wanglab/gogpt-training-data huggingface dataset:
Protein: Cell death-inducing p53-target protein 1 homolog (Protein LITAF homolog) (Q54HX8)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Late endosome membrane {ECO:0000250|UniProtKB:Q9H305}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H305}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9H305}. Lysosome membrane {ECO:0000250|UniProtKB:Q9H305}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H305}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9H305}.
Interaction partners:
- DNA helicase
Sequence:
MGQDNINLNKVDGQPSSPPQEQQQQQQYPPQGYPQQQQYPPQQGYPPQQYPPQQGYPPQQYPPQQGYPQQQPPQQYPAPVGAPQQPYMATQQVVVQQVYVQPTFGVVPVDCICQHCQTRMSTKTSYKSGSMVWLVCVLLIIFGCWLGCCLIPFGIDSLKDVQHKCSHCKKVLYRFDRMSGK
Protein: alpha-1,2-Mannosidase (EC 3.2.1.-) (O46091)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
Sequence:
MQQKPRNNGYPGTLICAVLLVLLSTGVSGQKQYSKARKLELREDVRRMFQHAYDGYLRHASNYDELRPLTCDGHDTWGSYSLTLIDALDTLATMGNFTEFRRAARLLEEKMDFDRDINVSVFETNIRIVGGLLSAHLLSKRAGVELEPGWPCKGPLLRLAEDVARRLLPAFVTNTGMPYGTVNLRYGVPKGETSITCTAGVGTFLIEFGTLSRLTGKTIYEDVAMKAVHALWAYRSPIGLFGNHIDVQSGRWTALDSGIGAGVDSLFEYLVKASVLLNRPELLELFHEARAAIDKYMRKEDWYVWVGMNKGRVTLPVFQSLEAFWPGILSIIGDTEPALRTISRYIGVWKKYGFLPEFYNIAAGEASPNREVYPLRPELIESAMYLYRATGNEYLLEFGEHMLETLEFSAKTKCGYATIRNVVTHEKENRMESFFLAETSKYLYLLFDEENFLHNDGSGGELLSTEDDVCVVQAGAYIFNTEAHPMDMSALHCCHAHNEDIYTSLDLQRFSPRAILERSKKRQVAVQEQWVPQCHPENNEFFNKEDESVQAQDSEKEQEREQSGTSTTMAVDIEVFDEFQQPAGDLLVSNFEQIREERELNESLHRNVVARNQLTVSDLDEFFAQRRESFASASEALNYVKTFMGNYTMDVAFIRGLQLYDTNMSSVLGTGAQKEYESRMRTLWQLYELQQQYVANIRVIQGLGLLTFPADGDRIPSHLTEVLDSLDKSAHLEHMDLQDLETRVSNTSSPQLAHIREVILKARNAYAIAMVNTSAMQEFAIRIYLSGTSEAGVRIHPLLEDAELSEEARKRPLKLAEERALFSYARRIVDFRKRMAETVDRLQTLMQDIPPPKRKEATTDSQAADASTVYTQTKAQMAAPAQQPEPSQEEKQSTQIQKGKLAENGSGLGEEESGCVWSQLVQTILRKTTVQRVKFDEAVLQENTRKALEKYARKELPHHLFACTGRSTLRDSPIGTFIRKRCKLAITSPTNTTDL
Protein: Meiotic recombination protein DMC1 homolog (AtDMC1) (Q39009)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May participate in meiotic recombination, specifically in homologous strand assimilation, which is required for the resolution of meiotic double-strand breaks. Mediates interhomolog recombination during meiosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:17785529}.
