wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription regulatory protein SNF12 (SWI/SNF complex component SWP73) (P53628)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in transcriptional activation. Component of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, which is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
Subcellular location: Nucleus.
Interaction partners:
- SWI/SNF chromatin-remodeling complex subunit SWI1
- SWI/SNF complex subunit SWI3
- Transcription regulatory protein SNF2
- Actin-like protein ARP9
- SWI/SNF global transcription activator complex subunit SWP82
- Transcription regulatory protein SNF6
- SWI/SNF chromatin-remodeling complex subunit SNF5
- Actin-related protein 7
- Transcription regulatory protein SNF11
- Transcription initiation factor TFIID subunit 14
Sequence:
MSKVMKPSNGKGSRKSSKAATPDTKNFFHAKKKDPVNQDKANNASQITPTVPHSHPSDMVIPDHLAELIPELYSFQQLVDSEKRLDHFIHLRNLHMKRMVAQWERSKLSQEFLYPHLNFPNVKFLRIFISNVSENQPWQMDTNNEADLMALENATWTMRIEGRLLDNVQANDPAREKFSSFIESIVVDFKNKENDNVPSTKFNAAPEENATEGPSDKKLNLNLPLQFSLPNGDNSTTTNTDQNNATMGEETAKKDMSSTTPKLESVKWQYDPNNPVDFDGLDIKRVGSENVECTISILRKSSPEEPFMSYSPQLTAIIGLKSGTSHDAIFSIYKYIHLNELLTNDESAFENLMGNRNNHNSNTSTSKMLDAASSQVSIVKLDTQLITLLPSSLKESSPDTMKLTDLLSLINSTHLLPLQPIEIDYTVRVDKASTYGELVLDIEVPDVNALKFNNTQRESQIGAAELNENARELEQIKPKIALQDKEITSVLSNLHESNKRYRFFKKISEDPVKALNECIASTSNALKVLSGDEGYNEDMVRRANFYKENEAMLRENIEVILSNGRM
Protein: DNA excision repair protein ERCC-1 (P07903)
Organism: Mus musculus (Mouse)
Function: Non-catalytic component of a structure-specific DNA repair endonuclease responsible for the 5'-incision during DNA repair. Responsible, in conjunction with SLX4, for the first step in the repair of interstrand cross-links (ICL). Participates in the processing of anaphase bridge-generating DNA structures, which consist in incompletely processed DNA lesions arising during S or G2 phase, and can result in cytokinesis failure. Also required for homology-directed repair (HDR) of DNA double-strand breaks, in conjunction with SLX4 (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P07992}.
Interaction partners:
- DNA repair protein complementing XP-A cells homolog
- DNA repair endonuclease XPF
- Structure-specific endonuclease subunit SLX4
- Fanconi anemia group M protein homolog
- Structure-specific endonuclease subunit MUS81
- Structure-specific endonuclease subunit SLX1
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- DNA excision repair protein ERCC-5
- DNA repair protein XRCC1
- X-ray repair cross-complementing protein 5
Sequence:
MDPGKDEESRPQPSGPPTRRKFVIPLEEEEVPCAGVKPLFRSSRNPTIPATSAHVAPQTYAEYAITQPPGGAGATVPTGSEPAAGENPSQTLKTGAKSNSIIVSPRQRGNPVLKFVRNVPWEFGEVIPDYVLGQSTCALFLSLRYHNLHPDYIHERLQSLGKNFALRVLLVQVDVKDPQQALKELAKMCILADCTLVLAWSAEEAGRYLETYKAYEQKPADLLMEKLEQNFLSRATECLTTVKSVNKTDSQTLLATFGSLEQLFTASREDLALCPGLGPQKARRLFEVLHEPFLKVPR
Protein: Cytoplasmic FMR1-interacting protein (A0A0G2K472)
Organism: Rattus norvegicus (Rat)
Subcellular location: Synapse, synaptosome {ECO:0000256|ARBA:ARBA00034102}.
