wanglab/gogpt-training-data huggingface dataset:
Protein: Importin subunit alpha-2 (Importin-1) (Karyopherin subunit alpha-2) (O94374)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope. Involved in nuclear protein import. Required for efficient nuclera import of both an SV40 nuclear localization signal-containing reporter protein and the pap1 component of the stress response MAP kinase pathway. Required for proper mitotic progression.
Subcellular location: Cytoplasm. Nucleus, nucleolus. Note=Nucleus; nucleolus; nuclear rim.
Interaction partners:
- Importin subunit beta-1
- Ran-specific GTPase-activating protein 1
- Nucleoporin nup124
- Nuclear cap-binding protein subunit 1
- Importin subunit beta-2
- Exportin-1
- Importin-alpha re-exporter
- Nuclear cap-binding protein subunit 2
- Importin subunit alpha-1
- Protein pim1
Sequence:
MESRYLSDRRSRFKSKGVFKADELRRQREEQQIEIRKQKREESLNKRRNLNAVLQNDIDVEEEADQSQVQMEQQMKDEFPKLTADVMSDDIELQLGAVTKFRKYLSKETHPPIDQVIACGVVDRFVQFLESEHHLLQFEAAWALTNIASGTTDQTRIVVDSGAVPRFIQLLSSPEKDVREQVVWALGNIAGDSSACRDYVLGNGVLQPLLNILQSSASDVSMLRNATWTLSNLCRGKNPPPNWSTISVAVPILAKLLYSEDVEIIVDACWAISYLSDGPNEKIGAILDVGCAPRLVELLSSPSVNIQTPALRSVGNIVTGTDAQTQIIIDCGALNAFPSLLSHQKENIRKEACWTISNITAGNTQQIQAIIESNLIPPLVHLLSYADYKTKKEACWAISNATSGGLGQPDQIRYLVSQGVIKPLCDMLNGSDNKIIQVALDAIENILKVGEMDRTMDLENINQYAVYVEEAGGMDMIHDLQSSGNNDIYLKAYSIIEKYFSDEDAVEDLAPETENGAFTFGNGPQAQGEFKFDSQDMAM
Protein: receptor protein-tyrosine kinase (EC 2.7.10.1) (F5H1T4)
Organism: Homo sapiens (Human)
Subcellular location: Cell envelope {ECO:0000256|ARBA:ARBA00004196}. Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNGDPLNNTTPVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQLALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTACPYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSANIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSLPDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHTVPWDQLFRNPHQALLHTANRPEDECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVARCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHS
Protein: Exonuclease mut-7 homolog (EC 3.1.-.-) (Exonuclease 3'-5' domain-containing protein 3 homolog) (Protein nibbler) (Q9VIF1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Possesses 3'-5' exoribonuclease activity. Required for 3'-end trimming of AGO1-bound miRNAs, in particular multiple-isoform miRNAs, which represents a critical step in miRNA maturation.
Interaction partners:
- RE54550p
- tRNA
- Protein piwi
- Histone chaperone asf1
- Mitochondrial cardiolipin hydrolase
- NHP2-like protein 1 homolog
- Protein NipSnap
- U3 small nucleolar RNA-associated protein 15 homolog
- LD30155p
- FI13065p
Sequence:
MARKSHMYNAIPAGFESDEENMENLMSNLKIKRLEDITTGAGIDGCNFDATLDAKAEEFFKLFREKWNMYSKKKSPHLRQEFGRALMGHQDPLLLALKIFANCPDSSNIKTKSLSHFVLDTVCKLHKDFPHLGEGCDPNTSMIAFNFVKTSGLLALNNAVIHAYSLRQIRDLLLPKLRELLDNGLYKEVTQWSISLQLTHEFDMLELAFPLIAIEKLPLAEEYLDHATQQRLPFVKFLDSLLHKEKSVLELCEHLLDRYKNLKISHNVLSYRPMAKIVARLAKKYGFDDAVTPNYKFTKTCSYLHYLYREYEKTRMNLASFREVVSVHAFNHELRTDFVKYLASAGAHSEAIYWYTEFNIDPKDCPLEIETQVSQNGAGKASGWESPGKERCPSSRCDMYLTMDLPDECLIIVNKADEFDRMLYHLQQECVIYLDSEWMQSVCGDNQLCVLQIATGHNVYLIDCLARESLRSEHWRLLGANIFNNVNIRKVGFSMVSDLSVLQRSLPLQLRLQMPHHYLDLRNLWLELKKQRFGVELPFGNVNRAGDALTDLSLACLGKKLNKSNQCSNWANRPLRREQILYAAIDARCLMLIYNTLIERVSFIQAVIEKSIASNNFLRRGAHVK
Protein: Ataxin 2 (A0A2R8YGV1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XYPVPVSPGVQPLYPIPMTPMPVNQAKTYRAVKYLELELLRYVPNMPQQRQDQHHQSAMMHPASAAGPPIAATPPAYSTQYVAYSPQQFPNQPLVQHVPHYQSQHPHVYSPVIQGNARMMAPPTHAQPGLVSSSATQYGAHEQTHAMYVSTGSLAQQYAHPNATLHPHTPHPQPSATPTGQQQSQHGGSHPAPSPVQHHQHQAAQALHLASPQQQSAIYHAGLAPTPPSMTPASNTQSPQNSFPAAQQTVFTIHP
Protein: DNA polymerase iota (EC 2.7.7.7) (Q9VHV1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Error-prone DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Favors Hoogsteen base-pairing in the active site (By similarity). Inserts the correct base with higher fidelity opposite an adenosine template. Exhibits low fidelity and efficiency opposite a thymidine template, where it will preferentially insert guanosine. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but may not have lyase activity (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9UNA4}.
