wanglab/gogpt-training-data huggingface dataset:
Protein: Gamma-crystallin D (Gamma-D-crystallin) (Gamma-crystallin 4) (P07320)
Organism: Homo sapiens (Human)
Function: Crystallins are the dominant structural components of the vertebrate eye lens.
Interaction partners:
- Gap junction alpha-8 protein
- Phakinin
- Gap junction alpha-3 protein
- Alpha-crystallin B chain
- Alpha-crystallin A2
- Pituitary homeobox 3
- CCA tRNA nucleotidyltransferase 1, mitochondrial
- Lens fiber membrane intrinsic protein
- N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase
- Filensin
Sequence:
MGKITLYEDRGFQGRHYECSSDHPNLQPYLSRCNSARVDSGCWMLYEQPNYSGLQYFLRRGDYADHQQWMGLSDSVRSCRLIPHSGSHRIRLYEREDYRGQMIEFTEDCSCLQDRFRFNEIHSLNVLEGSWVLYELSNYRGRQYLLMPGDYRRYQDWGATNARVGSLRRVIDFS
Protein: Inactive glycosyltransferase 25 family member 3 (Cerebral endothelial cell adhesion molecule) (Q5T4B2)
Organism: Homo sapiens (Human)
Function: Probable cell adhesion protein involved in leukocyte transmigration across the blood-brain barrier. Does not express any beta-galactosyltransferase activity in vitro.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}.
Interaction partners:
Sequence:
MRAARAAPLLQLLLLLGPWLEAAGVAESPLPAVVLAILARNAEHSLPHYLGALERLDYPRARMALWCATDHNVDNTTEMLQEWLAAVGDDYAAVVWRPEGEPRFYPDEEGPKHWTKERHQFLMELKQEALTFARNWGADYILFADTDNILTNNQTLRLLMGQGLPVVAPMLDSQTYYSNFWCGITPQGYYRRTAEYFPTKNRQRRGCFRVPMVHSTFLASLRAEGADQLAFYPPHPNYTWPFDDIIVFAYACQAAGVSVHVCNEHRYGYMNVPVKSHQGLEDERVNFIHLILEALVDGPRMQASAHVTRPSKRPSKIGFDEVFVISLARRPDRRERMLASLWEMEISGRVVDAVDGWMLNSSAIRNLGVDLLPGYQDPYSGRTLTKGEVGCFLSHYSIWEEVVARGLARVLVFEDDVRFESNFRGRLERLMEDVEAEKLSWDLIYLGRKQVNPEKETAVEGLPGLVVAGYSYWTLAYALRLAGARKLLASQPLRRMLPVDEFLPIMFDQHPNEQYKAHFWPRDLVAFSAQPLLAAPTHYAGDAEWLSDTETSSPWDDDSGRLISWSGSQKTLRSPRLDLTGSSGHSLQPQPRDEL
Protein: FRAT3 (Paternally expressed 12) (Q9WVA7)
Organism: Mus musculus (Mouse)
Interaction partners:
- Glycogen synthase kinase-3 beta
- Segment polarity protein dishevelled homolog DVL-2
- Segment polarity protein dishevelled homolog DVL-3
- Segment polarity protein dishevelled homolog DVL-1
- GSK-3-binding protein FRAT2
- Proto-oncogene FRAT1
- MAGE-like protein 2
- Necdin
Sequence:
MPCRREEEAGDEAEGEEDDNSFLLLQQSVTLGGSADVDRLIAQIGETLQLDARHDGPASPCAAPGPPPAPPRVLAALPADKAGAPARRLLRRAASAEAGDPAPPGAVRCVLGERGRLRGRAAPYCVAEIAPGASALPQQLGLEVSPGMGKVSIPQPLSGRCRRGWLRNAAASRRQQQRRGSQSETRTSDGDPPRLLQQLLLSGNLIKEAVRRLHSRGLQLQAKLPAHSFLGPLSAPVHEPPLPGSPRAACSDPGDCDGGHSSELGTTFLSLAANNPGGHSTNL
Protein: Sperm-tail PG-rich repeat (Q38DR1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSYLVEELPLSRAKVPGICAGGCTGPGVGPGSYDINVSYQRSCRGMAPFGSTSKRFGAEAAAAIPGVGTYNITPADLQKGCISTVPFNSKVERFAGYGANDFPGPGAYTVDGHPTKRRSRSHPIRFSRQPDTTGHIAPGPGYYDPNCKHRRSKSGTLCFDEYSGRKPLETNKCPGPGHYESAGSFTSIYNRKPTISFTSKTERSQNGGGSGNPGPGAYNLPSVFRSKEQYRAANPETLIAFGTKSARDGPYGPNPYPGPGAYTGEIAPRRPHVHSEEGRCKPFISVSERIKYPARSNIGPGSYDAQIPRKGPKYQLASVPFWSNVARFPTPKPAEERDDLVPHREAERVPRRIHPLRVLNEAVSEFIKPKAHQGTMNFLDDEHYDFIKPKCTSGGYLGSAPRLTSTATRSDYPGPGQYDVCHDSSFGRASSGRSKWGCDGRFKRTVDRFPGPGHYSCDTTFLKKSFNRTINQSDNM