Interaction partners:
- DNA repair protein XRCC3 homolog
- DNA repair protein XRCC2 homolog
- Protein BREAST CANCER SUSCEPTIBILITY 2 homolog B
- Protein BREAST CANCER SUSCEPTIBILITY 2 homolog A
- Crossover junction endonuclease MUS81
- DNA repair protein recA homolog 1, chloroplastic
- Meiotic recombination protein SPO11-1
- Meiotic nuclear division protein 1 homolog
- Meiosis-specific protein ASY1
- DNA mismatch repair protein MSH4
Sequence:
MMASLKAEETSQMQLVEREENDEDEDLFEMIDKLIAQGINAGDVKKLQEAGIHTCNGLMMHTKKNLTGIKGLSEAKVDKICEAAEKIVNFGYMTGSDALIKRKSVVKITTGCQALDDLLGGGIETSAITEAFGEFRSGKTQLAHTLCVTTQLPTNMKGGNGKVAYIDTEGTFRPDRIVPIAERFGMDPGAVLDNIIYARAYTYEHQYNLLLGLAAKMSEEPFRILIVDSIIALFRVDFTGRGELADRQQKLAQMLSRLIKIAEEFNVAVYMTNQVIADPGGGMFISDPKKPAGGHVLAHAATIRLLFRKGKGDTRVCKVYDAPNLAEAEASFQITQGGIADAKD
Protein: Dual specificity protein phosphatase (EC 3.1.3.16) (EC 3.1.3.48) (A0A0G2K3I9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Serine/threonine-protein kinase VRK3
- Tyrosine-protein phosphatase non-receptor type 7
- Mitogen-activated protein kinase 3
- Mitogen-activated protein kinase 10
- Mitogen-activated protein kinase 1
- Mitogen-activated protein kinase 12
- mitogen-activated protein kinase
- Mitogen-activated protein kinase 14
- Mitogen-activated protein kinase 13
- Mitogen-activated protein kinase 9
Sequence:
MSGSFELSVQDLNDLLSDGSGCYSLPSQPCNEVIPRVYVGNASVAQDITQLQKLGITHVLNAAEGRSFMHVNTSASFYKDTGITYMGIKANDTQEFNLSAYFERAADFIDQALAHKNEASWVHGSFPIQAIPKENSLPLDLEKFY
Protein: Fascin (P85845)
Organism: Rattus norvegicus (Rat)
Function: Actin-binding protein that contains 2 major actin binding sites. Organizes filamentous actin into parallel bundles. Plays a role in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers. Important for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration. Mediates reorganization of the actin cytoskeleton and axon growth cone collapse in response to NGF (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:19343716}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q16658}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q16658}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q16658}. Cell projection, growth cone {ECO:0000269|PubMed:8769857}. Cell projection, filopodium {ECO:0000269|PubMed:8769857}. Cell projection, invadopodium {ECO:0000250|UniProtKB:Q61553}. Cell projection, microvillus {ECO:0000250|UniProtKB:Q16658}. Cell junction {ECO:0000250|UniProtKB:Q16658}. Note=Colocalized with RUFY3 and F-actin at filipodia of the axonal growth cone. Colocalized with DBN1 and F-actin at the transitional domain of the axonal growth cone. {ECO:0000250|UniProtKB:Q16658, ECO:0000250|UniProtKB:Q61553}.
Interaction partners:
Sequence:
MTANGTAEAVQIQFGLISCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPPDEAGSAAVCLRSHLGPYLAADKDGNVTCEREVPDGDCRFLVVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQSVSPAEKWSVHIAMHPQVNIYSVTRKRYAHLSARPADEIAVDRDVPWGVDSLITLAFQDQRYSVQTSDHRFLRHDGRLVARPEPATGFTLEFRSGKVAFRDCEGRYLAPSGPSGTLKAGKATKVGKDELFALEQSCAQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTRKCAFRTHTGKYWTLTATGGVQSTASTKNASCYFDIEWCERRITLRASNGKFVTAKKNGQLAATVETAGDSELFLMKLINRPIIVFRGEHGFIGCRKVTGTLDANRSSYDVFQLEFNDGAYNIKDSTGKYWTVGSDSSVTSSSDTPVDFFLEFCDYNKVALKVGGRYLKGDHAGVLKACAETIDPATLWEY
Protein: UPF0306 protein YhbP (P67762)
Organism: Escherichia coli (strain K12)
Interaction partners:
Sequence:
METLIAISRWLAKQHVVTWCVQQEGELWCANAFYLFDAQKVAFYILTEEKTRHAQMSGPQAAVAGTVNGQPKTVALIRGVQFKGEIRRLEGEESDLARKAYNRRFPVARMLSAPVWEIRLDEIKFTDNTLGFGKKMIWLRDSGTEQA
Protein: Bcl-2-related protein A1 (A1-A) (Hemopoietic-specific early response protein) (Protein BFL-1) (Q07440)
Organism: Mus musculus (Mouse)
Function: Retards apoptosis induced by IL-3 deprivation. May function in the response of hemopoietic cells to external signals and in maintaining endothelial survival during infection. Can inhibit apoptosis induced by serum starvation in the mammary epithelial cell line HC11.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q16548}.
