wanglab/gogpt-training-data huggingface dataset:
Protein: Protein folded gastrulation [Cleaved into: Protein folded gastrulation; G protein-coupled receptor ligand] (P40795)
Organism: Drosophila melanogaster (Fruit fly)
Function: Coordinates cell shape changes during formation of the ventral furrow and invagination of the posterior midgut primordium, by inducing apical constriction of cells in spatially and temporally defined manners. Could function as a secreted signal to initiate apical constriction by acting as a ligand for an unidentified G protein-coupled receptor, which in turn activates the G protein alpha subunit encoded by concertina, in neighboring cells. Such an intracellular pathway would ultimately induce contraction of the apical actin-myosin network. In the ventral furrow, fog appears to ensure that all the cells initiate constriction within several minutes of each other. In the posterior midgut invagination, fog appears to direct the ordered progression of constriction initiations out from a central region and also to delimit the peripheral extent of this spreading.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305}.
Interaction partners:
- Guanine nucleotide-binding protein subunit alpha homolog
Sequence:
MSPPNCLLAVLALTVFIGANNALPITSRPIEGNVQRMVWEDWVNLDPEQRNLTKEKKITAKSIFTLPFRHCPQGHTLFNQLCIPQSNIDPTDLVKQELILAGGSNGSPPPPPIGDYDYGDDEESEEIVYDLSVIPTAMQDGLPPSVGTGDQALPSEDAPLKFNIFEKKFPTGTGEHEEMPLPPDMAAATYAKNISTTPETSTSITPTSTTTFAVPSVPSGEASNRIPGGVDLLAAPSDAFSTSTTLSMPTSNTTTTSNKDIGQVESIVLPADQEHDGLVHLVTSSLSDNDSDDSSTTLNGFNAEADLAQLLKVDAFWPVYDGSIELLPPLFSHRKVAPPLSADQDVKTKHAVDAAEKVGAELEEEVGEEEVTATDILPSEEDEYTTETATTTGDTTVAEASMDTSTATSTSGQSSPHPPEEPEIDERENRLVLIKSKVQPVQLTTTTSATATTAADVANSSSSTDRFHYQHFVEDESSTTTATPEPSSSTPGDPIEQSDMPASDNDNLMTNTIGGRGDDDDDGGHKATSEIHVQQELRLINELVKGKQRQQHQPQKQQLEPTSTEITSALTSTSTEDATTTTTTTTAYTNWSKVMPQLGQSTSETAATTETVATSGQVNEISLTATSASTEVKHFSITNRSYRNSKIIREDRLTVEPEGIVESAASTESAGTAATTPNSSSNPDGYTPLWWLPSIGWRLDRHLDGNGEDQSLLLRFFSTFRGSNTAATTR
Protein: Tyrosine-specific transport system (Tyrosine permease) (Tyrosine:H(+) symporter) (P0AAD4)
Organism: Escherichia coli (strain K12)
Function: Transports tyrosine across the cytoplasmic membrane. The transport system is energized by the proton motive force.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:6090409}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- HTH-type transcriptional regulatory protein TyrR
- Aromatic amino acid transport protein AroP
- Trp operon repressor
- Shikimate kinase 2
Sequence:
MKNRTLGSVFIVAGTTIGAGMLAMPLAAAGVGFSVTLILLIGLWALMCYTALLLLEVYQHVPADTGLGTLAKRYLGRYGQWLTGFSMMFLMYALTAAYISGAGELLASSISDWTGISMSATAGVLLFTFVAGGVVCVGTSLVDLFNRFLFSAKIIFLVVMLVLLLPHIHKVNLLTLPLQQGLALSAIPVIFTSFGFHGSVPSIVSYMDGNIRKLRWVFIIGSAIPLVAYIFWQVATLGSIDSTTFMGLLANHAGLNGLLQALREMVASPHVELAVHLFADLALATSFLGVALGLFDYLADLFQRSNTVGGRLQTGAITFLPPLAFALFYPRGFVMALGYAGVALAVLALIIPSLLTWQSRKHNPQAGYRVKGGRPALVVVFLCGIAVIGVQFLIAAGLLPEVG