Protein: Replication factor C subunit 4 (Activator 1 subunit 4) (P53016)
Organism: Caenorhabditis elegans
Function: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. This subunit may be involved in the elongation of the multiprimed DNA template (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Probable replication factor C subunit 5
- Replication factor C subunit 2
- Proliferating cell nuclear antigen
- Replication factor C subunit 3
- Replication factor C subunit 1
- Homolog of S. Pombe Rad
- AAA+ ATPase domain-containing protein
- Ctf8
- Sister chromatid cohesion protein DCC1
- SAP domain-containing protein
Sequence:
MEEPMEVDNKRPKVLTWTEKYRPKTLDDIAYQDEVVTMLKGALQGRDLPHLLFYGPPGTGKTSAALAFCRQLFPKNIFHDRVLDLNASDERGIAVVRQKIQSFSKSSLGHSHREDVLKLKIIILDEVDAMTREAQAAMRRVIEDFSKTTRFILICNYVSRLIPPVVSRCAKFRFKSLPAEIQVQRLRTICDAEGTPMSDDELKQVMEYSEGDLRRAVCTLQSLAPILKSGDDNARNCYLRGSSDSLLISNVCKSILTADVPQIIALTKDITKSCTGVAFIRRCFQQLMDEDVINDENIGVMGKLVATCEKRILDGCDLENNLLDFLLTLRETIQ
Protein: Serine protease 27 (EC 3.4.21.-) (Marapsin) (Pancreasin) (Q8BJR6)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Condensin-2 complex subunit G2
Sequence:
MRQPHIAALLLLPLLLRSGTEGARTLRACGHPKMFNRMVGGENALEGEWPWQVSIQRNGIHFCGGSLIAPTWVLTAAHCFSNTSDISIYQVLLGALKLQQPGPHALYVPVKQVKSNPQYQGMASSADVALVELQGPVTFTNYILPVCLPDPSVIFESGMNCWVTGWGSPSEQDRLPNPRVLQKLAVPIIDTPKCNLLYNKDVESDFQLKTIKDDMLCAGFAEGKKDACKGDSGGPLVCLVDQSWVQAGVISWGEGCARRNRPGVYIRVTSHHKWIHQIIPELQFQGRAGTQQQQKDSQGQQRLAGNSAPCLAAHAMVLALGALLLRIV
Protein: Insulin-like growth factor 2 (Insulin-like growth factor II) (Q8JIE4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU000406}.
Interaction partners:
- Cation-independent mannose 6-phosphate receptor
- Insulin-like growth factor-binding protein 2-A
- Tyrosine-protein kinase receptor.
- Tyrosine-protein kinase receptor.
- Insulin-like growth factor-binding protein 3
- Insulin-like growth factor-binding protein 6
- Insulin-like growth factor-binding protein 1
- Insulin-like growth factor-binding protein 6a.
- Insulin-like growth factor-binding protein 1
- Insulin-degrading enzyme
Sequence:
MEDQLKHHSVCHTCSRTDSFVNKVIKMFWSIRMPICILFLTLSAFEVASAETLCGGELVDALQFVCEDRGFYFSRPTSRSNSRRSQNRGIVEECCFSSCNLALLEQYCAKPAKSERDVSATSLQVIPVMPALKQEVPRKHVTVKYSKYDVWQRKAAQRLRRGIPAILRAKKFRRQAERIKAQEQLLHHRPLITLPSKLPPILLPTENYVSHK
Protein: Donuts protein 1 (Q05610)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the pathway that organizes the prospore membrane (PSM) during sporulation.
