wanglab/gogpt-training-data huggingface dataset:
Protein: Complex I assembly factor ACAD9, mitochondrial (Acyl-CoA dehydrogenase family member 9) (ACAD-9) (EC 1.3.8.-) (Q9H845)
Organism: Homo sapiens (Human)
Function: As part of the MCIA complex, primarily participates in the assembly of the mitochondrial complex I and therefore plays a role in oxidative phosphorylation. This moonlighting protein has also a dehydrogenase activity toward a broad range of substrates with greater specificity for long-chain unsaturated acyl-CoAs. However, in vivo, it does not seem to play a primary role in fatty acid oxidation. In addition, the function in complex I assembly is independent of the dehydrogenase activity of the protein.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:16020546, ECO:0000269|PubMed:20816094}; Peripheral membrane protein {ECO:0000269|PubMed:16020546}; Matrix side {ECO:0000269|PubMed:16020546}. Note=Essentially associated with membranes. {ECO:0000269|PubMed:16020546}.
Interaction partners:
- Complex I assembly factor TMEM126B, mitochondrial
- Complex I intermediate-associated protein 30, mitochondrial
- Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial
- Complex I assembly factor TIMMDC1, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex assembly factor 3
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- NADH-ubiquinone oxidoreductase chain 6
- NADH dehydrogenase 1 alpha subcomplex subunit 13
Sequence:
MSGCGLFLRTTAAARACRGLVVSTANRRLLRTSPPVRAFAKELFLGKIKKKEVFPFPEVSQDELNEINQFLGPVEKFFTEEVDSRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLGEIISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKHYILNGSKVWITNGGLANIFTVFAKTEVVDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIALTGLQHAGRILTTRIHELKQAKVSTVMDTVGRRLRDSLGRTVDLGLTGNHGVVHPSLADSANKFEENTYCFGRTVETLLLRFGKTIMEEQLVLKRVANILINLYGMTAVLSRASRSIRIGLRNHDHEVLLANTFCVEAYLQNLFSLSQLDKYAPENLDEQIKKVSQQILEKRAYICAHPLDRTC
Protein: Salivary glue protein Sgs-7 (P02841)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Salivary glue protein Sgs-5
- Salivary glue protein Sgs-4
- Ecdysone-induced gene 71Ee
- Salivary glue protein Sgs-3
- Sgs5bis
- Salivary glue protein Sgs-8
- Salivary gland secretion 1
- Uncharacterized protein, isoform A
- Uncharacterized protein, isoform A
Sequence:
MKLIAVTIIACILLIGFSDLALGGACECQPCGPGGKACTGCPEKPQLCQQLISDIRNLQQKIRKCVCGEPQWMI
Protein: RFX-like DNA-binding protein RFX1 (P48743)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Serine/threonine-protein kinase MEC1
- Serine/threonine-protein kinase RAD53
- DNA damage response protein kinase DUN1
- General transcriptional corepressor TUP1
- General transcriptional corepressor CYC8
- DNA-binding protein REB1
- CRE-binding bZIP protein SKO1
- Chromatin structure-remodeling complex subunit RSC2
- Chromatin structure-remodeling complex protein RSC3
- Imitation switch two complex protein 1
Sequence:
MVIFKERKPTENLFTRKIPAKYFIFSPSFLSVHYFEFYLPMSGDNNIEPTSRGSNDNSNGPSNGSSVNSNRYSLNAPKYSSQPPPASHTYLPPMSVNIPPIASKSSSIYSLLHQSSPRPETPNPILPPLIGSGPGSHKPSPTPTQPPAQPATQRQPATYSVYPASISLNRSNSSAYPLSFKSEETLNNNPPTAAKRTNTFPSIPSSTKKQKTSQEKRISSISRRNTQEIIAKQIAENNKSKTIEEYAQIVKHAEIKVLSMDSQNTSKAALQLAEQNRERERQVFALLWLMKNCKSQHDSYVPRGKIFAQYASSCSQNNLKPLSQASLGKLIRTVFPDLTTRRLGMRGQSKYHYCGLKLTVNESGSVSLNNNNASLSLVHNNDPISPLSSPSPSSPSPQVPNVSSPFSLNRKSLSRTGSPVKQSSNDNPNEPELESQHPNETEANKLDSLPPAANNPTGTLSSDELTFTHDLIEKVFNCNDKLSDNYNTQILSNTEHPLLTSYKLDFPKIPAGVLPTDTDSDVISSLESLYHIHCNSVYECIKFLKSDNISNALFFSNSNSISPTMFNLFISEPLIDWVTKCDLITYTGLIKFFSQFIIHSNEISDSIIQKLESMIKLLPEQINKAVLELPKALVQRKLSIINNFTKLVKKLIKLLKFILNFLKSFPIFKSGMNNDWKNIVNLDDILEMMINEDDTNSETNTIMQHLQGFCQVFVTKFLNSSMSVSNDPSVSIECKSLNEMIKDFCSFISLQSKFSCLKLIDCSTRFRNAIIGDISLKSNENLLSWLFLNNVMGQLLNYCFEVMKFVNGLKV
Protein: Elongation of very long chain fatty acids protein 4 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL4) (ELOVL fatty acid elongase 4) (ELOVL FA elongase 4) (Very long chain 3-ketoacyl-CoA synthase 4) (Very long chain 3-oxoacyl-CoA synthase 4) (Q6PBM2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|HAMAP-Rule:MF_03204}; Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_03204}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Acyl-CoA 6-desaturase
- Very-long-chain 3-oxoacyl-CoA reductase-B
- 20beta-hydroxysteroid dehydrogenase type 2
- Very-long-chain 3-oxoacyl-CoA reductase-A
Sequence:
MEIIQHIINDTVHFYKWSLTIADKRVEKWPLMDSPLPTLAISSSYLLFLWLGPKYMQGREPFQLRKTLIIYNFSMVILNFFIFKELFLAARAANYSYICQPVDYSDDPNEVRVAAALWWYFISKGVEYLDTVFFILRKKFNQISFLHVYHHCTMFTLWWIGIKWVAGGQSFFGAHMNAAIHVLMYLYYGLAAFGPKIQKFLWWKKYLTIIQMVQFHVTIGHTALSLYSDCPFPKWMHWCLIGYALTFIILFGNFYYQTYRRQPRRDKPRALHNGASNGALTSSNGNTAKLEEKPAESGRRRRKGRAKRD
Protein: Protein serine/threonine kinase-1 (EC 2.7.11.1) (Q8IL19)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- non-specific serine/threonine protein kinase
Sequence:
MTELNIIDNNEKHSKYKLYKYCRNYINDFKNKYMMGYSSNLYKNSPNKYYYDTRNNSNNNNNGYYYHNYNNGYQIRNKRNRSFETVSNSKNKHKISKKYKYNNEPHESFRDYDYKSKPSYSSVKKIYDREQKRYNKMFVESRYNENHKNKYINNYNLSRKRNYYSYKKKIYTDRRNFDTHFGQGNIIYNNEYYLINDGSSLNKKRLHYAKGSFRSRSRSKNYNTYNLEKSKKMKYSSRHNIYRYHNGNKNKSISRWEDNYTYKDIYQPSSSLHKYKRRSNFTRDDNSIKSKMYYENKKTDHLYSYEDKYYNKYDDKYDDKYDDKYDDKYDDKYDDKYDDKYDDKYDDKYDDNYDDKYDYGEEEHRQEYYKKKKISFNNSTNNKSSINYDDVKRELKKRKKKKYSNESKVYDSLKRDETNHHTNNNSYLNEINKKNSNLSNNYVAVRNKKRDKEYISDSNKSGFSNKGSYYMQKKKLHVDKYDNDSHNRTISRTSSDNYSRKKYTHKRNRTKTSDTEDKKERKKKKKKKENNESDDEIVHFSWKKGMLLNNAFLVIRKMGDGTFGRVLLCQHIDNKKYYAVKVVRNIKKYTRSAKIEADILKKIQNDDINNNNIVKYHGKFMYYDHMCLIFEPLGPSLYEIITRNNYNGFHIEDIKLYCIEILKALNYLRKMSLTHTDLKPENILLDDPYFEKSLITVRRVTDGKKIQIYRTKSTGIKLIDFGCATFKSDYHGSIINTRQYRAPEVILNLGWDVSSDMWSFGCVLAELYTGSLLFRTHEHMEHLAMMESIIQPIPKNMLYEATKTNGSKYVNKDELKLAWPENASSINSIKHVKKCLPLYKIIKHELFCDFLYSILQIDPTLRPSPAELLKHKFLEENYEYY
Protein: Peptidyl-prolyl cis-trans isomerase B (PPIase B) (EC 5.2.1.8) (Rotamase B) (P23869)
Organism: Escherichia coli (strain K12)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:1606970, ECO:0000269|PubMed:2007139}.
