWDSFRQSERGEETIEERFEITGTMRKLADQSLPPNFSSLENFRAYVDGFEPNGYIEGKLSQMSKEVNARIEPFLKTTPRPLRLPNGPPCSQRSKFLLMDALKLSIEDPSHEGEGIPLYDAIKCMRTFFGWKEPNVVKPHEKGINPNYLLSWKQVLAELQDIENEEKIPKTKNMKKTSQLKWALGENMAPEKVDFDDCKDVGDLKQYDSDEPELRSLASWIQNEFNKACELTDSSWIELDEIGEDVAPIEHIASMRRNYFTSEVSHCRATEYIMKGVYINTALLNASCAAMDDFQLIPMISKCRTKEGRRKTNLYGFIIKGRSHLRNDTDVVNFVSMEFSLTDPRLEPHKWEKYCVLEIGDMLIRSAIGQVSRPMFLYVRTNGTSKIKMKWGMEMRRCLLQSLQQIESMIEAESSVKEKDMTKEFFENKSETWPIGESPKGVEESSIGKVCRTLLAKSVFNSLYASPQLEGFSAESRKLLLIVQALRDNLEPGTFDLGGLYEAIEECLINDPWVLLNASWFNSFLTHALS
Protein: CD55 molecule (Cromer blood group) (A0A8I5ZMB7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MIRTRAPGTRAPPPPPLLLSLSLLLLLLSPTVSGDCGPPPDIPNATPNSGKHTKFAHQSQVTYSCNKGFKQIPDKPNTVVCLENDQWSNYETFCNKTCSAPLRLNYASLKKEYRNMNFFPIGTTVEFECRPGFQKVTSRTGKSTCLEELVWSPVVEFCKKRACPNPRELKNGHINIPTDILFGSEIIFSCDKGYKLVGVTSTFCSITGNAVDWDDVFPVCTTIFCPDPPKINNGRIREESDSYAYRQSVTYSCDQGFILVGNSSVHCTLNGEVGEWSSAPPKCIERHKVPTKTPPEVDIPSTMPHESTLINFPSTRAPLSHKPTTVKVPGTRVKPTSHKPTEVKVPATQHVPVSKTTVRHPTRTSKDRGESNSGGDHFIYGFVAVIVTIDSIILIKTLWWTILSSNRSSDLQGKKKRENVPE
Protein: Vacuolar protein sorting-associated protein 11 homolog (Q8SX81)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Late endosome membrane {ECO:0000250|UniProtKB:Q9H270}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H270}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9H270}. Lysosome membrane {ECO:0000250|UniProtKB:Q9H270}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H270}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9H270}.
Interaction partners:
- Vacuolar protein sorting-associated protein 41 homolog
- Vacuolar protein sorting-associated protein 8 homolog
- Vacuolar protein sorting-associated protein 39 homolog
- Vacuolar protein sorting-associated protein 16 homolog
- Vacuolar protein sorting-associated protein 18 homolog
- Vacuolar protein sorting 33B
- Vacuolar fusion protein CCZ1 homolog
- Ras-related protein Rab7
- LD27967p
- Vacuolar protein sorting-associated protein 33A
Sequence:
MDISVFEWKKVDLFNIIVVPFVKIPNTAEISCYCFPESKSSTEERNIKLVICDKNRNILIYLSNWECITFKSPSTRKAIALCSLTSNNSLATVTPDINNGIHIDIFDLNRLTKKQAAPIIASAYTQPSSTPLCLNADVIDDKLFALAIGLGNGDILLHYGKITKNFSANIRQHTVSGNAVNGIHFDFKTQPLDTTQIMFVTCVQGVYCFMLKEKCIMDTKFVLDNDKGNLNYRSIMCKAGGGEINDSMLVVGRADAVYCYTPEGRGPCFAIEGAKECLAWVGHYLIVGVKNSNLKQNATTLIVLDTENKIIVFQRQFQELFYVISENNFCYIVTNSGDTDACNMLMLEKNSIDVNIRLLVEKHMYNIALRLLHREGYTSSPETALVRFQYGNHLLQKGDFSRATQEFIKTIGFIKPYAVISKLLYSRYNTYLLNYLTEWKKKNESSSCHTRLIECCIKRDQIEHEMQQDDFKHYKSPAKIKHLATLSKMYFACTPSNQVPVEEEHLLHQLLEYGPASLAVDLTTYLNNITFENVKESKNILSFCSILADHNDYCAKMLAKIIEAFPVCDEKLLFYLLVFYFKLWRLDKVTSSFVSDFIKTHSLRMDKTIIVSRLYTFFNVTQRIHGHQKNTGTLHNETIDKCIENLIKNNPDVALNENLSKRSFLMMLKSSCSTEEIKAIKIKPIFKDRLLRSIVDSANELKLVENFNEKIKRSRSMLSLYTNNPIEFRNDKCDICREMLSMQSIYFLCQHSFHEECLNYKSTKRQEKFLCIICKTRNLLSPKHSSNFSCDSSDTIAVLAKIVSIGNKLETKLMIRGRQKSDGVTCNPFN
Protein: Zinc finger CCCH domain-containing protein 45 (AtC3H45) (Q94C33)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Zinc finger CCCH domain-containing protein 44
- Zinc finger CCCH domain-containing protein 43
- Zinc finger CCCH domain-containing protein 13
- tRNA-dihydrouridine
- Zinc finger CCCH domain-containing protein 55
- E3 ubiquitin-protein ligase makorin
- Zinc finger CCCH domain-containing protein 5
- Zinc finger CCCH domain-containing protein 18
- IQ domain-containing protein IQM3
- Vacuolar protein sorting-associated protein 32 homolog 1
Sequence:
MNNMKRSKKPRVSWPPGPKLCQVKVFRTEDSPANVASQPQRHSYPSRKPRGPDLPPGFEGNHYAVKPNVSNIPRIKWKRPPPKFSVNDTWLVGCGGGSSEWQNENLRISKVLEAIYPHRSAIPSRPSVSPAVEAECFDDSKTPAIRLTPIEDESESSSEESSNSKVESGVTANKQGQLETKPLCSTQEQVSGLTGLAPDLSLAASAALTALMKTKEQGSLVDTELLIKFLSDPKLIKNLITDTSGKSSETKNQPIVTNINSATRPVPQPVSAVTASPMARKPQPVIIPQEHSVAVSRSFTNPERRVSPPKPVNGSISPPKPITGKPSSIPMPVHFHVGIAKEQPQPARFPSSSLPMNLNFHRPPNVFSEPKVIVNPQPQHQPYSAFRTSEMNYVQSSIGLGRGPQTGFNSYPMNFSRADAIGSAKPVVQPMKGLDYFKNLIREHGTDNHETNQYHSQTGIFNGRIDNNNKIHQQCIYFGTANGCNMGDSCTYVHDRYRPNFEAAAPRAKRMKFGRYERNGF
Protein: DNA-binding protein Fis (D3GYQ2)
Organism: Escherichia coli O44:H18 (strain 042 / EAEC)
Interaction partners:
Sequence:
MFEQRVNSDVLTVSTVNSQDQVTQKPLRDSVKQALKNYFAQLNGQDVNDLYELVLAEVEQPLLDMVMQYTRGNQTRAALMMGINRGTLRKKLKKYGMN
Protein: Transcriptional regulator AguR (Q9I6J7)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- N-carbamoylputrescine amidohydrolase
- Agmatine deiminase
- DUF4350 domain-containing protein
- Purine nucleoside phosphorylase PA4543
- Probable periplasmic polyamine binding protein
- Chromosome partitioning protein ParA
