wanglab/gogpt-training-data huggingface dataset:
Protein: Autophagy protein 5 (Q12380)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in cytoplasm to vacuole transport (Cvt) and autophagic vesicle formation. Autophagy is essential for maintenance of amino acid levels and protein synthesis under nitrogen starvation. Required for selective autophagic degradation of the nucleus (nucleophagy). Also required for mitophagy, which eliminates defective or superfluous mitochondria in order to fulfill cellular energy requirements and prevent excess ROS production. Conjugation with ATG12, through a ubiquitin-like conjugating system involving ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 and ATG8 association to the vesicle membranes. ATG12-ATG5 rearranges the ATG3 catalytic center and enhances its E2 activity. Plays a role in the regulation of filamentous growth and chronological longevity.
Subcellular location: Preautophagosomal structure membrane {ECO:0000269|PubMed:11689437, ECO:0000269|PubMed:15155809, ECO:0000269|PubMed:17295840, ECO:0000269|PubMed:18497569, ECO:0000269|PubMed:23064152, ECO:0000269|PubMed:23549786}; Peripheral membrane protein {ECO:0000269|PubMed:11689437, ECO:0000269|PubMed:15155809, ECO:0000269|PubMed:17295840, ECO:0000269|PubMed:18497569, ECO:0000269|PubMed:23064152, ECO:0000269|PubMed:23549786}. Note=Localizes to the isolation membrane (IM), a membrane sac which is generated from the pre-autophagosomal structure (PAS). Ultimately, the IM expands to become a mature autophagosome. Also localizes to a dot at the junction between the IM and the vacuolar membrane, termed the vacuole-IM contact site (VICS). Correct localization to the PAS requires ATG21.
Interaction partners:
- Ubiquitin-like protein ATG12
- Autophagy-related protein 8
- Putative lipase ATG15
- Autophagy-related protein 3
- Serine/threonine-protein kinase ATG1
- Autophagy protein 16
- Ubiquitin-like modifier-activating enzyme ATG7
- Cysteine protease ATG4
- Autophagy-related protein 18
- Ubiquitin-like-conjugating enzyme ATG10
Sequence:
MNDIKQLLWNGELNVLVSIDPSFLMKGSPREIAVLRIRVPRETYLVNYMPLIWNKIKSFLSFDPLTDSEKYFWFEHNKTPIPWNYPVGVLFDCLAGKSATFTTSFENQVKDVLTFLRIHLVMGDSLPPTIIPIASSKTQAEKFWFHQWKQVCFILNGSSKAIMSLSVNEARKFWGSVITRNFQDFIEISNKISSSRPRHIPLIIQTSRTSGTFRISQPTISMTGVNPTLKDIEGDILDVKEGINGNDVMVICQGIEIPWHMLLYDLYSKLRSFDGFLYITLVPIKGGDKASSEL
Protein: Nuclear transition protein 2 (TP-2) (TP2) (P11378)
Organism: Mus musculus (Mouse)
Function: Plays a key role in the replacement of histones to protamine in the elongating spermatids of mammals. In condensing spermatids, loaded onto the nucleosomes, where it promotes the recruitment and processing of protamines, which are responsible for histone eviction. The histone H2AB1-H2BC1/TH2B dimer is required for loading of TNP2 onto chromatin.
Subcellular location: Nucleus {ECO:0000269|PubMed:15163613}. Chromosome {ECO:0000269|PubMed:28366643}. Note=Loaded onto the nucleosomes of condensing spermatids (PubMed:28366643). Inclusion of the H2AB1-H2BC1/TH2B dimer into chromatin opens the nucleosomes, releasing the nucleosomal DNA ends and allowing the invasion of nucleosomes by transition protein TNP2 (PubMed:28366643). Nuclear import is mediated by IPO4. Nucleolar localization requires the protein to be phosphorylated (By similarity). {ECO:0000250|UniProtKB:P11101, ECO:0000269|PubMed:28366643}.