Interaction partners:
- Phorbol-12-myristate-13-acetate-induced protein 1
- Bcl-2-like protein 11
- Bcl-2-modifying factor
- Bcl-2 homologous antagonist/killer
- Bcl-2-binding component 3
- BH3-interacting domain death agonist
- Bcl-2-like protein 2
- Activator of apoptosis harakiri
- Bcl-2-interacting killer
- Beclin-1
Sequence:
MAESELMHIHSLAEHYLQYVLQVPAFESAPSQACRVLQRVAFSVQKEVEKNLKSYLDDFHVESIDTARIIFNQVMEKEFEDGIINWGRIVTIFAFGGVLLKKLPQEQIALDVCAYKQVSSFVAEFIMNNTGEWIRQNGGWEDGFIKKFEPKSGWLTFLQMTGQIWEMLFLLK
Protein: RNases MRP/P 32.9 kDa subunit (RNA-processing protein POP4) (P38336)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for 5.8S rRNA and tRNA processing; associated with RNase MRP and RNase P.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Ribonuclease MRP protein subunit SNM1
- Ribonucleases P/MRP protein subunit POP8
- Ribonuclease P/MRP protein subunit RPP1
- Ribonucleases P/MRP protein subunit POP1
- Ribonucleases P/MRP protein subunit POP7
- Ribonuclease MRP protein subunit RMP1
- Ribonuclease P protein subunit RPR2
- Ribonuclease P/MRP protein subunit POP5
- Ribonucleases P/MRP protein subunit POP6
- Ribonucleases P/MRP protein subunit POP3
Sequence:
MDRTQTFIKDCLFTKCLEDPEKPFNENRFQDTLLLLPTDGGLTSRLQRQQRKSKLNLDNLQKVSQLESADKQLEKRDYQRINKNSKIALREYINNCKKNTKKCLKLAYENKITDKEDLLHYIEEKHPTIYESLPQYVDFVPMYKELWINYIKELLNITKNLKTFNGSLALLKLSMADYNGALLRVTKSKNKTLIGLQGIVIWDSQKFFIMIVKGNIIDEIKCIPKKGTVFQFEIPISDDDDSALRYSILGDRFKYRSVDRAGRKFKSRRCDDMLYYIQN
Protein: pH-response transcription factor pacC/RIM101 (pH-response regulator protein 2) (Q9UW14)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Transcription factor that mediates regulation of both acid- and alkaline-expressed genes in response to ambient pH. At alkaline ambient pH, activates transcription of alkaline-expressed genes (including RIM101 itself) and represses transcription of acid-expressed genes. Specifically recognizes and binds the consensus sequence 5'-CCAAGAA-3'. Required for the control of alkaline pH-induced filamentation (dimorphic switch) and virulence.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- pH-response regulator protein palA/RIM20
- Calpain-like protease palB/RIM13
- pH-response regulator protein palF/RIM8
- pH-response regulator protein palH/RIM21
- Vacuolar-sorting protein SNF7
- pH-response regulator protein palI/RIM9
- Transcriptional regulator NRG1
- Vacuolar protein-sorting protein BRO1
- Secreted aspartic protease 9