Interaction partners:
- UDP-2,3-diacylglucosamine hydrolase
- FKBP-type 22 kDa peptidyl-prolyl cis-trans isomerase
- NADH-quinone oxidoreductase subunit C/D
- Chaperone protein HtpG
- FKBP-type peptidyl-prolyl cis-trans isomerase FkpA
- Elongation factor G
Sequence:
MVTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEPIKNEANNGLKNTRGTLAMARTQAPHSATAQFFINVVDNDFLNFSGESLQGWGYCVFAEVVDGMDVVDKIKGVATGRSGMHQDVPKEDVIIESVTVSE
Protein: POU domain, class 2, transcription factor 2 (Lymphoid-restricted immunoglobulin octamer-binding protein NF-A2) (Octamer-binding protein 2) (Oct-2) (Octamer-binding transcription factor 2) (OTF-2) (P09086)
Organism: Homo sapiens (Human)
Function: Transcription factor that specifically binds to the octamer motif (5'-ATTTGCAT-3'). Regulates IL6 expression in B cells with POU2AF1 (By similarity). Regulates transcription in a number of tissues in addition to activating immunoglobulin gene expression. Modulates transcription transactivation by NR3C1, AR and PGR.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus.
Interaction partners:
- POU domain, class 2, transcription factor 1
- POU domain, class 2, transcription factor 3
- POU domain class 2-associating factor 1
- Host cell factor 2
- TATA-box-binding protein
Sequence:
MVHSSMGAPEIRMSKPLEAEKQGLDSPSEHTDTERNGPDTNHQNPQNKTSPFSVSPTGPSTKIKAEDPSGDSAPAAPLPPQPAQPHLPQAQLMLTGSQLAGDIQQLLQLQQLVLVPGHHLQPPAQFLLPQAQQSQPGLLPTPNLFQLPQQTQGALLTSQPRAGLPTQAVTRPTLPDPHLSHPQPPKCLEPPSHPEEPSDLEELEQFARTFKQRRIKLGFTQGDVGLAMGKLYGNDFSQTTISRFEALNLSFKNMCKLKPLLEKWLNDAETMSVDSSLPSPNQLSSPSLGFDGLPGRRRKKRTSIETNVRFALEKSFLANQKPTSEEILLIAEQLHMEKEVIRVWFCNRRQKEKRINPCSAAPMLPSPGKPASYSPHMVTPQGGAGTLPLSQASSSLSTTVTTLSSAVGTLHPSRTAGGGGGGGGAAPPLNSIPSVTPPPPATTNSTNPSPQGSHSAIGLSGLNPSTGPGLWWNPAPYQP
Protein: Solute carrier family 12 member 8 (A9C3V4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Mitochondrial fission regulator 1-like
- Extended synaptotagmin-3
- Deoxyribonuclease TATDN2 isoform X1
- Non-specific serine/threonine protein kinase.
- Rho guanine nucleotide exchange factor
- Cyclic nucleotide gated channel subunit alpha 2a isoform X1
Sequence:
MSPQVQELFHEDAQVQLFVWEPVLFGTWDGVFTTCMINIFGVVLFLRTGWLVGNTGVFLGMLLVSLVVLVALVTVMSGVGVSECCSVGNGGVYSMISTVLGGRIGGTVGLLYVFGQCVAGAMYITGFAESIAQVLSLQSTWVVRGISVAVLLGLLGINLAGVKWIVRLQLVLLGILAMSTLDFVIGTFSHLDPEHGFVGYSEKLLRKNTLPDYTAGETFFTVFGVFFPAATGVMAGFNMSSDLQRPEHNIPVGTLAAVCTSWFLYLVFVFLLGAICTREALRYDFLIAEKVSLVGFLFLLGLYISSLASCMGGLYGAPRILQCIAQERVIPVLAFLGKGRGPNKTPVAAICLTSLITMGFIFIGQVNVLAPIVTINFMLTYSVIDYCYFCVVKTYELQVQQRKKLISRSSSRKSLVSSTHPRYGSGGAISDPVNGTLLQFTKDMDQIFPLPSTEEQRASPASKARGRKTKIPAKEMLMNSFGLDLNSNAPLDKGKDERELEQAAGLDDDTSSQIGLIESDLKMGNQMNLSLPNSGPAELEQLPKEKIDRNGSETNLEGSEIRSIQSSVYARFCNPWVSLIGALCSFMIMFIIQWMYALINISAALILFIYIGTTSPGLPTGAASHFSFFKWLKTSLHNLGRQNGALQDQIVVTPSLSAVGMETRQLTEENADFALRDRYHHSSFITTTDKMVHPQSN
Protein: 3-hydroxyisobutyryl-CoA hydrolase (HIB-CoA hydrolase) (HIBYL-CoA-H) (EC 3.1.2.4) (3-hydroxyisobutyryl-coenzyme A hydrolase) (B8ZZZ0)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|RuleBase:RU369070}.