Interaction partners:
- DNA repair protein Rev1
- DNA polymerase zeta catalytic subunit
- DNA polymerase zeta subunit 2
- Proliferating cell nuclear antigen
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eL40 fusion protein
- Proliferating cell nuclear antigen 2
- Polyubiquitin
- GH17761p
- DNA-directed RNA polymerase I subunit RPA2
Sequence:
MDFASVLGKSEAHQRTIIHLDMDYFYAQVEEIRDPTLRSKALGIQQKNIVVTCNYVARAKGVTKLMLIAEAQRICPDLVLVNGEDLAPYRQMSQRIFDLLLNYTPLVEKLGFDENFMDVTALVELRQAHVAEALLRPPVGHTYPADGTPLSNCDCGCAQRLAIGTRIAQEIREELKLRLGITCCAGIAYNKLLAKLVGSSHEPNQQTVLVSTYAEQFMRELGDLKRVTGIGQKTQCLLLEAGMSSVEQLQQCDMDVMRKKFGFETATRLRDLAFGRDTSLVRPSGKPKTIGMEDACKPISVRTDVEERFRMLLKRLVEQVAEDGRVPIAIKVVLRKFDSQKKSSHRETKQANILPSLFKTSMCPGETGVSKVQLADGAQDKLLKIVMRLFERIVDMSKPFNITLLGLAFSKFQERKVGSSSIANFLIKKADLEVQSITSLTNTSLTSPTAESPTSDECAFRSSPTTFKPSDQFYRRRATTASPVPMLLDNGSESAATNSDFSDFSETEVEPSPKKSRIGRLLVSKRSRLAADVGDSAAEVASPSKLRVCDLRLNSRDSEKDFPMSTTPSTSTSAPAPRFRTVQPPNTLLQRIDGSLRFVTTRTASRLSSNASSTASSPLPSPMDDSIAMSAPSTTTLPFPSPTTTAVVTSSSSTATCDALTNIVCPAGVDAEVFKELPVELQTELIASWRSSLVAAVEQTNGTGAATSAAIASGAPATATTASGQKNTLYRYFLRNK
Protein: Companion of reaper protein (Companion of reaper, isoform A) (Companion of reaper, isoform B) (GH26991p) (Q9W3G9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MADIRSSLKVLFQGETNLITCGSSNTYEEVISQAMTRFAIPETQRKALILTNGKDYVFEAHLLEYFLLLFPCPEITFHLRFDWSKMRRSLGQTESLKRKRLVDLEQAEGQKEEDQEKEDPVPEYKPVPVYRMNCFLGSLPTAGAIPVHRQNCFLREQSQQQLDEISIPRLQEDDDQKEPPKKRQRVDVCSKPRRTASTSVGPSPVPVMRSIRI
Protein: LIN-7 (P90976)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MGLKGFTGSFQQIRGLLRPPKNLPFRGIFRKDGEVVRKDDLLVNQFKMNYHPGLNVYYENDRGERLLRAHCDGIVRISQEKCDPDYEIEEMKGYEYRKDVDLYKMTFNMDNPDGPNLERDVQRILELMEHVQKTGEVNNAKLASLQQVLQSEFFGAVREVYETVYESIDADTTPEIKAAATAKATVAAFAAAEGHAHPRIVELPKTDQGLGFNVMGGKEQNSPIYISRIIPGGVADRHGGLKRGDQLIAVNGNVEAECHEKAVDLLKSAVGSVKLVIRYMPKLLDEMERRFERQRIP
