wanglab/gogpt-training-data huggingface dataset:
Protein: Transmembrane protein (F4HXZ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase family protein
- Nucleic acid binding / zinc ion binding protein
- Methyltransferase-like protein 5
- Pentatricopeptide repeat-containing protein At4g18975
- Pentatricopeptide repeat-containing protein At4g01030
- Carbon catabolite repressor protein 4 homolog 4
- Phosphoglycerate mutase family protein
- Glyoxylate/succinic semialdehyde reductase 1
Sequence:
MKSYPIGSSKAFHAYSRSGDFDLESGGTIRKSRKPKTSFSKMIKSLGNRLHHMFKLHPVLVFVVCVSFGITVLILVSSIYGNRLGSTVSYYKKNDLDSDGYPFANLKNLVMVAGHSVYTSSDCGKVEKEDSWFLESYQKNPGQAATFLSHIQEGVEAAAKDDESLLLFSGGETRKDAGPRSEAQSYWAVAESKGWFGKNEVRSRALTEEHARDSFENLLFSVCRFRELTGSYPQNITVVSYDFKEERFAHLHRSAMGFPESRFFYLGTPASLSSKEGALKGEALVRSQFQEDPYGCVGSLWRKKLNRDPFHRTIPYPIGCPEIGGLFRYCGSAPFPGSLPWG
Protein: Carnosine N-methyltransferase (EC 2.1.1.22) (Q8N4J0)
Organism: Homo sapiens (Human)
Function: N-methyltransferase that catalyzes the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Anserine, a methylated derivative of carnosine (beta-alanyl-L-histidine), is an abundant constituent of vertebrate skeletal muscles. Also methylates other L-histidine-containing di- and tripeptides such as Gly-Gly-His, Gly-His and homocarnosine (GABA-His).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:26001783}. Nucleus {ECO:0000269|PubMed:26001783}.
Interaction partners:
- Carnosine synthase 1
- Beta-Ala-His dipeptidase
- Cytosolic non-specific dipeptidase
Sequence:
MQRRRRPPPPTSRLPEGCGGGGGGSEEVEVQFSAGRWGSAAAVSAAAAAATRSTEEEEERLEREHFWKIINAFRYYGTSMHERVNRTERQFRSLPANQQKLLPQFLLHLDKIRKCIDHNQEILLTIVNDCIHMFENKEYGEDGNGKIMPASTFDMDKLKSTLKQFVRDWSETGKAERDACYQPIIKEILKNFPKERWDPSKVNILVPGAGLGRLAWEIAMLGYACQGNEWSFFMLFSSNFVLNRCSEINKYKLYPWIHQFSNNRRSADQIRPIFFPDVDPHSLPPGSNFSMTAGDFQEIYSECNTWDCIATCFFIDTAHNVIDYIDTIWKILKPGGIWINLGPLLYHFENLANELSIELSYEDIKNVVLQYGFKVEVEKESVLSTYTVNDLSMMKYYYECVLFVVRKPQ
Protein: Probable beta-glucosidase F (EC 3.2.1.21) (Beta-D-glucoside glucohydrolase F) (Cellobiase F) (Gentiobiase F) (Q2UN12)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Function: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Probable glucan endo-1,3-beta-glucosidase eglC
- beta-glucosidase
- Glucanase
- Glucanase
- beta-glucosidase
- Probable endo-beta-1,4-glucanase B
- Probable beta-glucosidase I
- Probable beta-glucosidase H
- beta-glucosidase
- beta-glucosidase
Sequence:
MAAFPAYLALLSYLVPGALSHPEAKTLTSRASTEAYSPPYYPAPNGGWISEWASAYEKAHRVVSNMTLAEKVNLTSGTGIYMGPCAGQTGSVPRFGIPNLCLHDSPLGVRNSDHNTAFPAGITVGATFDKDLMYERGVGLGEEARGKGINVLLGPSVGPIGRKPRGGRNWEGFGADPSLQAFGGSLTIKGMQSTGAIASLKHLIGNEQEQHRMSSVITQGYSSNIDDRTLHELYLWPFAESVRAGAGSVMIAYNDVNRSACSQNSKLINGILKDELGFQGFVVTDWLAHIGGVSSALAGLDMSMPGDGAIPLLGTSYWSWELSRSVLNGSVPVERLNDMVTRIVATWYKMGQDKDYPLPNFSSNTEDETGPLYPGALFSPSGIVNQYVNVQGNHNVTARAIARDAITLLKNNENVLPLKRNDTLKIFGTDAGTNSDGINSCTDKGCNKGVLTMGWGSGTSRLPYLITPQEAIANISSNAEFHITDTFPLGVTAGPDDIAIVFINSDSGENYITVDGNPGDRTLAGLHAWHNGDNLVKAAAEKFSNVVVVVHTVGPILMEEWIDLDSVKAVLVAHLPGQEAGWSLTDILFGDYSPSGHLPYTIPHSESDYPESVGLIAQPFGQIQDDYTEGLYIDYRHFLKANITPRYPFGHGLSYTTFNFTEPNLSIIKALDTAYPAARPPKGSTPTYPTAKPDASEVAWPKNFNRIWRYLYPYLDNPEGAAANSSKTYPYPDGYTTEPKPAPRAGGAEGGNPALWDVTFSVQVKVTNTGSRDGRAVAQLYVELPSSLGLDTPSRQLRQFEKTKILAAGESEVLTLDVTRKDLSVWDVVVQDWKAPVNGEGVKIWVGESVADLRVGCVVGEGCSTL
Protein: Serine protease HTRA4 (EC 3.4.21.-) (High-temperature requirement factor A4) (P83105)
Organism: Homo sapiens (Human)
Function: Serine protease.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Serine protease 58
- Chorion-specific transcription factor GCMa
- Serine protease 1
Sequence:
MIRPQLRTAGLGRCLLPGLLLLLVPVLWAGAEKLHTQPSCPAVCQPTRCPALPTCALGTTPVFDLCRCCRVCPAAEREVCGGAQGQPCAPGLQCLQPLRPGFPSTCGCPTLGGAVCGSDRRTYPSMCALRAENRAARRLGKVPAVPVQWGNCGDTGTRSAGPLRRNYNFIAAVVEKVAPSVVHVQLWGRLLHGSRLVPVYSGSGFIVSEDGLIITNAHVVRNQQWIEVVLQNGARYEAVVKDIDLKLDLAVIKIESNAELPVLMLGRSSDLRAGEFVVALGSPFSLQNTATAGIVSTKQRGGKELGMKDSDMDYVQIDATINYGNSGGPLVNLDGDVIGVNSLRVTDGISFAIPSDRVRQFLAEYHEHQMKGKAFSNKKYLGLQMLSLTVPLSEELKMHYPDFPDVSSGVYVCKVVEGTAAQSSGLRDHDVIVNINGKPITTTTDVVKALDSDSLSMAVLRGKDNLLLTVIPETIN
Protein: Mesoderm posterior protein 2 (O08574)
Organism: Mus musculus (Mouse)
Function: Transcription factor with important role in somitogenesis. Defines the rostrocaudal patterning of the somite by participating in distinct Notch pathways. Regulates also the FGF signaling pathway. Specifies the rostral half of the somites. Generates rostro-caudal polarity of somites by down-regulating in the presumptive rostral domain DLL1, a Notch ligand. Participates in the segment border formation by activating in the anterior presomitic mesoderm LFNG, a negative regulator of DLL1-Notch signaling. Acts as a strong suppressor of Notch activity. Together with MESP1 is involved in the epithelialization of somitic mesoderm and in the development of cardiac mesoderm. May play a role with Tcf15 in the differentiation of myotomal and sclerotomal cells by regulating Pax family genes. Controls also the expression of the protocadherin PCDH8/PAPC, EPHA4, RIPPLY2, NOTCH2, FGFR1, and CER1. Binds to the E-boxes within the EPH4A and RIPPLY2 enhancers.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:15902259, ECO:0000269|PubMed:16996494}.