Protein: Ubiquitin conjugating enzyme E2 N (F8VV71)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAGLPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAGPQDSPFEGGTFKLELFLPEEYPMAAPKVRFMTKIYHPNVDKLGRICLDILKGKCYLYQHMLLLSFLLFLLSIPCLECKHYTKIREVCGREVKQFWACFFHALSYWACCLHR
Protein: Probable ubiquitin-conjugating enzyme E2 33 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme 33) (Ubiquitin carrier protein 33) (Q9FK29)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 6
- Ubiquitin-conjugating enzyme E2 34
- Ubiquitin-conjugating enzyme E2 22
- Probable ubiquitin-conjugating enzyme E2 26
- Probable ubiquitin-conjugating enzyme E2 16
- Ubiquitin-conjugating enzyme E2 27
- Probable ubiquitin-conjugating enzyme E2 25
- Probable ubiquitin-conjugating enzyme E2 17
- Probable ubiquitin-conjugating enzyme E2 18
- Ubiquitin-like modifier-activating enzyme atg7
Sequence:
MAEKACIKRLQKEYRALCKEPVSHVVARPSPNDILEWHYVLEGSEGTPFAGGFYYGKIKFPPEYPYKPPGITMTTPNGRFVTQKKICLSMSDFHPESWNPMWSVSSILTGLLSFMMDNSPTTGSVNTSVAEKQRLAKSSLAFNCKSVTFRKLFPEYVEKYSQQQVAEEEAATQQTTTSENQDFPQKDNAKVESEKSVGLKKESIQEVGLKERRRNKKEALPGWIVLLLVSIVGVVMALPLLQL
Protein: TAK1-associated binding protein 2, isoform C (A0A0B4KG87)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAATPPMPPGSNTHQLNGKTVGKGNPLAEAINQHFQRKKQNQHQSPNPSPNPNPNSPASRSGSYEQLELLDHATHPQQQQEASSGKAKPSCHCTNISIMHLFHEMKQEFPTIPDAIVTQCVNENCHQRENCIQMLRKELALHPIPVQSYPAKVLQQQQQQHHQNRQAKPPTPLKPSRIAPPQPEAVLSNGVATPPGVGSPHPDTQPRPRPTTLNLQRQFSTQLQQKIMQRQQRQQRDHQPAQLTPTSLSKPLRRAPPLPPPPKPKPGSFSNDSSCLTSPMSSSESELSLNAVPLSSPTSAAATAAAASAAIASTQQQPSPVRHRSVITLQPEPPYARDFRSIDFPPTTACTPRLPSPSSAASPSAPGGRKSFTSLNLTLRQPTGSAQSAIDITAGPAPSGQGSGITYSSVSFDARRGTQKNFQLTVTDEGSVFSAGSVRPRTLYATPCEPVTSVPANQQPPPPAAVVADGLGDADMTSDVFPYPTQEQNHIVASNYSNNHAVSDNNNIGISNSTDSSPTMPLYEGVMEECDREARAATIERQKQRRDKLANALRDNKKRLLVLEQEINILTEPVPVGESERLDRDIKQLTEDCNRLLDCLNEPQANGPGPAANPTNRQHLLPASNASQQQPQQQPQPFPRQRQSARVQAPPSSLRLHSVPAAPISQPVQDFGQHHSSAPTSACLTPQMQSQQQLLQLQQEPPPTYAQYYQFQQYLQQQRQQQLQQQMQQQQQLQHQMQQQQQPQPQQEEEFLSDSDVDEEEETLDSWACNMCTFRNHPQLNICEACENVRIQPAPVLSREDIHITLSPGENRIIHSWILS
Protein: Selenocysteine-tRNA-specific elongation factor, putative (Q583L1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Translation initiation factor, putative
- Elongation initiation factor 2 alpha subunit, putative
- Eukaryotic translation initiation factor 5, putative
- Eukaryotic translation initiation factor 3 subunit 8, putative
- Translation initiation factor, putative
- Eukaryotic translation initiation factor 3 subunit A
- Small ribosomal subunit protein uS5
- Eukaryotic translation initiation factor 1A, putative
- RNA-binding protein, putative