- DUF3375 domain-containing protein
- Chromosome partitioning protein
- HDOD domain-containing protein
- Histidine kinase
Sequence:
MQPTSPTRKPRASSQARIAAILDAARGLLADEGIGGLSIYSVAERAEMPPSSVYHFFPSVPALLQGLTGEVHAAFRACLEQPVDHAGLRCWRDLSRIVEERMLAVYARDAAARQLILASHGLAEVTQADRQHDVQLGQAMRALFERHFLLPPLPTDIEIFSLAMELGDRVYALSVQRHGIIDARLAEEGMRVFDAYLGLYLPPILEKRSEPLSGFISDLNR
Protein: Receptor protein-tyrosine kinase (EC 2.7.10.1) (Q4PLA5)
Organism: Gallus gallus (Chicken)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MPAAAGGLLWWSCCVLAAAAGAPRAAAAQAVCAGTENKLSSLSDLEQQYRALRKYYENCEVVMGNLEITSIEHNRDLSFLRSIREVTGYVLVALNQFEYLPLENLRIVRGTKLYEDRYALAIFLNYRKDGNFGLRELGLKNLTEILNGGVYVGQNKFLCFADTIHWQDIVRNPWASNFTLVPTNGSSGCGRCHKSCTGRCWGPTENHCQTLTKTVCAEQCDGRCYGPYVSDCCHRECAGGCSGPKDTDCFACMNFNDSGACVTQCPQTFVYNPTTFQLEHNHNAKYTYGAFCVKKCPHNFVVDSSSCVRACPSSKMEVEENGIKMCKPCTDICPKACDGIGTGSLVSAQTVDSSNIDKFINCTKINGNLIFLVTGIHGDPYHTIAAINPEKLNIFQTVREITGYLNIQSWPENMTDFRVFSNLVTIGGRALYSGLSLLILKQQGITSLQFQSLKQISAGNIYITDNSNLCYYHTVNWTSLFSTPSQKTVIHRNKKAENCTADGMVCNELCSSDGCWGPGPDQCLSCKRFIRGRTCIESCNLYDGEFREFANGSVCMECDPQCEKMEDNMITCYGPGPDHCTKCFHFKDGPNCVEKCPDGLQGANSFIFKYADEDRECHPCHPNCTQGCRGPASHDCIYYPWTRQSTLPQHARTPLIAAGVIGGLFIIVIMGLTFAVYVRRKSIKKKRALRRFLETELVEPLTPSGTAPNQAQLRILKETELKRVKVLGSGAFGTVYKGIWVPEGETVKIPVAIKILNETTGPKANVEFMDEALIMASMDHPHLVRLLGVCLSPTIQLVTQLMPHGCLLDYVHEHKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLLEGDEKEYNADGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTFGGKPYDGIPIREIPDLLEKGERLPQPPICTIDVYMVMVKCWMIDADSRPKFKELAAEFSRMARDPQRYLVIQGDDRMKLPSPNDSKFFQNLLDEEDLEDMMDAEEYLVPQAFNIPPPIYTSRTRIDSNRNQFVYRDGGYAAEQGVPMPYRAPGCIIPEAPVAQGATAEIFEDTCCIGTLRKQVATLAKEDSSTQRYSADPTVFIPERVIRGELDEDGYMTPMRDKPKTDYLNPVEENPFVSRRKNGDLQAVDNPEYHNAPNGQPKAEDEYVNEPLYLNTFASTLENAEYLKNNLPEKAKKAFDNPDYWNHSLPPRSTLQHPDYLQEYSTKYFYKQNGRIRPIVAENPEYLSEFSLKPGTVLPPPPYRHRNTVV
Protein: NADH-cytochrome b5 reductase (EC 1.6.2.2) (B5X1Q9)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00037811}; Lipid-anchor {ECO:0000256|ARBA:ARBA00037811}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00037811}. Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00037821}; Lipid-anchor {ECO:0000256|ARBA:ARBA00037821}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00037821}.