Interaction partners:
- Spermatid nuclear transition protein 1
- Protamine-2
- Protamine-3
- Sperm protamine P1
- Testis-specific H1 histone
Sequence:
MDTKMQSLPTTHPHPHSSSRPQSHTSNQCNQCTCSHHCRSCSQAGHAGSSSSPSPGPPMKHPKPSVHSRHSPARPSHRGSCPKNRKTFEGKVSKRKAVRRRKRTHRAKRRSSGRRYK
Protein: Lpc53E1 (I4AY78)
Organism: uncultured bacterium
Interaction partners:
Sequence:
MKSRLNDILEAGIASGAAPGAVAIVVNADGVLWEGAAGERAVGTGRSMTTDTVGAIFSMTKAITGAAAMQLVEQNRLDLDAPAGEIIPWLNEVQVLDGFDDSGEPVLRAPNSPVTLRNLLTHTSGFTYEFWNANEARWKEKTGALSLFTLENAALQTPLAFDPGTQWEYGIGIDWVGKMVEAVSGMTLGEYFAEYLTGPLGMTDTAFTHSASMLERASAVHARLPDGTFQTIDLPQPENQEFEMGGGGLQGTMHDYGKFIRMILNDGELNGVRVLRSETVATMCENHIGDLRVQKLVTVAPTITNDAEFFPGRPKSWGLTFQINERAEDTGRPAGTLMWAGVLNSFFWIDRTNGVGGAYLSQMLPFADARSLGLFYDIERAVYQSLA
Protein: GH04604p (Q8MSK4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
FVLGSISISDSEFANRHGQHSSHLLCRTRAPWPPQCHHQAQPGRFPGPDRRGDHRLQNSGQRSQEGRLRRLLLEVRCQQVLRAHEGRRSFPVLLGYVIPKHK
Protein: Scaper protein (Q501L8)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MASFQRSNSHDKVRRIVAEEGRTARNLIAWSVPLESKDDDGKPKCQTGGKSKRTIQGTHKTTKQNTAVECKITSTTGEKHFDKSPTKTRHPRKIDLRARYWAFLFDNLRRAVDEIYVTCESDQSVVECKEVLMMLDYYVRDFKALIDWIQLQEKLEKTDAQSRPTSLAWEVKKMSPGRHVIQSPSTDRMNVTSTARRSLNFGSLPGAVTAPCLAPTGVSWADKVKAHHTGSAPPEATPAQSCAPMTVQKTSRKNERKDAEGWETVQRGRPVRSRSTAVIPKVSLVTETLRSKDDSDKENICLLPEESIQKGKLEDRCSTVESLSKDSLLHSSDHPLSERTQFTVCILDDVKNSGSSQDSSVHTSEIPAIDSDAVCVAPQNTTALPTDRVPAETTGMVTEMTDPSDISNSMAEVLAKKEELADRLEKANEEAIASAIAEEEQLTREIEAEENNDINIETDNDSDFSASMGSGSLSFCGVSLDWNDVLADYEARESWRQNTSWGDIVEEEPARLPGHGIHMHEKLSSPSRKRTIAESKKKYEEKHMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHASTDYAPKLTPYERKKQCSLCNVLIASEVYLFSHIKGKKHQQAVRENSSIQGRELSDEEVEHLSLKKYVVDIVIESAAPPEPVKDGEERQKKKKK
Protein: Fructose-bisphosphate aldolase (EC 4.1.2.13) (Q9CPQ9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MPCPYPALTTEQKKELSDIAHRIVAPGKGILAADESIGSMGNRLQSIGTENTEENRRFFRQLLLTADDRVNPCIGGVILFHETLYEKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGKHTPSPLAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLSCCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACTQKFSNEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKEENLKAAQEEYIKRALANSLACQGKYTPSGKTGATASESLFISNHAY
Protein: Probable proteasome subunit alpha type-3 (Q09682)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable proteasome subunit beta type-7
- Probable proteasome subunit beta type-4
- Probable proteasome subunit beta type-2
- Probable proteasome subunit beta type-1
- Probable proteasome subunit alpha type-5
- 26S proteasome regulatory subunit rpn10
- Probable proteasome subunit beta type-3
- Probable proteasome subunit alpha type-2
- Probable proteasome subunit alpha type-6
- 26S proteasome regulatory subunit rpn11
Sequence:
MSRSYDSRTTIFSPEGRLYQVEYALEAINHAGVALGIVAKDGIVLAAEKKVTSKLLEQEESAEKLYHIGDNMLCAVAGLTADANILINYARRVGQQYLQTFNEEMPCEQLVRRVCDLKQGYTQYGGLRPFGVSFLYAGWDHIRGYQLFQSNPSGNYGSWQANSIGGNSTSVQSLMRQEYKDDINLDEASAMAVKFLSKTLDSNSLTHEKIEFATITKDTTKNKMVCKIWKSDEINEVLNKYQETQRQS
Protein: Copper transport protein (M9NE97)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|RuleBase:RU367022}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU367022}.