- 40S ribosomal protein S23, putative
Sequence:
MTEVNDVASVNINIGILGHVDSGKTSLARALSSTASTAAFDKSPESQRRGITLDLGFSATCVPTEGIAPDLFNAGIQQVQCTFVDCPGHASLIRTVLGGAQIIDMMILVIDACKGIQTQTAECIVIGEVLCKPLVLVINKVDAIQGSTSEEKRAAIDKLRKRLQKTFERTRWPSVAMVEVAAAPRREESGGTTCEGCMMSPINVEKVLPAVLSLVDADTIKRNKEAPLRPEDFVMMVDHCFALKGQGTVFTGTILRGQVSVGDSVVIPESHVVKKVKGLQVFRKPVQMARRGDRVGLSVVQFDAEGMERGLLCSALQQQQRQRSRADQAVHPVPVFESASVMVAEVSRVRFHQLPCNVHTKFHINIGHSTVMGTMRFFSRPTVCLPSDSQAGEELAEEPPFDLMQESQYVEELGEEAFITFECPSEDKHRWPGRPIAVKRGPLTYFAIVLLEKPILAAIGTPLIAARLDVERENMCRIALAGRVRALLHDDKDDAVMWRSMPIVRYKSRSLVVERVVSDRSCIASGVVTSEMHEARSGGGMSTNKKERDTKVKDALHAEVQKFIGLTVYFRPTSGDDGCCVNENGPGGLREGIIDSAFGKTGKVKLVFKEPVFAVDDRGAEAGKGKRNEVIFLSEGVVELTLKKYPLALHSQLQQ
Protein: Phorbol ester/diacylglycerol-binding protein unc-13 (G5EDN9)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MDDVGDYNDDQLSDGMSMRLLCITIKKARLQGAVDEFNSYVTVKLQTVKSTTVAVRGNLPCWEQEFIFETNRPDDGMVLELWAKGVLWDKLIGVHYMPLSEIRYSNAAGSGQWLQMDHELETRNGQTVGTRGPTGHNLLTDVRFELPFDVQGHDEDIQSRLLALNGLIEHDQLGPNNHHRAPFNHSGLSEDSDYTSDVSVPVNHHQLHPNSSAHQYESHLHPHRTRQLLHTREGATLQASYEDEEDAYHARHQPESDDYNHQDTYDQHSSYYNDEYAPSGSSSQYQRQGYQDQDQQHQNIYEDTVTPVREFGESAVPPAASSSRRQFDQVYGYASSSEERYDTPMSSGRLPRDEPILEHSEPEYVYDQNGYPEEDNYGINPTYSEDHFEGQTNDYSTTHQEPNDFRNDYNSSYQREYWNESEPLSYNSRPPNGHIRTGANTWREPSTSSRPTSSQAWNYQDDTHQYDEVDRGSRVSFTRTPSVDRTDRPSESGGGFYDEMSESGRPGRPDSHHNWRYDSIQEEDNEKDNWKQHVEGYEEGQEEKQKDNQKPNDHSAASPQDHYHRSDSTAQQDFGNNIVRQTIQEEEEKRNYQELWHNAYKRVCADLGIKSTVLDGNGSSAANAFYKSIDAAPNMNVARTKTSIPLVSELVLKTMATKRAQAGLANAARTTFSDTELKTHVYKKTLQALIYPISATTPHNFATTTFQTPTFCYECEGLLWGLARQGLRCTQCQVKVHDKCRELLSADCLQRAAEKSTKHGEADRTQSLVNVIRDRMKIQEQNKPEVFQMIRTVFDVDENIQKETLKTVKASILEGSSKWSAKITLTVLCAQGLIAKDKTGKSDPYVTAQVGKTKRRTRTIHQELNPVWNEKFHFECHNSTDRIKVRVWDEDNDLKSKLRQKLTRESDDFLGQTVIEVRTLSGEMDVWYNLEKRTDKSAVSGAIRLHINVEIKGEEKLAPYHVQYTCLHEHLFAAHCVDEEVKLPKVRGEDSWKVCFQETGQEIAEEFAMRYGIESIYQAMTHFACLCTRYMCAGVPAVLSTLLANINAYYAHTTATSAVSAPDRFAASNFGKERFVKLLDQLHNSLRIDLSAYRNHFPSSSPAKLQDLKSTVDLLTSITFFRMKVLELASPPRASTVVRECAKACMQQTYQLMFESCAEQFPILDTSVQFWYEFIDYIMRVIEEDQKNYTPALNQFPQELNVGNLSAETLWSMYKNDLKMALEEHAQKKRCKTPEYMNLYFKVKGFYFKYVADLSTYKSSIPEFPAWFIPFVMDWLNENDEHSMDILRNAYNVDKADNFPQTSEHTKFSNSVVDVFTQLNAALKLLKQMDCPNPEVAADMMKRFSKTLNKVLLAYADMVQKDFPKFAHDEKLACILMNNVQQLRVQLEKIYETMGGAELDEHIGQVLTVLQKKLNSVLDRLSAEFVTTLEPHIHEQTIKLGMLLVKIKGPQLQKTQVQPEADAVLEPLMDLLEGSLRRYADQCEKTVLKYILKELWKITIVNMEKRVVLPPLSDKALLKQLPNAKIGDVTKLMSTNIQSIKGMNSVKDMMDMARESEKSLTPRQCTVLDCALDAIKDSFHASGKGLKKSFFEKSPELQSLKYALSLYTQTTEQLIKTFITSQRQQDLPSQEQPVGEVSVQVDLFSHPGTGEQKVTVKILAANDLRWQTSSAFKPFVEVHLVGPHLSDKKRKWSTKTKAGNWAPKFNETFHFFLGNEGEPEHYELMFQVKDYCFARDDRVVGVGVLQLSSVVDQAGSCAMWVQLGTRLHIDETGLILLRILSQRQTDEVAKDFVRLKTECRYETETVMAASASSQNINRT