Interaction partners:
Sequence:
MPGMPGRARPGAASLPGQGPRRPARRGEEPSRRHRLTYPRRGDGARRSPARAPDPRRRGSGAGTLWFNAFKRTNTILHHLRMSKHTDAAEEVLLEKKGCTGVITLNRPKFLNALTLNMIRQIYPQLKKWEQDPETFLIIIKGAGGKAFCAGGDIRVISEAEKAKQKIAPVFFREEYMLNNAVGSCQKPYVALIHGITMGGGVGLSVHGQFRVATEKCLFAMPETAIGLFPDVGGGYFLPRLQGKLGYFLALTGFRLKGRDVYRAGIATHFVDS
Protein: Indole-3-acetic acid-amido synthetase GH3.15 (EC 6.3.2.-) (Auxin-responsive GH3-like protein 15) (AtGH3-15) (Protein GRETCHEN HAGEN 3.15) (Q8GZ29)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Indole-3-acetic acid-amido (IAA) synthetase that catalyzes the conjugation of amino acids to auxin specifically using the auxin precursor indole-3-butyric acid (IBA) and glutamine and, possibly, cysteine as substrates. Displays high catalytic activity with the auxinic phenoxyalkanoic acid herbicides 4-(2,4-dichlorophenoxy)butyric acid (2,4-DB) and to some extent 2,4-dichlorophenoxylacetic acid (2,4-D) as substrates, thus confering resistance to herbicides.
Interaction partners:
- Two-component response regulator ARR16
- Serine/threonine-protein kinase SRK2F
- Serine/threonine-protein kinase SRK2J
- Two-component response regulator ARR17
- Serine/threonine-protein kinase SRK2H
Sequence:
MLPKFDPTNQKACLSLLEDLTTNVKQIQDSVLEAILSRNAQTEYLRGFLNGQVDKQNFKKNVPVVTYEDIRSYIDRIANGEPSDLICDRPISVLLTSSGTSGGVPKLIPLTTEDLEQRISFSSLYAPLLYKHIDGLSEGKSLIFYFVTRESKTANGLMVRTMVTSFLKSIKQTNSFLWDSLQVSPHAITTCADTTQSMYCQLLCGLLERDNVARLGAPFASSFLKVIKFLEDHWPELCSNIRTGRLSDWITDATCTSGIGKFLTAPNPELASLIEQECSKTSWEAILKRLWPKAKCIESIITGTMAQYIPLLEFYSGGLPLTSSFYGSSECFMGVNFNPLCKPSDVSYTIIPCMGYFEFLEVEKDHQEAGHDPTEKPVVVDLVDVKIGHDYEPVVTTFSGLYRYRVGDVLRATGFYNNAPHFCFVGRQKVVLSIDMDKTYEDDLLKAVTNAKLLLEPHDLMLMDFTSRVDSSSFPGHYVIYWELGSKVKDAKFEPNRDVMEECCFTVEESLDAVYRKGRKNDKNIGPLEIKVVKPGAFDELMNFFLSRGSSVSQYKTPRSVTNEEALKILEANVISEFLSRKIPSWELHELHSGR
Protein: Kinesin-like protein KIN-14D (AtKIN14b) (F4JGP4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Kinesin that supports microtubule movement in an ATP-dependent manner and that functions as a minus-end directed motor as well as a plus-end tracking protein. During mitosis, is involved in early spindle assembly. Participates in the capture of antiparallel interpolar microtubules and helps in generating force to coalign microtubules.
Subcellular location: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, phragmoplast. Note=In interphase, is enriched specifically at growing microtubule plus-ends. In dividing cells, accumulates in spindle midzones and phragmoplast leading edges.