Interaction partners:
Sequence:
MLSYIIGLIRSSIDNIINLILSLFLSKKKRAITLEDPNIKYALKLIDKEIISHDTRKFRFALREKDCVLGLPIGQHIYLSAKPDGVLVVRPYTPVSSDDDVGFVDLVVKIYYKNVNPKFPEGGKMSQYLESIRIGDTIDFRGPSGLLVYQGNGAFAIKAEKKAEPVIKTAKQVGMIAGGTGITPMLQIITAIMKDPQDQTVCHLLFANQTEKDILLRPELEEIAANHPTRFKLWFTLDRAPEDWEYSQGFISEEMVRDHLPPPGDDTLILLCGPPPMIQFACNPNLDKVGHASSRRFTF
Protein: Mitogen-activated protein kinase kinase kinase 17 (EC 2.7.11.25) (O80888)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the abscisic acid (ABA) signaling pathway that may act as ABA signal transducer in the context of abiotic stresses. Triggers MPK7 activation in a MKK3-dependent manner. Mediates the ABA-dependent activation of the MKK3-MPK7 module.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9ZVP5}.
Interaction partners:
- Mitogen-activated protein kinase kinase 3
- Mitogen-activated protein kinase kinase kinase 18
Sequence:
MEWTRGRILGRGSTATVYAAAGHNSDEILAVKSSEVHRSEFLQREAKILSSLSSPYVIGYRGSETKRESNGVVMYNLLMEYAPYGTLTDAAAKDGGRVDETRVVKYTRDILKGLEYIHSKGIVHCDVKGSNVVISEKGEAKIADFGCAKRVDPVFESPVMGTPAFMAPEVARGEKQGKESDIWAVGCTMIEMVTGSPPWTKADSREDPVSVLYRVGYSSETPELPCLLAEEAKDFLEKCLKREANERWTATQLLNHPFLTTKPDIEPVLVPGLISNSPTSVTDQTFWRSVEEEEEEETEEIQKDSRDLDRLSLWGCYSERIGRLKCVGGLDGTRCDMEGGDWIMVRARCEGTMISGSQKELIISENVLVGEL
Protein: Probable protein phosphatase 2C 26 (AtPP2C26) (EC 3.1.3.16) (O64730)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein phosphatase 2C 57
- Serine/threonine-protein kinase STN7, chloroplastic
- Peptidyl-prolyl cis-trans isomerase CYP38, chloroplastic
- Thioredoxin family protein
- Serine/threonine-protein kinase STN8, chloroplastic
- Probable protein phosphatase 2C 52
- Photosystem II CP43 reaction center protein
- Protein MAINTENANCE OF PSII UNDER HIGH LIGHT 1
- Thioredoxin-like protein AAED1, chloroplastic
- Protein disulfide-isomerase LQY1, chloroplastic
Sequence:
MAIPVTRMMVPHAIPSLRLSHPNPSRVDFLCRCAPSEIQPLRPELSLSVGIHAIPHPDKVEKGGEDAFFVSSYRGGVMAVADGVSGWAEQDVDPSLFSKELMANASRLVDDQEVRYDPGFLIDKAHTATTSRGSATIILAMLEEVGILKIGNVGDCGLKLLREGQIIFATAPQEHYFDCPYQLSSEGSAQTYLDASFSIVEVQKGDVIVMGSDGLFDNVFDHEIVSIVTKHTDVAESSRLLAEVASSHSRDTEFESPYALEARAKGFDVPLWKKVLGKKLTGGKLDDVTVIVAKVVSS
Protein: Constitutive coactivator of peroxisome proliferator-activated receptor gamma (Constitutive coactivator of PPAR-gamma) (Constitutive coactivator of PPARG) (Protein FAM120B) (Q6RI63)
Organism: Mus musculus (Mouse)
Function: Functions as a transactivator of PPARG and ESR1. Functions in adipogenesis through PPARG activation.
Subcellular location: Nucleus {ECO:0000269|PubMed:17595322}.