- Mitogen-activated protein kinase HOG1
Sequence:
MNYNIHPVTYLNADSNTGASESTASHHGSKKSPSSDIDVDNATSPSSFTSSQSPHINAMGNSPHSSFTSQSAANSPITDAKQHLVKPTTTKPAAFAPSANQSNTTASQSYTQPAQQLPTQLHPSLNQAYNNQPSYYLHQPTYGYQQQQQQQQQHQEFNQPSQQYHDHHGYYSNNNILNQNQPAPQQNPVKPFKKTYKKIRDEDLKGPFKCLWSNCNIIFETPEILYDHLCDDHVGRKSSNNLSLTCLWENCGTTTVKRDHITSHLRVHVPLKPFHCDLCPKSFKRPQDLKKHSKTHAEDHPKKLKKAQRELMKQQQKEAKQQQKLANKRANSMNATTASDLQLNYYSGNPADGLNYDDTSRKRRYENNSQHNMYVVNSILNDFNFQQMAQAPQQPGVVGTAGSAEFTTKRMKAGTEYNIDVFNKLNHLDDHLHHHHPQQQHPQQQYGGNIYEAEKFFNSLSNSIDMQYQNMSTQYQQQHAGSTFAQQKPTQQASGQLYPSLPTIGNGSYTTSGSSHKEGLVNNHNGYLPSYPQINRSLPYSSGVAQQPPSALEFGGVSTYQKSAQSYEEDSSDSSEEDDYSTSSEDELDTLFDKLNIDDNKVEEVTIDGFNLKDVAKHREMIHAVLGYLRNQIEQQEKEKSKEQKEVDVNETKLYPTITAF
Protein: Phosphotransferase (EC 2.7.1.-) (Q9BK28)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
IVGTGANACYMERVEEAELFAAEDPRKKHVLINTEWGAFGDNGALDFVRTEFDRDIDVHSINPGKQTFEKMISGMYMGELVRLVLVKMTQAGILFNGQDSEVLNTRGLFFTKYVSEIEADEPGNFTNCRLVLEELGLTNATDGDCANVRYICECVSKRAAHLVSAGIATLINKMDEPTVTVGIDGSVYRFQPKFHNLMVEKISQLIKPGITFDLMLSEDGSGRGAALVAAVACREDILNGKK
Protein: Tim10-like domain-containing protein (Q57ZF1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Mitochondrial import inner membrane translocase subunit
- Mitochondrial translocase subunit
Sequence:
MQPPQTNPQLAGMAQRDVVVLAERQQLISNEGFNYCMRRCITHYGEDSIPYHPGEKACLDRCVNKIHNGLDLSCTIRKEFEEKIKKGDMPYRWMKEVLSENE
Protein: Arginine vasopressin-induced protein 1 (AVP-induced protein 1) (Arginine vasopressin-induced transcript 32 protein) (VIP32) (VIT32) (Q9D7H4)
Organism: Mus musculus (Mouse)
Function: May be involved in MAP kinase activation, epithelial sodium channel (ENaC) down-regulation and cell cycling.
Interaction partners:
Sequence:
MGTPASVVSEPPLWQVSTPQTRGRKQASANIFQDAELVQIQGLFQRSGDQLAEERAQIIWECAGDHRVAEALRRLRRKRPPKQNHCSRLRVPEPGSTASDPQASTTDTASSEQSGNSRRTSARAPRNWNKPGPTGYLHQIRH
Protein: Small nuclear ribonucleoprotein E (snRNP-E) (Sm protein E) (D3ZSP1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|RuleBase:RU365053}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365053}. Note=SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes. {ECO:0000256|RuleBase:RU365053}.
Interaction partners:
- Small nuclear ribonucleoprotein G
- Small nuclear ribonucleoprotein F
- Small nuclear ribonucleoprotein Sm D3
- Small nuclear ribonucleoprotein Sm D1
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein-associated protein B
- U1 small nuclear ribonucleoprotein 70 kDa