Interaction partners:
Sequence:
MAAQVTLEDALSNVDLLEELPLPDQQPCIEPPPSSLLYQPNFNTNFEDRNAFVTGIARYIEQATVHSSMNEMLEEGQEYAVMLYTWRSCSRAIPQVKCNEQPNRVEIYEKTVEVLEPEVTKLMNFMYFQRNAIERFCGEVRRLCHAERRKDFVSEAYLITLGKFINMFAVLDELKNMKCSVKNDHSAYKRAAQFLRKMADPQSIQESQNLSMFLANHNKITQSLQQQLEVISGYEELLADIVNLCVDYYENRMYLTPSEKHMLLKVMGFGLYLMDGSVSNIYKLDAKKRINLSKIDKYFKQLQVVPLFGDMQIELARYIKTSAHYEENKSRWTCTSSSSSPQYNICEQMIQIREDHMRFISELARYSNSEVVTGSGRQEAQKTDAEYRKLFDLALQGLQLLSQWSAHVMEVYSWKLVHPTDKYSNKDCPDNAEEYERATRYNYTTEEKFALVEVIAMIKGLQVLMGRMESVFNHAIRHTVYAALQDFSQVTLREPLRQAIKKKKNVIQSVLQAIRKTVCDWETGHEPFNDPALRGEKDPKSGFDIKVPRRAVGPSSTQLYLVRTMAESLSSAELLRQLKSLGMERLLHVVNAFLRQSYTYPPLLTFGETLQQCCDLSQLWFREFFLELTMGRRIQFPIEMSMPWILTDHILETKEASMMEYVLYSLDLYNDSAHYALTKFNKQFLYDEIEAEVNLCFDQFVYKLADQIFAYYKVMAGSLLLDKRLRSECKNQGATIHLPPSNRYETLLKQRHVQLLGRSIDLNRLITQRVSAAMYKSLELAIGRFESEDLTSVVELDGLLEINRMTHKLLSRYLTLDSFDAMFREANHNVSAPYGRITLHVFWELNYDFLPNYCYNGSTNRFVRTVLPFSQEFQRDKQPNAQPQYLHGSKALNLAYSSIYGSYRNFVGPPHFQVICRLLGYQGIAVVMEELLKVVKSLLQGTILQYVKTLMEVMPKICRLPRHEYGSPGILEFFHHQLKDIVEYAELKTVCFQNLREVGNAVLFCLLIEQSLSLEEVCDLLHAAPFQNILPRVHVKEGERVDAKMKRLESKYAPLHLVPLIERLGTPQQIAIAREGDLLTKERLCCGLSMFEVILTRIRTFLDDPIWRGPLPSNGVMHVDECVEFHRLWSAMQFVYCIPVGTHEFTVEQCFGDGLHWAGCMIIVLLGQQRRFAVLDFCYHLLKVQKHDGKDEIIKNVPLKKMVERIRKFQILNDEIITILDKYLKSGDGESTPVEHVRCFQPPIHQSLASS
Protein: Anthocyanidin 3-O-glucoside 5-O-glucosyltransferase 1 (EC 2.4.1.298) (UDP-glucose:anthocyanin 5-O-glucosyltransferase 3R4) (p3R4) (Q9ZR27)
Organism: Perilla frutescens (Beefsteak mint) (Perilla ocymoides)
Function: Catalyzes the glucosylation at the O-5 position of anthocyanidin 3-glucosides to form anthocyanidin 3,5-di-O-glucosides using UDP-glucose as sugar donor. Anthocyanidin 3,5-di-O-glucosides are molecules that are responsible for pigmentation. Also acts on anthocyanidin 3-O-(6-O-malonylglucoside). Much less active with hydroxycinnamoylglucose derivatives. No activity in the absence of the 3-O-glucoside group.
Interaction partners:
Sequence:
MVRRRVLLATFPAQGHINPALQFAKRLLKAGTDVTFFTSVYAWRRMANTASAAAGNPPGLDFVAFSDGYDDGLKPCGDGKRYMSEMKARGSEALRNLLLNNHDVTFVVYSHLFAWAAEVARESQVPSALLWVEPATVLCIYYFYFNGYADEIDAGSDEIQLPRLPPLEQRSLPTFLLPETPERFRLMMKEKLETLDGEEKAKVLVNTFDALEPDALTAIDRYELIGIGPLIPSAFLDGGDPSETSYGGDLFEKSEENNCVEWLDTKPKSSVVYVSFGSVLRFPKAQMEEIGKGLLACGRPFLWMIREQKNDDGEEEEEELSCIGELKKMGKIVSWCSQLEVLAHPALGCFVTHCGWNSAVESLSCGVPVVAVPQWFDQTTNAKLIEDAWGTGVRVRMNEGGGVDGSEIERCVEMVMDGGEKSKLVRENAIKWKTLAREAMGEDGSSLKNLNAFLHQVARA
Protein: NBPF family member NBPF14 (Neuroblastoma breakpoint family member 14) (Q5TI25)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MVVSAGPWSSEKAEMNILEINETLRPQLAEKKQQFRNLKEKCFLTQLAGFLANQQKKYKYEECKDLIKFMLRNERQFKEEKLAEQLKQAEELRQYKVLVHSQERELTQLREKLREGRDASRSLYEHLQALLTPYEPDKSQGQDLQEQLAEGCRLAQHLVQKLSPENDEDEDEDVQVEEAEKVLESSAPREVQKAEESKVPEDSLEECAITCSNSHGPCDSNQPHKNIKITFEEDEVNSTLVVDRESSHDECQDALNILPVPGPTSSATNVSMVVSAGPLSSEKAEMNILEINEKLRPQLAEKKQQFRNLKEKCFLTQLSGFLANQQKKYKYEECKDLIKFMLRNERQFKEEKLAEQLKQAEELRQYKVLVHAQERELTQLREKLREGRDASRSLNEHLQALLTPDEPDKSQGQDLQEQLAEGCRLAQHLVQKLSPENDNDDDEDVQVEVAEKVQKSSAPREMQKAEEKEVPEDSLEECAITYSNSHGSYDSNQPHRKTKITFEEDKVDSTLIGSSSHVEWEDAVHIIPENESDDEEEEEKGPVSPRNLQESEEEEVPQESWDEGYSTLSIPPEMLASYQSYSSTFHSLEEQQVCMAVDIGRHRWDQVKKEDQEATGPRLSRELLDEKGPEVLQDSLDRCYSTPSGCLELTDSCQPYRSAFYVLEQQRVGLAVDMDEIEKYQEVEEDQDPSCPRLSRELLDEKEPEVLQDSLDRCYSTPSGYLELPDLGQPYSSAVYSLEEQYLGLALDVDRIKKDEEEEEDQDPPCPRLSRELLEVVEPEVLQDSLDRCYSTPSSCLEQPDSCQPYGSSFYALEEKHVGFSLDVGEIEKKGKGKKRRGRRSKKERRRGRKEGEEDQNPPCPRLSRELLDEKEPEVLQDSLDRCYSTPSGYLELPDLGQPYSSAVYSLEEQYLGLALDVDRIKKDEEEEEDQDPPCPRLSRELLEVVEPEVLQDSLDRCYSTPSSCLEQPDSCQPYGSSFYALEEKHVGFSLDVGEIEKKGKGKKRRGRRSKKERRRGRKEGEEDQNPPCPRLSRELLDEKGPEVLQDSLDRCYSTPSGCLELTDSCQPYRSAFYVLEQQRVGLAVDMDEIEKYQEVEEDQDPSCPRLSRELLDEKEPEVLQDSLDRCYSTPSGYLELPDLGQPYSSAVYSLEEQYLGLALDVDRIKKDEEEEEDQDPPCPRLSRELLEVVEPEVLQDSLDRCYSTPSSCLEQPDSCQPYGSSFYALEEKHVGFSLDVGEIEKKGKGKKRRGRRSKKERRRGRKEGEEDQNPPCPRLSRELLDEKGPEVLQDSLDRCYSTPSGCLELTDSCQPYRSAFYVLEQQRVGLAVDMDEIEKYQEVEEDQDPSCPRLSRELLDEKEPEVLQDSLDRCYSTPSGYLELPDLGQPYSSAVYSLEEQYLGLALDVDRIKKDEEEEEDQDPPCPRLSRELLEVVEPEVLQDSLDRCYSTPSSCLEQPDSCQPYGSSFYALEEKHVGFSLDVGEIEKKGKGKKRRGRRSKKERRRGRKEGEEDQNPPCPRLSRELLHEKGPEVLQDSLDRCYSTPSGCLELTDSCQPYRSAFYILEQQRVGLAVDMDEIEKYKEVEEDQDPSCPRLSRELLDEKEPEVLQDSLDRCYSTPSGYLELPDLGQPYSSAVYSLEEQYLGLALDVDRFKKDEEEEEDQDPPCPRLSRELLEVVEPEVLQDSLDRCYSTPSSCLEQPDSCQPYGSSFYALEEKHVGFSLDVGEIEKKGKGKKRRGRRSKKERRRGRKEGEEDQNPPCPRLSRELLDEKGPEVLQDSLDRCYSTPSGCLELTDSCQPYRSAFYVLEQQRVGLAVDMDEIEKYKEVEEDQDPSCPRLSRELLDEKEPEVLQDSLDRCYSTPSGYLELPDLGQPYSSAVYSLEEQYLGLALDVDRIKKDQEEEEDQGPPCPRLSRELLEVVEPEVLQDSLDRCYSTPSSCLEQPDSCQPYGSSFYALEEKHVGFSLDVGEIEKKGKGKKRRGRRSKKERRRGRKEGEEDQNPPCPRLSRELLDEKGPEVLQDSLDRCYSTPSGCLELTDSCQPYRSAFYVLEQQRVGLAVDMDEIEKYKEVEEDQDPSCPRLSRELLDEKEPEVLQDSLDRCYSTPSGYLELPDLGQPYSSAVYSLEEQYLGLALDVDRIKKDQEEEEDQGPPCPRLSRELLEVVEPEVLQDSLDRCYSTPSSCLEQPDSCQPYGSSFYALEEKHVGFSLDVGEIEKKGKGKKRRGRRSKKERRRGRKEGEEDQNPPCPRLSRELLDEKGPEVLQDSLDRCYSTPSGCLELTDSCQPYRSAFYVLEQQRVGLAVDMDEIEKYKEVEEDQDPSCPRLSRELLDEKEPEVLQDSLDRCYSTPSGYLELPDLGQPYSSAVYSLEEQYLGLALDVDRIKKDQEEEEDQGPPCPRLSRELLEVVEPEVLQDSLDRCYSTPSSCLEQPDSCQPYGSSFYALEEKHVGFSLDVGEIEKKGKGKKRRGRRSKKERRRGRKEGEEDQNPPCPRLSRELLDEKGPEVLQDSLDRCYSTPSGCLELTDSCQPYRSAFYVLEQQRVGLAVDMDEIEKYKEVEEDQDPSCPRLSRELLDEKEPEVLQDSLDRCYSTPSGYLELPDLGQPYSSAVYSLEEQYLGLALDVDRIKKDQEEEEDQGPPCPRLSRELLEVVEPEVLQDSLDRCYSTPSSCLEQPDSCQPYGSSFYALEEKHVGFSLDVGEIEKKGKGKKRRGRRSKKERRRGRKEGEEDQNPPCPRLSRELLDEKGPEVLQDSLDRCYSTPSGCLELTDSCQPYRSAFYVLEQQRVGLAVDMDEIEKYQEVEEDQDPSCPRLSRELLDEKDPEVLQDSLDRCYSTPSGYLELPDLGQPYSSAVYSLEEQYLGLALDVDKIEKKGKGKKRRGRRSKKERRRGRKEGEEDQNPPCPRLNGVLMEVEEREVLQDSLDRCYSTPSMYFELPDSFQHYRSVFYSFEEQHISFALYVDNRFFTLTVTSLHLVFQMGVIFPQ
Protein: Type 2 DNA topoisomerase 6 subunit A (EC 5.6.2.2) (Type II DNA topoisomerase VI subunit A) (O05208)
Organism: Saccharolobus shibatae (strain ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12) (Sulfolobus shibatae)
Function: Relaxes both positive and negative supercoils and exhibits a strong decatenase and unknotting activity; it cannot introduce DNA supercoils. ATP is absolutely required for DNA cleavage; the nonhydrolyzable analog AMP-PNP generates nicked or linear products from a supercoiled dsDNA substrate. Generates staggered two-nucleotide long 5' overhangs. The enzyme is covalently attached transiently to the 5'-ends of the cleaved strands.