Protein: Fife, isoform F (Fife, isoform G) (Q9VZY3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLPTNVMSFMKKMVATDEQTSERQQHAADSGGGASQTGALNKMKATISSSLLTVTDKVNKMSPRPSLVPTDADTSGSYGSPSYQSQQQQQQDYGSSLNNNNNNSSGGGTATTGGGGGGAAAKQEPGRRAGACRVCLKSFKPDDYHKTCFECQQRVCEDCASYSKLDEHEDATMWRCSVCRRKMASRVCIPQDSTDSMLDVPVLEALQRRHSDAKLGSSTQTLAPSNGAALAPPRSPELRRHSDVSPASLKELERQLKGGRSMAPSRSNSPPRGEGPDGQPPFGAPLSRMQSRRGSRVARQHSYDDDMKTGPVGGSMGGGGPALGLGADGAGLGIPTMPRRKSAYDVFAPGLTQGGATPATQLQRSPGEGGIMPPIQLPGSRRPSFRVPHPSEDIQNDDSPGSPDKGSPVLTVDDDRRMRRRGSQLPDIAMLQNRGALPAVPPSSIPPPMASFTGPNLEDLEAPRRQTSMDGEAIRIVIHDVDSGPICASKRRIILRRDPTDKAHRTRGFGMRVVGGKTGADGRLFAYIVWTVPGGAAEKNGLQQGDKILEWNGMSLIDRSFEEVCSIMDRTGDVVELLVEHATDFRMCDLFDENLPPGNAGGQSGPRRSGDGPVGLGLIAEPETTTDKSPASPTRRKLPKTPV
Protein: Tripartite terminase subunit 3 (EC 3.1.-.-) (Terminase large subunit) (P03219)
Organism: Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Function: Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM1 and TRM2 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM3 carries an RNase H-like nuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04013}. Note=Responsible for the nuclear localization of the two others subunits TRM1 and TRM2. {ECO:0000255|HAMAP-Rule:MF_04013}.
Interaction partners:
Sequence:
MLYASQRGRLTENLRNALQQDSTTQGCLGAETPSIMYTGAKSDRWAHPLVGTIHASNLYCPMLRAYCRHYGPRPVFVASDESLPMFGASPALHTPVQVQMCLLPELRDTLQRLLPPPNLEDSEALTEFKTSVSSARAILEDPNFLEMREFVTSLASFLSGQYKHKPARLEAFQKQVVLHSFYFLISIKSLEITDTMFDIFQSAFGLEEMTLEKLHIFKQKASVFLIPRRHGKTWIVVAIISLILSNLSNVQIGYVAHQKHVASAVFTEIIDTLTKSFDSKRVEVNKETSTITFRHSGKISSTVMCATCFNKNSIRGQTFHLLFVDEANFIKKEALPAILGFMLQKDAKIIFISSVNSADQATSFLYKLKDAQERLLNVVSYVCQEHRQDFDMQDSMVSCPCFRLHIPSYITMDSNIRATTNLFLDGAFSTELMGDTSSLSQGSLSRTVRDDAINQLELCRVDTLNPRVAGRLASSLYVYVDPAYTNNTSASGTGIAAVTHDRADPNRVIVLGLEHFFLKDLTGDAALQIATCVVALVSSIVTLHPHLEEVKVAVEGNSSQDSAVAIASIIGESCPLPCAFVHTKDKTSSLQWPMYLLTNEKSKAFERLIYAVNTASLSASQVTVSNTIQLSFDPVLYLISQIRAIKPIPLRDGTYTYTGKQRNLSDDVLVALVMAHFLATTQKHTFKKVH
Protein: Krueppel homolog 1 (Krueppel homologous protein 1) (P08155)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a general role in the hierarchies of gene expression leading to metamorphosis.