Subcellular location: Prospore membrane {ECO:0000269|PubMed:10899120}. Note=Towards the end of meiosis I, or early stages of meiosis II, it forms circular structures above the meiotic plaque. As soon as an assembled prospore membrane is visible during meiosis II, it is detected at the leading edge, which cover the ring-shape opening of the PSMs. Probably recruited to the leading edges by ADY3.
Interaction partners:
- Ubiquitin-binding protein CUE5
- 26S proteasome regulatory subunit RPN12
- Accumulates dyads protein 3
- Sporulation-specific protein 21
Sequence:
MGKKNRKGKENNAAKTSFLKVENIKNTNSGLELPSQDYTNVEEKESSPKTDFPLITKEHVNTKTDSNILDYPTIGDLVSSVEKLCVLKELKIAFPEVDDTLIKAILIASQGVLEPAFNSLLYYSSPEENTDFALPMKPISVEDYSKINVSEILQREIFDDIEDEFSGQGINGSMVISKIESELSSLAEHIGNISTPGSNREVAESTRNVAVAEGHNTILSNEDSILKGKEKGKEEEKEKGEEKGVNSLKGAAVKVVAKSLKNNRIPVTVKRNEPSNNLFDVLNCDESEEEEEQDVETNTSNQERKNQGGNTEVPEAQRDSADRLPAKDDGGYKSAFGTDSCGLFAADAKDEKKQVHPSRQELSFT
Protein: GM15173p (Q8MSG0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTVQNLAAIAAMTQPSLSNAAAAAAAATSPGSAQLTNTAALLWSDPNPMASAYMSTAAGLPQFGSASALSTSPLASVALSAAAAAAAGKQIEGPEGCNLFIYHLPQEFTDTDLASTFLPFGNVISAKVFIDKQTSLSKCFGFVSFDNPDSAQVAIKAMNGFQVGTKRLKVQLKKPKDSKPY
Protein: Serpin 28F (Q9VLQ7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- ACP53C14A
- Accessory gland-specific peptide 26Aa
- Accessory gland protein Acp76A
- Serpin 38F, isoform A
- ACP53C14B
- IP20609p
- Accessory gland protein Acp36DE
- Accessory gland protein Acp53Ea
- GH21475p
- Accessory gland protein Acp29AB
Sequence:
MKHLCLLLLATSVSCRFADDFYQLLAKENAANNLISSPLSVEIALSMAYMGARAKTAQEMRNVLKLPDDKKEVAAKYKDLLSKLEGREKVATLSLANRIYVNKKFQLVPSYNQMVKDSFMAEAEAIDIVDPNKASSIVNNWVDNQTRGKIKDLVSSNDMSKMELIVLNAIYFKGQWEYKFNPKLTKKRNFRVSDQKSVPVEMMSLFQSFRAAHDSELGAKIIELPYRNSSLSMLIFLPDQVDGLSELEKKIVGFKPKLSKMDVTLRLPKFKIEFFAQLNKVLVAMGIQDAFEKSADFKDLVENSNVHVKKVIHKAFIEVNEEGAEAAAATALLFVRYSMPMPSSQMVFNADHPFAYVIRDRETIYFQGHFVKPNE
Protein: steroid 11beta-monooxygenase (EC 1.14.15.4) (Cytochrome P450C11) (A1XRK1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004325}.
Interaction partners:
Sequence:
MFSSCAGSVCARPHLCVRASVCVRPLHQSSRSAGAARLFQEIPDTGSNGWMNLLRFWRDGRFSRMHKHMEESFRRLGPIYREHLGSQSSVNIMLPMDTGELFRSEGLHPRRMTLQPWATHRETRRHSKGVFLKNGTEWRADRLLLNREVMVSSSVHRFLPLLDEVAQDFCRSLRRRVQADGFEKAGQHTLTLDPSPDLFRFALEASCHVLYGERIGLFSSCPSDESERFISAVERMLATTPPLLYLPPRLLLRLRASLWTTHATAWDDIFSHAEQRIQRSYQRLQARPSAAPDCSFPGVLGKLMEAGQLSLELIRANITELMAGGVDTTAVPLQFALFELARNPDVQECVRAQVLSSWQQASGDPLKALQGAPLLKGTIKETLRLYPVGITVQRYPVRDIVLQNYHVPAGTLVQVCLYPLGRSAEVFSRPECFDPSRWSADADAGSAGGFRSLAFGFGSRQCVGRRIAENEMQLLLMHILRTFKLTVSSTEELSTKYTLILQPECPPRITFSTLTHQH
Protein: CBL-interacting serine/threonine-protein kinase 1 (EC 2.7.11.1) (SNF1-related kinase 3.16) (SOS2-like protein kinase PKS13) (Q8RWC9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner.