Interaction partners:
Sequence:
MAQSSPPQSLQGLVPLGLLPGLGLGSAIGLHVSGLVLRFVRFLPFYATRRPSQPAGPARSTRTTQATAPRRTRPAPAGGQRQSASEREKLRMRTLARALQELRRFLPPSVAPAGQSLTKIETLRLAIRYIGHLSALLGLSEDSLRRRRRRSADAAFSHRCPQCPDGGSPSQAQMLGPSLGSAMSSGVSWGCPPACPGPLISPENLGNRISNVDPRVTPPYCPQIQSPLHQSLERAADSSPWAPPQACPGMQMSPEPRNKTGHWTQSTEPAELTKVYQSLSVSPEPRLSLGSPLLLPRPSCQRLQPQPQPQPQWGCWGHDAEVLSTSEDQGSSPALQLPVASPTPSSGLQLSGCPELWQEDLEGPPLNIFY
Protein: Antitoxin TacA (O05910)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- tRNA-acetylating toxin
- Probable NAD
- Uncharacterized protein
Sequence:
MHRAGAAVTANVWCRAGGIRMAPRPVIPVATQQRLRRQADRQSLGSSGLPALNCTPIRHTIDVMATKPERKTERLAARLTPEQDALIRRAAEAEGTDLTNFTVTAALAHARDVLADRRLFVLTDAAWTEFLAALDRPVSHKPRLEKLFAARSIFDTEG
Protein: Kinase (EC 2.7.-.-) (Q57X56)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGEEENLRRNSLRSSVRPSVVAILDLPESNECRSVSRKATENARASHLEKAKGSTDDADGYRSSAELTPAQKHSDGNHSFTTVPMWERRTSGVGNGSSDLHTDACDNSNALVGFPTAEGGGGPGSGRHIDKIRSIVESTSSSNVQRELSRTNDTIGKRRVSGSTQCSACSDNDENNAPTETPVWRWMDDVHWPSLDGERESCSVTQSPVTARRPAHAEQSADNHPLPRDGSMSRSSYNDAHSGFTPSDEAETEHCSCRISGNSTVASRVLGRVPGEGGRCINLLQRRRRVANGFSTARATGLFGTGGGSQTSVSPAEGFTATLSGGHSSIGGHHLAFQHNGVFMKESCSRREESFYEMLKPVQEYVERYAVFFAALYASEEAAYCRDKMGDVDDKVVVEGNATTEEDTKAPLTPGVCEDEFVAECDASGDDGDPDSSNTLVGPPRDWKAGGHGASGTYGVAGDCAEDIGEGNGEEAVGGEGGFPISHDMSSSTEGHLFSRDVKNWEFLVRLAPFVPRYHGLYHVRVNPTGDVDSVRAEAVESAQECALTSSAPRETTENRSGEGEKIAGVGLRQMIVLEDICSGFQHPCVLDLKMGKRQYGLNPPEAKLRSKEHKAAQTTTKLYGVRLAGMRRWCPDKQRYETRSKLAGRLLSLDGLRDTIYRFMQRSSRIQQVFKRQIMRLRRAFFQDHVYRFFTSSLLFVYDADDPLTSARVVMVDFAFTYEREELLRGGDADAEQDKDVGYIEALKTVLDMLT
Protein: Envelope glycoprotein M (gM) (P52370)
Organism: Bovine herpesvirus 1.1 (strain Cooper) (BoHV-1) (Infectious bovine rhinotracheitis virus)
Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network.
Subcellular location: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
Interaction partners:
Sequence:
MAGSAQPAAVHWRLWLAQVGVFAGLALLLLITLIGAASPGAGLPCFYAAIVNYNARNLSADGGAWAQRELGARHPALFLETPTTAAFSAYTAVVLLAVAAFDVAAAIIIRRENSGGFAAAYHMNALATLATPPGALLLGALAAWTLQAAVLLLSHKIMVLAAATYLAHLAPPAAFVGLFCTAGLPGAEYAQAVHALRERSPRAHRLLGPGRAVMINLAGGLLALIIGTAPLMLGQLLGAGLGLSLAQTVVAGVTVFCLAAVLFLVLTELVLSRYTQVLPGPAFGTLVAASCIAVASHDYFHQLRGVVRTQAPRAAARVKLALAGVALLAVAMLVLRLVRACLHHRRKGSAFYGHVSAARQQAARYIARARSSRGMAPLEGDAAALLDRGVASDDEEAVYEAHAPPRPPTIPLRRPEVPHSRASHPRPPPRSPPPAHVK
Protein: UBA domain-containing protein 8 (O94685)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- AP-2 complex subunit alpha
- Cytoskeletal protein syp1
- Epsin-1
- Uncharacterized calcium-binding protein C800.10c
- Probable clathrin heavy chain
- Actin cytoskeleton-regulatory complex protein end3
- Cell division control protein 42 homolog
- Polyubiquitin
- Clathrin light chain
- AP-2 complex subunit sigma
Sequence:
MQPLQLSPIEQQEFDRLLESLHPEQKDLIPGSVIGPFLLKFGLPQKILAKIWDYCDQEDKGSLDRNQVYACFRLISQAQRGATLQELDYNKAGDPPILPKQAKDDHHIKRSSSETADFTPFRIPINPDERSEYEKEFRENLRGHEDSARPGCMPSSIAKPILLKSSLHYAVLAQIWNLADSAHVGYLEMYQYVIARHLVAICKQYNLIHLPRSLPADVIESAKSETPAMNTNIEQGVTQPSLVNTEQLSHQQSISSTKSSKLDEISADNNAQSAVDNKYSSPPQTIDPQANIKALITPEDRSNFYQLFSKIDNENKGYIVGGEAVPFFMASHLDSEELARIWDTVDTQDRGYIDKDEFAVAMEIIKLRLSGKSLASILAYDDNPTEPTMQQNLVSDDTNASTAVPVAFTNDNVSNVPLSVADNEPNSTLNLLASSDTAAFEPTAVSLHENPSSSLEDLQSAFQNTSFQDQVSTQNQANTADISQNTESGSSTQGQMFGIPPTTQSIPLKMAGFPGGVNSSLTDIKEEEAVSENAPQQEERSFEQIKTSIHIAPENISAIEESKSVPLPTSFATTIPGSTSAALDDQQTTEAPFEEPDEPAHEPTEEEQEEMRKLEEKIESTKYGLETIQTSGKTIKQRIEQKKTRLMILREELQELDAIKEEAQKQISQSLIADQQLSTQIGSVGMGKKQAVKELRKLQAKIDSIIADSMSPMGTGAVNSPAIKPQVTPAPPTPAPTPAVKHHPPPPPVRSSISPSMPPAPLTHANSSTPMNYVSQPESPPQSYESIQNDNELLQELLSMGFPREKAVIALEATNYDVNEAANILLSSV
Protein: Fas-binding factor 1 C-terminal domain-containing protein (Q9XWN2)
Organism: Caenorhabditis elegans
Interaction partners:
- TRAF3-interacting protein 1
- 5'-3' exoribonuclease 2 homolog
- Centriolar and ciliogenesis-associated protein hyls-1
- DNA-directed RNA polymerase II subunit RPB1
- GAS
- DNA-directed RNA polymerase II subunit RPB2
- Cilia- and flagella-associated protein 157
- Cytoplasmic dynein 2 light intermediate chain 1
- TALPid3
- Kinesin-associated protein
Sequence:
MSDDEWGDLLDNLDTEPPQPAPPPPPNLPGNSKNSRPKSSGLDFLLDSDLDKEPQAPKTVNFATNREENTSEMRAAGRSTNALSDLFGTSTGSGLGASGAASAPRRPAGASTLDDLFGTAPRAATVTPGVTVAAPAASQPTATAPPPDNFDAGRILRLEAELERVNRELEDTKRKKREDEEDLENFWKTKLEIQSKDSEKALEDSKTAQRAQISKLQDEHHVELERLKANYDRQLENVTSSTSQVGDLVAVVGKVDTISTNIDKIAADVVASTNKVSSEQSALFHLQEELLKIRETKLSEDVAALKLEQLKVHELNLSLKDLVKNQQDENEQEKWRTKEEWNRLKIERQIFKENQDRVIENVQREKLDLANKLKFYHKDQTELLFRLSSERELLEQEKSEFFAKRDQDIKRIKAEAYELDLKSQQISTADQHVTEMKLVTEAKYRQLQHLETLLTAECSEIERIRNEQKIGGNVDSGRDARRISREEELFGSNNSNQNSHRHRSESVRASLKKHYENLEKYAGQKVAHVAPQNN
Protein: Uncharacterized protein (Q38FF8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPTPRETVVAFLTQACCGTIVALHRMGGMEVMLYKEQLVVMLTRYFNSCWNSLLSGDDPYVVESFNMMKHDNPGCVMRYLFSVGTSVLPDEPPQEIARYSPEDTDDLEAARVTISETLQQLLAERIAVDPFQHSCEGLSLSAERTAWSEKGCPPQNFFEIS
Protein: 17kDa alpha-amylase/trypsin inhibitor 2 (allergen Ory s 17kD) (Q7X8H9)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Seed storage protein.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Os05g0392050 protein
- Os05g0392000 protein
- Expressed protein
- Os10g0372500 protein
- Kinesin-like protein KIN-14I
- ARF GAP-like zinc finger-containing protein ZIGA2, putative, expressed
- Os11g0209700 protein
- Coatomer subunit gamma-1
- Coatomer subunit gamma-2
- Os05g0210600 protein
Sequence:
MALASDKFVLSAIVLAVLTVAAAAAGYGGYGDVGEYCRVGKAVSRNPVPSCRNYIARWCAVAGGRLDSGKQPPRQLLEPCCRELAAVPMQCRCDALSVLVRGVVTEEGDRVAGMISQHAAPGCDAATIAGMASALTDYGRCNLQHTGFFGCPMFGGGMD
Protein: ATP-dependent RNA helicase mss116, mitochondrial (EC 3.6.4.13) (O13622)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: ATP-dependent RNA helicase required for mitochondrial splicing of group I and II introns. Also required for efficient mitochondrial translation (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Nucleolar protein 58
- KRR1 small subunit processome component homolog
- Ribosome biogenesis protein erb1
- GTPase grn1
- Uncharacterized RNA-binding protein C1827.05c
- Pescadillo homolog
- Ribosome production factor 2 homolog
- ATP-dependent RNA helicase dbp4
- Probable nucleolar GTP-binding protein 1
- Ribosome biogenesis protein bms1
Sequence:
MNISLKGAIFSTVGRFNLPKVQGFIRWNSTMKSQQPTLFSEVASLSSTFKNSLSRAGFEKMTPVQQRVLNEVFPNEENAVVQAKTGTGKTLAFLLVAFKDVLKGKPRLNSSKIHSVILSPTRELALQIFEEARKLTYGTGIRVSYAIGGNSKMREENAIRRGNANLLIATPGRLEDHLQNPRILESLSTDSFILDEADRLMDMGFAESILNIHEAVTTTKTRKLCFSATMPPKVSNVFRGILGTDFKLINCLDPNEPPTHERVPQFVIETKLDKVFSSSLSLLQQLTSSNPSSRIIVFLPTISMVDFVGGVLENHLKIPCFILHSGLTTAQRRSITESFRKCQSGILFATDVVARGMDFPNITQVVQITGPSNTDDYIHRIGRTGRAGKTGEAYLILLEQEKPFLNSIKHLPLKRATIEPLSDQALSTLRSDIEKSSKFSRTNALKTLYGSKPHVFSGSSQRRATGKNIHESAIALFSLHDVPGLMEELIYKSRGRGSPKGFRGSQLKYPSSSSSSFQRRPRSLPSRGRYQQSRR
Protein: Formin-like protein 1 (Formin-related protein) (Q9JL26)
Organism: Mus musculus (Mouse)
Function: Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics and cell shape. May play a role in the control of cell motility and survival of macrophages.
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane; Lipid-anchor. Cytoplasmic vesicle, phagosome. Note=Recruited to actin-rich phagosomes during phagocytosis. Translocates to the plasma membrane upon activation by RAC1.
Interaction partners:
- Cell division control protein 42 homolog
- Profilin-1
- Profilin-2
- SLIT-ROBO Rho GTPase-activating protein 2
- Ras-related C3 botulinum toxin substrate 1
- Teratocarcinoma-derived growth factor
- Profilin-4
- Profilin-3
- Profilin
- SLIT-ROBO Rho GTPase-activating protein 3
Sequence:
MGNAAGSAEQPAGPTASPPKQPAVPKQPMPAAGELEERFTRVLNCMNLPPDKVQLLSQYDNEKKWELICDQERFQVKNPPAAYIQKLKSYLDTGGVSRKVASDWMSNLGFKRRVQESTQVLRELETSLRTNHIGWVQEFLNEENRGLDVLLEYLAFAQCSVAYDMESTDSVASGAEKSKPLDQSVEDLSKAPPSSVPKSRLTIKLTPAHSRKALRNSRIVSQKDDVHVCIMCLRAIMNYQSGFSLVMNHPACVNEIALSLNNKSPRTKALVLELLAAVCLVRGGHDIILAAFDNFKEVCGEQHRFEKLMEYFRHEDSNIDFMVACMQFINIVVHSVENMNFRVFLQYEFTHLGLDLYLERLRLTESDKLQVQIQAYLDNVFDVGTLLEETETKNAVLEHMEELQEQVATLTERLRDTENDSMAKIAELEKQLSQARKELETLRERFSESTPMGTSRRIPEPEKVPVPTVVRPSALELKVEELEEKGLIRILRGPGDVVSIEILPGAAATPSGDDAQAPRVSTDSPSTAESIPEAASPPPPPPPPPPPLPNLQSQQEAPPSAPPLAPPLPGCAEPPPAPPLPGDLPPPPPPPPLGTDGPVPPPPPPPPGGPPDILGGQGPDIGPGVKAKKPIQTKFRMPLLNWVALKPSQITGTVFTELNDEKVLQELDMNDFEEHFKTKSQGPCLDISALKGKASQKAPTKTILIEANRAKNLAITLRKGNLGADRICQAIETYDLQTLSLDFLELLTRFLPTDYERSLIARFEKEQRPMEELSEEDRFMLRFSRIQRLPERMNTLTFLGNFPDTAQLLMPQLNAIIAASMSIKSSDKLRQILEIVLAFGNYMNSSKRGAAYGFRLQSLDALLEMKSTDRKQTLLHYLVKVIAEKYPQLTGFHSDLHFLDKAGSVSLDSVLGDVRSLQRGLELTQREFVRQDDCLVLKEFLRANSPTMDKLLADSKTAQEAYESVVEYFGENPKTTSPSMFFSLFSRFTKAYKKAEQEVEQWKKEAAADTSGREEPPTPKSPPKARRQQMDLISELKRKQQKEPLIYESDRDGAIEDIITDLRNQPYIRADTGRRSARRRPPGPPLPVTTDLAL