Interaction partners:
- P-type Cu
- Copper transport protein ATOX1
- Superoxide dismutase
- Protein Malvolio
Sequence:
MDHAHHSAPGVDHSMHHDHVGMHHDHSGIPAATASPMDAASMFDLIPDTSDLQASHAGHAAHGAHNHGGGSGTGMEHMMPMAFHFGYNETILFSWWHIETVAGLIGSMIAIFLLALMYEGLKYYREYLFWKTYNLLEYRPVTGPQRNPEAPRIPSPAAAAPSPVQYVGEVVHKQPPSMLSINHLLQTLLHVLQVTLSFLLMLIFMTYNVWLCLMVVLGAAVGYFLFCWKKSVIVDVTEHCH
Protein: EG:133E12.4 protein (Enhanced adult sensory threshold, isoform E) (Enhanced adult sensory threshold, isoform F) (O46048)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LD42063p
- Bonus, isoform C
Sequence:
MSSRKVPGGSGGADESTAAAAPLDDNANASVEIPDSSEEPAMGVGEEMSIISKTRTSTLSVEPAKEPTVTAELEGEKELESNPVSKTPRSTPTPTLTPAVTPTASDGVAAKSVRVTRHSSPLLLIISPTTSRREVGDGELDTEEPTGSGGQRKSSVERSLAPVIRGRKSIKDLKEAKEVKSEEPPAAASESRAASGVTPGQVKEQHVADGNEMESLPITDKKDHKDTKDKGDERETDQEEEKEKSADTEIIADTEKTSEKQKYTEKDKAADKDGGKEKDIDANKDIDKEKEKVKEVLPPVVPIAPVTPTCNRVTRKSHAQEQAINTRVTRNRRQSSTVGANSTASLVAASSSVTEQPPPSRGRRKKPVVVAPPLEPAVKRKRSQDVEADSDANNSTKYSKVEVVKSEEAEAPEEDSSAVPIKQESVDGNEVSSISPTVTPTPTPAPTPAPVPGSRRGRGRPQNRNSSSPATTTRATRLSKAGSPVILTPVAQEPAPPKRRRVGSSTRKTVSASSLAPSSQGGAGDEDSKDSMASSMDDLLMAAADIKQEKLTPDFDDSLMPEGLPSTSGASSANGHSCTEPLTVDTEINVKPADSKVKPKESPVVAVEESPSQSETQSAKVSAHAGKAPSLSPDMISEGVSAVSVRKFYKKPEFLENNLGIEKDPELGEIVQTVSNNDTETDVEMAVDGEVNQPSTPKSQDKKKEEQEKNQKSGLKAAKKAPAKLEPKAEDISEILTDVPVDISTEAVEIIEEAEEDTCSNSSIKPGELRLDESNDEPELLLEDALIVNGDENETPDQPEEKEDQVEFFHTGEYDDFEHEIMVELAKEGVLDASGNALSQQKVELEHPEDVTLHESKNDIEAEESVERKPLKDPSVADEMEDMNEESYIDIKDQTNQLLVEHLAEEAMEADCGPEDNKENLSTSASSTAADGLDIQLAIKEDDDEEKPLAVIADEQKPGLLLTNDMKVDEKPNGKQESVCDEHVQLVPNLRQEQEIHLQNLGLLTHQAAEHRRKCLLEAQARQAQMQLQQHHHHQHKRQGARGGGSATHVESSGTLKTVIKLNRSSNGGVSGSGGLPTGTVIHGGCGSSSASSTSSSSVGSATRKSSGTLGSGAGAGAGVRRQSLKMTFQKGRARGHGAADRSADQYGAHAEDSYYTIQNENEGAKKFVVTTGNTGRKTNNRFSSTNNYHSTVALHGSNSALQYYSSHSESQGQTDHGFYQMVKKDEKEKILIPEKASSFKFHPGRLCEDQCYYCSGKFGLYDTPCHVGQIKSVERQQKILANEEKLTVDNCLCDACFRHVDRRANVPSYKKRLSASGHLEMGSAAGSALEKQFAGDSGVITESGGEAGSTAAVAVQQRSCGVKDCVEAARHSLRRKCIRKRVKKYQLSLEIPAGSSNVGLCEAHYNTVIQFSGCVLCKRRLGKNHMYNITTQDTIRLEKALSEMGIPVQLGMGTAVCKLCRYFANLLIKPPDSTKAQKAEFVKNYRKRLLKVHNLQDGSHELSEADEEEAPNATETERPTSDGHEDPEMPMVADYDGPTDSNSSSSSTAALDTSKQMSKLQAILQQNVGADAAGAAGTGTVAASPGGSGSGADISNVLRGNPNISMRELFHGEEELGVQFKVPFGCSSSQRTPEGWTRVQTFLQYDEPTRRLWEELQKPYGNQSSFLRHLILLEKYYRNGDLVLAPHASSNATVYTETVRQRLNSFDHGHCGGLNIAGSPSSSGSGKRSGVPQPTGASVLATALTTPLTSHSSSSASISSEQHSSVDPVIPLVDLNDDDEGEDGAGGAGERESTNRQQDVILECLRTASVDKLTKQLSSNAVTIIARPKDKSQLSCNSGSSTSISSSSSAISSPEEVAVTKVTAVAPVQSKDAPPLAPASSGVSNSRSILKTNLLGMNKAVELVPLTTAPHAYKPTGCHKPEKQQKILDVANKQPGSQGEPVPSSALLGLQSKLKPPTHQQQVSGSGAGTSGSQKPSNVAQLLSSPPELISLHRRQTSGAAAGSSSFLQGKRLQLPRSGAGPSGAGTGTGAGAAGSRSAGGPPPPNVVILPDALTPQERHESKSWKPTLIPLEDQHKVPNKSHALYQTADGRRLPALVQVQSGGKPYLISIFDYNRMCILRREKLMRDQLLKSNAKPKPQNQQQQQGQTHQQQQNSAASAAAFSNMVKLAQQHTARQQLQQLQQKPQQQQQLPTLQPGGVRLARLPQKLLMPPLTNPQIGSQAPNLQPLLSSTLDNSNNCWLWKNFPDPNQYLLNGNGGGAGSSSSKLPHLTAKPATATSSSGAANKSAGSLFTLKQQQHQQKLIDNAIMSKIPKSLTVIPQQMGGNTGGDMGGSSSSGKD
Protein: Vacuolar basic amino acid transporter VSB1 (Vacuolar storage of basic amino acids 1) (P53273)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:32776922}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}. Note=Localizes to the vacuolar membrane both under nitrogen replete and deplete conditions. {ECO:0000269|PubMed:32776922}.
Interaction partners:
- Sulfate permease 2
- Sulfate permease 1
- Uncharacterized protein YGR045C
- GTP-binding protein YPT1
- Putative uncharacterized protein YDR250C
- Protein ISD11
Sequence:
MGRTIRRRRSNSSLSEAISVSLGINQDSSVNKMHRASVSAMSPPLCRSYMSGFFTGGNSPMINNLSDSKLPISNKQHPKVIHGSENLHRQTAQLSNEFCSSSVEENSPTIKDYMDIIGNGDRKDDQSMRTIEENIDEEYSDEYSRLLLSPASSNVDDDRNRGLQNSSLPELEDGYAGGYQSLRPSHNLRFRPRNLWHMCTSFPSKFAHYLPAAVLGLLLNILDALSYGMIIFPITEPVFSHLGPTGISMFYISTIISQAVYSGGWSSFPSGIGSEMIEITPFYHTMALAIKEALAGNDDEIITTTIFCYVISSMLTGVVFYALGKLRLGKIVGFFPRHILIGCIGGVGYFLIITGIEVTTRVAKFEYSWPFFSGLFTDYDTLAKWLLPVLLTVVLIGTQRYFKNSLVLPSFYILTLVLFHFIVAIIPTLSLDALRQAGWIFPIANSDSKWYDHYRLFNVHKVHWSLVLQQIPTMMALTFFGILHVPINVPALAMSLQMDKYDVDRELIAHGYSNFFSGLLGSVQNYLVYTNSVLFIRAGADSPFAGFLLIALTICIMIIGPVIISFIPICIVGSLIFLLGYELLVEALVDTWNKLNRFEYLTVVIIVFTMGIFDFVLGIIVGILIACFSFLVDSTKLQTINGEYNGNVARSTVYRDYVQTKFLDGIGEQIYVLKLQNLLFFGTIISIEEKIERLLQISNKDATKRRIKYLILDFKNINADNIDYSAAEGFNRIKRFTETKRIKLIISSIKERDRIYNAFNNVGLLNDVELFADLNSALEWCENEFLFQYKQLRKKAKERLEEGKQNNVVSAVIAATKNKKIDTIGNGLNRGSNGDTARNLMSLPTNTPRNYQILSVAQNVFVNDEQAVKNFKKEYKDDEPVLPILLFALKQYRPDIISEVQKVREKEIKFWAQLCPYFTRRRLASQSHLLHADNIFFLVETGMLKATYELPQGTLYEIFSNGTCFGKIIAPGNAMPREQKLTIETETDSVLWVIDSSSLNKLKEDNLALYVEVALMVMCIKDTRFKELLGYTLVSA
Protein: ABC transporter ced-7 (Cell death protein 7) (P34358)
Organism: Caenorhabditis elegans
Function: Functions in the engulfment of cell corpses during embryonic programmed cell death to translocate molecules that mediate homotypic adhesion between cell surfaces of the dying and engulfing cells.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cell death protein 6