Interaction partners:
- Calcineurin B-like protein 1
- Calcineurin B-like protein 9
- Calcineurin B-like protein 4
- Calcineurin B-like protein 3
- YTH domain-containing protein ECT1
- Calcineurin B-like protein 2
- YTH domain-containing protein ECT2
- Calcineurin B-like protein 10
Sequence:
MVRRQEEEKKAEKGMRLGKYELGRTLGEGNFGKVKFAKDTVSGHSFAVKIIDKSRIADLNFSLQIKREIRTLKMLKHPHIVRLHEVLASKTKINMVMELVTGGELFDRIVSNGKLTETDGRKMFQQLIDGISYCHSKGVFHRDLKLENVLLDAKGHIKITDFGLSALPQHFRDDGLLHTTCGSPNYVAPEVLANRGYDGAASDIWSCGVILYVILTGCLPFDDRNLAVLYQKICKGDPPIPRWLSPGARTMIKRMLDPNPVTRITVVGIKASEWFKLEYIPSIPDDDDEEEVDTDDDAFSIQELGSEEGKGSDSPTIINAFQLIGMSSFLDLSGFFEQENVSERRIRFTSNSSAKDLLEKIETAVTEMGFSVQKKHAKLRVKQEERNQKGQVGLSVTAEVFEIKPSLNVVELRKSYGDSCLYRQLYERLLKDVGTSSPEQEIVT
Protein: Anion exchange protein (Anion transporter ABTS-4a) (Q58QG8)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Nicotinic receptor-associated protein 1
- Innexin-3
- Multidrug resistance protein pgp-3
Sequence:
MSNGSPGRHSNKAFSIGSDDGENENVFVEETSTPPKTPLGTLLTNCTEQSPLILPMPTRPRLEDSPVAEHDHHIVVDVFTVNNDDGTWKQASRFARYEEDCEGFDNHLGRPHVPCIPMGTYDALKMVTAKSILFPKVQYESLDEFVNFLETKIVDPDVPKLGEKIAKLINDRIAEIEKMRPLHQRNSSSTQSLDASNPQTISTVGIFPRSLLSAPNNLGSLAHHPMRRLPTSHSGLRFGSSFLPQQPVVSQLEPVIWDEDNEISMLVAGEIPHVNVCRFIAIRFVETTAMEKIFPNMTNVRHLFFLIGPALENVTYLDLGRALASVVSNPPATTTFDQLKSPDSITKAIERFLAGTVVIAPGRIDNKNLVRSDLIRKLVNMQGEKTETKIVHPKDVDVERNATKKAEEAEDKPFRLFSGVTSDLRNRAKHYFSDYRDGFNISIFTVVFYMFCVTVVPTLTFGAIMGAGTSGLLAVKECLVSQALSGLIWSVLSCQPLLVMSPTGPFLVFEKALFKFTDQNDMDFLEVRFYTGIFLFFISIVGAATNCAHLIHYVTIYTEDIFCALISLIFFSEVVEFIHLQEEHNSIENLKYYIENAANCTVTEVKDCALSRPNTFLLQLIMVVVSIAIFHYLRQVSRSTFFGRTFRNLCKNFGGIFAVIAVSIAYRILFQNVGVAVVDIPVAVGQSRPFDGIFVIPSAPPTASTLTIALISSILLFVLIFVETEIPEQMALREGRKLKKGGGLHWDLIVVGFCTLVSSVLGLPWMCPAAVQSLAHITSLTEYKKSAPGVPSRISHVIEQRVSGMVTYLLLGTFAILGHFLAIPAATIFGVFFYLGVRNLEGSKMILRLKLCFLPSKYRGSHKFLEIAPFYTIQIYTVIQYLIAGAMFAAKSSKIGGLLFPLFIVSNAIFVKHGLSVIFDKELLEALDSEDHDNDDADRDNEENPEDFYQNTRIPV
Protein: Probable ketoamine kinase TTHA1179 (EC 2.7.1.-) (Q5SJ35)
Organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Function: Ketoamine kinase that phosphorylates ketoamines, such as erythruloselysine and ribuloselysine, on the third carbon of the sugar moiety to generate ketoamine 3-phosphate. Has higher activity on free lysine (erythruloselysine and ribuloselysine), than on ribuloselysine and erythruloselysine residues on glycated proteins.
