wanglab/gogpt-training-data huggingface dataset:
Protein: Ribosome biogenesis protein BMS1 (EC 3.6.5.-) (Q08965)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May act as a molecular switch during maturation of the 40S ribosomal subunit in the nucleolus. The depletion of BMS1 interferes with processing of the 35S pre-rRNA at sites A0, A1, and A2, and the formation of 40S subunits.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11565749}. Nucleus, nucleolus {ECO:0000269|PubMed:11565749}.
Interaction partners:
- U3 small nucleolar ribonucleoprotein protein IMP4
- U3 small nucleolar RNA-associated protein 9
- Small ribosomal subunit protein eS27A
- Something about silencing protein 10
- Small ribosomal subunit protein eS1A
- U3 small nucleolar RNA-associated protein 14
- U3 small nucleolar RNA-associated protein 10
- U3 small nucleolar RNA-associated protein 7
- Small ribosomal subunit protein eS4A
- U3 small nucleolar RNA-associated protein 12
Sequence:
MEQSNKQHRKAKEKNTAKKKLHTQGHNAKAFAVAAPGKMARTMQRSSDVNERKLHVPMVDRTPEDDPPPFIVAVVGPPGTGKTTLIRSLVRRMTKSTLNDIQGPITVVSGKHRRLTFLECPADDLNAMIDIAKIADLVLLLIDGNFGFEMETMEFLNIAQHHGMPRVLGVATHLDLFKSQSTLRASKKRLKHRFWTEVYQGAKLFYLSGVINGRYPDREILNLSRFISVMKFRPLKWRNEHPYMLADRFTDLTHPELIETQGLQIDRKVAIYGYLHGTPLPSAPGTRVHIAGVGDFSVAQIEKLPDPCPTPFYQQKLDDFEREKMKEEAKANGEITTASTTRRRKRLDDKDKLIYAPMSDVGGVLMDKDAVYIDIGKKNEEPSFVPGQERGEGEKLMTGLQSVEQSIAEKFDGVGLQLFSNGTELHEVADHEGMDVESGEESIEDDEGKSKGRTSLRKPRIYGKPVQEEDADIDNLPSDEEPYTNDDDVQDSEPRMVEIDFNNTGEQGAEKLALETDSEFEESEDEFSWERTAANKLKKTESKKRTWNIGKLIYMDNISPEECIRRWRGEDDDSKDESDIEEDVDDDFFRKKDGTVTKEGNKDHAVDLEKFVPYFDTFEKLAKKWKSVDAIKERFLGAGILGNDNKTKSDSNEGGEELYGDFEDLEDGNPSEQAEDNSDKESEDEDENEDTNGDDDNSFTNFDAEEKKDLTMEQEREMNAAKKEKLRAQFEIEEGENFKEDDENNEYDTWYELQKAKISKQLEINNIEYQEMTPEQRQRIEGFKAGSYVRIVFEKVPMEFVKNFNPKFPIVMGGLLPTEIKFGIVKARLRRHRWHKKILKTNDPLVLSLGWRRFQTLPIYTTTDSRTRTRMLKYTPEHTYCNAAFYGPLCSPNTPFCGVQIVANSDTGNGFRIAATGIVEEIDVNIEIVKKLKLVGFPYKIFKNTAFIKDMFSSAMEVARFEGAQIKTVSGIRGEIKRALSKPEGHYRAAFEDKILMSDIVILRSWYPVRVKKFYNPVTSLLLKEKTEWKGLRLTGQIRAAMNLETPSNPDSAYHKIERVERHFNGLKVPKAVQKELPFKSQIHQMKPQKKKTYMAKRAVVLGGDEKKARSFIQKVLTISKAKDSKRKEQKASQRKERLKKLAKMEEEKSQRDKEKKKEYFAQNGKRTTMGGDDESRPRKMRR
Protein: DNA helicase (EC 3.6.4.12) (Q8I5T7)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- ATPase AAA-type core domain-containing protein