Interaction partners:
- Kinesin-like protein KIN-10A
- Microtubule-associated protein RP/EB family member 1C
- Kinesin-like protein KIN-5A
- Serine/threonine-protein kinase Aurora-1
- Microtubule-associated protein RP/EB family member 1B
- Kinesin-like protein KIN-5C
- Kinesin-like protein KIN-12B
- Serine/threonine-protein kinase Aurora-2
- Kinesin-like protein KIN-12D
- Kinesin-like protein KIN-5B
Sequence:
MPLRNQNRAPLPSPNVKKEALSSIPFDKRRKETQGTGRRQVLSTVNRQDANSDVGSTEECGKVEFTKDEVLALLNERAKAGKFDTKGKIEQMTDIIKKLKVCVRWYQQVDETHVQDKENLSSSLQSAEKRYSDKELDAKTKEEELRATITEMKENIESLQEKLSKEKLSKLDAIENHRREKDCRVVAEKLQVSLREELDKVKEEKMAAKQKVTSLEDMYKRLQEYNTSLQQYNTKLQTDLEVAREAHTRAEKEKSSILENLTTLRGHSKSLQDQLASSRVSQDEAVKQKDSLLMEVNNLQSELQQVRDDRDRHVVQSQKLAGEILMYKESVGKSSHELDILIAKSGSLEETCSLQKERIKMLEQELAFAKEKLKMVDLSMSHTMTEFEEQKQCMHELQDRLADTERQLFEGELLRKKLHNTILELKGNIRVFCRVRPLLPDDGGRQEASVIAYPTSTESLGRGIDVVQSGNKHPFTFDKVFDHGASQEEVFFEISQLVQSALDGYKVCIFAYGQTGSGKTYTMMGRPETPEQKGLIPRSLEQIFKTSQSLSTQGWKYKMQVSMLEIYNESIRDLLSTSRTIAIESVRADSSTSGRQYTITHDVNGNTHVSDLTIVDVCSIGQISSLLQQAAQSRSVGKTHMNEQSSRSHFVFTLRISGVNESTEQQVQGVLNLIDLAGSERLSRSGATGDRLKETQAINKSLSALSDVIFALAKKEDHVPFRNSKLTYLLQPCLGGDSKTLMFVNISPDPSSTGESLCSLRFAARVNACEIGIPRRQTSAKLLDSRLSYG
Protein: Syncrip, isoform D (Q9VDI8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MLSQMEASKVQKDEGGGEALSRTILKTPSSFRTPSPIPSCSKMAEGNGELLDDINQKADDRGDGERTEDYPKLLEYGLDKKVAGKLDEIYKTGKLAHAELDERALDALKEFPVDGALNVLGQFLESNLEHVSNKSAYLCGVMKTYRQKSRASQQGVAAPATVKGPDEDKIKKILERTGYTLDVTTGQRKYGGPPPHWEGNVPGNGCEVFCGKIPKDMYEDELIPLFENCGIIWDLRLMMDPMTGTNRGYAFVTFTNREAAVNAVRQLDNHEIKPGKCLKINISVPNLRLFVGNIPKSKGKDEILEEFGKLTAGLYEVIIYSSPDDKKKNRGFCFLEYESHKAASLAKRRLGTGRIKVWGCDIIVDWADPQEEPDEQTMSKVKVLYVRNLTQDVSEDKLKEQFEQYGKVERVKKIKDYAFIHFEDRDSAVEAMRGLNGKEIGASNIEVSLAKPPSDKKKKEEILRARERRMMQMMQARPGIVGNLSPTHPSIMSLTPMRPGARMPLRTPIPREYDYFYDFFGFSDYRQGGSFGNNVSYYDDMYRWIDGDYNYYDYPNGGGGGSGGGGGSVSGGTVLPLSAGGSQNSPMASGQRSARGSASGPSASPSLMGVGRGHGITVPRGRVVGQRGSISRLGAQTVPQAAGAAAAAGQAAAAVAQRGATGQGAPAATGGFRGVLPTRPSARGTQHVKPLQNLPAGAAFKTFMEGN
Protein: Nuclear pore complex protein Nup93 (93 kDa nucleoporin) (Nucleoporin Nup93) (Q8N1F7)
Organism: Homo sapiens (Human)
Function: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. May anchor nucleoporins, but not NUP153 and TPR, to the NPC. During renal development, regulates podocyte migration and proliferation through SMAD4 signaling.
Subcellular location: Nucleus membrane {ECO:0000250|UniProtKB:Q66HC5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q66HC5}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:9348540}. Nucleus envelope {ECO:0000269|PubMed:26878725, ECO:0000269|PubMed:9348540}. Note=Localizes at the nuclear basket and at or near the nuclear entry to the gated channel of the pore. {ECO:0000269|PubMed:9348540}.
