wanglab/gogpt-training-data huggingface dataset:
Protein: L-aspartate oxidase, chloroplastic (EC 1.4.3.16) (Protein FLAGELLIN-INSENSITIVE 4) (Q94AY1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the oxidation of L-aspartate to iminoaspartate. Can complement nadB-deficient E.coli mutant. Plays a role in stomatal immunity.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:16698895}.
Interaction partners:
- Nicotinate-nucleotide pyrophosphorylase [carboxylating], chloroplastic
- Quinolinate synthase, chloroplastic
- Succinate dehydrogenase iron-sulfur subunit 1, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 3, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 2, mitochondrial
- Aspartate aminotransferase, cytoplasmic isozyme 2
- NADH dehydrogenase flavoprotein 1, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- ATP-citrate synthase beta chain protein 1
Sequence:
MAAHVSTGNIHNFYLAGQVYRGQAFSWSSASTFMANPFKEPSWSSGVFKALKAERCGCYSRGISPISETSKPIRAVSVSSSTKYYDFTVIGSGVAGLRYALEVAKQGTVAVITKDEPHESNTNYAQGGVSAVLCPLDSVESHMRDTMVAGAHLCDEETVRVVCTEGPERIRELIAMGASFDHGEDGNLHLAREGGHSHCRIVHAADMTGREIERALLEAVLNDPNISVFKHHFAIDLLTSQDGLNTVCHGVDTLNIKTNEVVRFISKVTLLASGGAGHIYPSTTNPLVATGDGMAMAHRAQAVISNMEFVQFHPTALADEGLPIKLQTARENAFLITEAVRGDGGILYNLGMERFMPVYDERAELAPRDVVARSIDDQLKKRNEKYVLLDISHKPREKILAHFPNIASECLKHGLDITRQPIPVVPAAHYMCGGVRAGLQGETNVLGLFVAGEVACTGLHGANRLASNSLLEALVFARRAVQPSTELMKRTRLDVCASEKWTRPVVATARLLGDEVIAKIIALTKEVRRELQEVMWKYVGIVRSTIRLTTAERKIAELEAKWETFLFEHGWEQTVVALEACEMRNLFCCAKLVVSSALARHESRGLHYMTDFPFVEESKRIPTIILPSSPTTASWSSRRLQNISSSSLIDC
Protein: Replicase large subunit (EC 2.1.1.-) (EC 2.7.7.-) (EC 2.7.7.48) (EC 3.6.4.13) (183 kDa protein) (RNA-directed RNA polymerase) [Cleaved into: Replicase small subunit (EC 2.1.1.-) (EC 2.7.7.-) (EC 3.6.4.13) (126 kDa protein) (Methyltransferase/RNA helicase) (MT/HEL)] (P03586)
Organism: Tobacco mosaic virus (strain vulgare) (TMV) (Tobacco mosaic virus (strain U1))
Function: Is an RNA-dependent RNA polymerase active in viral RNA replication.
Interaction partners:
Sequence:
MAYTQTATTSALLDTVRGNNSLVNDLAKRRLYDTAVEEFNARDRRPKVNFSKVISEEQTLIATRAYPEFQITFYNTQNAVHSLAGGLRSLELEYLMMQIPYGSLTYDIGGNFASHLFKGRAYVHCCMPNLDVRDIMRHEGQKDSIELYLSRLERGGKTVPNFQKEAFDRYAEIPEDAVCHNTFQTMRHQPMQQSGRVYAIALHSIYDIPADEFGAALLRKNVHTCYAAFHFSENLLLEDSYVNLDEINACFSRDGDKLTFSFASESTLNYCHSYSNILKYVCKTYFPASNREVYMKEFLVTRVNTWFCKFSRIDTFLLYKGVAHKSVDSEQFYTAMEDAWHYKKTLAMCNSERILLEDSSSVNYWFPKMRDMVIVPLFDISLETSKRTRKEVLVSKDFVFTVLNHIRTYQAKALTYANVLSFVESIRSRVIINGVTARSEWDVDKSLLQSLSMTFYLHTKLAVLKDDLLISKFSLGSKTVCQHVWDEISLAFGNAFPSVKERLLNRKLIRVAGDALEIRVPDLYVTFHDRLVTEYKASVDMPALDIRKKMEETEVMYNALSELSVLRESDKFDVDVFSQMCQSLEVDPMTAAKVIVAVMSNESGLTLTFERPTEANVALALQDQEKASEGALVVTSREVEEPSMKGSMARGELQLAGLAGDHPESSYSKNEEIESLEQFHMATADSLIRKQMSSIVYTGPIKVQQMKNFIDSLVASLSAAVSNLVKILKDTAAIDLETRQKFGVLDVASRKWLIKPTAKSHAWGVVETHARKYHVALLEYDEQGVVTCDDWRRVAVSSESVVYSDMAKLRTLRRLLRNGEPHVSSAKVVLVDGVPGCGKTKEILSRVNFDEDLILVPGKQAAEMIRRRANSSGIIVATKDNVKTVDSFMMNFGKSTRCQFKRLFIDEGLMLHTGCVNFLVAMSLCEIAYVYGDTQQIPYINRVSGFPYPAHFAKLEVDEVETRRTTLRCPADVTHYLNRRYEGFVMSTSSVKKSVSQEMVGGAAVINPISKPLHGKILTFTQSDKEALLSRGYSDVHTVHEVQGETYSDVSLVRLTPTPVSIIAGDSPHVLVALSRHTCSLKYYTVVMDPLVSIIRDLEKLSSYLLDMYKVDAGTQXQLQIDSVFKGSNLFVAAPKTGDISDMQFYYDKCLPGNSTMMNNFDAVTMRLTDISLNVKDCILDMSKSVAAPKDQIKPLIPMVRTAAEMPRQTGLLENLVAMIKRNFNAPELSGIIDIENTASLVVDKFFDSYLLKEKRKPNKNVSLFSRESLNRWLEKQEQVTIGQLADFDFVDLPAVDQYRHMYKAQPKQKLDTSIQTEYPALQTIVYHSKKINAIFGPLFSELTRQLLDSVDSSRFLFFTRKTPAQIEDFFGDLDSHVPMDVLELDISKYDKSQNEFHCAVEYEIWRRLGFEDFLGEVWKQGHRKTTLKDYTAGIKTCIWYQRKSGDVTTFIGNTVIIAACLASMLPMEKIIKGAFCGDDSLLYFPKGCEFPDVQHSANLMWNFEAKLFKKQYGYFCGRYVIHHDRGCIVYYDPLKLISKLGAKHIKDWEHLEEFRRSLCDVAVSLNNCAYYTQLDDAVWEVHKTAPPGSFVYKSLVKYLSDKVLFRSLFIDGSSC
Protein: Eukaryotic translation initiation factor 3 subunit D (eIF3d) (Eukaryotic translation initiation factor 3 subunit 7) (eIF-3-zeta) (Q9FKV6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03003}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit K
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit L
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit F
Sequence:
MVFEAFEVGTVPFNSDGWGPPDASDTSSTSVAAANLLPNVPFASFSRSEKLGRVADWTRALSNPSARPHTGSKSDPSAIFDFSAFAVDEGFGLTNSGGNADEDAAFRLVDGKPPPRPKFGPKWRFNQYHNRNQLPQRRDEEVEAKKREAEKDRARRDRLYNNNRNNIHQQRREAAAFKSSVDIQPEWNMLEQIPFSTFSKLSFTVSEPEDLLLCGGLESYDRSFDRITPKADRRLERFKNRSFKVTTSDDLVIRRLAKEDKATVFATDAILAALMCAPRSVYSWDLVIQRVGNKLFFDKRDGSPLDLLSVHETSQEPLPEGKDDINSAHSLGLEAAYINQNFAQQVLVKNGKRETFDEPIPNVNEGEENASIAYRYRRWKLDDSMYLVARCELQSTVDLNNQRSFLTLNALNEFDPKYSGVDWRQKLETQRGAVLANELKNNGNKLAKWTAQALLANADMMKIGFVSRVHPRDHFNHVILSVLGYKPKDFAGQINLNTNNMWGIVKSIVDLCMKLSEGKYVLVKDPSKPQVRIYEVPADAFDNDYVEEPLPEDEQVQPPEENTDAGAETNGVSSTNVAVEDKKSEVEA
Protein: TATA-binding protein-associated factor mot1 (EC 3.6.4.-) (Modifier of transcription 1) (TBP-associated factor mot1) (O43065)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Regulates transcription in association with TATA binding protein (TBP). Removes TBP from the TATA box via its ATPase activity (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:10759889}. Note=Localized on chromatin.