Interaction partners:
Sequence:
MDPLALLRKAGLEAEGPALPLHGGDISRVWRVGRFVVKTAQDPPPGLFRAEARGLQALAERGVRVPRVHWVGEEGLVLAYLEPGPEDWEGLARTLAALHRRREGSYLAEPGFLGTFPLPGREGGEWTAFFYERCVLPLLEATWDRLQGLGPKVEALYQRPLPAEGPAPLHGDLWHGNVYFAREGPALLDPSFFVGERGVDLAMMRLFGGFPRRFWEVYGELYPVPEEVERALPRYQVYYLLAHVHFFGQGYLGALWRAISAS
Protein: Dephosphocoenzyme A carrier, isoform B (Dephosphocoenzyme A carrier, isoform E) (Q8IN53)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MISGAAAGALAKTVIAPLDRTKINFQIRNDVPFSFRASLRYLQNTYANEGVLALWRGNSATMARIVPYAAIQFTAHEQWRRILHVDKDGTNTKGRRFLAGSLAGITSQSLTYPLDLARARMAVTDRYTGYRTLRQVFTKIWVEEGPRTLFRGYWATVLGVIPYAGTSFFTYETLKREYYEVVGNNKPNTLVSLAFGAAAGAAGQTASYPLDIVRRRMQTMRVNTAGGDRYPTILETLVKIYREEGVKNGFYKGLSMNWIKGPIAVGISFSTYDLIKAWLTELANLRRVEK
Protein: Glyceraldehyde-3-phosphate dehydrogenase A (GAPDH-A) (EC 1.2.1.12) (NAD-dependent glyceraldehyde-3-phosphate dehydrogenase) (P0A9B2)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Triosephosphate isomerase
- Phosphoglycerate kinase
- Fructose-bisphosphate aldolase class 2
- Glucose-6-phosphate isomerase
- Enolase
- Malate dehydrogenase
- Transketolase 1
- Glucose-6-phosphate 1-dehydrogenase
- Transaldolase B
- Fructose-bisphosphate aldolase class 1
Sequence:
MTIKVGINGFGRIGRIVFRAAQKRSDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDNTPMFVKGANFDKYAGQDIVSNASCTTNCLAPLAKVINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYSNKVLDLIAHISK
Protein: Erythrocyte membrane protein band 4.1-like 3 (F7FPP7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MTTESGSDSESKPDQEAEPQEAAGPQEQAGAQAAPEPAGGNVEEQPGLEQFPEAAAHSTPVKREVSDKDRDFAAAAAKQLEYQQFEDDKLSQKSSSSKLSRSPLKIVKRPKSMQCKVTLLDGSEYGCDVDKRSRGQVLFDKVCEHLNLLEKDYFGLTYRDAENQKNWLDPAKEIKKQIRSGAWHFSFNVKFYPPDPAQLSEDITRYYLCLQLRDDIVSGRLPCSFVTLALLGSYTVQSELGDYDPDECGNDYISEFRFAPNHTKELEDKVIELHKSHRGMTPAEAEMHFLENAKKLSMYGVDLHHAKDSEGVEIMLGVCASGLLIYRDRLRINRFAWPKVLKISYKRNNFYIKIRPGEFEQFESTIGFKLPNHRAAKRLWKVCVEHHTFFRLLLPEAPPKKFLTLGSKFRYSGRTQAQTRRASALIDRPAPYFERSSSKRYTMSRSLDGASVNENHEIYMKDSMSAAEVGTGQYATTKVISQTNLITTVTPEKKAEEEHVEEEDRRKKAEEATPVAALRHEGKTDSERTDTAADGETSATEELDKTQDELVKHQTNISELKRTFLETSTETALTNEWEKRLSTSPVRLAARQEDAPMIEPLVPEETKQSSGEKLMDGSEILSLLESARKPTEFIGGVSSTTQSWVQKLETKTETIETEVEPTPHPQPLSTEKVLQETVLVEERHVMNVHASGDASHTARDDVDATESAPADRHSGNGKEGSSVTEAAKEQRGEEADKSAPEQEQPATVSQEEDQVSAIHSSEGLEQKSHFESSTVKVESISVGSVSPGGVKLETSTKEVPVVHTETKTITYESSQVDPGADLEPGVLMSAQTITSETTSTTTTTHITKTVKGGISETRIEKRIVITGDADIDHDQALAQAIKEAKEQHPDMSVTKVVVHKETEITPEDGED