Interaction partners:
- Ecdysone receptor
- Juvenile hormone acid O-methyltransferase
- Krueppel homolog 2
- Taiman, isoform G
Sequence:
MTESKNDTKSWAPKQIWIKDVLKKSGTELLDISKSPAKAVAVKKSPAKDSATTKMVYYSANQLLIKTEQSSQAQFCLQVPPPLTATTTSVGLGVPPSGGQQEHFELLQTPQQRQMQLQLQDQHQQEQQQFVSYQLAIQQHQKQQQQQQHESITNAAPTAAPSAQRIKTEPVGGFPASAAVVSQVRKPSASKPQFKCDQCGMTFGSKSAHTSHTKSHSKNQDLSLNGASGAGVAAPVSTAAIELNDAGLPVGIPKSPTIKPLANVAAGADPYQCNVCQKTFAVPARLIRHYRTHTGERPFECEFCHKLFSVKENLQVHRRIHTKERPYKCDVCGRAFEHSGKLHRHMRIHTGERPHKCSVCEKTFIQSGQLVIHMRTHTGEKPYKCPEPGCGKGFTCSKQLKVHSRTHTGEKPYHCDICFRDFGYNHVLKLHRVQHYGSKCYKCTICDETFKNKKEMEAHIKGHANEVPDDEAEAAAASAAASTSAGSSAGSPSLQGVSSNSESSNHSPPSSPPATKKPRQARQPRVSKTVAATLSIPTSSPLSPSSLSSTYSPSASSMASPPPTSAHYLPVQMEADALSRDSGVSSAQPAHSTYADEEPTDLSMQQVQGQLPESTVDYYQAPPSLLELQPQPAGLTINPALLEAASIARRHDDNDDQVQDEDVHAAAWQMMQLCRGHGSLPPTEQPAPSHQPQVPTLHVSDLAANYDDTHEATVLIEHFKRGDLARHGLHKGYAPVPKYESALPNPDVVRRVEAAIGLRSSTESPERSSSPESDSLMMADRNVMTLPLRKRKHYMNKGDDGQVDSEKASGDGTSAAGGAASVGAGDGPGSKVMRMSSVIQFAKAS
Protein: Fusion protein SYT-SSX1 (A4PIV7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSVAFAAPRQRGKGEITPAAIQKMLDDNNHLIQCIMDSQNKGKTSECSQYQQMLHTNLVYLATIADSNQNMQSLLPAPPTQNMPMGPGGMNQSGPPPPPRSHNMPSDGMVGGGPPAPHMQNQMNGQMPGPNHMPMQGPGPNQLNMTNSSMNMPSSSHGSMGGYNHSVPSSQSMPVQNQMTMSQGQPMGNYGPRPNMSMQPNQGPMMHQQPPSQQYNMPQGGGQHYQGQQPPMGMMGQVNQGNHMMGQRQIPPYRPPQQGPPQQYSGQEDYYGDQYSHGGQGPPEGMNQQYYPDGHNDYGYQQPSYPEQGYDRPYEDSSQHYYEGGNSQYGQQQDAYQGPPPQQGYPPQQQQYPGQQGYPGQQQGYGPSQGGPGPQYPNYPQGQGQQYGGYRPTQPGPPQPPQQRPYGYDQIMPKKPAEDENDSKGVSEASGPQNDGKQLHPPGKANISEKINKRSGPKRGKHAWTHRLRERKQLVIYEEISDPEEDDE
Protein: Platelet-activating factor acetylhydrolase IB subunit alpha1 (EC 3.1.1.47) (PAF acetylhydrolase 29 kDa subunit) (PAF-AH 29 kDa subunit) (PAF-AH subunit gamma) (PAFAH subunit gamma) (Q29460)
Organism: Bos taurus (Bovine)
Function: Alpha1 catalytic subunit of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)) heterotetrameric enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and modulates the action of PAF. The activity and substrate specificity of PAF-AH (I) are affected by its subunit composition. Both alpha1/alpha1 homodimer (PAFAH1B3/PAFAH1B3 homodimer) and alpha1/alpha2 heterodimer(PAFAH1B3/PAFAH1B2 heterodimer) hydrolyze 1-O-alkyl-2-acetyl-sn-glycero-3-phosphoric acid (AAGPA) more efficiently than PAF, but they have little hydrolytic activity towards 1-O-alkyl-2-acetyl-sn-glycero-3-phosphorylethanolamine (AAGPE). Plays an important role during the development of brain.
Subcellular location: Cytoplasm.