Interaction partners:
Sequence:
MSSEFISKVDKEARRKAANILRDKFLNLVEQLKKGEPLVMEIPMRTLSNAIYDEKRKLLLLGEKKLRRNFLDLNEAKRFMQTVLMASIIYDALVSDEYPTIRDLYYRGKHSLLLKSIEGNKIVSEENTWDEQKESDSVIVDIEVFTSLLREEMLILSKEKGKVVGNLRIRSGNDVIDLSKTGHGAYAIEPTPDLIDFIDVDAEFVLVVEKDAVFQQLHRAGFWKQYKSILITSAGQPDRATRRFVRRLNEELKLPVYILTDADPYGWYIFSVFRIGSISLSYESERLATPDAKFLGVSMGDIFGNSRKKPYLSEAERKNYIIKAKDADIKRAEEIKNYEWFKTKAWQEEINTFLQRKAKLEIEAMASKGLKFLAFQYIPEKITNKDYIA
Protein: RE04053p (Upf2) (Q9W3L1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Regulator of nonsense transcripts 1 homolog
- Serine/threonine-protein kinase Smg1
- FI21285p1
- LD23870p
- LD36341p
- RNA-binding protein 8A
- Eukaryotic initiation factor 4A-III
- GH14566p
- Serine/arginine repetitive matrix protein 1
- Eukaryotic translation release factor 3, isoform A
Sequence:
MLANDSATTDSEVSTPPSSRKDLADGVAEGDNDNDIDTGDTDANADEDVDAAAAIALEAEEREELQQFISELREKIESKRQLRLQNSTIELPGEEYFAKLDSNLKKNTAFVKKLKLFTATQLDGLLREISALNLSKYISEICAALVEAKLKMTDVPAVVTLASRLHCTYADFDVHFLEAWQKALNIKATEKIGNPSKLRVDLRLFAELVSSGVIQMKPGLAQLGVVLVHLIALDKDDHSNFSIILSFCRHCGEEYAGLVPQKMQQLATKYGVEVPKSDFLTADKQLNLRTMLKGYFKALCKHVLAEQAELMNMTKNIRRTMECKGEISTEKREKCELMQAGFDKLLASAQSLSELLGEPLPELAKESEGCNPGTVIDNMLDSASFGVLDPWGDEETRAFYTDLPDLRQFLPNFSAPKVDLETLEEPSELTEEAIDANLDAEMDLDDPPSTTSDTTPENPIEEQPTTPVAAAEDLKPQKMGNALMELGRQQQQQSQLNQNPIQIQNQMRQQFDGFLVNLFNCVNKELIDSAAIEFLLNFNTKHQRKKLTRTIFSVQRTRLDILPYLSRFVAIVHMCNTDVATDLAELLRKEFKWHIHKKNQLNIETKLKIVRFIGELVKFGLFKKFDALGCLKMLLRDFQHHQIEMACAFVEVTGVYLYNCRDARLLMNVFLDQMLRLKTATAMDSRHAAQIESVYYLVKPPESSKREPMVRPAMHEYIRYLIFEELCKQNVDRCIKMLRRIDWQDPETNCYAIKCLSKAYLLRFQLIRCLADLVSGLSSYQPRAVTIVIDNVFEDIRAGLEIHSPRMAQRRIAMAKYLGEMYNYKLVESTNILNTLYSIISLGVSNDQNVVSPLDPPDSLFRLKLACMLLDTCAPYFTSQATRKKLDYFLVFFQHYYWFKKSHPVFSKTENTSDLFPILMDHTYRDCLLNVRPKLKIYKSLEQAKAAIDHLQEKLYPQLKTTNNAQDPSLGTISEISEIDEGGTDEDSGSSNDQRERQVSGQEQDQSNDWTENEAEPPLPPLPPPEKSKEDLEFEQLYEKMTTDSYQERLKEPIKATAKDIPVPMMARLQKKSYDQITGAQTIGPGINNMSQISKSVPNQDGTPGSPGADSPDGNGKSGGGVGGSDVGAAGAAGASGATSVPFVLMVRGHKGGKQQFKSFVAPSDSHLATNLKRQEQMIREEKEKVKRLTLNITERIEEEDYQESLMPPQHRNFTQSYYQKPNKHKFKHQKGAPDADLIFH
Protein: Betacellulin (A0A8J8YRH0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MDQLLYQDWSLLILSASSYLSGDWAPVPLLSAFVMSLVILQCVVADGNTTRTPETNGSLCGAPGENCTGTTPRQKSKTHFSRCPKQYKHYCIHGRCRFVMDEQTPSCICEKGYFGARCEQVDLFYLQQDRGQILVVCLIGVMVLFIILVIGVCTCCHPLRKHRKKKKEEKMETLSKDKTPISEDIQETNIA
Protein: Prion-like protein doppel (Doppelganger) (Dpl) (PrPLP) (Q9QUG3)
Organism: Mus musculus (Mouse)
Function: Required for normal acrosome reaction and for normal male fertility. Can bind Cu(2+) (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:10842180}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10842180}.