- DNA helicase
- DNA replication licensing factor MCM3
- DNA helicase
- DNA helicase
- DNA replication licensing factor MCM2
- DNA helicase
- Origin recognition complex subunit 5
- MCL1 domain-containing protein, putative
- Origin recognition complex subunit 1
Sequence:
MDLIIELYFNKSELNDDVKTLILNWVSFFKTNWKDLFNIDKEVILKLEFFLDNKKIISKNAPPNNEVYLHELKKNPEVVLKFMKVSLHLLLFRFLCLDKETGDITIPGDDKNEEGNKNGKGNKNGKGNKYGKGNKYGKGNKYGKGNKNEKNNKNNNDNNIEENDNYNDKEKITKKKNINHNNSNRNNNNNIYCSNKYQMDLFSSKDEIDKFGNEDFLITKLKYDRYKESEIFRNFFFTNKVTIYLYNWNKVDKFESLKSEKVNQLICLRGSVLRVSPIQLLITNLNFVCDKCKCIIKVEFMDGKFEPPKKCMTNNCDGKQFLPIRESAKSLEYQKIILKENRKIVNNIYETNDTNIKNLTVTLEASKFFVNSCIPGNYVEALGILKVISFNNSHLINGKNSLFNMYIDCLSIFPLSSKKYLNNNYFNVDKIKEIKNKIHTSFLWESYIDKVDKRMLIYKRNNNNYLKNKLIESVHVEDDNEHADKKKKNTYLFKDKQDGSHHNILNSNKNNNKINCEENEKGTIHKKNCNQQTNEQLNNNTDIPPYKNNERNFVGPYKYNNDQNEDISELKSGDIFFEDKYKSFENDIFRDNVINMYGDYINEENDFNRNVHYINSSDEENENYHEKNRDNNSLHLNKEIDSKVLEFIHDMEKVGYNKFYLLISSFCPRIIMNSYIKAGLLLSLLGGKTIYDDNNQIKRRGNIHNLLIGDPGLGKSRILQYISNIMEKSLFICSTSTTINGLTACAVKDTTNNEYSLEGGALVLSDKGVCCIDELDKISLNDQQSFLECMENQSINITKAGIVCNLKTRCTIIAASNPKEGKYNYKKSIFDNIKIPFPLLSRFDLVFLLADNISEEKDYHISNYLINPNKNKNDLSEDDHTQHTDFQSDDNSKEGSYNFSESDKEEYRNNKKKEKHGIKRKRHDYSPYIFSIKDALLYKCKQINEQNYLPLELIGVYIKYCRKYIFPKLSEDAKKYIRKFYLHLRNLANTHNDISVPITIRQLESLIRLCQARARADLSHMVTLKHAKEVVEIYQKTIFYPLHLKTLNFKEKPTTKKNKGKSLAALSHVFKQKIIEQAKLKHNQIYNKELHNLARSIILSADSNVTDEALIHFVNNEGFILYKGGYWQVDSFYLK
Protein: L-cystine transporter TcyP (S-sulfocysteine transporter) (P77529)
Organism: Escherichia coli (strain K12)
Function: Involved in L-cystine import. Low affinity L-cystine transporter that is mainly involved in L-cystine uptake from outside as a nutrient. Is the primary transporter at high concentrations of cystine. Probably functions as a proton symporter (Probable). Can also transport D-cystine, cysteine and homocystine as a methionine precursor. Mediates accumulation of the toxic compounds L-selenaproline (SCA) and L-selenocystine (SeCys). Can also transport S-sulfocysteine and is required for growth on S-sulfocysteine as a sulfur source. Plays the principal role in the 3-mercaptopyruvate sulfurtransferase (3MST)-mediated generation of endogenous hydrogen sulfide (H2S).