Interaction partners:
- Platelet-activating factor acetylhydrolase IB subunit alpha2
- Platelet-activating factor acetylhydrolase IB subunit beta
- Platelet-activating factor acetylhydrolase 2, cytoplasmic
- Lysophosphatidylcholine acyltransferase 2
- Lysophosphatidylcholine acyltransferase 1
- Platelet-activating factor acetylhydrolase
- Choline/ethanolaminephosphotransferase 1
- LPCAT4 protein
- Cholinephosphotransferase 1
- Phospholipase A2
Sequence:
MSGDENPASKPTPVQDVQGDGRWMSLHHRFVADSKDKEPEVVFIGDSLVQLMHQCEIWRELFSPLHALNFGIGGDSTQHVLWRLENGELEHIRPKIVVVWVGTNNHGHTAEQVTGGIKAIVQLVNERQPQARVVVLGLLPRGQHPNPLREKNRRVNELVRAALAGHPRAHFLDADPGFVHSDGTISHHDMYDYLHLSRLGYTPVCRALHSLLLRLLTQDQGQGGAPLPEPSP
Protein: Circumsporozoite- and TRAP-related protein (O97267)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
- GDP-fucose protein O-fucosyltransferase 2
Sequence:
MKKAFVLIFSCFLLFLPLHIVRTHYAKNEETNKKDTKLKKKRNVKTFNKKLTNKSFLQVQHTVATRSVPPPPCLGDDCFCQNYYDLTLILDESASIGSKNWKNHVIPFTDKIIKDLTISKNEVHVGILLFSSKNRDYVTYGDELRYQKDELLKKVEKLKKDYYCGGGTKILGALKYSLENYTKHKNIRYDAPKVTILFTDGNENSASNKQLLEMGLTYRRERVKLLVLGVAAAEDNKLKLIAGCEENTNCPYSMKAEWETINDITKRLTNKICHTESEIEPEPKPEPSTPTHCQGDDCFCEDYYDLTLILDESRSITLDKWKKDVVPFAEKVLNNLNIDKDKIHVGIMRFAKSMKTDIGYEQETRYMKNDLIKLVRELKDKYGYGGATHLVDALQYSLKTFTRHPNNRVDAPKVTILFTDGNETSKKEKDIRDVGLLYRKENVKLIVVGVNLATEKSLKLLAGCTENEECLRVIKCEWNDLTNITKILTDKICNTGSVELPKPEENPEPVEKPNPEENPNPVEKPTPEENPNPVEKPTPEENPNPVEKPEPEKNPCINMEDCYCKDFYDITLVLDESASISDLIWRNEVIPFSLEIIKRINISYKNVHMGVLLFSEYTRDIVRFYDNARYEKGTLQTKINDLKRDYRSGKKTYIIQALQYALTYYSKLSNRKEAPKVTMLFTDGNDSYESEKGLQDIALLYRKENVKLLVVGVSTASENKLKMLVGCAPNVVCPFVIKTEWGLLKNVSEVFVKKICDNGVVLPPGSPSESTPGSPSESTPGSPSESTPGSPSESTPGNPSESTPGSPSESTPGNPSESTPGSPSESTPGSPSESTPCSGTECLCHNTYDLTLIIDESASIGYSNWEKEVVPFTIGLASNLEISEKKVNMGILLFSDKIREFIKYGQKESYDKNNLVRRIHDLKKYYKSGGFSYIVEALKYGLYSYAKSTSSRLNVPKVNILLTDGNNTDTSDFILTEVSSLYKKENVKLLLIGIGGPTIHKLRLLGGCDKSDGDCPYVVKAEWNNLKYTSNLIIDKICHTDKPVENPGDNSSVCNSKDDCICANYFDLTYIEVPTLNSTYTWRSDFMDCSKNIMNSLVIDKNKVHVSLIISLEKKSVHQGFDDVNSYNKNELIKTLGKLENSTVLNKTNILDSLVYGIQQSFGKGNRENAPKVTMLLTNSNSDISDEKALQDIYLNYKEKSIKLLIIGIGITNTGKLFNAGGCNMNGDNCPHVYASKSFSYIGGVDTFLEVNKCDSSIDNNGGDNGNGTEGNVNPDTPSCNDNDDDDKCNNDDSNIICTKVLDIAVVLDQSSNISKDQWNVYIKQFVINTVNQNYLSKYRSHITIVKMGKSTKEKWSLNKKISYQKKKIIKEINKLPISYSKKKDIAKSLKYVRTKVFKKSETNRKKLIIMLVEGKSNSNMNDLRKEVGLLKVNNIDFFAYAIDNIDETEYKILGDCEGSVDMGLMGNSPPSPSYLPCKNIVKVSWDTLLSSTDIHMKYICNGYPEDAECSEWEEWSPCPETCPTINNNNNNSSGSNNSSRTNIRTYFPQLSKRERKGPYTLKGEEYMGEKYGSSCMELKSIEYRSCPINAGCNDMCGDFGEWSECSATCGEGIRVRNRDNSLDNDDKCKLFNSTEMEACNIQECDDNNNVDICEDIGEWSDWSSCSKTCGYSTRSRTFTILPEYIGEYPNCKIFERSETEVCAFIPACSDENCFEWEEWNEWSSPCSPRKRVQKARVLKKDDVIISSGDNNNNNNNNAKRGMGHKNSTFTSYNNKKSDICEEEVRHYLDKVEYDEESTCENKNPCGDWSDWSECDRTCNVGVRIRHFISHMFDMVGDEDEKECLEYYNKVETQDCLHLPPCDGGECSDWETWVECKEEDMIGNNCHKRNKKILTRKLELLKNKDITRTKNTSDVCNDYTLFREEDCPQSNDTCINALCNEWEEWGDCSSTCGEGSFKIRKRKEPLELIPASQDINGNIGLTCAQQNIKVEEREACIVPACEDESTNGGTEVEGSTPSSPSDSNNNDGSSGDNTGDSNDKKGMGTGEKVSLAAGVIGLVALAAGGLIYGYNTLNGGEPPHSSNMEFENVENNSGTEEEENEDFEVVDADDPMWN