Interaction partners:
- Major prion protein
- Shadow of prion protein
- Prion-like protein doppel
Sequence:
MKNRLGTWWVAILCMLLASHLSTVKARGIKHRFKWNRKVLPSSGGQITEARVAENRPGAFIKQGRKLDIDFGAEGNRYYAANYWQFPDGIYYEGCSEANVTKEMLVTSCVNATQAANQAEFSREKQDSKLHQRVLWRLIKEICSAKHCDFWLERGAALRVAVDQPAMVCLLGFVWFIVK
Protein: Post-transcriptional regulator ComN (O32049)
Organism: Bacillus subtilis (strain 168)
Function: Required for post-transcription initiation control of the comE operon. Promotes the accumulation of its target comE mRNA to septal and polar sites.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22582279}. Note=Localizes to the division site and cell poles, in a DivIVA-dependent manner. Polar localization is not essential for competence development.
Interaction partners:
- Cell division topological determinant MinJ
- Septum site-determining protein DivIVA
- Chromosome-anchoring protein RacA
- Protein translocase subunit SecDF
- dTTP/UTP pyrophosphatase
- Cell division protein FtsL
- Uncharacterized membrane protein YrrS
- Sporulation-specific transcription factor SpoVIF
- ATP synthase protein I
Sequence:
MEKHPADLYKDHVRPFLYSKLEEFKILGYDDVELESLWSYLTDKKWKKKTELSIYELASDILSVKIGEFMNYATVESFKTSNWLGSEEGQEALEELLR
Protein: Cytoplasmic linker associated protein 1 (F1LNR1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000256|ARBA:ARBA00004629}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}. Golgi apparatus, trans-Golgi network {ECO:0000256|ARBA:ARBA00004601}.
Interaction partners:
Sequence:
MEPRMESCLAQVLQKDVGKRLQVGQELIDYFSDKQKSADLEHDQTMLDKLVDGLATSWVNSSNYKVVLLGMDILSALVTRLQDRFKAQIGTVLPSLIDRLGDAKDSVREQDQTLLLKIMDQAANPQYVWDRMLGGFKHKNFRTREGICLCLIATLNASGAQTLTLSKIVPHICNLLGDPNSQVRDAAINSLVEIYRHVGERVRADLSKKGLPQSRLNVIFTKFDEVQKSGNMIQSANDKNFDDEDSVDGNRPSSASSSSSKAPSSSRRNVSMGTTRRLMASSLGSKSSAAKEGAGAVDEEDFIKAFDDVPVVQIYSSRDLEESINKIREILSDDKHDWEQRVNALKKIRSLLLAGAAEYDNFFQHLRLLDGAFKLSAKDLRSQVVREACITLGHLSSVLGNKFDHGAEAIMPTIFNLIPNSAKIMATSGVVAVRLIIRHTHIPRLIPVITSNCTSKSVAVRRRCFEFLDLLLQEWQTHSLERHISVLAETIKKGIHDADSEARIEARKCYWGFHSHFSREAEHLYHTLESSYQKALQSHLKNSDSIVSLPQSDRSSSSSQESLNRPLSAKRSPTGSTASRGSTVSTKSMSTTGSLQRSRSDIDVNAAASAKSKVSSSSGSTAFSSAAALPPGSYASLESRHMREDLEYVGLDAGRIRTRRQSSGSTTNVASTSSDSRGRSRAKVVSQSQPGSRSSSPGKLLGSGYGGLAGGSSRGPPVTPSSEKRSKIPRSQGCSRETSPNRIGLDRFGLGQSGRIPGSVSAMRVLSTSTDLEAAVADALKKPVRRRYEPYGMYSDDDANSDASSVCSERSYGSRNGGIPHYLRQTEDVAEVLNHCASSNWSERKEGLLGLQNLLKSQRTLSRVELKRLCEIFTRMFADPHSKVFSMFLETLVDFIIIHKDDLQDWLFVLLTQLLKKMGADLLGSVQAKVQKALDVTRDSFPFDQQFNILMRFIVDQTQTPNLKVKVAILKYIESLARQMDPTDFVNSSETRLAVSRIITWTTEPKSSDVRKAAQIVLISLFELNTPEFTMLLGALPKTFQDGATKLLHNHLKNSSNAGVGSPSNTIGRTPSRHPSSRTSPLTSPTNCSHGGLSPSMLDYDTENLNSEEIYSSLRGVTEAIEKFSFRSQEDLNEPIKRDGKKDCDIVSRDGGAASPATEGRGGSEVEGGRMALDNKTSLLNTQPPRAFPGPRAREYNPYPYSDTINTYDKTALKEAVFDDDMEQLRDVPIDHSDLVADLLKELSNHNERVEERKGALLELLKITREDSLGVWEEHFKTILLLLLETLGDKDHSIRALALRVLREILRNQPARFKNYAELTIMKTLEAHKDSHKEVVRAAEEAASTLASSIHPEQCIKVLCPIIQTADYPINLAAIKMQTKVVERITKESLLQLLVDIIPGLLQGYDNTESSVRKASVFCLVAIYSVIGEDLKPHLAQLTGSKMKLLNLYIKRAQTTNSNSSSSSDVSTHS
Protein: Protein farnesyltransferase subunit beta (FTase-beta) (EC 2.5.1.58) (Q19752)
Organism: Caenorhabditis elegans
Interaction partners:
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- CAAX prenyl protease 2
- CAAX prenyl protease 1 homolog
- Farnesyl pyrophosphate synthase
- Alkyl transferase
- All trans-polyprenyl-diphosphate synthase PDSS1
- Uncharacterized protein F23B12.7
- Ras protein let-60
- Chromatin assembly factor 1 subunit A dimerization domain-containing protein
- Guanine nucleotide-binding protein subunit gamma
Sequence:
MTSSIPFRSFNEKYECNDDDNFTYSSTEQKRIETMLFENYNSLVLEPFKTTSDEDLAELTIFRQKHASYLLRYLKNCPSSYATLDASRSWMCYWGVNALKILDAEIPNDVIENIIVFLKSCEHPEGGYGGGPGQLAHLAPTYAAVMCLVSLQKEEALRSINRVTLFNFLKKCKHESGGFYMHEGGEIDMRSAYCALATCEIVGLPMDEISNGVAEWIISCQSFEGGFGGEPYTEAHGGYTFCAVASLVLLNRFRLADMEGLLRWATRRQMRFEGGFQGRTNKLVDGCYSFWQGAIFPLLDGEMEREGRSLEKGLFEARMLEEYILVGCQSVHGGFKDKPDKPVDLYHTCYVLSGLSVAQKYSLARDGKILGGDVNMLAEINPVFNVTIASEQFAKEFFTSH
Protein: Putative lysozyme-like protein (Q54M35)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Membrane-associated sulfotransferase kil1
- Signal peptidase complex subunit 3
- Alpha-L-fucosidase
- Lysozyme B
Sequence:
MRLLLVLLALIFSVVSAQQNTCAQLCKDNKDMCCSLSKNSEYLLTTHNKEEKTQSCGDKFNSEDYYVAGSNRFGCGNSVTICKVQSDDSKIEITPNRRFGHHGGGVAGSIANAASSISSVANSVSSMTNSVSSLANSVSSLAGSMSSSGSSSSSGSSGSSSSSSGSSGGGSSGGGSGGGGGGSGLVVGKERRFGKHGGGGIAGSMNSAATSLSSLASDVSSVASVVSSLSSSSSADAGSSGAQGSGSTSGDGNAPPGSTGGTGGSSGSSGGGSGGGGGGSGLVVGERKFGHHGGGGVAGSIANAASSIASVANSVSSMTNSVSSLANSVSSLAGSMSSSGSSSSSGSSGSSSSSSSSGSSGGSSGGGSSGGGSGGGGGGSGLVVGERKFGHHGGGGVAGSIANAASSIASVANSVSSMTNSVSSLANSVSSLAGSSSSSGSSGSSSSSSSSGSSGGSSGGSSGGGGGSGELLSQNQVFATCVRVISTNVGPNVDIEDKIGKPIMDASTKVCEDLFGSPYCQWTDNHIVTAVSSKLDDGFPTQGAFNVTRSQYGYIMENGHYLNNKGNSVRIN
Protein: DDB1 and CUL4 associated factor 17 (H7C244)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XEIKLNDFCKASEVNISKLMFVPSASGYKAKNGIQEMDCCSLESDWIYFHPDASGRIIHVGPNQVKVLKLTEIENNSSQHQISEDFVILANRENHKNENVLTVTASGRVVKKSFNLLDDDPEQETFKIVDYEDELDLLSVVAVTQIDAEGKAHLDFHCNEYGTLLKSIPLVESWDVTYSHEVYFDRDLVLHIEQKPNRVFSCYVYQMICDTGEEEETINRSC
Protein: GPN-loop GTPase 3 (Q9XW68)
Organism: Caenorhabditis elegans
Interaction partners:
- GPN-loop GTPase 1
- Putative RNA polymerase II subunit B1 CTD phosphatase rpap-2
- DNA-directed RNA polymerase RpoA/D/Rpb3-type domain-containing protein
- Nucleolar protein 6
- Transcription initiation factor TFIID subunit 11
- Probable prefoldin subunit 6
- Large ribosomal subunit protein uL2 C-terminal domain-containing protein
- Pre-mRNA-splicing factor 38
- Mediator of RNA polymerase II transcription subunit 29
- CTCHY-type domain-containing protein
Sequence:
MKYAQLVMGPAGSGKSTYCSVMYNHCLSTGRTLRMVNLDPACEVFNYPAVVDVRDLISVNDVQEDEELILGPNGALVFCMEYLVQNLEWLHDELDEGEDDYFVIDCPGQIELYSHLPVMRQIVDALKSWDFNVCSVFLIDTNFVLDAEKFISGALTALSAMVAIETPAINVLTKMDLLSERNKQLVDEFLETDTRSIVDQDETVWNSKHRKLTRTIAQVLEDYSIVKFVPLNCEDEESIDQLLLTIDTTIQYGEDLEVKDHYPEELDPEQQE
Protein: Protein FAM32A (G5EDH3)
Organism: Caenorhabditis elegans
Interaction partners:
- Pre-mRNA-splicing factor CWC22 homolog
- Pre-mRNA-splicing factor SLU7
- Replication stress response regulator SDE2
- Uncharacterized protein F37A4.2
- Pre-mRNA-splicing factor syf-2
- NF-kappa-B-activating protein C-terminal domain-containing protein
- Peptidyl-prolyl cis-trans isomerase
- Pre-mRNA-processing factor 17
- Probable pre-mRNA-splicing factor ATP-dependent RNA helicase mog-5
- Pre-mRNA-splicing factor 8 homolog
Sequence:
MKDTVVKGSLKLKKVSTEAPKKTKKSKPAMDLKQVDMTIRRDSRNTSGGGPHKTEAELRFEARRQANMAERMLKQAALSHREKVEKLNKQLGEMTEFNDIPKVSWTK
Protein: Annexin A9 (Annexin XXXI) (Annexin-31) (Annexin-9) (Q9JHQ0)
Organism: Mus musculus (Mouse)
Function: May act as a low affinity receptor for acetylcholine.
Interaction partners:
Sequence:
MSASCGPLGTSLTQEILSSLGLADKTAAWGTLGTLRTFLSFSVDKDVQRLLKAIAGQGVDYDTIVDVLTNRSREQRQLISRAFQERTKQDLLKSLQAALSGNLEKIVVALLQPAAQFDAQELRTALKTSGSAEDVALEILATRAAPGLQACLAVYKHDFQVEAEEDIRTETNGILQDLLLALSKGDRESYSGIIDYNLEEQDVRALQQAGESSTAGQWVLLLTQRSPEHLIRVFDQYRRCTGQELEDAIRNCFHGDAQLALISLASMLRNTALYFANKLHQALQETEPNFQVLTRVLISRSESDLLSIRAEFKKKFGKSLYSSLQDVVRGDCRSALLALCRAEDI
Protein: MICOS complex subunit MIC60 (Mitofilin) (B9A067)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|RuleBase:RU363000}; Single-pass membrane protein {ECO:0000256|RuleBase:RU363000}.