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Inner membrane protein YdjM
- Thiosulfate transporter TsuA
- Sulfite reductase flavoprotein alpha-component
- Putative sulfur carrier protein TsuB
- Cysteine synthase A
- Sulfate adenylyltransferase subunit 2
- L-cystine-binding protein TcyJ
- L-cystine transport system ATP-binding protein TcyN
- Adenylyl-sulfate kinase
- Phosphoadenosine 5'-phosphosulfate reductase
Sequence:
MNFPLIANIVVFVVLLFALAQTRHKQWSLAKKVLVGLVMGVVFGLALHTIYGSDSQVLKDSVQWFNIVGNGYVQLLQMIVMPLVFASILSAVARLHNASQLGKISFLTIGTLLFTTLIAALVGVLVTNLFGLTAEGLVQGGAETARLNAIESNYVGKVSDLSVPQLVLSFIPKNPFADLTGANPTSIISVVIFAAFLGVAALKLLKDDAPKGERVLAAIDTLQSWVMKLVRLVMQLTPYGVLALMTKVVAGSNLQDIIKLGSFVVASYLGLLIMFAVHGILLGINGVSPLKYFRKVWPVLTFAFTSRSSAASIPLNVEAQTRRLGVPESIASFAASFGATIGQNGCAGLYPAMLAVMVAPTVGINPLDPMWIATLVGIVTVSSAGVAGVGGGATFAALIVLPAMGLPVTLVALLISVEPLIDMGRTALNVSGSMTAGTLTSQWLKQTDKAILDSEDDAELAHH
Protein: Putative cystathionine gamma-lyase 2 (EC 4.4.1.1) (Gamma-cystathionase) (P55216)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Putative cystathionine beta-synthase cbs-2
- Cystathionine beta-synthase cbs-1
- Putative thiosulfate sulfurtransferase mpst-1
- Cysteine dioxygenase 1
- Adenosylhomocysteinase
- Bifunctional L-3-cyanoalanine synthase/cysteine synthase
- Cysteine synthase 1
- Probable methionine synthase
- Cysteine synthase
- Cysteine synthase 3
Sequence:
MATFPHFGTAAIHVGQEPEQWDMNQVVPPISLSSTYKQDNPGEPKGHDYSRAGNPTRDVLQKNLAALEDAKHCQVFSSGLAATSAIINLLKYGDHIVCSDDVYGGTQRYIRRVAVPNHGLEVDSVDLTDVQNLEKAIKPNTKMVWFESPSNPLLKVVDIAAVVQTAKKANPEIVVVVDNTFMSPYFQRPISLGADVVVHSITKYINGHSDVVMGAVITDNDEFQQHLFFMQLAVGAVPSPFDCFLVNRGLKTLHIRMRAHYENALAVAKYLEANDRIESVLYPALPSHPQHEVHEKQTKGMSGMISFYLKGELQESRAFLSALKVFTLAESLGGYESLAELPSIMTHASVPAETRIVLGITDNLIRISVGIEDLDDLVADLDQALKIAIPKV
Protein: Zinc finger protein 70 (Zinc finger protein N27C7-1) (Q9UC06)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Zinc finger protein 69
Sequence:
MEVPPATKFGETFAFENRLESQQGLFPGEDLGDPFLQERGLEQMAVIYKEIPLGEQDEENDDYEGNFSLCSSPVQHQSIPPGTRPQDDELFGQTFLQKSDLSMCQIIHSEEPSPCDCAETDRGDSGPNAPHRTPQPAKPYACRECGKAFSQSSHLLRHLVIHTGEKPYECCECGKAFSQSSHLLRHQIIHTGEKPYECRECGKAFRQSSALTQHQKIHTGKRPYECRECGKDFSRSSSLRKHERIHTGERPYQCKECGKSFNQSSGLSQHRKIHTLKKPHECDLCGKAFCHRSHLIRHQRIHTGKKPYKCDECGKAFSQSSNLIEHRKTHTGEKPYKCQKCGKAFSQSSSLIEHQRIHTGEKPYECCQCGKAFCHSSALIQHQRIHTGKKPYTCECGKAFRHRSALIEHYKTHTREKPYVCNLCGKSFRGSSHLIRHQKIHSGEKL
Protein: Ubiquilin 5 (Q9D4I8)
Organism: Mus musculus (Mouse)
Interaction partners:
- Uncharacterized protein
- Fibronectin type III domain-containing protein 8
- Tumor protein D52-like 3
- SCP2 sterol-binding domain-containing protein 1
Sequence:
MARAREEAGDSQLVSGREPSSRIIRVSVKTPQDCHEFFLAENSNVRRFKKQISKYLHCNADRLVLIFTGKILRDQDILSQRGILDGSTVHVVVRSHLKGSACTGTLVGPTGQYTHRSEPSAKLGRLAGTSPDLADFFSQRVQLLPAAPESVVQLLEDPLIQGLANEKHANGVHIPETSKTVQKRDPALKFPETLQKPAQSQEVLQEHKQRLEALKAVPGGDNAMHPSCSDIHQVMLSTLALLVASKGHISALELCRGETNNAHSSSDPTTIPATSPLVRTLAQEVSTGGVSQVKGIVSSQASLGCRPGMLDLHSGSDIPCQESQQPLEKVPLTCQPRLSPCVLRLALTVLQQNPSLAHQLATGSPLLHHLPLLPILTNPRALQALLQIEEGLQILSREVPELGPLFRDSAKPRGARGAQETRGRRQAHREDTTQHSLAFLQLFHSLARACSQSSQTALPTSLFTEGRYQQELEELKALGFANRDANLQALVATDGDIHAAIEMLLGAPQD
Protein: Exosome complex component RRP46 homolog (Cell death-related nuclease 5) (G5EG59)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9NQT4}. Nucleus {ECO:0000250|UniProtKB:Q9NQT4}.