Interaction partners:
- TATA-box-binding protein
- Transcription regulator complex subunit bur6
- Negative cofactor 2 complex subunit beta
- Hsp90 co-chaperone Cdc37
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 11
Sequence:
MTTRLDRLVVLLDSGSTSVVRETAAKQIGDIQKVHPDELYNLLGRVVPYLKSKNWDTRVAAAKAIGGIVENVPVWNPNRTSPVKKEETEDLPSFNGDTEEKPFIKTEEGAPASSQSQVVVSSNLTSNSEVSKLEEERLSTRSHSQEIKPIVDFGPDEETAKELNTELKGKFENSLLSFESFDIANVLKAGKKLLGSASRDYDVNPANYSTHYLQQLSNLKSRLDLAGEYLDDSIMNDLGDNVGSNSKGSPTTSIPEHKTSINNNKPEDTPTPSENVHLSARQRNALKRKARQMKNSQKVRVIDVAPTLVHQQNSTSSADKKTGADYNFTAQSRSDRLVVEHKAPIVPSAAVAVTSDSVWPFETLVELLLIDMFDPSWEIRHGACMGLREIIRYAGFGYGRVVGKSEAENEQLNKKYFDDLLCRIACVFALDRFGDYLADQVVAPIRESVSQVLGVALIYVPNDSVFSMYKVLHSLVFQNELGLTNTVWEAAHGGMLGIKYLVAVKYPLFFSHSDYLDSLINTVIHGLANHDDDVRAVSALTLLPIADKLVQEKLSSCKNLLKVLWDCLDDVKDDLSSSTSCVMDLLSSLCSFTEVMNLMQETANSDPEFSFETLVPRLFHLMRYTLTGVRRSVVYALTKFISVQTSCSWITGLTLRLCFQNVLLEQQEDISKSSCELAQRVMDILYRDGPESFSKLLYSHIEPMLKVSITPIGSFRRPYPLDTTLIVKPSGQPYAPSTSRERNNNISELSNSRTKHRAKDDPKGSFCFSVDEPMLNGDVEFVGEERMLKARLRASSLLGRIIGRWKRDEILLFFKPFLQACLTSSFSTPVVLGSRLIESFFEVEDNDLTIQKDELYHLLCDQFATVPRENYANLVSQLHVVRAQCNALLNTFLDVGRLSRSKIPSLAVVVKGDPEAGPIAFGIADAEKLVGPTYENLCKLLSPSQKAQSSKALNEIKYLIIDEISIYKIAKERQDIQCSASIASAMVTYDKLPKKLNSIIKGIMESIKKEQFSCLQMHSASAMMKLISACYKESRQVISEKIVRNLCAYVCMDTTETPIFHDSGKNGILSLHSIGTSDDNDEQVSGKLVDDSDDVSNDRKSSLSSVSDKDAAVLQRMGAQLTLQQMAQNFGSSLFSRVPVLSQCLFVPLQQYAESGFPSEVDQASCTVGQDLLDAMSILRFLVAYLDSGLQSEIVSTLPHLLATLQSNYSAVRNMASKCFAAITESNAAGSKALHLLVEDVVPLLGDASSTIHRQGAIECIYHVVQRLGVRILPYILYLIIPLLGRMSDADQDVRVLATTSFATLVKLVPLEAGLPDPPDLPQYLLDSREKERKFLEQMLNPSKVEAFSIPVPISADLRKYQQEGVNWLAFLNKYELHGILCDDMGLGKTLQTICIVASDHYNRQKLFEESGSPKFAHVPSLIVCPSTLAGHWQQELSTYAPFLKVSAYVGPPAERAKIRSKMKKSDVVVTSYDICRNDVDELVKIDWNYCVLDEGHVIKNARAKLTKAVKSLRSYHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKTFQERFVRPIAASRDAKSSSKERERGTLALEAIHKQVLPFMLRRLKEDVLADLPPKIIQDYYCDMSDLQRKLLNDFVSQLNINEELEDDETEKTQGTRKKKSQKAHIFQALQYMRKLCNHPALILTEKHPKRNAIVKQLAKENSGLHDLKHAPKLTALGQLLRDCGLGNSSVNSNGIDSALTNAVSEHRVLIFCQLKDMLDMVEKDLLQATMPDVTYMRLDGSVEPTKRQEAVTKFNNDPSIDVLLLTTHVGGLGLNLTGADTVIFVEHDWNPMRDLQAMDRAHRIGQKKVVNVYRLITRGCLEEKIMGLQRFKMNVASTVVNQQNAGLSSIGTDQILDLFNTTADEQQTVQNIDKEESEDAAGRGLSGTSKKALEGLPEMWDESQYDEFNLDGFISTLPKDAS
Protein: Transmembrane protein (Q9ZW05)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSATTTPSLSLSNFRPRFQTPVKGHHISPLSWSVSRRKILSFRVLRLHQEKTQLWRVSATPEEISQEIVSSDSSSSSGAVVSSGGQDGVALIIQVLLFVAFLALTVLTIGVVYIGVTEFLGKREREKFEKDEAAKKSKKGGKKKAMRARAGPRGFGQKIEDDDIDIDLE
Protein: DNA-directed RNA polymerase subunit Rpo2 (EC 2.7.7.6) (DNA-directed RNA polymerase subunit beta) (B8YB55)
Organism: Saccharolobus shibatae (strain ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12) (Sulfolobus shibatae)
Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (Probable). This subunit is involved in DNA promoter recognition.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22848102}.