Protein: EF-hand domain-containing protein (Q57XP5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKTAKVNSTIKKGKAKKVKTTKSTEKTPLTWTFSFHEVKRQQASLLFIAWDEDDSGRIPRQHLLSILYALFPSANSMGDGKVGERPSALSLREIRDAFLMTVGRPLSEMSYVTLKDVCSVLDSLWASPARRERMAQGCLYSVFTSVADSGHMMTRSALVEACNHIAGAAISEGMAEAILSPHGIAAGLLNEGESKINFSGFCKIMLPLLAV
Protein: Activated RNA polymerase II transcriptional coactivator p15 (Positive cofactor 4) (PC4) (SUB1 homolog) (Single-stranded DNA-binding protein p9) (p14) (P11031)
Organism: Mus musculus (Mouse)
Function: General coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. May be involved in stabilizing the multiprotein transcription complex. Binds single-stranded DNA. Also binds, in vitro, non-specifically to double-stranded DNA (ds DNA).
Subcellular location: Nucleus.
Interaction partners:
- Symplekin
- Translation machinery-associated protein 7
- Proteasome maturation protein
Sequence:
MPKSKELVSSSSSGSDSDSEVEKKLKRKKQAVPEKPVKKQKPGETSRALASSKQSSSSRDDNMFQIGKMRYVSVRDFKGKILIDIREYWMDSEGEMKPGRKGISLNMEQWSQLKEQISDIDDAVRKL
Protein: Trehalose 2-sulfotransferase (EC 2.8.2.37) (O53699)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the sulfuryl group transfer from 3'-phosphoadenosine-5'-phosphosulfate (PAPS) to trehalose, leading to trehalose-2-sulfate (T2S). The sulfation of trehalose is the first step in the biosynthesis of sulfolipid-1 (SL-1), a major cell wall glycolipid and the most abundant sulfated metabolite found in Mycobacterium tuberculosis, that is a potential virulence factor thought to mediate host-pathogen interactions.
Interaction partners:
- Probable sulfatase
- Trehalose-2-sulfate acyltransferase PapA2
- Acyltransferase PapA3-trehalose mycolipenoyltransferase)
- 2'-acyl-2-O-sulfo-trehalose
Sequence:
MSRAVRPYLVLATQRSGSTLLVESLRATGCAGEPQEFFQYLPSTGMAPQPREWFAGVDDDTILQLLDPLDPGTPDTATPVAWREHVRTSGRTPNGVWGGKLMWNQTALLQQRAAQLPDRSGDGLRAAIRDVIGNEPVFVHVHRPDVVSQAVSFWRAVQTQVWRGHPDPKRDSQAVYHAGAIAHIIRNLRDQENGWRAWFAEEGIDPIDIAYPVLWRNLTAIVASVLDAIGQDPKLAPAPMLERQANQRSDEWVDRYRAEAPRLGLPT
Protein: Rho guanine nucleotide exchange factor 10-like protein (GrinchGEF) (Q9HCE6)
Organism: Homo sapiens (Human)
Function: Acts as guanine nucleotide exchange factor (GEF) for RHOA, RHOB and RHOC.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16112081}.