Interaction partners:
- Exosome complex component RRP4 homolog
- Exosome complex component CSL4 homolog
- Ribosomal RNA-processing protein 42
- Exosome complex component 10 homolog
- Exosome complex component RRP40
- Exosome complex component RRP45
- Putative exosome complex component RRP41
- Exoribonuclease phosphorolytic domain-containing protein
- Nuclear nucleic acid-binding protein C1D
- mRNA transport homolog 4
Sequence:
MAGRLREMRCELSFLKNADGSACFSQGATCIWASCSGPGDVHASKASDEAMTLDISYRANCGDNKFNVLNNIIHSTLSNAINLELFPHTTISVTVHGIQDDGSMGAVAINGACFALLDNGMPFETVFCGVLIVRVKDELIIDPTAKQEAASTGRVLFSVCKGSDGHPEVCAMDAIGHWDFIQLEAAWSLAQPSASAIFDFYKTVMKRKLSVDEQ
Protein: RuBisCO chaperone RbcX (Q44177)
Organism: Picosynechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum)
Function: An RbcL-specific chaperone. Required for assembly of the RbcL8 core, acting downstream of the major chaperonin (GroEL-GroES). Acts on newly folded RbcL, has a transient dynamic interaction with RbcL and is eventually displaced by RbcS. The central cleft of the RbcX homodimer (RbcX2) binds the C-terminus of an RbcL monomer, stabilizing the C-terminus and probably preventing its reassociation with chaperonin GroEL-ES. At the same time the peripheral region of RbcX2 binds a second RbcL monomer, bridging the RbcL homodimers in the correct orientation. The RbcX2(2)-bound RbcL dimers then assemble into the RbcL8 core (RbcL8-(RbcX2)8). RbcS binding triggers the release of RbcX2 (By similarity). Required for optimal reconstitution of RuBisCO into its RbcL8S8 holoenzyme form upon expression of rbcL-rbcS subunits in E.coli, and probably also in situ. A frameshift mutation that replaces half the protein reduces accumulation of both RbcL and RbcS subunits and halves activity of RuBisCO in situ and in E.coli.
Subcellular location: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00855}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00855}. Note=Most protein is cytoplasmic, but some is in the carboxysome. This cyanobacterium makes beta-type carboxysomes (Probable). {ECO:0000255|HAMAP-Rule:MF_00855, ECO:0000305}.
Interaction partners:
- Ribulose bisphosphate carboxylase large chain
- Ribulose bisphosphate carboxylase small subunit
- RuBisCO accumulation factor 1
- Carboxysome assembly protein CcmM
- CO2 hydration protein
- Carbon dioxide concentrating mechanism protein
- CO2 hydration protein
- TIGR02652 family protein
- Mo-dependent nitrogenase C-terminal domain-containing protein
- Mo-dependent nitrogenase C-terminal domain-containing protein
Sequence:
MEFKKVAKETAITLQSYLTYQAVRLISQQLSETNPGQAIWLGEFSKRHPIQESDLYLEAMMLENKELVLRILTVRENLAEGVLEFLPEMVLSQIKQSNGNHRRSLLERLTQVDSSSTDQTEPNPGESDTSEDSE
Protein: TPR-repeat-containing chaperone protein DNAJ, putative (Q584G5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
METTCKEDVPQVRFPSPTSSKSMTTSPQKLSILGDITAEPLSARRSFNDVSKVREPDGRWCRKFLSTYFRCELCQNVVTDPVQILPNVLLVCRRCALSRRVPSKDLQELPVSLTRAFEDLYEGQREVQLPSASRMSEIGRASTTSDEAICKRRMVRVKRPDAVQEGSDHSQTFPLAASINGTLNASGRSSVPLLLNKALCELENKEYCMRVEIESAEASGALELKKSYNSDMRKITARSCGTSKTLKTDADQKYEQAEYTLALELYTKAIELQPRDRLTRLTALYGNRSSAYFMAMRYAECIADCMKVVELDPNNVKLFARAAKAAAIMGDLTAAVSHMESIPEERVTPNIISEREKYKNGLDTYKRAESSFGKSDSDDAWQMLVAQFSDTIFFRIRYAESLQNQKRFLKAVEVLDVVPQERRTPKLLYIMAACLFMCGFEHFDKARTCLEDVQQLDENCAQLLKVLNIVDEGKQKGNQYFQQKKFVAAMEHYTTAIGAAVNNNQILRILYCNRAASYKEVGKYREAIEDCTRTIQLDPAFSKAYARRARCHQALSDFASAIRDFKAAIKYDPNDQELPRELRSCEQSMAKEGERERDYYYVLGVSRNATEREIKARYRELSLRWHPDKCMSLPEEERVVAERKFKIIVEAHTTLIDAVKRRDYDLKMEKERLTRSGGFGGFNGYSSETFRGHSNRFRQGSSGFW