Protein: Centrosomal protein 131 (I3L2J8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKGTRAIGSVPERSPAGVDLSLTGLPPPVSRRPGSAATTKPIVRSVSVVTGSEQKRKVLEATGPGGSQAINNLRRSNSTTQVSQPRSGSPRPTEPTDFLMLFEGSPSGKKRPASLSTAPSEKGATWNVLDDQPRGFTLPSNARSSSALDSPAGPRRKECTVALAPNFTANNRSNKGAVGNCVTTMVHNRYTPSERAPPLKSSNQTAPSLNNIIKAATCEGSESSGFGKLPKNVSSATHSARNNTGGSTGLPRRKEVTEEEAERFIHQVNQATVTIQRWYRHQVQRRGAGAARLEHLLQAKREEQRQRSGEGTLLDLHQQKEAARRKAREEKARQARRAAIQELQQKRALRAQKASTAERGPPENPRETRVPGMRQPAQELSPTPGGTAHQALKANNTGGGLPAAGPGDRCLPTSDSSPEPQQPPEDRTQDVLAQDAAGDNLEMMAPSRGSAKSRGPLEELLHTLQLLEKEPDVLPRPRTHHRGRYAWASEVTTEDDASSLTADNLEKFGKLSAFPEPPEDGTLLSEAKLQSIMSFLDEMEKSGQDQLDSQQEGWVPEAGPGPLELGSEVSTSVMRLKLEVEEKKQAMLLLQRALAQQRDLTARRVKETEKALSRQLQRQREHYEATIQRHLAFIDQLIEDKKVLSEKCEAVVAELKQEDQRCTERVAQAQAQHELEIKKLKELMSATEKARREKWISEKTKKIKEVTVRGLEPEIQKLIARHKQEVRRLKSLHEAELLQSDERASQRCLRQAEELREQLEREKEALGQQERERARQRQRAELEELRQQLEESSSALTRALRAEFEKGREEQERRHQMELNTLKQQLELERQAWEAGRTRKEEAWLLNREQELREEIRKGRDKEIELVIHRLEADMALAKEESEKAAESRIKRLRDKYEAELSELEQSERKLQERCSELKGQLGEAEGENLRLQGLVRQKERALEDAQAVNEQLSSERSNLAQVIRQEFEDRLAASEEETRQAKAELATLQARQQLELEEVHRRVKTALARKEEAVSSLRTQHEAAVKRADHLEELLEQHRRPTPSTK
Protein: CAP-Gly domain-containing linker protein 3 (Cytoplasmic linker protein 170-related 59 kDa protein) (CLIP-170-related 59 kDa protein) (CLIPR-59) (Q96DZ5)
Organism: Homo sapiens (Human)
Function: Functions as a cytoplasmic linker protein. Involved in TGN-endosome dynamics. May modulate the cellular compartmentalization of AKT kinase family and promote its cell membrane localization, thereby playing a role in glucose transport in adipocytes.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24001771}; Lipid-anchor {ECO:0000269|PubMed:24001771}. Cytoplasm {ECO:0000269|PubMed:24001771}. Golgi apparatus, Golgi stack {ECO:0000269|PubMed:24001771}. Note=Localized to Golgi stacks as well as on tubulovesicular elements juxtaposed to Golgi cisternae.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase CYLD
Sequence:
MTKTDPAPMAPPPRGEEEEEEEEDEPVPEAPSPTQERRQKPVVHPSAPAPLPKDYAFTFFDPNDPACQEILFDPQTTIPELFAIVRQWVPQVQHKIDVIGNEILRRGCHVNDRDGLTDMTLLHYACKAGAHGVGDPAAAVRLSQQLLALGADVTLRSRWTNMNALHYAAYFDVPDLVRVLLKGARPRVVNSTCSDFNHGSALHIAASSLCLGAAKCLLEHGANPALRNRKGQVPAEVVPDPMDMSLDKAEAALVAKELRTLLEEAVPLSCALPKVTLPNYDNVPGNLMLSALGLRLGDRVLLDGQKTGTLRFCGTTEFASGQWVGVELDEPEGKNDGSVGGVRYFICPPKQGLFASVSKISKAVDAPPSSVTSTPRTPRMDFSRVTGKGRREHKGKKKTPSSPSLGSLQQRDGAKAEVGDQVLVAGQKQGIVRFYGKTDFAPGYWYGIELDQPTGKHDGSVFGVRYFTCPPRHGVFAPASRIQRIGGSTDSPGDSVGAKKVHQVTMTQPKRTFTTVRTPKDIASENSISRLLFCCWFPWMLRAEMQS
Protein: Phosphatidylinositol 4-kinase PIK1 (PI4-kinase) (PtdIns-4-kinase) (EC 2.7.1.67) (P39104)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts on phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol 1,4,5,-trisphosphate. PIK1 is part of a nuclear phosphoinositide cycle and could control cytokinesis through the actin cytoskeleton. Involved in the response to mating pheromone.