Interaction partners:
Sequence:
MSSNLSIDERWKVIEAYFKSKGLVRQHLDSYNDFVRNKLQEIIDEQGEIPTEIPGLKVRLGKIRIGKPRVRESDRGEREISPMEARLRNLTYAAPLWLTMIPVENNIEAEPEEVYIGDLPIMLKSAIDPISQYTLDKLIEIGEDPKDPGGYFIVNGSERVIVTQEDLAPNRVLVDTGKTGSNITHTAKIISSTAGYRVPVTIERLKDGTFHVSFPAVPGKIPFVILMRALGILTDRDIVYAVSLDPEIQNELFPSLEQASSIANVDDALDFIGSRVAIGQKRENRIEKAQQIIDKYFLPHLGTSADDRRKKAYYLAYAISKVIELYLGRREPDDKDHYANKRLRLAGDLFASLFRVAFKAFVKDLTYQLEKSKVRGRKLALKALVRPDIVTERIRHALATGNWVGGRTGVSQLLDRTNWLSMLSHLRRVISSLARGQPNFEARDLHGTQWGRMCPFETPEGPNSGLVKNLALMAQIAVGINEKIVEKTLYEMGVVPVEEVIRRVTEGGEDQNEYLKWSKVILNGRLVGYYRDGEELAKKIRERRRKGEISDEVNVGHIVTDFINEVHVNCDSGRVRRPLIIVSNGNPLVTREDIEKLDSGSITFDDLVRQGKIEYLDAEEEENAYVALEPSDLTPEHTHLEIWSPAILGITASIIPYPEHNQSPRNTYQSAMAKQALGLYAANYQLRTDTRAHLLHYPQRPLVQTRALDIIGYTNRPAGNNAILAVISFTGYNMEDSIIMNRSSVERGMYRSTFFRLYSTEEVKYPGGQEDKIVMPEPGVRGYKGKEYYRLLEDNGVVSPEVEVKGGDVLIGKVSPPRFLQEFKELSPEQAKRDTSIVTRHGEMGIVDLVLITETAEGNKLVKVRVRDLRIPSIGDKFASRHGQKGVIGMLIPQVDMPYTVKGVVPDVILNPHALPSRMTLGQIMEGIAGKYAALSGNIVDATPFYKTPIEQLQNEILKYGYLPDATEVTYDGRTGQKIKSRIYFGVVYYQKLHHMVADKIHARARGPVQILTRQPTEGRAREGGLRFGEMERDCLIGFGTAMLLKDRLLDNSDRTTIYVCDQCGYIGWYDKNKNKYVCPIHGDKSNLFPVTVSYAFKLLIQELMSMIISPRLILEDRVGLSGGKGNE
Protein: Iron-sulfur cluster assembly protein SufB (P77522)
Organism: Escherichia coli (strain K12)
Function: The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation.