- CED-5
- Cell death abnormality protein 12
- Ras-related protein ced-10
- Cell death abnormality protein 2
- Cell death abnormality protein 1
- Transthyretin-like protein 52
- Cell death abnormality protein 8
- Nose resistant to fluoxetine protein 5
- Cell death protein 3
Sequence:
MNRLRQFSLLLWKDWVLLRRNKVWTLFELIIPCLLLGPLVYLVVKNADHTSSPENIYDNFQVKGTVEDVFLESNFIKPIYKRWCLRSDVVVGYTSKDAAAKRTVDDLMKKFAERFQSAKLKLSVKNESSEEQLLTVLRNDLPMLNETFCAINSYAAGVVFDEVDVTNKKLNYRILLGKTPEETWHLTETSYNPYGPSSGRYSRIPSSPPYWTSAFLTFQHAIESSFLSSVQSGAPDLPITLRGLPEPRYKTSSVSAFIDFFPFIWAFVTFINVIHITREIAAENHAVKPYLTAMGLSTFMFYAAHVVMAFLKFFVIFLCSIIPLTFVMEFVSPAALIVTVLMYGLGAVIFGAFVASFFNNTNSAIKAILVAWGAMIGISYKLRPELDQISSCFLYGLNINGAFALAVEAISDYMRRERELNLTNMFNDSSLHFSLGWALVMMIVDILWMSIGALVVDHIRTSADFSLRTLFDFEAPEDDENQTDGVTAQNTRINEQVRNRVRRSDMEIQMNPMASTSLNPPNADSDSLLEGSTEADGARDTARADIIVRNLVKIWSTTGERAVDGLSLRAVRGQCSILLGHNGAGKSTTFSSIAGIIRPTNGRITICGYDVGNEPGETRRHIGMCPQYNPLYDQLTVSEHLKLVYGLKGAREKDFKQDMKRLLSDVKLDFKENEKAVNLSGGMKRKLCVCMALIGDSEVVLLDEPTAGMDPGARQDVQKLVEREKANRTILLTTHYMDEAERLGDWVFIMSHGKLVASGTNQYLKQKFGTGYLLTVVLDHNGDKRKMAVILTDVCTHYVKEAERGEMHGQQIEIILPEARKKEFVPLFQALEAIQDRNYRSNVFDNMPNTLKSQLATLEMRSFGLSLNTLEQVFITIGDKVDKAIASRQNSRISHNSRNASEPSLKPAGYDTQSSTKSADSYQKLMDSQARGPEKSGVAKMVAQFISIMRKKFLYSRRNWAQLFTQVLIPIILLGLVGSLTTLKSNNTDQFSVRSLTPSGIEPSKVVWRFENGTIPEEAANFEKILRKSGGFEVLNYNTKNPLPNITKSLIGEMPPATIGMTMNSDNLEALFNMRYYHVLPTLISMINRARLTGTVDAEISSGVFLYSKSTSNSNLLPSQLIDVLLAPMLILIFAMVTSTFVMFLIEERTCQFAHQQFLTGISPITFYSASLIYDGILYSLICLIFLFMFLAFHWMYDHLAIVILFWFLYFFSSVPFIYAVSFLFQSPSKANVLLIIWQVVISGAALLAVFLIFMIFNIDEWLKSILVNIFMFLLPSYAFGSAIITINTYGMILPSEELMNWDHCGKNAWLMGTFGVCSFALFVLLQFKFVRRFLSQVWTVRRSSHNNVQPMMGDLPVCESVSEERERVHRVNSQNSALVIKDLTKTFGRFTAVNELCLAVDQKECFGLLGVNGAGKTTTFNILTGQSFASSGEAMIGGRDVTELISIGYCPQFDALMLDLTGRESLEILAQMHGFENYKAKAELILECVGMIAHADKLVRFYSGGQKRKISVGVALLAPTQMIILDEPTAGIDPKARREVWELLLWCREHSNSALMLTSHSMDECEALCSRIAVLNRGSLIAIGSSQELKSLYGNNYTMTLSLYEPNQRDMVVQLVQTRLPNSVLKTTSTNKTLNLKWQIPKEKEDCWSAKFEMVQALAKDLGVKDFILAQSSLEETFLRLAGLDEDQLDTHSTVEISHSTHV
Protein: Mannose-1-phosphate guanylyltransferase catalytic subunit beta (EC 2.7.7.13) (GDP-mannose pyrophosphorylase B) (GTP-mannose-1-phosphate guanylyltransferase beta) (Q7JZB4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Mannose-1-phosphate guanylyltransferase regulatory subunit alpha