Protein: Glycerol-3-phosphate dehydrogenase (EC 1.1.5.3) (C8VRM5)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Dihydroxyacetone kinase
- Glycerol-3-phosphate dehydrogenase [NAD
- Glycerol-3-phosphate dehydrogenase [NAD
- glycerol kinase
- glycerol kinase
- Probable D-xylulose kinase A
- Glycerol-3-phosphate acyltransferase Sct1, putative
- PAP2 domain protein
- PAP2 domain protein
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
Sequence:
MASRNTRRILRPLLYGTAAVTTVGAGALYFSIRPRNIPGLEAPAVPPPGYHEGKLVPPSFPKIKSRLEQIEDLKRSSSGDDADVYDLLVIGGGATGSGIALDAATRGLKVAVVERDDFSAGTSSKSTKLVHGGVRYLEKAVWELDYNQYKLVKEALRERKYFLNTAPHLSSWLPIMVPVQKWWQIPYFWAGTKCYDWLAGSEGIESSYFLPKSKAIEAFPMLRKDNVLGAMVYYDGAHNDSRMNVSLAMTAALYGSTVVNHMEVTGLTKDASGRLNGARLRDCIPERDGQGAEEISIRAKGIINATGPFTDSIRKMDDPNTKEIVAPSSGVHVILPGYYSPSNMGLIDPSTSDGRVIFFLPWQGNTIAGTTDAPTEITRQPQPSEKDIDWILKEIRGYLAPDINVGRSDVLAAWAGIRPLVRDPKVKSSEALVRNHLITVSSSGLLTCAGGKWTTYRQMAEEAVDEAIKEFNLKPCELHDVPDISGVGGRGLVADNASLDGSCQTHQVRLIGAHGWSKTLFINLIQHYGLETDVARHLTTSYGDRAWQVAALSSPTQTRFPVRGQRISALYPFIDGEVRFAVRHEYAQTAVDVIARRTRLAFLNAQAALEALPTVIDLMGEELHWDKNRKEVEWKDSVQFLASMGLAPDLLNVTRDQVENGKVQQLLASERGAFTRTEPPADVLAKTHNPVMGSEAGANK
Protein: Tripartite motif-containing protein 5 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM5) (TRIM5alpha) (Q5C8U3)
Organism: Chlorocebus tantalus (Tantalus monkey) (Cercopithecus tantalus)
Function: Capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses. Blocks viral replication early in the life cycle, after viral entry but before reverse transcription. In addition to acting as a capsid-specific restriction factor, also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Binding to the viral capsid triggers its E3 ubiquitin ligase activity, and in concert with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N (also known as UBC13-UEV1A complex) generates 'Lys-63'-linked polyubiquitin chains, which in turn are catalysts in the autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1, TAB2, and TAB3). Activation of the MAP3K7/TAK1 complex by autophosphorylation results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes, thereby leading to an innate immune response in the infected cell. Restricts infection by human immunodeficiency virus type 1 (HIV-1), simian immunodeficiency virus (SIV-mac) and N-tropic murine leukemia viruse (N-MLV). Plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q0PF16}. Nucleus {ECO:0000250|UniProtKB:Q0PF16}. Note=Predominantly localizes in cytoplasmic bodies. Localization may be influenced by the coexpression of other TRIM proteins, hence partial nuclear localization is observed in the presence of TRIM22 or TRIM27. In cytoplasmic bodies, colocalizes with proteasomal subunits and SQSTM1. {ECO:0000250|UniProtKB:Q0PF16}.