Interaction partners:
- Iron-sulfur cluster assembly protein SufD
- Cysteine desulfuration protein SufE
- Cysteine desulfurase
- Probable ATP-dependent transporter SufC
- Iron-sulfur cluster assembly protein SufA
- Iron-sulfur cluster assembly scaffold protein IscU
- Cysteine desulfurase CsdA
- Iron-binding protein IscA
- Iron-sulfur cluster insertion protein ErpA
- Sulfur acceptor protein CsdE
Sequence:
MSRNTEATDDVKTWTGGPLNYKEGFFTQLATDELAKGINEEVVRAISAKRNEPEWMLEFRLNAYRAWLEMEEPHWLKAHYDKLNYQDYSYYSAPSCGNCDDTCASEPGAVQQTGANAFLSKEVEAAFEQLGVPVREGKEVAVDAIFDSVSVATTYREKLAEQGIIFCSFGEAIHDHPELVRKYLGTVVPGNDNFFAALNAAVASDGTFIYVPKGVRCPMELSTYFRINAEKTGQFERTILVADEDSYVSYIEGCSAPVRDSYQLHAAVVEVIIHKNAEVKYSTVQNWFPGDNNTGGILNFVTKRALCEGENSKMSWTQSETGSAITWKYPSCILRGDNSIGEFYSVALTSGHQQADTGTKMIHIGKNTKSTIISKGISAGHSQNSYRGLVKIMPTATNARNFTQCDSMLIGANCGAHTFPYVECRNNSAQLEHEATTSRIGEDQLFYCLQRGISEEDAISMIVNGFCKDVFSELPLEFAVEAQKLLAISLEHSVG
Protein: P2Y purinoceptor 14 (P2Y14) (G-protein coupled receptor 105) (UDP-glucose receptor) (Q9ESG6)
Organism: Mus musculus (Mouse)
Function: Receptor for UDP-glucose coupled to G-proteins.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- P2X purinoceptor 1
- P2Y purinoceptor 12
- P2X purinoceptor 6
- P2X purinoceptor
- P2Y purinoceptor 13
- P2X purinoceptor 2
- P2X purinoceptor 4
- P2X purinoceptor 7
Sequence:
MNNSTTTDPPNQPCSWNTLITKQIIPVLYGMVFITGLLLNGISGWIFFYVPSSKSFIIYLKNIVVADFLMGLTFPFKVLGDSGLGPWQVNVFVCRVSAVIFYVNMYVSIVFFGLISFDRYYKIVKPLLTSIVQSVNYSKLLSVLVWMLMLLLAVPNIILTNQGVKEVTKIQCMELKNELGRKWHKASNYIFVSIFWVVFLLLIVFYTAITRKIFKSHLKSRKNSTSVKRKSSRNIFSIVLVFVVCFVPYHIARIPYTKSQTEGHYSCRTKETLLYAKEFTLLLSAANVCLDPIIYFFLCQPFREVLNKKLHMSLKVQNDLEVSKTKRENAIHESTDTL
Protein: Inner membrane protein YohD (P33366)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Inner membrane protein YabI
- TVP38/TMEM64 family inner membrane protein YdjZ
- Inner membrane protein YohC
- TVP38/TMEM64 family membrane protein YdjX
- Inner membrane protein YqaA
Sequence:
MDLNTLISQYGYAALVIGSLAEGETVTLLGGVAAHQGLLKFPLVVLSVALGGMIGDQVLYLCGRRFGGKLLRRFSKHQDKIERAQKLIQRHPYLFVIGTRFMYGFRVIGPTLIGASQLPPKIFLPLNILGAFAWALIFTTIGYAGGQVIAPWLHNLDQHLKHWVWLILVVVLVVGVRWWLKRRGKKKPDHQA
Protein: Histone-binding protein RBBP7 (Histone acetyltransferase type B subunit 2) (Nucleosome-remodeling factor subunit RBAP46) (Retinoblastoma-binding protein 7) (RBBP-7) (Retinoblastoma-binding protein p46) (Q60973)
Organism: Mus musculus (Mouse)
Function: Core histone-binding subunit that may target chromatin remodeling factors, histone acetyltransferases and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the type B histone acetyltransferase (HAT) complex, which is required for chromatin assembly following DNA replication; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; and the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- Polycomb protein EED