Protein: Renin receptor (ATPase H(+)-transporting lysosomal accessory protein 2) (ATPase H(+)-transporting lysosomal-interacting protein 2) (Renin/prorenin receptor) [Cleaved into: Renin receptor extracellular fragment; Renin receptor cytoplasmic fragment] (Q6AXS4)
Organism: Rattus norvegicus (Rat)
Function: Multifunctional protein which functions as a renin, prorenin cellular receptor and is involved in the assembly of the lysosomal proton-transporting V-type ATPase (V-ATPase) and the acidification of the endo-lysosomal system (By similarity). May mediate renin-dependent cellular responses by activating ERK1 and ERK2 (By similarity). By increasing the catalytic efficiency of renin in AGT/angiotensinogen conversion to angiotensin I, may also play a role in the renin-angiotensin system (RAS) (By similarity). Through its function in V-type ATPase (v-ATPase) assembly and acidification of the lysosome it regulates protein degradation and may control different signaling pathways important for proper brain development, synapse morphology and synaptic transmission (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9CYN9}; Single-pass type I membrane protein {ECO:0000305}. Lysosome membrane {ECO:0000250|UniProtKB:Q9CYN9}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q9CYN9}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, dendritic spine membrane {ECO:0000250|UniProtKB:Q9CYN9}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000250|UniProtKB:Q9CYN9}. Endosome membrane {ECO:0000250|UniProtKB:Q9CYN9}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:32165585}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:32165585}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- V-type proton ATPase subunit S1
- Renin
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase subunit C 1
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit B, brain isoform
- V-type proton ATPase subunit D
Sequence:
MAVLVVLLSSLVSSALANEFSILRSPGSVVFRNGNWPIPGDRIPDVAALSMGFSVKEDLSWPGLAVGNLFHRPRATIMVTVKGVDKLALPTGSVISYPLENAVPFSLDSVANSIHSLFSEETPVVLQLAPSEERVYMVGKANSVFEDLSVTLRQLRNRLFQENSVLNSLPLNSLSRNNEVDLLFLSELQVLHDISSLLSRHKHLAKDHSPDLYSLELAGLDELGKRYGEDSEQFRDASRILVDALQKFADDMYSLYGGNAVVELVTVKSFDTSLVRKSRTILETKQENTQSPYNLAYKYNLEYSVVFNLVLWIMTGLALAVIITSYNIWNMDPGYDSIIYRMTNQKIRMD
Protein: Neutrophil elastase (EC 3.4.21.37) (Bone marrow serine protease) (Elastase-2) (Human leukocyte elastase) (HLE) (Medullasin) (PMN elastase) (P08246)
Organism: Homo sapiens (Human)
Function: Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis. Capable of killing E.coli but not S.aureus in vitro; digests outer membrane protein A (ompA) in E.coli and K.pneumoniae.
Subcellular location: Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:10947984}. Note=Localized in phagolysosomes following ingestion of E.coli by neutrophils. {ECO:0000269|PubMed:10947984}.