Interaction partners:
Sequence:
MASGILVNVKEEVTCPICLELLTEPLSLPCGHSFCQACITANHKESMLYKEEERSCPVCRISYQPENIQPNRHVANIVEKLREVKLSPEEGQKVDHCARHGEKLLLFCQEDSKVICWLCERSQEHRGHHTFLMEEVAQEYHVKLQTALEMLRQKQQEAEKLEADTREEKASWKIQIDYDKTNVSADFEQLREILDWEESNELQNLEKEEEDILKSLTKSETEMVQQTQYMRELISDLEHRLQGSMMELLQGVDGIIKRIENMTLKKPKTFHKNQRRVFRAPDLKGMLDMFRELTDVRRYWVDVTLAPNNISHAVIAEDKRQVSYQNPQIMYQAPGSLFGSLTNFNYYTGVRGSQSITSGKLTNFNYCTGVLGSQSITSGKHYWEVDVSKKSAWILGVCAGFQPDATYNIEQNENYQPKYGYWVIGLQEGDKYSVFQDGSSHTPFAPFIVPLSVIICPDRVGVFVDYEACTVSFFNITNHGFLIYKFSQCSFSKPVFPYLNPRKCTVPMTLCSPSS
Protein: Protein CUSTOS (Q96C57)
Organism: Homo sapiens (Human)
Function: Plays a role in the regulation of Wnt signaling pathway during early development.
Subcellular location: Nucleus envelope {ECO:0000250|UniProtKB:A9C3N6}.
Interaction partners:
- DNA-directed RNA polymerase III subunit RPC9
- Cyclin-dependent kinase 2-interacting protein
Sequence:
MAAPSGTVSDSESSNSSSDAEELERCREAAMPAWGLEQRPHVAGKPRAGAANSQLSTSQPSLRHKVNEHEQDGNELQTTPEFRAHVAKKLGALLDSFITISEAAKEPAKAKVQKVALEDDGFRLFFTSVPGGREKEESPQPRRKRQPSSSSEDSDEEWRRCREAAVSASDILQESAIHSPGTVEKEAKKKRKLKKKAKKVASVDSAVAATTPTSMATVQKQKSGELNGDQVSLGTKKKKKAKKASETSPFPPAKSATAIPAN
Protein: Morphogenesis-related protein MSB1 (Multicopy suppressor of bud emergence 1) (P21339)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May play a role in polarity establishment and bud formation. The MSB1 gene may be functionally redundant.
Interaction partners:
- Bud emergence protein 1
- Cell division control protein 42
- GTPase-activating protein BEM2/IPL2
- Cell division control protein 24
- Profilin
- Serine/threonine-protein kinase SKM1
Sequence:
MNDMAKPLPTPPTAEIRKSRSNSPKKAQKTNLSPNKNQNNEKNVPRSNGRTKNEHNSMDDEEFEFFHQFSREKVKGVIHVITAELKEKGPDVEFLMIPFRPEQTNDKLLTLLNQLFPLGNGQPVNEKKQLRIVSKADVWTLFQCLKYIWCRLPNSEIIGWKSYLEFKFREEDKKFPRKSFLEIMPQCLASPNHASIVYDFFDLIISISSNSRVNKMSARKISKMCAIWAFSKQIPNSDIQDYDFESAAMKSFAPNNSIQDGLDQWIPASDAMFHLLLAFLRSFVPQDLESAKLPRTLKSLLFNNQYPPRKSTAYTSETILTIPLVTLKTDVFSRKPWQLLERCNDLLDFSDHDAFEAREDYALLKSLFRKKNTVEGISRKMSQESRRLMKAMSTKHSTFQPGWAPRECIENISHLKECIEVKRLDIDDYFIWTWLSSLSFEQTSEKKKIFGRSIILEFEFDGFKKWVVFQECDITLDYNKKGQLKKKTSAQSPTTEKELPPDDFELEDPPLSKSPTLSQTYKKFQAEVPQQSTVRRDSAPDNQGIYHTVISKNALTKNKHNVNLHSFEHKISKWNPLNNLRKKSGSNSSSSSFEEKSKDAPIREEYHTNKNHKSKKEERVLSQFSTLNPDEYQLPVIETGSSNFKIEIPELMYEHDDDDSDKLKNSQKRATDSAIEELNGMVEEMMINEPDDVKISITEAETFESLTKFDQYKPSNITDDDLQSSHSSAVHSLKLSTNTNDSCADSSKYTADRKLAEPRKISEESKVNDDSSSYYSPNINNLPASRMPSQPTYSNSDSKKAFTNESRLNVLQGAVSPSQQVTPKPYKNAPGDCVSPVQQKYYQNDRRNEMSPASAPVPPSAYSPARSPQFSTNSAGFKQNTINVPVGYNDPAHVLANQPHMTYRDQHNYPSHQQKQRPFQNNIVPPELKSRNQRADASPIPQHMVPVKQGVPNLPSNVPLYQQMERMNPNHQHPVNTYKVTQPPYHNNTTNAYGNSRAGNAHMLDGKWSNNPPQMVPKGVRPNQYPQQHVNRYSPQAQPVVPAEYYNGPPPMRAPPMMSHMVPAQEPIRYTAGANRRSFPQGMQQNAYSVPAQPMGAVNSEFYLPEAPQGNKLHGNINKRQERKKLYDNIRSGNFGI