- Phosphomannomutase
- Dolichol-phosphate mannosyltransferase subunit 1
- GDP-mannose 4,6 dehydratase
- ALG1, chitobiosyldiphosphodolichol beta-mannosyltransferase
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Dolichol-phosphate mannosyltransferase subunit 3
- Eukaryotic translation initiation factor 2 subunit 2
- Eukaryotic translation initiation factor 2 subunit 1
- UDP-glucose 6-dehydrogenase
Sequence:
MCGNPAVGNGTRALILVGGYGTRLRPLTLSTPKPLVEFANKPILLHQLEALVDAGCRQVILAVSYRAEQMEKELKVEAKKLGVELIFSHETEPLGTAGPLALAKTILAASSEPFFVLNSDVICDFPFKQLVQFHCNHGKEGTIVVTKVEEPSKYGVVLYDENGCIKNFIEKPQEFVSNKINAGIYIFNPSVLDRIEVKPTSIEKEVFPEMTQQQELYAMDLTGFWMDIGQPKDFLTGMCLYLSSLRQKQSPKLYTGPGVVGNVLVDPTAKIGEGCRIGPNVTIGPDVVIEDGVCIKRSTILKGAIVRSHSWLDSCIVGWRSTVGRWVRIEGITVLGEDVIVKDELYINGGQVLPHKSIAASVPEPQIIM
Protein: UDP-galactose/UDP-glucose transporter 7 (AtUTr7) (Q94B65)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Nucleotide-sugar transporter that transports UDP-glucose and UDP-galactose. Plays a role in lateral root and root hair development.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:22933714}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Solute carrier family 35 protein
- Arginine-glutamic acid dipeptide repeat protein
- Protein SPEAR1
- Protein SIEL
- Cationic amino acid transporter 7
Sequence:
MEVQAEMEPTSSISLVAAVSYGIASMAMVFINKAVIMQYPHSMTVLTLQQLATSLLIHFGRRMGYTRAKGIDMATAKKLLPVSIFYNANVAFALASLKGVNIPMYIAIKRLTPLAVLISGVLFGKGKPTTQVALSVLLTAAGCVIAALGDFSFDLFGYGLALTSVFFQTMYLVLVEKSGAEDGLSSIEIMFYNSFLSLPFLSILIIVTGEFPNSLSLLLAKCSYLPFLVILILSLVMGIVLNFTMFLCTIVNSALTTTIVGVLKGVGSTTLGFVLLGGVEVHALNVSGLVVNTAGGVWYSYAKYRQKKAKPAKLMSDLEAHKK
Protein: Kelch repeat and BTB domain-containing protein 7 (Q8WVZ9)
Organism: Homo sapiens (Human)
Function: As part of the CUL3(KBTBD6/7) E3 ubiquitin ligase complex functions as a substrate adapter for the RAC1 guanine exchange factor (GEF) TIAM1, mediating its 'Lys-48' ubiquitination and proteasomal degradation. By controlling this ubiquitination, regulates RAC1 signal transduction and downstream biological processes including the organization of the cytoskeleton, cell migration and cell proliferation. Ubiquitination of TIAM1 requires the membrane-associated protein GABARAP which may restrict locally the activity of the complex.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:25684205}. Nucleus {ECO:0000305|PubMed:25684205}.