Subcellular location: Nucleus {ECO:0000269|PubMed:8194527}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:19898464}.
Interaction partners:
- Phosphatidylinositol 4-kinase LSB6
- Calcium-binding protein NCS-1
- Phosphatidylinositol 4-phosphate 5-kinase MSS4
- Phosphatidylinositol-3-phosphatase SAC1
- GTP-binding protein YPT31/YPT8
- ADP-ribosylation factor 1
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Phosphatidylinositol 4-kinase STT4
- GTP-binding protein YPT32/YPT11
- Polyphosphatidylinositol phosphatase INP53
Sequence:
MHKASSSKKSFDDTIELKKNEQLLKLINSSEFTLHNCVELLCKHSENIGIHYYLCQKLATFPHSELQFYIPQLVQVLVTMETESMALEDLLLRLRAENPHFALLTFWQLQALLTDLSTDPASYGFQVARRVLNNLQTNLFNTSSGSDKNVKIHENVAPALVLSSMIMSAIAFPQLSEVTKPLVESQGRRQKAFVFKLARSAMKDFTKNMTLKNTLLNKKTSRSKRVSSNRSSTPTSPIDLIDPIKTKEDASFRKSRHSEVKLDFDIVDDIGNQVFEERISSSIKLPKRKPKYLDNSYVHRTYDGKNINRDGSISNTAKALDGNKGDYISPKGRNDENNEIGNNEDETGGETEEDADALNSDHFTSSMPDLHNIQPRTSSASSASLEGTPKLNRTNSQPLSRQAFKNSKKANSSLSQEIDLSQLSTTSKIKMLKANYFRCETQFAIALETISQRLARVPTEARLSALRAELFLLNRDLPAEVDIPTLLPPNKKGKLHKLVTITANEAQVLNSAEKVPYLLLIEYLRDEFDFDPTSETNERLLKKISGNQGGLIFDLNYMNRKENNENRNESTLTSNNTRSSVYDSNSFNNGASRNEGLSSTSRSDSASTAHVRTEVNKEEDLGDMSMVKVRNRTDDEAYRNALVIQSAANVPILPDDSQDRSPELNFGSNLDEVLIENGINSKNIHSQTDALADQMRVSAVMLAQLDKSPQQLSESTKQIRAQIISSMKEVQDKFGYHDLEALHGMAGERKLENDLMTGGIDTSYLGEDWATKKERIRKTSEYGHFENWDLCSVIAKTGDDLRQEAFAYQMIQAMANIWVKEKVDVWVKRMKILITSANTGLVETITNAMSVHSIKKALTKKMIEDAELDDKGGIASLNDHFLRAFGNPNGFKYRRAQDNFASSLAAYSVICYLLQVKDRHNGNIMIDNEGHVSHIDFGFMLSNSPGSVGFEAAPFKLTYEYIELLGGVEGEAFKKFVELTKSSFKALRKYADQIVSMCEIMQKDNMQPCFDAGEQTSVQLRQRFQLDLSEKEVDDFVENFLIGKSLGSIYTRIYDQFQLITQGIYS
Protein: CUG triplet repeat, RNA binding protein 1, isoform CRA_c (CUGBP Elav-like family member 1) (G5EA30)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAAFKLDFLPEMMVDHCSLNSSPVSKKMNGTLDHPDQPDLDAIKMFVGQVPRTWSEKDLRELFEQYGAVYEINVLRDRSQNPPQSKGCCFVTFYTRKAALEAQNALHNMKVLPGMHHPIQMKPADSEKNNAVEDRKLFIGMISKKCTENDIRVMFSSFGQIEECRILRGPDGLSRGCAFVTFTTRAMAQTAIKAMHQAQTMEGCSSPMVVKFADTQKDKEQKRMAQQLQQQMQQISAASVWGNLAGLNTLGPQYLALYLQLLQQTASSGNLNTLSSLHPMGGLNAMQLQNLAALAAAASAAQNTPSGTNALTTSSSPLSVLTSSAGSSPSSSSSNSVNPIASLGALQTLAGATAGLNVGSLAGMAALNGGLGSSGLSNGTGSTMEALTQAYSGIQQYAAAALPTLYNQNLLTQQSIGAAGSQKEGPEGANLFIYHLPQEFGDQDLLQMFMPFGNVVSAKVFIDKQTNLSKCFGFVSYDNPVSAQAAIQSMNGFQIGMKRLKVQLKRSKNDSKPY
Protein: Immunity-related GTPase family Q protein (Q8WZA9)
Organism: Homo sapiens (Human)
Subcellular location: Lysosome {ECO:0000269|PubMed:39481378}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:39481378}.