- U7 snRNA-associated Sm-like protein LSm10
- PHD finger-like domain-containing protein 5A
Sequence:
MAYLGQGQKVQKVMVQPINLIFRYLQNRSRIQVWLYEQVNMRIEGCIIGFDEYMNLVLDDAEEIHSKTKSRKQLGRIMLKGDNITLLQSVSN
Protein: DNA-directed RNA polymerase family protein (RNA polymerase subunit) (Q9C6C2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- DNA-directed RNA polymerase III subunit 2
- DNA-directed RNA polymerase III subunit 1
- DNA-directed RNA polymerase I subunit 2
- DNA-directed RNA polymerase subunit
- DNA binding / DNA-directed RNA polymerase
- RNApolymerase 14 kDa subunit
- DNA-directed RNA polymerase I subunit 1
- DNA-directed RNA polymerases II, IV and V subunit 10
- DNA-directed RNA polymerase III subunit RPC6
- DNA-directed RNA polymerase III subunit RPC3
Sequence:
MVTKAEKQFAKNFNIDDLPDVPAGLPPHLKAQQTRVVSKNNAPAHTASAIYSGTYVSSTEEDDNVKLGNFYDNFKVDVVSLTKTDMEFDMIGIDAAFANAFRRILIAEVPSMAIEKVLIAYNTSVIIDEVLAHRMGLIPIAADPRLFEYLSEHDQANEKNTIVFKLHVKCPKNRPRLKVLTSDLKWLPNGSELLRESENKTSKPKTYTSFSCSQDSLPEFANNPITPCDLDILIAKLAPGQEIELEAHAVKGIGKTHAKWSPVGTAWYRMHPEVVLRGEVEDELAERLVNVCPQNVFDIEDMGKGKKRATVAQPRKCTLCKECVRDDDLVDHVDLGSVKNHFIFNIESTGSLPPEVLFTEAVKILEAKCEAITDF
Protein: Neurabin-1 (Q5R3Y6)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
METRRGLSPERPDVDLTNRKVSFSTAPIPVFSAFSVEDYDRKNEDIDPVASCAEYELERRLERMDLFEVDLEKGAEGLGVSIIGMGVGADSGLEKLGIFVKSITPGGAVHRDGRIRVCDQIVSVDGKSLVGVSQLYAANTLRSTSNRVTFTIGREQNLEESEVAQLIQQSLEHDRMRMMGDEEDDIEEPPPPPSQMPQLPIEQDRPTTSMITKEEIEIRSKIAALELELDVTHKKAEQYHEVLSSTKSHCDQLEKQNEQANYMIKNYQEREKELLNREENHVEQLRDKDVHYASLVRQLKERIDELESKLEEAEERRHSIQNLELIELREKLKEKVEKRNEGMAYRPGGELPHEDKAVMVNLETITPSTKKDAEVSVGSSWTEEYSSPCESPVPRISEPASPALPHKLTHRKLLFPLRKKYAENEFWRATCQPVGLQALHWTVDDVCQLLVSMGLDKYVPEFTINKIDGAKFLELDGNKLKAMGIQNHSDRSLIKKKVKGMKNKIERERKQLERESRTRVIAHTIPM
Protein: Dual specificity protein phosphatase (EC 3.1.3.16) (EC 3.1.3.48) (E5RHD0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MCPGNWLWASMTFMARFSRSSSRSPVRTRGTLEEMPTVQHPFLNVFELERLLYTGKTACNHADEVWPGLYLGDQDMANNRRELRRLGITHVLNASHSRWRGTPEAYEGLGIRYLGVEAHDSPAFDMSIHFQTAADFIHRALSQPG
Protein: Glypican-4 (K-glypican) [Cleaved into: Secreted glypican-4] (P51655)
Organism: Mus musculus (Mouse)
Function: Cell surface proteoglycan that bears heparan sulfate. May be involved in the development of kidney tubules and of the central nervous system.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side.; SUBCELLULAR LOCATION: [Secreted glypican-4]: Secreted, extracellular space {ECO:0000250}.