Protein: Probable lipoprotein LpqZ (O50459)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- ABC-type quaternary amine transporter
- Possible osmoprotectant transport integral membrane protein ABC transporter ProW
- Probable transmembrane protein
- Possible osmoprotectant binding lipoprotein ProX
- Possible osmoprotectant transport integral membrane protein ABC transporter ProZ
Sequence:
MRITRILALLLAVLLAVSGVAGCSADTGDRHPELVVGSTPDSEAMLLAAIYVAALRSYGFAAHAETAADPVAKLDSGAFTVVPAFTGQMLQTLQPDASVRSDAQVYRAIVSALPEGIAAGDYTTAAEDKPALVVTQSTAKAWGGGDLSELPSHCRGLLVGRVAGAHTPAAVGPCRLPAPREFRNDATMFAALRAGQLVAAWTTTADPDIPADLIMLTDGKPALIRAENIVPLYRRNALTERQLLAVNEVAGVLDTTALIGMRRQVAAGADPAAVAAGWLAEHPLGR
Protein: Uncharacterized protein YidQ (P0ADM4)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Putative type II secretion system M-type protein YghD
Sequence:
MIRNVLLAFMICSGMTLLGGCSSVMSHTGGKEGTYPGTRASATMIGDDETNWGTKSLAILDMPFTAVMDTLLLPWDVFRKDSSVRSRVEKSEANAQATNAVIPPARMPDN
Protein: Probable inactive UDP-arabinopyranose mutase 2 (OsUAM2) (Reversibly glycosylated polypeptide 2) (UDP-L-arabinose mutase 2) (Q7FAY6)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable inactive UDP-L-arabinose mutase. Inactive in vitro, but associates with UAM1 and UAM3.
Subcellular location: Golgi apparatus {ECO:0000250|UniProtKB:Q9SRT9}.
Interaction partners:
- UDP-arabinopyranose mutase 3
- UDP-arabinopyranose mutase 1
Sequence:
MSLEIQDSEVDIVIAALQPNLTTFFEAWRPFFSRFHIIVVKDPDMAEELQIPTGFDLKVYTKSDMGVLGATSIDFSGHSCRYFGYLVSRKKYVISIDDNCLPAKDNGGLTVDAVAQHMSNLKTPATPFFFNTLYDPFRKGADFVRGYPFSLREGVECMLSCGLWLHNADYDPMTHVVKRNQRNTTYVDAVMTVPLGAMMPVSGINVAFNREVLGPVMFPALRLRKEGKHRWDTLEDVWNGLCAKVVCDRLRYGVKTGLPYVMRSDAEAGKALESLKEWEGVKVMDVVLPFFESLKLSSTSVTVEDCVKELTSIVKEKLGPQNAIFAKAADAMEEWTKLWKSHGAQSA
Protein: MICOS complex subunit MIC27 (Mitochondrial outer membrane abnormal protein 1) (Q21154)
Organism: Caenorhabditis elegans
Function: Sustains mitochondrial morphology probably through maintaining cristae morphology. May act as a component of the MICOS complex, a large protein complex of the mitochondria (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:21248201}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- MICOS complex subunit MIC60-1
- MICOS complex subunit MIC19
- MICOS complex subunit MIC60-2
- MICOS complex subunit MIC13
- MICOS complex subunit Mic10
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 12
- Sodium/hydrogen exchanger
- Sodium/hydrogen exchanger
Sequence:
MTQDKPIVETISNAGEQVTNVFGQFWQLVTSKNTTNNGDSKPIKIEQLPIYAEDNAPLKQKFLPEEPLPLQREFATIRIACEQEYDRVAERFKVVDCAMTQTKKAATKCNAYLTEEWTALPKAAAITVGGMAGFVLGLKRGPVGRLLTTTIGLATMAAFCYPIEAVDVAKTGRAHAEQTWYSFQESPTPSAIVKTNLSPPK