Interaction partners:
- Alpha-1-antitrypsin
- Azurocidin
- Defensin alpha 4
- Myeloperoxidase
- Cathepsin G
- Antileukoproteinase
- Lactotransferrin
- Myeloblastin
- Cathelicidin antimicrobial peptide
- Bactericidal permeability-increasing protein
Sequence:
MTLGRRLACLFLACVLPALLLGGTALASEIVGGRRARPHAWPFMVSLQLRGGHFCGATLIAPNFVMSAAHCVANVNVRAVRVVLGAHNLSRREPTRQVFAVQRIFENGYDPVNLLNDIVILQLNGSATINANVQVAQLPAQGRRLGNGVQCLAMGWGLLGRNRGIASVLQELNVTVVTSLCRRSNVCTLVRGRQAGVCFGDSGSPLVCNGLIHGIASFVRGGCASGLYPDAFAPVAQFVNWIDSIIQRSEDNPCPHPRDPDPASRTH
Protein: FI18828p1 (Puratrophin-1-like, isoform C) (Q7KU87)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTPGPKTEEPGAGKLAAEIANYVTSWMGSDGAENLQKFSQLHWDNESQLRTQEQEFEKYYFIAMKHLAKGRDLHAAALKVSVLSESANNLKSALDQFAQKLELAHERYDAAGRLLHLLTQHQRENAAREELQRLAEQLGATSLLEKHWPVMRKTHTLPVASSTPAAAAGKRVSYRCSSASRSSFEGGPSSSNCSCWRESRNLEDMDQMEEEEEEQDHDCDGGDGEEQQSKIADSGLGVCDNCERNPKLARICSCQSLNEKSHDELLEDECFDRPSKRYMDIMHSPMEANAHLQCHGSSLELPKLEELSCLDPKIQKTLLLIMREMIGTERDYVRSLYYVIENYIDELLREDIPQPLRGQRNVIFGNIEKIFEFHNSHFLGELERYERNPLKVGAAFLEMESKFYLYALYNKNKPKSDTLLSEYGSSFFKPKQMQLQDKLDLASYLLKPVQRMGKYALLLQQLVKACKGVEGAALQEIAADVEELQRAEEMVKFQLRHGNDLLAMDSLRDCDVNVKEQGRLLRQNEFLVWQGRGGKKTLRQVFLFEELVLFSKARRFPDHKNLDIYIYKNSIKTSDIGLTAHTGDSATKFEIWFRKRKPDDTWMLQCMSEDIKNAWTEEISKLLWKQAKRNREVRLAEMSSMGIGSKPCLDIRPSNNQISDRSIPLAQLNKTPKLRHSEPGKGSMRRPNSLISESSLSSGTSTTSGSSISGGSSSGHNDGGGRHSLHFGKLPGAHSASSTNCSATLELINETQALKLAKSPSGGGIKGADTAADGGNTSGNGNGNGNAFRSSKRNHKRSTTIVSQLSMESGIVSDMCVTPDQEQSAAESSRSSWSTSTTGASGASTTSASTVILRRYRSYAHAAESASPESGK
Protein: Interferon regulatory factor 3 (M0R3E9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGTPKPRILPWLVSQLDLGQLEGVAWVNKSRTRFRIPWKHGLRQDAQQEDFGIFQAWAEATGAYVPGRDKPDLPTWKRNFRSALNRKEGLRLAEDRSKDPHDPHKIYEFVNSGVGDFSQPDTSPDTNGGGSTSDTQEDILDELLEWEFEVTAF
Protein: Alcohol dehydrogenase transcription factor Myb/SANT-like family protein (O80512)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Basic-leucine zipper
- Ethylene-responsive transcription factor ERF070
- AP2/ERF and B3 domain-containing transcription factor ARF14
- Lysine-specific demethylase JMJ18
- GATA transcription factor 24
Sequence:
MSDPDSPMNHDPIPDPSPLAPLPPPLSSSAHDDASTEPASNTDLKSASIPTASKNSRRLPPPCWSLEETIALIDAYRDKWYALNRGNLKANHWEEVAEAVGANCPDVILKKTAVQCRHKMEKLRKRYRTEIQRARSVPVARFISSWVHFKRMEAMENRPEIKQGNESGDDDDHDDGNYTARYQFSGGGGGARTTPRFFNRNGTAGSGGGGGSSSSGGIRIRIPTGVSIAQPGPRFPGKIDQKYTASPSAGVSSNPRAGRGIGAGGSSYGARVVRIPEGGGKRGREMMMKTEEDDNDPMVEIASAIKLLGDTLVRTEQTRMEMTREIEAMRMDTEMKRTKMILESQQRIVEAFAKSLSDYTTTEEQDKKKKAR
Protein: Coiled-coil domain-containing protein 117 (Q8IWD4)
Organism: Homo sapiens (Human)
Function: Facilitates DNA repair, cell cycle progression, and cell proliferation through its interaction with CIAO2B.
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:30742009}. Nucleus {ECO:0000269|PubMed:30742009}. Note=Mitotic spindle. {ECO:0000269|PubMed:30742009}.