Protein: Structure-specific endonuclease subunit SLX4 (Mutagen-sensitive protein 312) (Q9VS48)
Organism: Drosophila melanogaster (Fruit fly)
Function: Regulatory subunit that interacts with and increases the activity of different structure-specific endonucleases. Has several distinct roles in protecting genome stability by resolving diverse forms of deleterious DNA structures originating from replication and recombination intermediates and from DNA damage (By similarity). Component of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA (By similarity). Interacts with the structure-specific MEI-9-ERCC1 endonuclease to generate meiotic crossovers.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Bifunctional glutamate/proline--tRNA ligase
- Structure-specific endonuclease subunit SLX1 homolog
- DNA repair endonuclease XPF
- DNA excision repair protein ERCC-1
- Crossover junction endonuclease MUS81
- Methyl methanesulfonate sensitivity 4
- Tyrosine--tRNA ligase
- Fanconi anemia group D2 protein homolog
- RecQ-like DNA helicase Blm
- Salivary gland secretion 1
Sequence:
MDRKTRRANFKNLQPRLTRSTKAAADTLSLSNFFATPENAEEVPSCLADIPVQPDPPAPKIKPIRTSNVFEKPGPKPKKAPKLKASTVSTSSGARRGRGKSKQQPSISNFLRNEQIFAEVTAQHCMADNFSADDIEMALALSKSESEKHGRLRLHDDDDAVVDLLDDEEKSTERIRHKLQKYGFRTAAKEDYKSLAVLPVVASKGGRRGKWANRFTSLTLRNPDVQQKKLEEKVSALLGQEMRGKEPNGEDCCLTPYTVITAALKELRAEGESRILREPSEGPIDDLESYYVTDLFEVSRTPAHHLLKNWAAIQGRDFSPERETQKCRQLRQQHELVYAELERYYGDPQKLEEEVMQELDELEKLVADNMIEDDSVVINIVEAESSSTGSSPSKEPPDKRPKMTMEDKENLQPTTSKASLTVPAQSTRCTSPDLFADSEDEPDIVTTAISNEPEDVRNLSMKVYKNVSISERSSSVAEIEIVSSNDEPSQITTYEVFSSDEVKTVSNATQEKISFDDDFIDLTQEFDMVEFNESKPRTPNLIASSETDSNVDNLNGDTILDFSSQEVSCPISKELYAKYAKVETFPVWNAAAEEEDKIEFSLSMERDLKSSEQSSHQLGILTTPNDTEHSSSFSELNFSRNSLRRSVSLSTDLSFKSPLNWKMNSSAEKRVSPAASPYKQSDASVDLTQNSDDENDAILLSDEEINYSIWKGNKTVKDLDIGDDSSDSCFASPVTKKRAIPQFQTEEDLDAFLMDFSTDGNGSQGSHSPNKSALSKERAEFGILDAAPSQPFSLSELQSHADKEKSSDNEINWAEASFLDAPAKPLSRRSSHKFNELLAKISKPAHNSGDDFDEFDQMVFQSTKEAASSAGETSDMPQGLDLLLKGEIKTTAIPETRAPGNQTPIEPQQVDVDGNVYSVRVCHTPKPDFATLPESEILQQLYKYGIKPLKRKQAVKMLEFIYNQTHPIMKTAAVQDLPARSEPIVRSKSTPVIMERPHSQVAKSTSKTLKAIGTKKDLTFNDATGEELLRFSQSLAPSLCDDFETFVMQTNVTKKTPQPLVPLHIAWHNLICANPQLHESVLTYEPIDLQAVYLHLKHMGHRYDPKDLKTFFDRRCIIFRYELGAPGKQAERHVRRHTKKPSKRK
Protein: Small conjugating protein ligase-like protein (G0SCM5)
Organism: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila)
Interaction partners:
- Putative vacuolar protein sorting-associated protein
- SNAP receptor-like protein
- Probable vacuolar protein sorting-associated protein 16 homolog
- CNH domain-containing protein
- E3 ubiquitin-protein ligase PEP5