Interaction partners:
- Leucine-rich repeat transmembrane neuronal protein 4
- Frizzled-2
- Frizzled-7
- Frizzled-8
- Frizzled-3
- Frizzled-1
- Frizzled-5
- Frizzled-9
- Frizzled-4
- Frizzled-6
Sequence:
MARLGLLALLCTLAALSASLLAAELKSKSCSEVRRLYVSKGFNKNDAPLYEINGDHLKICPQDYTCCSQEMEEKYSLQSKDDFKTVVSEQCNHLQAIFASRYKKFDEFFKELLENAEKSLNDMFVKTYGHLYMQNSELFKDLFVELKRYYVAGNVNLEEMLNDFWARLLERMFRLVNSQYHFTDEYLECVSKYTEQLKPFGDVPRKLKLQVTRAFVAARTFAQGLAVARDVVSKVSVVNPTAQCTHALLKMIYCSHCRGLVTVKPCYNYCSNIMRGCLANQGDLDFEWNNFIDAMLMVAERLEGPFNIESVMDPIDVKISDAIMNMQDNSVQVSQKVFQGCGPPKPLPAGRISRSISESAFSARFRPYHPEQRPTTAAGTSLDRLVTDVKEKLKQAKKFWSSLPSTVCNDERMAAGNENEDDCWNGKGKSRYLFAVTGNGLANQGNNPEVQVDTSKPDILILRQIMALRVMTSKMKNAYNGNDVDFFDISDESSGEGSGSGCEYQQCPSEFEYNATDHSGKSANEKADSAGGAHAEAKPYLLAALCILFLAVQGEWR
Protein: Integrin alpha-6 isoform X2 (Integrin, alpha 6a) (A8WHQ7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
Interaction partners:
Sequence:
MELFEKALSLNLCVFSWLVWTSASAFNLDTQNVLRKSGQPGSLFGFSIALHRQLQPHDKTILLIGAPKARALSNQGANVTGGLYSCDITTHPNDCSRVDFDNDVDVRVENKENQWMGVTVQSQGPGGKIVTCAHRYQRLLFPNTPQEARDITGRCYMLSQDLSIDNQSDEDGGNWKFCDGRTRGHERFGACQQGLAATFTKDYHYVIFGAPGAYNWKGIVRIEQKNNTLLEMGLFDDGPYEVGDENRLDPNLVPVPANSYLGFSLDSGHSITEKGKLIIVSGAPRANHSGAVVFLRKEGELSSMLTPEHILEGPGLASSFGYDVAVVDLNGDGWQDVVVGAPQFFQRDEEVGGAVYVYINKAGRWRDVTPVRLNGTKDSMFGLSVENIGDVNLDSFEDIAVGAPYADSGFGSVYIYHGSADGISTKPAQILEGKQHNTKMFGYSLAGNMDLDHNSYPDLAVGSLSDTVFIYRSKNVISIKKDIKVTPKEIDLTKKTCGNSICLTVEACFSYRANPTTYNPKITISCTFEAEWYRRKLGLPSRVVFLDKTEIDQDYQSTGTLELRGQNKKACYKTKLRLQDGIRDKLRAIPIEVSVAIQSAKRGKRQSSLPQLVPILDSTVPNKTLTEVNFLKEGCGTDNICQSNLNLQYRFCYRESKQDIFPPLPLENGVPVISLSDQKDIALEVTVRNRNGDDAHEAKLVSHFDDSLSYSGFRSLRTNDKHVICAANQNGSLADCELGNPFKRDSEVTFYIILSTGKISLETKEVEIDLQLETTSSQEGLSKVKAKAKVVIELLLSVQGVAKPSQVYFGGEVKGMSAMKKEEEVGSLIEYEFRVINLGKPLKSFGTASLNIQWPKESSVGKWLLYLMKINTRDLQLVTCSPEREINPLKLREDSSIRKKRELEERRPSEGNKISLFTDKRKHKILSCSGDARCVEIKCPLQGLDSTAVIVLKSRLWNSTFLEDFASYNYLDIIVKASISLDVSAKNIVLKNPETQVRLTVFPETTATPFGGVPWWIILVAVLAGILMLALLVLLLWKCGFFKRAQKDEYDAAFHKAEIHAQPSDKLSTEA
Protein: LOG family protein YJL055W (P47044)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Inosine triphosphate pyrophosphatase
Sequence:
MTMEKNGGNSSRGGQVGGKSVCVYCGSSFGAKALYSESAEELGALFHKLGWKLVYGGGTTGLMGKIARSTMGPDLSGQVHGIIPNALVSKERTDEDKEDVNKALLESVENHKGATPISEEYGETTIVPDMHTRKRMMANLSDAFVAMPGGYGTFEEIMECITWSQLGIHNKPIILFNIDGFYDKLLEFLKHSIQERFISVKNGEIIQVASTPQEVVDKIEKYVVPEGRFNLNWSDEGHAHEDCAK
Protein: 3-ketoacyl-CoA thiolase B, peroxisomal (EC 2.3.1.155) (EC 2.3.1.16) (EC 2.3.1.9) (Acetyl-CoA acyltransferase B) (Beta-ketothiolase B) (Peroxisomal 3-oxoacyl-CoA thiolase B) (P07871)
Organism: Rattus norvegicus (Rat)
Function: Responsible for the thiolytic cleavage of straight chain 3-keto fatty acyl-CoAs (3-oxoacyl-CoAs). Plays an important role in fatty acid peroxisomal beta-oxidation. Catalyzes the cleavage of short, medium, long, and very long straight chain 3-oxoacyl-CoAs. Medium chain straight 3-oxoacyl-CoAs are preferred substrates.