Interaction partners:
- Stress-induced-phosphoprotein 1
Sequence:
MAALGRPFSGLPLSGGSDFLQPPQPAFPGRAFPPGADGAELAPRPGPRAVPSSPAGSAARGRVSVHCKKKHKREEEEDDDCPVRKKRITEAELCAGPNDWILCAHQDVEGHGVNPSVSGLSIPGILDVICEEMDQTTGEPQCEVARRKLQEIEDRIIDEDEEVEADRNVNHLPSLVLSDTMKTGLKREFDEVFTKKMIESMSRPSMELVLWKPLPELLSDKPKPSSNTKNYTGESQAKHVAAGTAFPQRTELFSEPRPTGMSLYNSLETATSTEEEMEL
Protein: S-adenosyl-L-methionine-dependent methyltransferases superfamily protein (Q9FML3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Zinc finger
- F21J9.19
- Zinc finger A20 and AN1 domain-containing stress-associated protein 7
- Desiccation-related protein At2g46140
- Pentatricopeptide repeat-containing protein At5g21222
Sequence:
MARELVSLQYLRPPLHISRQFLNLSSPPLTLNLRPKPPQNPIFIRTDSHRNKTSADDNGIPAEDVKTIAKFKSRHNYIRVIEVSRKTNHPLAGSRLLLLDNPGNIHSISFLLKTLTDSYFDVFATLPPIIPPGPIGILGFGAGSTARLILELYPPEIAVHGWELDPSVIDVGREFFGLSKLERDHKDRIFINIGDALNASVKTGFSGILVDLFSKGSVIKELQDPQVWEDLKSRLRYRGRIMVNVGGKCVEAEDSDRDGALVMEETLRVMSQVFGDKLFVLTLGNGNDSSVALTGDLPDLDAWKKRLPRSELRSYVDMWIPYREFCLRY
Protein: Acyl-lipid omega-3 desaturase (cytochrome b5), endoplasmic reticulum (EC 1.14.19.25) (Omega-3 fatty acid desaturase 3, endoplasmic reticulum) (Q59J82)
Organism: Mortierella alpina (Oleaginous fungus) (Mortierella renispora)
Function: omega(3) desaturase that uses both 18-carbon and 20-carbon n-6 polyunsaturated fatty acids as substrates.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAPPHVVDEQVRRRIVVEDEIKSKKQFERNYVPMDFTIKEIRDAIPAHLFIRDTTKSILHVVKDLVTIAIVFYCATFIETLPSLALRVPAWITYWIIQGTVMVGPWILAHECGHGAFSDSKTINTIFGWVLHSALLVPYQAWAMSHSKHHKGTGSMTKDVVFIPATRSYKGLPALEKPAVEEEVSEQEHHHHEESIFAETPIYTLGALLFVLTFGWPLYLIVNFSGHEAPHWVNHFQTVAPLYEPHQRKNIFYSNCGIVAMGSILTYLSMVFSPLTVFMYYGIPYLGVNAWIVCITYLQHTDPKVPHFRDNEWNFQRGAACTIDRSFGTIVNHLHHHIGDSHQCHHMFSQMPFYNAVEATKYLKAKLGKYYIFDDTPIAKALYRNWRECKFVEDEGDVVFYKH
Protein: UPF0496 protein At2g18630 (Q56XQ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MMGGKSSKSKKNVEFGSPSTPVQIKINSEYTEHLSSYERACSEDPKLESFDSALHERTNRVINKLASGVEIKSLSFDSLREVTQCLLDMNQDVVKVILQDKEDIWNNQDLFSLVNLYFESTAKTMDFCSELENCLNRARRSQVIIQFAVNQFEEENEDKENRKYEKTLEELKRFKVAGEPFTKEFFALFDLVYKQQVMMLEELHKLKRKLDKRLRNIKTWRRVSNMVFVTAFVSVLIFSVVAAAVAAPPVVAAIAGALAVPVGSVGKWCNTLWTKYEKVVRGQKEIITSIRIGTYISVKEMDNISILVRKVEVEIESLLKKAEFAITEEKEVRLAIDEIKKKLDVFTETIEELGEHAGKYCSDVTKARTVILQRIIRYPAGSPKDEAPWTEMM
Protein: Seripauperin-15 (P40585)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Seripauperin-3
- Seripauperin-16
- Seripauperin-14
- Seripauperin-12
- Seripauperin-20
- Seripauperin-24
- Seripauperin-2
- Seripauperin-5
- Seripauperin-18
- Seripauperin-13
Sequence:
MVKLTSIAAGVAAIAAGVAAAPATTTLSPSDERVNLVELGVYVSDIRAHLAQYYLFQAAHPSETYPVEIAEAVFNYGDFTTMLTGIPAEQVTRVITGVPWYSTRLRPAISSALSKDGIYTAIPK
Protein: ATP synthase epsilon chain (ATP synthase F1 sector epsilon subunit) (F-ATPase epsilon subunit) (P9WPV1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- ATP synthase subunit b
- ATP synthase gamma chain
- ATP synthase subunit alpha
- ATP synthase subunit beta
- ATP synthase subunit c
- ATP synthase subunit b-delta
- ATP synthase subunit a
- Uncharacterized protein Rv1507c
- Cytochrome bc1 complex Rieske iron-sulfur subunit
- Inorganic pyrophosphatase
Sequence:
MAELNVEIVAVDRNIWSGTAKFLFTRTTVGEIGILPRHIPLVAQLVDDAMVRVEREGEKDLRIAVDGGFLSVTEEGVSILAESAEFESEIDEAAAKQDSESDDPRIAARGRARLRAVGAID
Protein: Phosphatidylinositol 4-kinase, putative (EC 2.7.1.67) (Q580E2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 1-phosphatidylinositol 4-kinase
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Inositol/phosphatidylinositol phosphatase, putative
- Phosphatidylinositol 4-phosphate 5-kinase alpha, putative
- 1-phosphatidylinositol-3-phosphate 5-kinase
- Phosphoinositide phospholipase C
- phosphatidylinositol 3-kinase
- Small GTP-binding protein Rab11
- non-specific serine/threonine protein kinase
- Small GTPase
Sequence:
MSNALFCLHRLLEVLLYLPRGSQDEQMALVQNLHEFPLATIERVFLQISHACITHKGPEVSNRLRRFMHWLAGRSFTLALRLSWTVDSVRDVFSAVGLGGRVKEVHDKIESFAINRKGVADRTNNTDGVEEEIRRKELRLKLFNDERAFLNLITNLSKHLISFTKRDRRQHELKKELDEINKSLRSQSLICPLGCNDDPVKWIVNIVVEDSVVFFSRERAPFLLRCEVIVDSTATVNDPTTSKLRLPNGKFKISAESDELMEEQSLDRRGEDVGGEVTAIKSASPDMKLFRKVFGELPEERAARLREKSFFGRHPNWGTATFVVKGGDNLRQEELALQLVDLFNNIWKNAGLTCSLVPYRALAVGVDSGIIECVEGACSIDGIKKSCQMAYLPQFFNEAFGGKGSQRYREAQRNFVETMAGYSIFTYILQVKDRHNGNILIRADGRLVHIDFGFMLVTSPGGVNFESAPFKLSQELLEVMGGVGSSPFNYFKLLFFLGMRAIREKADDIVALVSLMTPYNTLPCFGASPEVAIQQLRSRFRLDLEDEGDFALYIKELIVGSVDNWRTRRYDQFQTLQNGIL
Protein: Biotin synthase, mitochondrial (EC 2.8.1.6) (P32451)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Dethiobiotin synthetase
- Adenosylmethionine-8-amino-7-oxononanoate aminotransferase
- Biotin--protein ligase
- 7-keto 8-aminopelargonic acid transporter
- Lipoyl synthase, mitochondrial
- Vitamin H transporter
- 5-aminolevulinate synthase, mitochondrial
- Cysteine desulfurase, mitochondrial
- NifU-like protein
- Iron-sulfur assembly protein 1
Sequence:
MMSTIYRHLSTARPALTKYATNAAVKSTTASSEASTLGALQYALSLDEPSHSWTKSQLKEIYHTPLLELTHAAQLQHRKWHDPTKVQLCTLMNIKSGGCSEDCKYCAQSSRNDTGLKAEKMVKVDEVIKEAEEAKRNGSTRFCLGAAWRDMKGRKSAMKRIQEMVTKVNDMGLETCVTLGMVDQDQAKQLKDAGLTAYNHNIDTSREHYSKVITTRTYDDRLQTIKNVQESGIKACTGGILGLGESEDDHIGFIYTLSNMSPHPESLPINRLVAIKGTPMAEELADPKSKKLQFDEILRTIATARIVMPKAIIRLAAGRYTMKETEQFVCFMAGCNSIFTGKKMLTTMCNGWDEDKAMLAKWGLQPMEAFKYDRS