- Polycomb protein Suz12
- Histone deacetylase 2
- Histone deacetylase 1
- Zinc finger protein AEBP2
- Histone-lysine N-methyltransferase EZH2
- DNA helicase
- Histone-lysine N-methyltransferase EZH1
- Protein Jumonji
- Chromodomain-helicase-DNA-binding protein 4
Sequence:
MASKEMFEDTVEERVINEEYKIWKKNTPFLYDLVMTHALQWPSLTVQWLPEVTKPEGKDYALHWLVLGTHTSDEQNHLVVARVHIPNDDAQFDASHCDSDKGEFGGFGSVTGKIECEIKINHEGEVNRARYMPQNPHIIATKTPSSDVLVFDYTKHPAKPDPSGECNPDLRLRGHQKEGYGLSWNSNLSGHLLSASDDHTVCLWDINAGPKEGKIVDAKAIFTGHSAVVEDVAWHLLHESLFGSVADDQKLMIWDTRSNTTSKPSHLVDAHTAEVNCLSFNPYSEFILATGSADKTVALWDLRNLKLKLHTFESHKDEIFQVHWSPHNETILASSGTDRRLNVWDLSKIGEEQSAEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWVICSVSEDNIMQIWQMAENIYNDEESDVTASELEGQGS
Protein: Nucleolar protein interacting with the FHA domain of MKI67 (C9J808)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
MNNYLFGERLLECHFMPPEKVHKELFKDWNIPFKQPSYPSVKRYNRNRTLTQKLRMEERFKKKERLLRKKLAKKGIDYDFPSLILQKTESISKTNRQTSTKGQVLRKKKKKVSGTLDTPEKTVDSQGPTPVCTPTFLERRKSQVAELNDDDKDDEIVFKQPISC
Protein: Exo-1,4-beta-xylosidase bxlB (EC 3.2.1.37) (1,4-beta-D-xylan xylohydrolase bxlB) (Beta-xylosidase bxlB) (Xylobiase bxlB) (Q5ATH9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Xylan 1,4-beta-xylosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Active against rye arabinoxylan and xylohexaose, but not paranitrophenyl-beta-xyloside.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Exo-1,4-beta-xylosidase xlnD
- Beta-xylosidase C-terminal Concanavalin A-like domain-containing protein
- Exopolygalacturonase X-1
- Probable exopolygalacturonase Bgalacturonohydrolase B)
- Endopolygalacturonase AN8327
- Exopolygalacturonase X-2
- Endopolygalacturonase B
- Probable endopolygalacturonase D
- Beta-glucuronidase
- alcohol dehydrogenase
Sequence:
MAVFKSWNLALLSSLFIPALCQSNYPDCTTGPLSELPICDTSLSPLERAKSLVSALTLEEKINNTGHEAAGSSRLGLPAYNWWNEALHGVAEKHGVSFEESGDFSYATSFPAPIVLGAAFNDALIRRVAEIISTEARAFSNSDHAGIDYWTPNVNPFKDPRWGRGQETPGEDPLHCSRYVKEFVGGLQGDDPEKPKVVATCKHLAAYDLEEWGGVSRFEFDAKVSAVDLLEYYLPPFKTCAVDASVGAFMCSYNALNGVPACADRYLLQTVLREHWGWEGPGHWVTGDCGAVERIQTYHHYVESGPEAAAAALNAGVDLDCGTWLPSYLGEAERQGLISNETLDAALTRLYTSLVQLGYFDPAEGQPLRSLGWDDVATSEAEELAKTVAIQGTVLLKNIDWTLPLKANGTLALIGPFINFTTELQSNYAGPAKHIPTMIEAAERLGYNVLTAPGTEVNSTSTDGFDDALAIAAEADALIFFGGIDNTVEEESLDRTRIDWPGNQEELILELAELGRPLTVVQFGGGQVDDSALLASAGVGAIVWAGYPSQAGGAGVFDVLTGKAAPAGRLPITQYPKSYVDEVPMTDMNLQPGTDNPGRTYRWYEDAVLPFGFGLHYTTFNVSWAKKAFGPYDAATLARGKNPSSNIVDTFSLAVTNTGDVASDYVALVFASAPELGAQPAPIKTLVGYSRASLIKPGETRKVDVEVTVAPLTRATEDGRVVLYPGEYTLLVDVNDEYPTAKFEIKGDVQVLEKFPLSGNDSD
Protein: Single-stranded DNA-binding protein 2 (Sequence-specific single-stranded-DNA-binding protein 2) (P81877)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- LIM domain-binding protein 1
- Single-stranded DNA-binding protein 3
- Insulin gene enhancer protein ISL-1