Interaction partners:
- Cullin-3
- Kelch repeat and BTB domain-containing protein 6
- Kelch repeat and BTB domain-containing protein 8
- E3 ubiquitin-protein ligase RBX1
- Speckle-type POZ protein-like
- BTB/POZ domain-containing protein KCTD17
- Kelch-like protein 9
- Kelch-like protein 42
- Kelch-like protein 8
- Kelch-like protein 20
Sequence:
MQSREDVPRSRRLASPRGGRRPKRISKPSVSAFFTGPEELKDTAHSAALLAQLKSFYDARLLCDVTIEVVTPGSGPGTGRLFSCNRNVLAAACPYFKSMFTGGMYESQQASVTMHDVDAESFEVLVDYCYTGRVSLSEANVQRLYAASDMLQLEYVREACASFLARRLDLTNCTAILKFADAFDHHKLRSQAQSYIAHNFKQLSRMGSIREETLADLTLAQLLAVLRLDSLDIESERTVCHVAVQWLEAAAKERGPSAAEVFKCVRWMHFTEEDQDYLEGLLTKPIVKKYCLDVIEGALQMRYGDLLYKSLVPVPNSSSSSSSSNSLVSAAENPPQRLGMCAKEMVIFFGHPRDPFLCYDPYSGDIYTMPSPLTSFAHTKTVTSSAVCVSPDHDIYLAAQPRKDLWVYKPAQNSWQQLADRLLCREGMDVAYLNGYIYILGGRDPITGVKLKEVECYSVQRNQWALVAPVPHSFYSFELIVVQNYLYAVNSKRMLCYDPSHNMWLNCASLKRSDFQEACVFNDEIYCICDIPVMKVYNPARGEWRRISNIPLDSETHNYQIVNHDQKLLLITSTTPQWKKNRVTVYEYDTREDQWINIGTMLGLLQFDSGFICLCARVYPSCLEPGQSFITEEDDARSESSTEWDLDGFSELDSESGSSSSFSDDEVWVQVAPQRNAQDQQGSL
Protein: Homeobox protein nob-1 (G5EFY5)
Organism: Caenorhabditis elegans
Function: Transcription factor, involved in posterior embryonic patterning, morphogenetic movements of the posterior hypodermis, and cell fate specification. Binds to the 5'-TAGT-3' motif in regulatory elements of genes, including Meis protein psa-3 and microRNA mir-57. Involved in a negative regulatory loop with mir-57 to specify posterior cell identities. Required for asymmetric division of the T hypodermal cell, acting via the regulation of asymmetric expression of psa-3 in cooperation with ceh-20 and the Wnt-MAPK pathway. Involved in the regulation of the onset of non-apoptotic cell death in the linker cell, acting together with the Wnt signaling pathway. Involved in promoting embryogenesis, in concert with orphan nuclear receptor nhr-25. May regulate expression of transcription factor dmd-3.
Subcellular location: Nucleus {ECO:0000255|RuleBase:RU000682}.
Interaction partners:
- Homeobox protein ceh-20
- Homeobox protein ceh-40
- Transcriptional coregulator psa-3
- C2H2-type domain-containing protein
- T-box transcription factor tbx-8
- Nuclear hormone receptor family member nhr-25
- Homeobox protein unc-62
- T-box transcription factor tbx-9
- Homeobox protein ceh-60
Sequence:
MISVMQQMINNDSPEDSKESITSVQQTPFFWPSAAAAIPSIQGESRSERESETGSSPQLAPSSTGMVMPGTAGMYGFGPSRMPTANEFGMMMNPVYTDFYQNPLASTGWYSYGQPYQFTANYSIPSLDGNLSDITIPTTAGSSAATTPNAAMHLPWAISHDGKKKRQPYKKDQISRLEYEYSVNQYLTNKRRSELSAQLMLDEKQVKVWFQNRRMKDKKLRQRHSGPFPHGAPVTPCIERLIN
Protein: Survival of motor neuron-related-splicing factor 30 (Survival motor neuron domain-containing protein 1) (Q95RI7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}. Nucleus, Cajal body {ECO:0000256|ARBA:ARBA00004408}.
Interaction partners:
- Pre-mRNA-processing factor 6
- Probable U2 small nuclear ribonucleoprotein A'
- Probable ATP-dependent RNA helicase DDX46