Subcellular location: Peroxisome {ECO:0000269|PubMed:10064897}. Note=Transported into peroxisomes following association with PEX7. {ECO:0000250|UniProtKB:P09110}.
Interaction partners:
Sequence:
MHRLQVVLGHLAGRSESSSALQAAPCSAGFPQASASDVVVVHGRRTPIGRAGRGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGNISSRLLENEKARDCLIPMGITSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTVLDDKGDRKTITVSQDEGVRPSTTMEGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFASQALYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRAYGVVSMCIGTGMGAAAVFEYPGN
Protein: Large ribosomal subunit protein uL16m (39S ribosomal protein L16, mitochondrial) (O46082)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLSLKLVSQLFKQSLAFCNKPLKLFFAAGNMAIVNTAGLKYFAPPIKYQNVEQPERPKLRVIERQPQLPPNIRPPKMQKRLRYMRGPEMVHNTLLHKQYAIVATGGGRLRWGHYEMMRLTIGRKMNVNTMFATWRVPAPWQPITKKGQGQRMGGGKGAIDHYVTPIKAGRVIVEIAGKCEFVEVKQFLQQVANQLPFQATVVSQEMLDEQRVAEEEQTRQNENPFTMKYVIQNNLSGCHRWLSPVDHKWFGKHL
Protein: Probable beta-galactosidase A (EC 3.2.1.23) (Lactase A) (Q5BFC4)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Alpha-L-arabinofuranosidase B
- Xylanolytic transcriptional activator xlnR
- Probable alpha-galactosidase B
- Probable beta-glucosidase A
- DNA-binding protein creA
- Exo-1,4-beta-xylosidase xlnD
- Endo-1,4-beta-xylanase B
Sequence:
MRLLPVWTAALLAAQAAGVALTHKLNGFTITEHPDAEKRELLQKYVTWDDKSLFINGERIMIFGAEIHPWRLPVPSLWRDILQKVKALGFNCVSFYVDWALLEGKPGEYRAEGSFAWEPFFDAASDLGIYLIARPGPYINAEASGGGFPGWLQRLNGTIRSSDQSYLDATENYVSHIGGLIAKYQITNGGPVILYQPDNEYSGGCCGQEFPNPDYFQYVIDQARRAGIVVPTISNDAWPGGHNAPGTGKGEVDIYGHDNYPLGFDCANPDVWPEGNLPTDYRDLHLEISPSTPYALVEYQVGAFDPWGGPGFEQCAALTGYEFERVFHKNTFSFGVGILSLYMTFGGTNWGNLGHPGGYTSYDYGSPIKETREITREKYSELKLLGNFIKSSPGYLLATPGKLTNTTYTNTADLTVTPLLGNGTGSFFVLRHSDYSSQASTPYKLRLPTSAGQLTIPQLGGSLVLNGRDSKVHLVDYDVAGTKILYSTAEVFTWKKFHDGKVLVLYGGPGEHHELAVSSKAKVKVVEGLGSGISSKQIRGAVVVAWDVEPARRIVQIGDLKIFLLDRNSAYNYWVPQLGTETSIPYATEKAVAASVIVKAGYLVRTAYVKGRDLHLTADFNATTPVEVIGAPKTAENLFINGKKAHHTVDKNGIWSTEVGYSPPKIVLPVLEDLKWKSIDTLPEIQPSYDDSPWPDANLPTKNTIYPLRTPTSLYASDYGFHTGYLLFRGHFTANGRESNFSIQTQGGQAFGSSVWLSGTYLGSWTGDNDYQDYNATYTLPSLKAGKEYVFTVVVDNMGLNENWIVGQDEMKKPRGILNYELSGHEASDITWKLTGNFGGEDYVDKVRGPLNEGGLYAERHGYHQPYPPTKSKDWKSSTPLTGLSKPGISFYTASFDLDIKSGWDVPIYFEFGNSTTPAPAYRVQLYVNGWQYGKYVNNIGPQTRFPVPEGILNYKGTNWVAVTLWALEGSGAKLDSFKLVHGIPVRTALDVEGVELPRYQSRKGVY