Interaction partners:
- Nuclear pore complex protein Nup98-Nup96
- Nucleoporin p58/p45
- Nucleoporin NUP35
- Nuclear pore complex protein Nup107
- Nuclear pore complex protein Nup85
- Nuclear pore complex protein Nup155
- Nucleoporin SEH1
- Nuclear pore glycoprotein p62
- Nuclear pore complex protein Nup205
- Nucleoporin p54
Sequence:
MDTEGFGELLQQAEQLAAETEGISELPHVERNLQEIQQAGERLRSRTLTRTSQETADVKASVLLGSRGLDISHISQRLESLSAATTFEPLEPVKDTDIQGFLKNEKDNALLSAIEESRKRTFGMAEEYHRESMLVEWEQVKQRILHTLLASGEDALDFTQESEPSYISDVGPPGRSSLDNIEMAYARQIYIYNEKIVNGHLQPNLVDLCASVAELDDKSISDMWTMVKQMTDVLLTPATDALKNRSSVEVRMEFVRQALAYLEQSYKNYTLVTVFGNLHQAQLGGVPGTYQLVRSFLNIKLPAPLPGLQDGEVEGHPVWALIYYCMRCGDLLAASQVVNRAQHQLGEFKTWFQEYMNSKDRRLSPATENKLRLHYRRALRNNTDPYKRAVYCIIGRCDVTDNQSEVADKTEDYLWLKLNQVCFDDDGTSSPQDRLTLSQFQKQLLEDYGESHFTVNQQPFLYFQVLFLTAQFEAAVAFLFRMERLRCHAVHVALVLFELKLLLKSSGQSAQLLSHEPGDPPCLRRLNFVRLLMLYTRKFESTDPREALQYFYFLRDEKDSQGENMFLRCVSELVIESREFDMILGKLENDGSRKPGVIDKFTSDTKPIINKVASVAENKGLFEEAAKLYDLAKNADKVLELMNKLLSPVVPQISAPQSNKERLKNMALSIAERYRAQGISANKFVDSTFYLLLDLITFFDEYHSGHIDRAFDIIERLKLVPLNQESVEERVAAFRNFSDEIRHNLSEVLLATMNILFTQFKRLKGTSPSSSSRPQRVIEDRDSQLRSQARTLITFAGMIPYRTSGDTNARLVQMEVLMN
Protein: Transcription factor MYB54 (Myb-related protein 54) (AtMYB54) (Q9FX36)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that regulates secondary cell wall (SCW) biosynthesis, especially in interfascicular and xylary fibers.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:18952777}.
Interaction partners:
- NAC domain-containing protein 66
- NAC domain-containing protein 10
- NAC domain-containing protein 73
- NAC domain-containing protein 12
- Homeobox protein knotted-1-like 7
- NAC domain-containing protein 43
- NAC domain-containing protein 30
- NAC domain-containing protein 104
Sequence:
MIMCSRGHWRPAEDEKLKDLVEQYGPHNWNAIALKLPGRSGKSCRLRWFNQLDPRINRNPFTEEEEERLLAAHRIHGNRWSIIARLFPGRTDNAVKNHWHVIMARRTRQTSKPRLLPSTTSSSSLMASEQIMMSSGGYNHNYSSDDRKKIFPADFINFPYKFSHINHLHFLKEFFTGKIALNHKANQSKKPMEFYNFLQVNTDSNKSEIIDQDSGQSKRSDSDTKHESHVPFFDFLSVGNSAS
Protein: aspartate--tRNA ligase (EC 6.1.1.12) (Aspartyl-tRNA synthetase) (Q8I2B1)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Proline--tRNA ligase
- aspartate--tRNA ligase
- glutamate--tRNA ligase
- Glutamyl-tRNA
- glutamine--tRNA ligase
- isoleucine--tRNA ligase
- leucine--tRNA ligase
- Glutamyl-tRNA
- tRNA import protein tRIP
- arginine--tRNA ligase
Sequence:
MINCLLQLNGRLNYLKKYLLLINLFNLKNKDINFILVRKGLFVCGLRKMEKDDVVSSTPAATEEAVMNDKKKEKKAKKLAEKELKLAKKLERENLKNEAAKVLDYVCEDINKDNYGYIKVSTLQKYADSIMELYNLEDIYNFFVKSEDCENEKREICVDKNVGDVKDAYNEENLLGKKKIWVRGRIHDIRSKGSIAFIILRHKLYSLQCILDIKNNNNDKNMMKWVSNLSLECIVDIYGEIKKPEIPIDSTNIKYEIHINKIFCLSKTMKELPFLLKDANMKETNDEITIKVNQDNRLNNRCFDLRTYANYSIFSLQSVICHIFRTFLLQHNFVEIHTPKLLGESSEGGANAFKINYFNQNGYLAQSPQLYKQMCINSGFDKVFEVGPVFRAENSNTYRHLCEYVSLDIEMTYKFDYMENVHFYDSMFKHIFKELTNNEKNKTFIKTIKNQYPSDDFVWLDKTPIFTYEEAIKILIKNGKLFLKEEDILTYDLTTDLEKELGKLIKLSHNTDYYIIINFPSSLRPFYTMYKEDDPKISNSYDFFMRGEEILSGSQRISDMKLLLENIKLFNLDPNKLNFYIDSFAYSSYPHSGCGIGLERVLMLFLGLNNIRKTSLFPRDPKRLIP
Protein: Leucine-rich repeat-containing G-protein coupled receptor 5 (G-protein coupled receptor 49) (G-protein coupled receptor 67) (G-protein coupled receptor HG38) (O75473)
Organism: Homo sapiens (Human)
Function: Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and acts as a stem cell marker of the intestinal epithelium and the hair follicle. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. Involved in the development and/or maintenance of the adult intestinal stem cells during postembryonic development.