Interaction partners:
- Peroxisome proliferator-activated receptor gamma
- Programmed cell death protein 2
Sequence:
MGVRGLQGFVGSTCPHICTIVNIHELAERHRNKYPGCTPTIVVDAMCCLRYWYTAESWVCGGQWREYYCALRNFVAAFTSAGIKLIFFFDGMVEPGKRDEWVKRRLKNNREISKIFHYIKSKRDQPGRNMFFIPSGLAIFTRFALKTLGQETFCSLQEADYEVASYGLQHNCLGILGEDTDYLIYDTCPYFSIGDLCLESLQTIMLCREKLCESLGLRVADLPLLACLLGNDITPESMFESFRYKCLSSYASVKENAGKKGNIILAVSDYISKVLHLYQGEKKIEEMLPLGPNKALFYKGVTSYLLPGQKSPWLVQKPKGMITDKQQMVSLNPESKQEVPMCIDPEFKQEVPVCTNPESMQEVPMCMDPEPNQEASMCTDPESKQEVPMCTDSESKPEVSQYTNPESKQKLPSGIDTEFNLEALMCTHPEFKQEDVMDMEPEIKQVTMVSESEILKVARMHHVHSESYLVYNILSSGEIECSNTLEDELDQALPSQAFIYRPVRQRVYALLLGDWKDGASTGPVVKEWFVYPGNSLKHPDLVRPLQMTVQGGTPSLEVLWLSQEPAVQAQRLDTLLACFNLSSSREELQAVESPLRALCCLLIYLFVQVDTLSLEDLHAFIAQALCLQGKSTSQLMHLQLDYINSRAVQLGSLLVRGLTTLVLVNSACGFPWTTSEFMPWNVFDGKLFHQKYLQSEKGYAVEVLLEQNRSWLTKFHNLKAVVCKACSKENRRIVGRTHWDSPYTGRQGRQGYSSYRTDSTHGHSGQSWRNQGSGGRQHERNHWRRY
Protein: Matrix metalloproteinase-20 (MMP-20) (EC 3.4.24.-) (Enamel metalloproteinase) (Enamelysin) (O60882)
Organism: Homo sapiens (Human)
Function: Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix: aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation. Cleaves aggrecan at the '360-Asn-|-Phe-361' site.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- WD repeat-containing protein 72
- Kallikrein-4
- Enamelin
- Ameloblastin
- Amelogenin, X isoform
- Amelotin
- Protein FAM83H
- Hemopexin
- Odontogenic ameloblast-associated protein
- Odontogenesis associated phosphoprotein
Sequence:
MKVLPASGLAVFLIMALKFSTAAPSLVAASPRTWRNNYRLAQAYLDKYYTNKEGHQIGEMVARGSNSMIRKIKELQAFFGLQVTGKLDQTTMNVIKKPRCGVPDVANYRLFPGEPKWKKNTLTYRISKYTPSMSSVEVDKAVEMALQAWSSAVPLSFVRINSGEADIMISFENGDHGDSYPFDGPRGTLAHAFAPGEGLGGDTHFDNAEKWTMGTNGFNLFTVAAHEFGHALGLAHSTDPSALMYPTYKYKNPYGFHLPKDDVKGIQALYGPRKVFLGKPTLPHAPHHKPSIPDLCDSSSSFDAVTMLGKELLLFKDRIFWRRQVHLRTGIRPSTITSSFPQLMSNVDAAYEVAERGTAYFFKGPHYWITRGFQMQGPPRTIYDFGFPRHVQQIDAAVYLREPQKTLFFVGDEYYSYDERKRKMEKDYPKNTEEEFSGVNGQIDAAVELNGYIYFFSGPKTYKYDTEKEDVVSVVKSSSWIGC
Protein: Chanoclavine-I aldehyde reductase easA (EC 1.3.1.100) (Ergot alkaloid synthesis protein A) (Old yellow enzyme 3 homolog) (Q4WZ70)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Aldehyde reductase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid. DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan. The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde. EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline. EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine. Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A. Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus.