Protein: Geranylgeranyl transferase type-1 subunit beta (EC 2.5.1.59) (Geranylgeranyl transferase type I subunit beta) (Q24172)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEDRTDTEPVLLSKHAKNLLRFLNLLPARMASHDNTRSTIVFFAVCGLDVLNSLHLVPPQLRQDIIDWIYGGLVVPRDNEKNCGGFMGCRAMVPKTEDAEILECMRNYQWGHLAMTYTSLAVLVTLGDDLSRLDRKSIVDGVAAVQKPEGSFSACIDGSEDDMRFVYCAATICYMLDYWGDVNKETMFQFITRSLRYDYGFSQELEGEAHGGTTFCALAALHLSGQLHRLDATTVERMKRWLIFRQMDGFQGRPNKPVDTCYSFWIGASLCILNGFELTDYARNREFILSTQDKLIGGFAKWPQATPDPFHTYLGLCGLAFTGEPGLSPVNPSLNMSMAAYAHLQHLHEQWRSADGRGDEDISVSSAFKQQLHLSKGVEATSTTTTSNSPLISAQ
Protein: F-box/WD repeat-containing protein 11 (F-box and WD repeats protein beta-TrCP2) (F-box/WD repeat-containing protein 1B) (Homologous to Slimb protein) (HOS) (Q9UKB1)
Organism: Homo sapiens (Human)
Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins. SCF(FBXW11) mediates the ubiquitination of phosphorylated CTNNB1 and participates in Wnt signaling regulation. SCF(FBXW11) mediates the ubiquitination of phosphorylated NFKBIA, which degradation frees the associated NFKB1 to translocate into the nucleus and to activate transcription. SCF(FBXW11) mediates the ubiquitination of IFNAR1. SCF(FBXW11) mediates the ubiquitination of CEP68; this is required for centriole separation during mitosis. Involved in the oxidative stress-induced a ubiquitin-mediated decrease in RCAN1. Mediates the degradation of CDC25A induced by ionizing radiation in cells progressing through S phase and thus may function in the intra-S-phase checkpoint. Has an essential role in the control of the clock-dependent transcription via degradation of phosphorylated PER1 and phosphorylated PER2. SCF(FBXW11) mediates the ubiquitination of CYTH1, and probably CYTH2.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q5SRY7}. Nucleus {ECO:0000250|UniProtKB:Q5SRY7}.
Interaction partners:
- S-phase kinase-associated protein 1
- Cullin-1
- E3 ubiquitin-protein ligase RBX1
- F-box/WD repeat-containing protein 1A
- Catenin beta-1
- NF-kappa-B inhibitor alpha
- S-phase kinase-associated protein 2
- F-box only protein 5
- NF-kappa-B inhibitor beta
- Transcriptional activator GLI3
Sequence:
MEPDSVIEDKTIELMCSVPRSLWLGCANLVESMCALSCLQSMPSVRCLQISNGTSSVIVSRKRPSEGNYQKEKDLCIKYFDQWSESDQVEFVEHLISRMCHYQHGHINSYLKPMLQRDFITALPEQGLDHIAENILSYLDARSLCAAELVCKEWQRVISEGMLWKKLIERMVRTDPLWKGLSERRGWDQYLFKNRPTDGPPNSFYRSLYPKIIQDIETIESNWRCGRHNLQRIQCRSENSKGVYCLQYDDEKIISGLRDNSIKIWDKTSLECLKVLTGHTGSVLCLQYDERVIVTGSSDSTVRVWDVNTGEVLNTLIHHNEAVLHLRFSNGLMVTCSKDRSIAVWDMASATDITLRRVLVGHRAAVNVVDFDDKYIVSASGDRTIKVWSTSTCEFVRTLNGHKRGIACLQYRDRLVVSGSSDNTIRLWDIECGACLRVLEGHEELVRCIRFDNKRIVSGAYDGKIKVWDLQAALDPRAPASTLCLRTLVEHSGRVFRLQFDEFQIISSSHDDTILIWDFLNVPPSAQNETRSPSRTYTYISR