Interaction partners:
Sequence:
MPPPQGDVTALFLGPPGLGKSALIAALCDKDVETLEAPEGRPDSGVPSLRAAGPGLFLGELSCPPAAPGPWAAEANVLVLVLPGPEGNGEPLAPALGEAALAALARGTPLLAVRNLRPGDSQTAAQARDQTAALLNSAGLGAADLFVLPANCGSSDGCEELERLRAALQSQAEALRRLLPPAQDGFEVLGAAELEAVREAFETGGLEAALSWVRSGLERLGSARLDLAVAGKADVGLVVDMLLGLDPGDPGAAPASVPTAPTPFPAPERPNVVLWTVPLGHTGTATTAAAASHPTHYDALILVTPGAPTEKDWAQVQALLLPDAPLVCVRTDGEGEDPECLGEGKMENPKGESLKNAGGGGLENALSKGREKCSAGSQKAGSGEGPGKAGSEGLQQVVGMKKSGGGDSERAAALSPEDETWEVLEEAPPPVFPLRPGGLPGLCEWLRRALPPAQAGALLLALPPASPSAARTKAAALRAGAWRPALLASLAAAAAPLPGLGWACDVALLRGQLAEWRRGLGLEPTALARRERALGLASGELAARAHFPGPVTRAEVEARLGAWAGEGTAGGAALGALSFLWPAGGAAATGGLGYRAAHGVLLQALDEMRADAEAVLAPPEPAQ
Protein: General transcription factor IIH subunit 1 (Basic transcription factor 2 62 kDa subunit) (BTF2 p62) (General transcription factor IIH polypeptide 1) (TFIIH basal transcription factor complex p62 subunit) (Q9DBA9)
Organism: Mus musculus (Mouse)
Function: Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription.
Subcellular location: Nucleus.
Interaction partners:
- General transcription and DNA repair factor IIH helicase subunit XPD
- General transcription factor IIH subunit 4
- CDK-activating kinase assembly factor MAT1
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- General transcription factor IIH subunit 3
- General transcription factor IIH subunit 2
- General transcription factor IIE subunit 1
- General transcription factor IIH subunit 5
- General transcription factor IIE subunit 2
- Cyclin-H
Sequence:
MATSSEEVLLIVKKVRQKKQDGALYLMAERIAWAPEGKDRFTISHMYADIKCQKISPEGKAKIQLQLVLHAGDTTNFHFSNESTAVKERDAVKDLLQQLLPKFKRKANKELEEKNRMLQEDPVLFQLYKDLVVSQVISAEEFWANRLNVNATDSSTSSHKQDVGISAAFLADVRPQTDGCNGLRYNLTSDIIESIFRTYPAVKMKYAETVPHNMTEKEFWTRFFQSHYFHRDRLNTGSKDLFAECAKIDEKGLKTMVSLGVKNPMLDLTSLEDKPLDEGYSISSVPSTSNSKSIKENSNAAIIKRFNHHSAMVLAAGLRKQQAQNGQNGEPSSVDGNSGDTDCFQPAVKRAKLQESIEYEDLGNNNSVKTIALNLKKSDRYYHGPTPIQSLQYATSQDIINSFQSIRQEMEAYTPKLTQVLSSSAASSTITALSPGGALMQGGTQQAVNQMVPNDIQSELKHLYVAVGELLRHFWSCFPVNTPFLEEKVVKMKSNLERFQVTKLCPFQEKIRRQYLSTNLVSHIEEMLQTAYNKLHTWQSRRLMKKT
Protein: Apolipoprotein C-III (Apo-CIII) (ApoC-III) (Apolipoprotein C3) (P06759)
Organism: Rattus norvegicus (Rat)
Function: Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma. Plays a multifaceted role in triglyceride homeostasis. Intracellularly, promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and secretion; extracellularly, attenuates hydrolysis and clearance of triglyceride-rich lipoproteins (TRLs). Impairs the lipolysis of TRLs by inhibiting lipoprotein lipase and the hepatic uptake of TRLs by remnant receptors. Formed of several curved helices connected via semiflexible hinges, so that it can wrap tightly around the curved micelle surface and easily adapt to the different diameters of its natural binding partners.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P02656}.