Interaction partners:
Sequence:
MLRACQLSGVTAAAQSCLCGKFVLRPLRPCRRYSTSGSSGLTTGKIAGAGLLFVGGGIGGTILYAKWDSHFRESVEKTIPYSDKLFEMVLGPAAYNVPLPKKSIQSGPLKISSVSEVMKESKQPASQLQKQKGDTPASATEASSSSIRERPPEEVAARLAQQEKQEQVKIESLAKSLEDALRQTASVTLQAIAAQNAAVQAVNAHSNILKAAMDNSEIAGEKKSAQWRTVEGALKERRKAVDEAADALLKAKEELEKMKSVIENAKKKEVAGAKPHITAAEGKLHNMIVDLDNVVKKVQAAQSEAKVVSQYHELVVQARDDFKRELDSITPEVLPGWKGMSVSDLADKLSTDDLNSLIAHAHRRIDQLNRELAEQKATEKQHITLALEKQKLEEKRAFDSAVAKALEHHRSEIQAEQDRKIEEVRDAMENEMRTQLRRQAAAHTDHLRDVLRVQEQELKSEFEQNLSEKLSEQELQFRRLSQEQVDNFTLDINTAYARLRGIEQAVQSHAVAEEEARKAHQLWLSVEALKYSMKTSSAETPTIPLGSAVEAIKANCSDNEFTQALTAAIPPESLTRGVYSEETLRARFYAVQKLARRVAMIDETRNSLYQYFLSYLQSLLLFPPQQLKPPPELCPEDINTFKLLSYASYCIEHGDLELAAKFVNQLKGESRRVAQDWLKEARMTLETKQIVEILTAYASAVGIGTTQVQPE
Protein: Minor histocompatibility antigen H13 (EC 3.4.23.-) (Presenilin-like protein 3) (Signal peptide peptidase) (Q9D8V0)
Organism: Mus musculus (Mouse)
Function: Catalyzes intramembrane proteolysis of some signal peptides after they have been cleaved from a preprotein, resulting in the release of the fragment from the ER membrane into the cytoplasm. Required to generate lymphocyte cell surface (HLA-E) epitopes derived from MHC class I signal peptides. Involved in the intramembrane cleavage of the integral membrane protein PSEN1. Cleaves the integral membrane protein XBP1 isoform 1 in a DERL1/RNF139-dependent manner (By similarity). May play a role in graft rejection.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12972007, ECO:0000269|PubMed:16730383}; Multi-pass membrane protein {ECO:0000305}. Membrane {ECO:0000250|UniProtKB:Q8TCT9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TCT9}; Lumenal side {ECO:0000250|UniProtKB:Q8TCT9}.; SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000269|PubMed:16730383}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- E3 ubiquitin-protein ligase RNF139
- Derlin-1
- E3 ubiquitin-protein ligase AMFR
- Transitional endoplasmic reticulum ATPase
- E3 ubiquitin-protein ligase synoviolin
- Protein sel-1 homolog 1
- Endoplasmin
- Heme oxygenase 1
- Selenoprotein S
Sequence:
MDSAVSDPHNGSAEAGTPANGTTRPPSTPEGIALAYGSLLLMALLPIFFGALRSVRCARGKSSSDMPETITSRDAARFPIIASCTLLGLYLFFKIFSQEYINLLLSMYFFVLGILALSHTISPFMNKFFPANFPNRQYQLLFTQGSGENKEEIINYEFDTKDLVCLGLSSVVGVWYLLRKHWIANNLFGLAFSLNGVELLHLNNVSTGCILLGGLFIYDIFWVFGTNVMVTVAKSFEAPIKLVFPQDLLEKGLEADNFAMLGLGDIVIPGIFIALLLRFDISLKKNTHTYFYTSFAAYIFGLGLTIFIMHIFKHAQPALLYLVPACIGFPVLVALAKGEVAEMFSYEESNPKDPAAETESKEESTEASASKRLEKKEK
Protein: Protein CURVATURE THYLAKOID 1B, chloroplastic (Photosystem I protein P) (Thylakoid membrane phosphoprotein 14 kDa) (Q8LCA1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Determines thylakoid architecture by inducing membrane curvature.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:23839788}; Multi-pass membrane protein {ECO:0000269|PubMed:23839788}. Note=Located almost exclusively at grana margins. {ECO:0000269|PubMed:23839788}.
Interaction partners:
- Photosystem I reaction center subunit V, chloroplastic
- Photosystem I chlorophyll a/b-binding protein 5, chloroplastic
- PsbP-like protein 1, chloroplastic
- Photosystem II 22 kDa protein, chloroplastic
- Chlorophyll a-b binding protein CP26, chloroplastic
- Chlorophyll a-b binding protein 3, chloroplastic
- Chlorophyll a-b binding protein
- ATP synthase gamma chain 1, chloroplastic
- Photosystem I reaction center subunit XI, chloroplastic
- Light-harvesting complex-like protein 3 isotype 1, chloroplastic
Sequence:
MASLSVSSSSTIIDSRAPPSRLASASASSPSCISLPTLPIQSHTRAAKATAYCRKIVRNVVTRATTEVGEAPATTTEAETTELPEIVKTAQEAWEKVDDKYAIGSLAFAGVVALWGSAGMISAIDRLPLVPGVLELVGIGYTGWFTYKNLVFKPDREALFEKVKSTYKDILGSS
Protein: Tubulin (Q8GCC5)
Organism: Prosthecobacter dejongeii
Interaction partners:
Sequence:
MKVNNTIVVSIGQAGNQIAASFWKTVCLEHGIDPLTGQTAPGVAPRGNWSSFFSKLGESSSGSYVPRAIMVDLEPSVIDNVKATSGSLFNPANLISRTEGAGGNFAVGYLGAGREVLPEVMSRLDYEIDKCDNVGGIIVLHAIGGGTGSGFGALLIESLKEKYGEIPVLSCAVLPSPQVSSVVTEPYNTVFALNTLRRSADACLIFDNEALFDLAHRKWNIESPTVDDLNLLITEALAGITASMRFSGFLTVEITLRELLTNLVPQPSLHFLMCAFAPLTPPDRSKFEELGIEEMIKSLFDNGSVFAACSPMEGRFLSTAVLYRGIMEDKPLADAALAAMREKLPLTYWIPTAFKIGYVEQPGISHRKSMVLLANNTEIARVLDRICHNFDKLWQRKAFANWYLNEGMSEEQINVLRASAQELVQSYQVAEESGAKAKVQDSAGDTGMRAAAAGVSDDARGSMSLRDLVDRRR