Subcellular location: Cell membrane; Multi-pass membrane protein. Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. Note=Rapidly and constitutively internalized to the trans-Golgi network at steady state. Internalization to the trans-Golgi network may be the result of phosphorylation at Ser-861 and Ser-864; however, the phosphorylation event has not been proven (PubMed:23439653). {ECO:0000269|PubMed:23439653}.
Interaction partners:
- R-spondin-1
- R-spondin-2
- E3 ubiquitin-protein ligase RNF43
- E3 ubiquitin-protein ligase ZNRF3
- R-spondin-3
- R-spondin-4
- Leucine-rich repeat-containing G-protein coupled receptor 4
- Leucine-rich repeat-containing G-protein coupled receptor 6
- Prominin-1
- Olfactomedin-4
Sequence:
MDTSRLGVLLSLPVLLQLATGGSSPRSGVLLRGCPTHCHCEPDGRMLLRVDCSDLGLSELPSNLSVFTSYLDLSMNNISQLLPNPLPSLRFLEELRLAGNALTYIPKGAFTGLYSLKVLMLQNNQLRHVPTEALQNLRSLQSLRLDANHISYVPPSCFSGLHSLRHLWLDDNALTEIPVQAFRSLSALQAMTLALNKIHHIPDYAFGNLSSLVVLHLHNNRIHSLGKKCFDGLHSLETLDLNYNNLDEFPTAIRTLSNLKELGFHSNNIRSIPEKAFVGNPSLITIHFYDNPIQFVGRSAFQHLPELRTLTLNGASQITEFPDLTGTANLESLTLTGAQISSLPQTVCNQLPNLQVLDLSYNLLEDLPSFSVCQKLQKIDLRHNEIYEIKVDTFQQLLSLRSLNLAWNKIAIIHPNAFSTLPSLIKLDLSSNLLSSFPITGLHGLTHLKLTGNHALQSLISSENFPELKVIEMPYAYQCCAFGVCENAYKISNQWNKGDNSSMDDLHKKDAGMFQAQDERDLEDFLLDFEEDLKALHSVQCSPSPGPFKPCEHLLDGWLIRIGVWTIAVLALTCNALVTSTVFRSPLYISPIKLLIGVIAAVNMLTGVSSAVLAGVDAFTFGSFARHGAWWENGVGCHVIGFLSIFASESSVFLLTLAALERGFSVKYSAKFETKAPFSSLKVIILLCALLALTMAAVPLLGGSKYGASPLCLPLPFGEPSTMGYMVALILLNSLCFLMMTIAYTKLYCNLDKGDLENIWDCSMVKHIALLLFTNCILNCPVAFLSFSSLINLTFISPEVIKFILLVVVPLPACLNPLLYILFNPHFKEDLVSLRKQTYVWTRSKHPSLMSINSDDVEKQSCDSTQALVTFTSSSITYDLPPSSVPSPAYPVTESCHLSSVAFVPCL
Protein: Protein DEK (P35659)
Organism: Homo sapiens (Human)
Function: Involved in chromatin organization.
Subcellular location: Nucleus {ECO:0000269|PubMed:17524367, ECO:0000269|PubMed:19695025}. Note=Enriched in regions where chromatin is decondensed or sparse in the interphase nuclei.