- SOSS complex subunit C
- Single-stranded DNA-binding protein, mitochondrial
- Integrator complex subunit 3
- LIM domain transcription factor LMO4
- LIM domain-binding protein 2
- Insulin gene enhancer protein ISL-2
- Single-stranded DNA-binding protein 4
Sequence:
MYGKGKSNSSAVPSDSQAREKLALYVYEYLLHVGAQKSAQTFLSEIRWEKNITLGEPPGFLHSWWCVFWDLYCAAPERRETCEHSSEAKAFHDYSAAAAPSPVLGNIPPGDGMPVGPVPPGFFQPFMSPRYPGGPRPPLRIPNQALGGVPGSQPLLPSGMDPTRQQGHPNMGGPMQRMTPPRGMVPLGPQNYGGAMRPPLNALGGPGMPGMNMGPGGGRPWPNPTNANSIPYSSASPGNYVGPPGGGGPPGTPIMPSPADSTNSGDNMYTLMNAVPPGPNRPNFPMGPGSDGPMGGLGGMESHHMNGSLGSGDMDSISKNSPNNMSLSNQPGTPRDDGEMGGNFLNPFQSESYSPSMTMSV
Protein: Putative leucine--tRNA ligase, cytoplasmic (EC 6.1.1.4) (Leucyl-tRNA synthetase) (LeuRS) (Q10490)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Isoleucine--tRNA ligase, cytoplasmic
- Probable glutamate--tRNA ligase, cytoplasmic
- Probable glutamine--tRNA ligase
- Lysine--tRNA ligase, cytoplasmic
- Putative proline--tRNA ligase C19C7.06
- Lysine--tRNA ligase, mitochondrial
- Isoleucine--tRNA ligase, mitochondrial
- Probable methionine--tRNA ligase, cytoplasmic
- Glutamate--tRNA ligase, mitochondrial
- Tyrosine--tRNA ligase, cytoplasmic
Sequence:
MATTEPSVEQLETKTAKLKLENTTKRDTLIELEKKYQQKWQEEKAFEVDAPLEDVPIDELRKKYPKFFGNMPYPYMNGALHLGHAFTLSKVEFTTAFERLNGKRVLFPMGFHCTGMPICASADRLSREIEMFGPSFDVPEEKEEEVEVEVKTPNAREDVTKHSGKKSKAAAKTAAVKYQFQIMESLGVPRTEIHKFADAKYWLSYFPPLCQRDCTEFGLGIDWRRSFITTDVNPYYDSFVRWQVNHLHDSGKIKFGERYTVYSIKDGQPCMDHDRKSGEGVGPQEYTGIKMEVLEFPEAARKALQSIDLSNKKVCMIAATLRPETMYGQTNCYVGPNITYGIYESNVPNELFICTRRAANNMAYQKLSKERGVVSELGTIKGQDLIGALVNAPLSVHKQVYVLPMETVLATKGTGVVTSVPSDSPDDFATLTELRKKAEFYHLNPEWMKYEAVPIIRTPSYGDMCAEFLCKKLKIQSPKDVKQLAQAKELAYKECFYQGTMIIGKYSGEKVETAKPKVRKELIDQGLAFVYNEPEGQVISRSGDDCIVALCDQWFLDYGEASWKAVTEKALDRLNTFSPEVRNGFLKTLDWLSQWACARSYGLGTRLPWDPQFLVESLTDSTIYMAYYTICHLLHSDVYGKVPGALNIKPEQMTPEVWDHVFRQAPKPKNTSISDEALARLCREFQYFYPFDIRASGKDLVPNHLTFCLYTHTAIFDEKYWPKGIRANGHLLMNGEKMSKSTGNFMTLHEATKKFGADATRLALADAGDTVDDANFEEALANSAILRLYTQEAWCKEMMENLDNLRTGPYNFHDKVFENEINQLIESSREAFSATLFKAALKSCFYDLQNARDWYREVTADRKMHRDLVCRWIETQVLLLATFAPHWSEHIWLTTLKKPQSIHVSGRFPQVSSPVNTALSNSLLYIRTLSRVIREAEAAQLKRQKKGKGMLFDPSKPKRLTVFVAEKFPEWQAQYVALLQKYYNESENKFDDKAIISSVDKKEMKRAMPFIQQFKQSVINRGEHVSANSIFSRELGFNELEVLREVKPYLVRNVGIQELRIVLLQKPADKSSAAIGLVESGSDAGATVEIAPNFANTVPGQPTFLFENVSA
Protein: Lipid A deacylase PagL (EC 3.1.1.77) (LPS 3-O-deacylase PagL) (Outer membrane enzyme PagL) (PhoP/PhoQ-activated gene product L) (Q9HVD1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Has lipid A 3-O-deacylase activity. Hydrolyzes the ester bond at the 3 position of lipid A, a bioactive component of lipopolysaccharide (LPS), thereby releasing the primary fatty acyl moiety. Lacks fatty acyl chain-length specificity as removes both 3-OH C10 and 3-OH C14 fatty acids from lipid A.