Interaction partners:
- Apolipoprotein C-I
- Apolipoprotein A-II
- Apolipoprotein B-100
- Apolipoprotein C-II
- Apolipoprotein A-IV
- Apolipoprotein E
- Apolipoprotein A-V
- Apolipoprotein C-I-like.
- Beta-2-glycoprotein 1
- Lipoprotein lipase
Sequence:
MQPRMLLIVALVALLASARADEGEGSLLLGSMQGYMEQASKTVQDALSSMQESDIAVVASRGWMDNRFKSLKGYWSKFTDKFTGLWESGPEDQLTTPTLEP
Protein: Casein kinase I homolog hhp2 (EC 2.7.11.1) (P40236)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in DNA repair. May regulate the activity of protein(s) involved in double strand break repair caused by gamma rays.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Casein kinase I homolog hhp1
- Protein LTV1
- Uncharacterized protein C13G1.09
- Serine/threonine-protein kinase rio2
- Protein kinase gsk31
- Ribosome biogenesis protein tsr1
Sequence:
MTVVDIKIGNKYRIGRKIGSGSFGQIYLGLNTVNGEQVAVKLEPLKARHHQLEYEFRVYNILKGNIGIPTIRWFGVTNSYNAMVMDLLGPSLEDLFCYCGRKFTLKTVLLLADQLISRIEYVHSKSFLHRDIKPDNFLMKKHSNVVTMIDFGLAKKYRDFKTHVHIPYRDNKNLTGTARYASINTHIGIEQSRRDDLESLGYVLLYFCRGSLPWQGLQADTKEQKYQRIRDTKIGTPLEVLCKGLPEEFITYMCYTRQLSFTEKPNYAYLRKLFRDLLIRKGYQYDYVFDWMILKYQKRAAAAAAASATAPPQVTSPMVSQTQPVNPITPNYSSIPLPAERNPKTPQSFSTNIVQCASPSPLPLSFRSPVPNKDYEYIPSSLQPQYSAQLRRVLDEEPAP
Protein: Complex III assembly factor LYRM7 (LYR motif-containing protein 7) (Q5U5X0)
Organism: Homo sapiens (Human)
Function: Assembly factor required for Rieske Fe-S protein UQCRFS1 incorporation into the cytochrome b-c1 (CIII) complex. Functions as a chaperone, binding to this subunit within the mitochondrial matrix and stabilizing it prior to its translocation and insertion into the late CIII dimeric intermediate within the mitochondrial inner membrane.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:23168492}.
Interaction partners:
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Iron-sulfur cluster co-chaperone protein HscB
- Acyl carrier protein, mitochondrial
- Tetratricopeptide repeat protein 19, mitochondrial
- Large ribosomal subunit protein uL23m
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein mL46
- Mitochondrial chaperone BCS1
Sequence:
MGRAVKVLQLFKTLHRTRQQVFKNDARALEAARIKINEEFKNNKSETSSKKIEELMKIGSDVELLLRTSVIQGIHTDHNTLKLVPRKDLLVENVPYCDAPTQKQ
Protein: Large ribosomal subunit protein eL43A (60S ribosomal protein L43-A) (L37A) (Q9HGL8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein eL18A
- Large ribosomal subunit protein eL21A
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL29
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein eL39
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL6
- Small ribosomal subunit protein uS17A
Sequence:
MTKRTKKVGVTGKYGVRYGASLRRDVRKIEVQQHSRYQCPFCGRNTVKRTAAGIWCCNGKGCKKVLAGGAWTVTTAAATSARSTIRRLREMVEV
Protein: LPS-assembly protein LptD (Q83SQ0)
Organism: Shigella flexneri
Function: Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane.
Subcellular location: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_01411}.