Interaction partners:
- Regulator of nonsense transcripts 1
- Serine/arginine repetitive matrix protein 1
- RNA-binding protein with serine-rich domain 1
- Tyrosine-protein kinase BAZ1B
- Nuclear pore complex protein Nup214
- Myb-binding protein 1A
- Splicing factor 3B subunit 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5
- Nucleolar RNA helicase 2
- Splicing factor U2AF 35 kDa subunit
Sequence:
MSASAPAAEGEGTPTQPASEKEPEMPGPREESEEEEDEDDEEEEEEEKEKSLIVEGKREKKKVERLTMQVSSLQREPFTIAQGKGQKLCEIERIHFFLSKKKTDELRNLHKLLYNRPGTVSSLKKNVGQFSGFPFEKGSVQYKKKEEMLKKFRNAMLKSICEVLDLERSGVNSELVKRILNFLMHPKPSGKPLPKSKKTCSKGSKKERNSSGMARKAKRTKCPEILSDESSSDEDEKKNKEESSDDEDKESEEEPPKKTAKREKPKQKATSKSKKSVKSANVKKADSSTTKKNQNSSKKESESEDSSDDEPLIKKLKKPPTDEELKETIKKLLASANLEEVTMKQICKKVYENYPTYDLTERKDFIKTTVKELIS
Protein: Mangetout, isoform G (A0A0B4KF15)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MTTANIVAAPAAPTISPAITSTATRIGGKAVPTPRLLGSGAANVAQILAKSLDSPSPSSSSGWPVKHAAVLEGDVILGGLMMVHSREDSITCGPIMPQGGIQALEAMLYTLDQVNKQQLLPNVTLGAHLLDDCDKDTYGLEMAVDFIKAHIQINSEYITVKTEAKAKMKTFCDESKWSVQICLLLLLVVLSTCHILQTESQVVGDIEQADDGVASSHRRSRSHSASHQAHVGNGNNPGCKHLHHRQHRGKSHARKHRQSHYEMLELEQRQQRMGKHWRQWMSHLQSPDYANDDPLPDGRRSSPANADLTYDHFELEDYQRYANIDLASPRSGRHRGRHLPLNNMNLMLPLSSADGSGKYLRSLPDSVSFQNDRLYATQPQRHWPVKREAIVEGDVILGGLMMVHSREDSITCGPIMPQGGIQALEAMLFTIDRINREQLLPNITLGAHILDDCDKDSYGLEMAVDFIKGSISNIDDAEYHCNKTQVRKVISGVVGAASSVTSIQVANLLRLFRIPQVSYFSTSPELSNKQRFEYFSRTIPSDHYQVKAMVEIVKRMGWSYVSIIYEESNYGIKAFEELEELLARHNICIAIKEKLVKDSGVAEDIAYDNIVQKLLTKPRARGAIIFGSDQEVRQVMRAVRRANATGSFSWIGSDGWSARNLVSDDYEPEVEGTLSVQPQANPVRGFEEYFLSLTVENNQRNPWFVEFWEDHFQCRYPGSTSTPYNNYTKQCTTKERLSRQNTDFEDQLQFVSDAVMAFAYALRDMHRDLCGGGPSLCEAMKPTKGADLLKYLRKVEFEGLSGDEFRFDGNGDGPARYNIIHFKQSQAGQYHWVKVGEYTEGELRLNMTEVKFKRLSPKPPESVCSLPCLVGQAKKYVEGESCCWHCFNCTTYQIRHPDDETHCKLCKLGTLPDAHKQYCRPIPEIYLRPESAWAIGAMAFSATGILVTLFVMGVFVRHNDTPIVRASGRELSYILLAGIFMCYGVTFALVLKPTNIVCAIQRFGVGFCFTVVYAALLTKTNRIARIFKAGKQSAKRPSFISPKSQLVICACLVSVQILINGVWMVIAPSHAMHHYPTREDNLLVCDSYIDASYMIAFSYPIFLIVICTVYAVLTRKIPEAFNESKHIGFTMYTTCVIWLAFVPLYFGTANHVPLRITSMSVTISLSASVTIACLFSPKLYIILIRPERNVRQSMMPPRYGNMHRTAGTGPSSMMAAAVVTAATCAQEEKIQKHITPTNTENSLKTKKLCEMATQTISSIITSLDINAYNQIPYADQYVPNNATTATTTPTDKGSGNGNSNSNSNTNGSSNSNSNSNGDGDVATEQVVANNNKINQRQHGQPAVAFAITSTNNHISGPAATITTTAATGETTTEALVATITTPLATVDGSETMSVAPNNGHGNNGSQRPPVLQTNLXLNAQQLQQQLLKEQQRQQAELQTQHPQQQHGTQSSSSDTASTGSGSAAKKRAAIPV
Protein: Calponin-homology (CH) domain-containing protein (O01542)
Organism: Caenorhabditis elegans
Interaction partners:
- Actin
- Protein unc-87
- Calmodulin-like protein
- Calmodulin
- Alpha-actinin, sarcomeric
- EF-hand domain-containing protein
- Calmodulin-like protein
- Calponin-homology
- EF-hand domain-containing protein
- EF-hand domain-containing protein
Sequence:
MANRTTAGGIGFAVRQKQDSKFIDKEATLLLEWIKKLSGENISTSGERDNFHNLLKDGTLLCKAANGIEAGSIKKVQKPISTFACMENINAFVEFAKKQGVPNEETFQSVELVEGRDLFSVCVTLLSLGRVLQKAGKTNPFA