Subcellular location: Cell outer membrane {ECO:0000269|PubMed:15611102, ECO:0000269|PubMed:16352835, ECO:0000269|PubMed:16632613}; Multi-pass membrane protein {ECO:0000269|PubMed:15611102, ECO:0000269|PubMed:16352835, ECO:0000269|PubMed:16632613}.
Interaction partners:
- Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase
- Tetraacyldisaccharide 4'-kinase
- 3-deoxy-D-manno-octulosonic acid transferase
- Two-component response regulator PhoP
- Two-component sensor PhoQ
- Glycine zipper 2TM domain-containing protein
- Outer membrane porin F
- Lipid A biosynthesis acyltransferase
- Response regulator protein PmrA
- LPS-assembly protein LptD
Sequence:
MKKLLPLAVLAALSSVHVASAQAADVSAAVGATGQSGMTYRLGLSWDWDKSWWQTSTGRLTGYWDAGYTYWEGGDEGAGKHSLSFAPVFVYEFAGDSIKPFIEAGIGVAAFSGTRVGDQNLGSSLNFEDRIGAGLKFANGQSVGVRAIHYSNAGLKQPNDGIESYSLFYKIPI
Protein: Protein GPR107 (Lung seven transmembrane receptor 1) (Q5VW38)
Organism: Homo sapiens (Human)
Function: Has been proposed to act as a receptor for neuronostatin, a peptide derived from the somatostatin/SST precursor. Involved in blood sugar regulation through the induction of glucagon in response to low glucose (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:D3ZWZ9}; Multi-pass membrane protein {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:25031321}.
Interaction partners:
- LIM homeobox transcription factor 1-beta
Sequence:
MAALAPVGSPASRGPRLAAGLRLLPMLGLLQLLAEPGLGRVHHLALKDDVRHKVHLNTFGFFKDGYMVVNVSSLSLNEPEDKDVTIGFSLDRTKNDGFSSYLDEDVNYCILKKQSVSVTLLILDISRSEVRVKSPPEAGTQLPKIIFSRDEKVLGQSQEPNVNPASAGNQTQKTQDGGKSKRSTVDSKAMGEKSFSVHNNGGAVSFQFFFNISTDDQEGLYSLYFHKCLGKELPSDKFTFSLDIEITEKNPDSYLSAGEIPLPKLYISMAFFFFLSGTIWIHILRKRRNDVFKIHWLMAALPFTKSLSLVFHAIDYHYISSQGFPIEGWAVVYYITHLLKGALLFITIALIGTGWAFIKHILSDKDKKIFMIVIPLQVLANVAYIIIESTEEGTTEYGLWKDSLFLVDLLCCGAILFPVVWSIRHLQEASATDGKGDSMGPLQQRANLRAGSRIESHHFAQADLELLASSCPPASVSQRAGITAAINLAKLKLFRHYYVLIVCYIYFTRIIAFLLKLAVPFQWKWLYQLLDETATLVFFVLTGYKFRPASDNPYLQLSQEEEDLEMESVVTTSGVMESMKKVKKVTNGSVEPQGEWEGAV
Protein: Cathelicidin B1 (R4GJF1)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MGRMWASEVLLLLLLGSSRAVTPGLDVSTAPGLDGSIPPGLDGSIPPGLDGSVSPGLDGSVSPGLDGSVSPGLDGSASPGLDGSTPAGRDGTITPKLEGTITPKQDGSISPSWPWRWPITYLDAILAAVRLLNQRISGPCILRLREAQPRPGWVGTLQRRREVSFLVEDGPCPPGVDCRSCEPGALQHCVGTVSIEQQPTAELRCRPLRPQPIRNWWIRIWEWLNGIRKRLRQRSPFYVRGHLNVTSTPQP