- Tgf beta receptor associated protein 1-like protein
- Vacuolar assembly protein
- Vacuolar protein sorting-associated protein 8 central domain-containing protein
- Synaptobrevin homolog YKT6
- CCZ1/INTU/HSP4 first Longin domain-containing protein
Sequence:
MAGQFAAKRLGKELQKIRNSLPPGIELVSADNFEEWLLDIRVLDDNPLYANQTYRLRFRFGSTYPIEPPEVVFVKSADRPIPIHPHIYSNGIICLDLLGHQGWSPVQNVESVCMSLQTPRLPTPTWIHNHQTPHGGLVSMAPRAGFDAEQVRDKARKDLLHLLEGVRGKKNLVIEKDLAGPLGVIVKASTLRDYGVDNFFFLENKNTGTSQRNIVFIARGESVRNAHAIAAQIKRIQRESQTSHDFHIFWVPRRTLFSDKVLEEAGVLGDANISELPLYFFPLERDVLSLELNDSFRDLYLAKDPTPVFLLSRALMGIQKKHGLFPRIIGKGENAKRVADLLSRMRQELLAGEEAGESDRAGLSPSTTIESVIIIDREVDFVTPLLTQLTYEGLIDEYFGIQNNQTDVDAVIVGAPAQSAASTSTAVPTNSSQSRKRKIQLDGSDSLYSQLRDANFAIVGSLLNTVARRLKSDYESRHNTKTTAELKEFVKKLPGYQAEQQSLKIHSNIAEEIINYTRTEIFNKLLEVQQNLAAGADPSSQFDSIEELVARDTPLPQVLRLLCLYSCISGGIKTKELDHFRRLVLQGYGHQHLLTLHNLERLQMFLSKSSPLASMITMSGSSGGPDQKTNYTYLRKQLRLIVDEVNEQDPNDIAYVYSGYAPLSIRLVQCVLQKQYLLSITKGSGTVIAAGPVAGGGAQGWKGFEEIVKHARGPTFDEIQKGEDKAVKARALLSGSSGDKKTVFVVFVGGITFTEIAALRFIAKQEEARRNIVICTTSIINGNRMMNAAIETATFEKTTVTTAAAQ
Protein: Myosin light chain kinase family member 4 (EC 2.7.11.1) (Sugen kinase 85) (SgK085) (Q86YV6)
Organism: Homo sapiens (Human)
Interaction partners:
- Myosin light chain 6B
- Myosin regulatory light chain 12A
- Myosin light chain 3
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- Myosin light chain 4
- Myosin light polypeptide 6
- Myosin regulatory light polypeptide 9
- Myosin regulatory light chain 12B
- cAMP-dependent protein kinase catalytic subunit gamma
- cAMP-dependent protein kinase catalytic subunit alpha
Sequence:
MLKVKRLEEFNTCYNSNQLEKMAFFQCREEVEKVKCFLEKNSGDQDSRSGHNEAKEVWSNADLTERMPVKSKRTSALAVDIPAPPAPFDHRIVTAKQGAVNSFYTVSKTEILGGGRFGQVHKCEETATGLKLAAKIIKTRGMKDKEEVKNEISVMNQLDHANLIQLYDAFESKNDIVLVMEYVDGGELFDRIIDESYNLTELDTILFMKQICEGIRHMHQMYILHLDLKPENILCVNRDAKQIKIIDFGLARRYKPREKLKVNFGTPEFLAPEVVNYDFVSFPTDMWSVGVIAYMLLSGLSPFLGDNDAETLNNILACRWDLEDEEFQDISEEAKEFISKLLIKEKSWRISASEALKHPWLSDHKLHSRLNAQKKKNRGSDAQDFVTK
Protein: Sad1-interacting factor 3 (Q09877)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MSTKDKLNLPPKRTINTRLSTPVHIPPPINSESTRITPQHGSPPRFGDHRISAAQGLFQRRRNARKIDHPLGWFLKNRHAAAHIPQRTTKTSQKLVLLPENHAVNSFNEEESNYEDLLTPSDAYNLIKLENLPRDKREELGFPRATAYCVCEAFQLPKVKHFLKHYHKVRAKKYDEVLYAVYHLPLVYGRSESCRVSSGPAPDDMPSSASNHNQKHLDSDKPDNENFDSHIISQLYRISEIFVFSYGVVVFWNFSLSQEKDILADLTFGGDNSLMVKPLAEEECEIEDLHFHYAPNTKRPRIYNDMIHIPSADNKMKLAMSHALAQSVKLSRFELRTDVTMNSALFYPKKLALYGHLGLSRVEVVRMSGHLFQLRVDVNLISNILDTPDFLWDSEPLLLPLYTAFREYLEIGPRTNVLNRRCKVIFDMLDIFGKSSADRKMNSITWIIIILISLFVIIFTLEVILRLRWAHR
Protein: Cathepsin B-like cysteine proteinase 4 (EC 3.4.22.-) (Cysteine protease-related 4) (P43508)
Organism: Caenorhabditis elegans
Function: Thiol protease which shows activity against the fluorogenic substrate z-Arg-Arg-AMC.