Interaction partners:
- Chanoclavine-I dehydrogenase easD
- Festuclavine dehydrogenase easG
- Catalase easC
- 4-dimethylallyltryptophan N-methyltransferase easF
- FAD-linked oxidoreductase easE
- Tryptophan dimethylallyltransferase
Sequence:
MREEPSSAQLFKPLKVGRCHLQHRMIMAPTTRFRADGQGVPLPFVQEYYGQRASVPGTLLITEATDITPKAMGYKHVPGIWSEPQREAWREIVSRVHSKKCFIFCQLWATGRAADPDVLADMKDLISSSAVPVEEKGPLPRALTEDEIQQCIADFAQAARNAINAGFDGVEIHGANGYLIDQFTQKSCNHRQDRWGGSIENRARFAVEVTRAVIEAVGADRVGVKLSPYSQYLGMGTMDELVPQFEYLIAQMRRLDVAYLHLANSRWLDEEKPHPDPNHEVFVRVWGQSSPILLAGGYDAASAEKVTEQMAAATYTNVAIAFGRYFISTPDLPFRVMAGIQLQKYDRASFYSTLSREGYLDYPFSAEYMALHNFPV
Protein: Protein CHLOROPLAST IMPORT APPARATUS 2 (Q9LU68)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Responsible for specific up-regulation of the translocon genes TOC33 and TOC75 in leaves. Involved in the general chloroplast protein import pathway regulation, including protein import and protein translation efficiencies.
Subcellular location: Plastid, chloroplast {ECO:0000305}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00357, ECO:0000269|PubMed:11549763}.
Interaction partners:
- MMS19 nucleotide excision repair protein homolog
- Protein NAR1
- Cytosolic Fe-S cluster assembly factor NBP35
- Protein AE7
- Activator of spomin::LUC2
- Translocase of chloroplast 33, chloroplastic
- Fe-S cluster assembly factor HCF101, chloroplastic
- Anamorsin homolog
- Protein TOC75-3, chloroplastic
- FAD/NAD
Sequence:
MSACLSSGGGGAAAYSFELEKVKSPPPSSSTTTTRATSPSSTISESSNSPLAISTRKPRTQRKRPNQTYNEAATLLSTAYPNIFSSNLSSKQKTHSSSNSHFYGPLLSDNDDASDLLLPYESIEEPDFLFHPTIQTKTEFFSDQKEVNSGGDCYGGEIEKFDFSDEFDAESILDEDIEEGIDSIMGTVVESNSNSGIYESRVPGMINRGGRSSSNRIGKLEQMMMINSWNRSSNGFNFPLGLGLRSALRENDDTKLWKIHTVDFEQISPRIQTVKTETAISTVDEEKSDGKKVVISGEKSNKKKKKKKMTVTTTLITESKSLEDTEETSLKRTGPLLKLDYDGVLEAWSDKTSPFPDEIQGSEAVDVNARLAQIDLFGDSGMREASVLRYKEKRRTRLFSKKIRYQVRKLNADQRPRMKGRFVRRPNESTPSGQR
Protein: Short transient receptor potential channel 1 (C0JJ14)
Organism: Sus scrofa (Pig)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MMAALYPSTDFSGASSSSLPSSPSSSSSPNEVMALKDVREVKEENTLNEKLFLLACDKGDYYMVKKILEENSSGDLNINCVDVLGRNAVTITIENENLDILQLLLDYGCQKLMERIQNPEYSTTMDVAPVILAAHRNNYEILTMLLKQDVSLPKPHAVGCECTLCSAKNKKDSLRHSRFRLDIYRCLASPALIMLTEEDPILRAFELSADLKELSLVEVEFRNDYEELARQCKMFAKDLLAQARNSRELEVILNHTSSDEPLDKRGLLEERMNLSRLKLAIKYNQKEFVSQSNCQQFLNTVWFGQMSGYRRKPTCKKIMTVLTVGIFWPVLSLCYLIAPKSQFGRIIHTPFMKFIIHGASYFTFLLLLNLYSLVYNEDKKNTMGPALERIDYLLILWIIGMIWSDIKRLWYEGLEDFLEESRNQLSFVMNSLYLATFALKVVAHNKFHDFADRKDWDAFHPTLVAEGLFAFANVLSYLRLFFMYTTSSILGPLQISMGQMLQDFGKFLGMFLLVLFSFTIGLTQLYDKGYTPKEQKDCVGIFCEQQSNDTFHSFIGTCFALFWYIFSLAHVAIFVTRFSYGEELQSFVGAVIVGTYNVVVVIVLTKLLVAMLHKSFQLIANHEDKEWKFARAKLWLSYFDDKCTLPPPFNIIPSPKTICYMISSLSKWICSHTSKGKVKRQNSLKEWRNLKQKRDENYQKVMCCLVHRYLTSMRQKMQSTDQATVENLNELRQDLSKFRNEIRDLLGFRTSKYAMFYPRN
Protein: UPAR/Ly6 domain-containing protein (Q9D8K1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MFWSSVSKSLLAVCVFTEFAVIFVESLSCENSMCTNGLCQPMGTCNTSKSCFSQTQEFKMPELSTSLSVQQKGCSLDECTGLAFSATLGDQRTFRYDQRCCTTDKCNQVDTKPSQVPAKANGVQCLACYMEAGRVCIPTPLKCTGSETKCVAVIGTAVGSSSPLSVVMVGSGCATESACNLNMTVLDFVNIRTFCSSGFPVLPTPSSAPDGLGLRSASISTVPVLISLLLLKVLV
Protein: 26S proteasome non-ATPase regulatory subunit 8 (26S proteasome regulatory subunit RPN12) (26S proteasome regulatory subunit S14) (Q9CX56)
Organism: Mus musculus (Mouse)
Function: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair.