Interaction partners:
- LPS-assembly lipoprotein LptE
- Lipopolysaccharide export system protein LptA
- Chaperone SurA
- Lipopolysaccharide export system protein LptC
- Lipopolysaccharide export system permease protein LptF
- Outer membrane protein assembly factor BamA
- Lipopolysaccharide export system ATP-binding protein LptB
- Putative permease, YjgP/YjgQ family
- Conserved hypothetical protein.
- Conserved hypothetical protein
Sequence:
MKKRIPTLLATMIATALYSQQGLAADLASQCMLGVPSYDRPLVQGDTNDLPVTINADHAKGDYPDDAVFTGSVDIMQGNSRLQADEVQLHQKEAPGQPEPVRTVDALGNVHYDDNQVILKGPKGWANLNTKDTNVWEGDYQMVGRQGRGKADLMKQRGENRYTILDNGSFTSCLPGSDTWSVVGSEIIHDREEQVAEIWNARFKVGPVPIFYSPYLQLPVGDKRRSGFLIPNAKYTTTNYFEFYLPYYWNIAPNMDATITPHYMHRRGNIMWENEFRYLSQAGAGLMELDYLPSDKVYEDEHPNDDSSRRWLFYWNHSGVMDQVWRFNVDYTKVSDPSYFNDFDNKYGSSTDGYATQKFSVGYAVQNFNATVSTKQFQVFSEQNTSSYSAEPQLDVNYYQNDVGPFDTRIYGQAVHFVNTRDDMPEATRVHLEPTINLPLSNNWGSINTEAKFLATHYQQTNLDWYNSRNTTKLDESVNRVMPQFKVDGKMVFERDMEMLAPGYTQTLEPRAQYLYVPYRDQSDIYNYDSSLLQSDYSGLFRDRTYGGLDRIASANQVTTGVTSRIYDDAAVERFNISVGQIYYFTESRTGDDNITWENDDKTGSLVWAGDTYWRISERWGLRGGIQYDTRLDNVATSNSSIEYRRDEDRLVQLNYHYASPEYIQATLPKYYSTAEQYKNGISQVGAVASRPIADRWSIVGAYYYDTNANKQADSMLGVQYSSCCYAIRVGYERKLNGWDNDKQHAVYDNAIGFNIELRGLSSNYGLGTQEMLRSNILPYQNTL
Protein: Dual specificity protein kinase lkh1 (EC 2.7.12.1) (Q10156)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Protein kinase that may act as a negative regulator of filamentous growth and flocculation. Appears to have a role in normal cell wall and septum formation and in cell separation. May have antagonistic function in the regulation of beta-glucan distribution between the sites for cell wall and septum assembly.
Interaction partners:
- RNA-binding post-transcriptional regulator csx1
- Leucine-rich repeat-containing protein sog2
- Protein kinase dsk1
- Transcriptional repressor tup12
- Transcriptional repressor tup11
- Maintenance of ploidy protein mob2
Sequence:
MHSLKRRRNHAPDWQDFYKNGVPQEVIVIEDSASPRLTPNLPPPFSVHQLQSFVPPQPPSSSSPSTTGTVAVPINGANAVYPSTNSVSLPQSYDPWLDANGVVPLPHDVASHPSYMVQSPTSYHACSNNQSPFPHSHHPPLHNPLPVSCQPVLRPPPVPQVPSHWYPVSLPSPNLPHQPISKPPVIPNLPKLQVHPNRLPHPIHNHPYSSPTSYPPPLCPATYCPSNPPQLAPATAIAPSSQSSQHKSVNYSVTPSSINNHTAVPLSPTLAVWLPMTQPTFQPPSANVYQPASNANQVITPVSISDYRPPKKRKRAAWPPYKKVDRVNVPVVHDTTAFDPSTFDDDDGHYKVVPNSKFANRYTVVRLLGHGTFGKVIQCYDQSTGRHCAIKVTRAIPKYREASLIELRVLQTIAHSDPTNENKCIQLRDYFDYRKHICIVTDLFGWSVFDFLKNNNYIPFPLKHIQMLSQQLFKSVAFLHSLGLVHTDLKPENVLLVSNASRTIRLPYRNYSQKVLNSCEIRLIDFGSATFEDEYHSSVVSTRHYRAPEIILGLGWSYPCDVWSIGCILVELFTGQALFQTHEDSEHLCMMEKILGPFDRNMISRSSRTSQRFFKSDGKVRYPLSNTPKKSINYLQSLQTLEQIFAVSSPEVALLLDLLKKVFVYDPKRRITAKEALWHPFFTQPISSNL