Subcellular location: Secreted {ECO:0000269|PubMed:28723894}. Note=Secreted from animals irradiated with ultraviolet or ionizing gamma rays into the culture medium. {ECO:0000269|PubMed:28723894}.
Interaction partners:
- Aspartic protease 3
- Aspartic protease 4
- legumain
- Peptidase A1 domain-containing protein
- Neprilysin-2
- Neprilysin-1
- Neprilysin-11
Sequence:
MKYLILAALVAVTAGLVIPLVPKTQEAITEYVNSKQSLWKAEIPKDITIEQVKKRLMRTEFVAPHTPDVEVVKHDINEDTIPATFDARTQWPNCMSINNIRDQSDCGSCWAFAAAEAASDRFCIASNGAVNTLLSAEDVLSCCSNCGYGCEGGYPINAWKYLVKSGFCTGGSYEAQFGCKPYSLAPCGETVGNVTWPSCPDDGYDTPACVNKCTNKNYNVAYTADKHFGSTAYAVGKKVSQIQAEIIAHGPVEAAFTVYEDFYQYKTGVYVHTTGQELGGHAIRILGWGTDNGTPYWLVANSWNVNWGENGYFRIIRGTNECGIEHAVVGGVPKV
Protein: Diacylglycerol kinase (DAG kinase) (DAGK) (EC 2.7.1.107) (P9WP29)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the phosphorylation of diacylglycerol (DAG) into phosphatidic acid. Is involved in the biosynthesis of phosphatidylinositol mannosides (PIMs), probably via a role in the biosynthesis of phosphatidylinositol (PI), a PIM precursor, which is derived from phosphatidic acid.
Subcellular location: Secreted, cell wall {ECO:0000250|UniProtKB:P9WP28}.
Interaction partners:
- Possible flavoprotein
- Protein Rv2250A
- Glycerol-3-phosphate dehydrogenase 1
- Phosphatidate cytidylyltransferase
- 1-acylglycerol-3-phosphate O-acyltransferase
- Triacylglycerol lipase
- Putative diacyglycerol O-acyltransferase Rv3087
- Putative diacyglycerol O-acyltransferase Rv2484c
- Putative diacyglycerol O-acyltransferase Rv3480c
- Putative diacyglycerol O-acyltransferase Rv2285
Sequence:
MSAGQLRRHEIGKVTALTNPLSGHGAAVKAAHGAIARLKHRGVDVVEIVGGDAHDARHLLAAAVAKGTDAVMVTGGDGVVSNALQVLAGTDIPLGIIPAGTGNDHAREFGLPTKNPKAAADIVVDGWTETIDLGRIQDDNGIEKWFGTVAATGFDSLVNDRANRMRWPHGRMRYYIAMLAELSRLRPLPFRLVLDGTEEIVADLTLADFGNTRSYGGGLLICPNADHSDGLLDITMAQSDSRTKLLRLFPTIFKGAHVELDEVSTTRAKTVHVECPGINVYADGDFACPLPAEISAVPAALQVLRPRHG
Protein: 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase (EC 5.3.3.5) (Cholestenol Delta-isomerase) (Cholesterol-5,6-epoxide hydrolase subunit EBP) (EC 3.3.2.11) (Delta(8)-Delta(7) sterol isomerase) (D8-D7 sterol isomerase) (Emopamil-binding protein) (Sterol 8-isomerase) (Q9JJ46)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the conversion of Delta(8)-sterols to their corresponding Delta(7)-isomers.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q15125}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q15125}. Nucleus envelope {ECO:0000250|UniProtKB:Q15125}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q15125}. Note=During interphase, detected on the endoplasmic reticulum and the nuclear envelope. During mitosis, detected on cytoplasmic vesicles. {ECO:0000250|UniProtKB:Q15125}.
Interaction partners:
- Lathosterol oxidase
- Delta
- Transmembrane 7 superfamily member 2.
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- 7-dehydrocholesterol reductase
- Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating
- Lanosterol synthase
- Lanosterol 14-alpha demethylase
- Squalene monooxygenase
- Methylsterol monooxygenase 1
Sequence:
MTTNMLPLHPYWPRHLRLDNFVPNDLPTWHILVGLFSFSGVLIVITWLLSSRVSVVPLGTGRRLALCWFAVCTFIHLVIEGWFSFYHEILLEDQAFLSQLWKEYSKGDSRYILSDGFIVCMESVTACLWGPLSLWVVIAFLRHQPFRFVLQLVVSVGQIYGDVLYFLTELRDGFQHGELGHPLYFWFYFVIMNAIWLVIPGILVFDAIKHLTNAQSMLDNKVMKIKSKHN