Interaction partners:
- 26S proteasome regulatory subunit 10B
- 26S proteasome non-ATPase regulatory subunit 12
- 26S proteasome regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 3
- 26S proteasome regulatory subunit 6B
- 26S proteasome non-ATPase regulatory subunit 14
- 26S proteasome non-ATPase regulatory subunit 1
- 26S proteasome regulatory subunit 8
- 26S proteasome non-ATPase regulatory subunit 13
- 26S proteasome non-ATPase regulatory subunit 7
Sequence:
MFIKGRAAKTPRGEPRRSSRGGRKLAVVAPPPVLGSTSRPHFRRESIARRRCRKSGRRLAASRKMAATAATVNGSTTVSSSGPAATSVGILQAAAGMYEQLKDEWNRKNPNLSKCGEELGRLKLVLLELNFLPTTGTKLTKQQLILARDILEIGAQWSILCKDIPSFERYMAQLKCYYFDYKEQLPESAYMHQLLGLNLLFLLSQNRVAEFHTELERLPAKDIQTNVYIKHPVSLEQYLMEGSYNKVFLAKGNIPAESYTFFIDILLDTIRDEIAGCIEKAYEKILFAEATRILFFSTPKKMTDYAKKRGWVLGPNNYYSFASQQQKPEDSTIPSTELAKQVIEYARQLEMIV
Protein: Dynamitin homolog (p50 subunit of dynactin) (Eurofung) (C8V4E0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- P150 dynactin NUDM
- Arp11 homolog
- Dynactin subunit 4
- Dynactin subunit 5
- Cytoplasmic dynein intermediate chain
- F-actin-capping protein subunit beta
- Actin-related protein
- Dynein heavy chain, cytoplasmic
- Actin, gamma
- Dynein light intermediate chain
Sequence:
MAFNKKYAGLPDLDLAPDIYETPDLTDEASTVPTATLRTASNPDDTGSDSDIDREPVNADEARAHFLGATVDARHVNFSDSIATKRKSYRSKSRQRRKDTLADEEDSDEETESVERKLARLQREVEELKDEMAASQNRPTSESGDVSGEAKDTSDDSVEKLSQALDNLYASSRGLLQPHSAAALISRKLASAPTQASEVSGGQSKAAASTEAETTVPVAGILSHAASFDTRLALIESAMGISTSLNPFVTEGSSEPPLQPVLPALDHLNSRLSTLITLLVGPTPIPAVPTTSAAATSTAVTTPHLEMLSTRVRKLTADAEALASARKRALDSAKAAHSSRHRTASDFSSPIDPEQAAQRDEQATKIQALYATLPTIQSLHPILPSVLERLRSLRAIHAGAAQAAESLDELEKRQADMAGEIEQWQEGLKVVEEKMSQSEAALKSNIELVEPWVRDLEKRMEKLESGK