- Survival of motor neuron-related-splicing factor 30
- Splicing factor 45
- PHD finger-like domain-containing protein 5A
- U1 small nuclear ribonucleoprotein A
- LD21442p
- Splicing factor 3A subunit 2
- Poly
Sequence:
MADDLHNYKLQLQQVEAALQTDPENEELLKLRSDLDEVITLTRDLIQTQLEEQNKSSYVEPSSTKRDSSNYFDEIEAALLEAEKLVSAAKIWKKGDKCQAKWKEDRQYYDATIEDISSTGEVNVIFDAYQNRSTTHVNELRERTIRNEVFPSNKRHRPNQKEYLKKRKQKKQQRFKDLEEERESDKNKWLNFNNKNQKKNGMKARSIFASPDNVSGRVGVGTCGTAGKGMTDFTVGEKYRKGL
Protein: Neurexin 2a alpha (Neurexin 2a precursor) (A1XQX4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MMTRKWRCVKLSPAFVWLGLVVLSVTTALEFDGLPGQWVRYGPWEAGATGELSFTMKTNISKAIVLYLDDGGNCDFLELLINDGRLQLRFAIHCGEPASLHMETHISDERWHRVLLTRNYRETMLVMDGESKVAEVKSKRREMMVASDLYVGGIPPDVRLSALTSSTVKYEPPFRGLIANLKLGETAPALLDSQGVKNDLDYLCTKQNPCSNGGRCSIQGSEVLCDCSNTGYKGKYCTEVLQQVLGGLAHLTLKSQAPGAAPLMATPAAGDPKSGQVESVATFKGNEFFSYDLSQKPIQSSTDEITLSFRTLQRNGLLLHTGKSADYVNLSLKSGAVCLVINLGSGAFEALVEPSDGKFNDNAWHAVRVSRNLRQRAGVGLPTVNKLHYMVTISVDGLLTTTGYTQEDYTMLGSDDFFYVGGSPNTADLPGSPVSNNFMGCLKDVVYTNNEFRLELSHLAELRDPKVTLHGDLTFRCEDVAALDPVSFDAPTAYVTLPRWNGKKAGSVSFDFRTTEPNGLLLFSHGRPQGSKDHRPRVDFFAMELLDGFLHLLMDMGSGSIKIKVGNKKVNDGEWCHVDFQREGRKGSISVNGRSLPFSTNEGSEILDLDGEMYLGGLPENSGDLSLPPEVWTARLRLGFVGCVRDLFVDGRSKDLRRLAELQSAPGVSSFCTRETHRRCSSEPCVHGGRCREGWNRHVCDCTGTGYMGPNCEMESAVLSYDGSMFLKVLMPHAAHSEAEDVSLRFMSQRAYGLLMATTSKESADTLRLELDGGRVKLTVNLDCIGIDCNLISTGKGPETLFAGHKLNDNEWHSVKVVRRGKSLQLSVDNVTVEGQMSGAHTQLEFHHIETGIMTERRFISVMPSNFIGHLQGLSFNGMPYLDQCKNGDISYCELNARFGMRRIVADPVSFRNRASYVALSTLQAYASMHLFFQFKTTSPDGLILFNSGDGSDFIVIELVKGYIHYVFDLGNGPSLMKGNSDKPLNDNQWHNVMVSRDDSNVHTLKIDSRTVTQHSNGARNLDLKGELYIGGVGKSMYNSLPKLIASRDGYQGCPASVDLNGRLSDLIADALHRVGQVERGCEAGPGTTCTEDSCSNQGVCLQQWEGFTCDCTMTTYGGPLCSDPGTTYIFGRGGALITYTWAPNDRPSTRADRLAVGFSTQQSDAILVQVESSQGLGDYLQLHIEQGKVGVIFNVGTDDITIDEPAVTVNDGKYHVVRFTRSGGNATLQVDNQPVIERFPSGNIDNERLAIARQRIPYRLGRVVDEWLLDKGRQLTIFNSQAAIKVGGQDKGRPFQGQISGLYYNGLQVLKLAAEGDPNVQVAGNLRLVGDAPSVLSTETTSATPPAAADMSTTIMETTTTMATTTTRRQRSPSLKDSITQNSDDLLVASAECPSDDEDLEECEPGTGGELVLPIITVDTQDPISMATRYPAIPAPPTSLTPLQTTKESLILSDPRPPCPPDQEDCGDPMEVSAFGSGEMTESDDEDFNRNSPMVTDRTVLPPPPGVGKSGHGDHRPPVPAPTTHPNQLHIPAGKMNTRDQVLLPPVPSSRHTPGLTYPPDFPHVPTAHPTDLMEKGRPGAVEVIRESSSTTGMVVDIVAAAALCILILLYAMYKYRNRDEGSYQVDQSRNSGSESNGAVVKEKTPSTTAAVAKTTTKGKKDKDKEYYV
Protein: Keratin, type I cuticular Ha8 (Hair keratin, type I Ha8) (Keratin-38) (K38) (O76015)
Organism: Homo sapiens (Human)
Interaction partners:
- Keratin-associated protein 8-1
- Keratin-associated protein 11-1
- Keratin, type I cuticular Ha3-II
Sequence:
MTSSYSSSSCPLGCTMAPGARNVSVSPIDIGCQPGAEANIAPMCLLANVAHANRVRVGSTPLGRPSLCLPPTCHTACPLPGTCHIPGNIGICGAYGENTLNGHEKETMQFLNDRLANYLEKVRQLEQENAELEATLLERSKCHESTVCPDYQSYFHTIEELQQKILCSKAENARLIVQIDNAKLAADDFRIKLESERSLRQLVEADKCGTQKLLDDATLAKADLEAQQESLKEEQLSLKSNHEQEVKILRSQLGEKLRIELDIEPTIDLNRVLGEMRAQYEAMLETNRQDVEQWFQAQSEGISLQDMSCSEELQCCQSEILELRCTVNALEVERQAQHTLKDCLQNSLCEAEDRFGTELAQMQSLISNVEEQLSEIRADLERQNQEYQVLLDVKTRLENEIATYRNLLESEDCKLPCNPCSTSPSCVTAPCAPRPSCGPCTTCGPTCGASTTGSRF