Interaction partners:
- Transforming protein RhoA
Sequence:
MASSNPPPQPAIGDQLVPGVPGPSSEAEDDPGEAFEFDDSDDEEDTSAALGVPSLAPERDTDPPLIHLDSIPVTDPDPAAAPPGTGVPAWVSNGDAADAAFSGARHSSWKRKSSRRIDRFTFPALEEDVIYDDVPCESPDAHQPGAERNLLYEDAHRAGAPRQAEDLGWSSSEFESYSEDSGEEAKPEVEVEPAKHRVSFQPKLSPDLTRLKERYARTKRDILALRVGGRDMQELKHKYDCKMTQLMKAAKSGTKDGLEKTRMAVMRKVSFLHRKDVLGDSEEEDMGLLEVSVSDIKPPAPELGPMPEGLSPQQVVRRHILGSIVQSEGSYVESLKRILQDYRNPLMEMEPKALSARKCQVVFFRVKEILHCHSMFQIALSSRVAEWDSTEKIGDLFVASFSKSMVLDVYSDYVNNFTSAMSIIKKACLTKPAFLEFLKRRQVCSPDRVTLYGLMVKPIQRFPQFILLLQDMLKNTPRGHPDRLSLQLALTELETLAEKLNEQKRLADQVAEIQQLTKSVSDRSSLNKLLTSGQRQLLLCETLTETVYGDRGQLIKSKERRVFLLNDMLVCANINFKPANHRGQLEISSLVPLGPKYVVKWNTALPQVQVVEVGQDGGTYDKDNVLIQHSGAKKASASGQAQNKVYLGPPRLFQELQDLQKDLAVVEQITLLISTLHGTYQNLNMTVAQDWCLALQRLMRVKEEEIHSANKCRLRLLLPGKPDKSGRPISFMVVFITPNPLSKISWVNRLHLAKIGLREENQPGWLCPDEDKKSKAPFWCPILACCIPAFSSRALSLQLGALVHSPVNCPLLGFSAVSTSLPQGYLWVGGGQEGAGGQVEIFSLNRPSPRTVKSFPLAAPVLCMEYIPELEEEAESRDESPTVADPSATVHPTICLGLQDGSILLYSSVDTGTQCLVSCRSPGLQPVLCLRHSPFHLLAGLQDGTLAAYPRTSGGVLWDLESPPVCLTVGPGPVRTLLSLEDAVWASCGPRVTVLEATTLQPQQSFEAHQDEAVSVTHMVKAGSGVWMAFSSGTSIRLFHTETLEHLQEINIATRTTFLLPGQKHLCVTSLLICQGLLWVGTDQGVIVLLPVPRLEGIPKITGKGMVSLNGHCGPVAFLAVATSILAPDILRSDQEEAEGPRAEEDKPDGQAHEPMPDSHVGRELTRKKGILLQYRLRSTAHLPGPLLSMREPAPADGAALEHSEEDGSIYEMADDPDIWVRSRPCARDAHRKEICSVAIISGGQGYRNFGSALGSSGRQAPCGETDSTLLIWQVPLML
Protein: Transmembrane protease serine 9 (EC 3.4.21.-) (Polyserase-I) (Polyserine protease 1) (Polyserase-1) [Cleaved into: Serase-1; Serase-2; Serase-3] (P69525)
Organism: Mus musculus (Mouse)
Function: Serase-1 and serase-2 are serine proteases that hydrolyze the peptides N-t-Boc-Gln-Ala-Arg-AMC and N-t-Boc-Gln-Gly-Arg-AMC. In contrast, N-t-Boc-Ala-Phe-Lys-AMC and N-t-Boc-Ala-Pro-Ala-AMC are not significantly hydrolyzed (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MEPTAPDLQLVPEVTKAVSVSAPDPGPCRTAVIAVVGISMAIVTLGVLSAFFSAQGAHVEHIAELHGIRFTSSLQQENSDFYRLLTHALQTLLHFLLRALQPLSLKQEADILQKGIQARLQEQGLSLAAYGTIVSVELTGRCEGPVTERDLKSGHCPGNVFSCQNGQCVSKENPECDDRVDCSDESDEAQCDCGWQPAWRSAGRIVGGVEAAPGEFPWQVSLRENHEHFCGATIIGARWLVSAAHCFNEFQDPAQWAAQAGSVHLSGSEASAVRTRVLRIAKHPAYDADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPGKKCLISGWGYLKEDFLVKPEVLQKATVELLDQSLCSSLYGHSLTDRMVCAGYLDGKVDSCQGDSGGPLVCEEPSGRFFLAGIVSWGIGCAEARRPGVYTRVTRLRDWILEVTSAADMPVVPTATPAPATPSTPWPTSPESWAPNTFAKPTAAPSPVPLHPSTTAKPQECGARPAMDKPTRIVGGISAVSGEVPWQASLKEGPRHFCGATVVGDRWLLSAAHCFNHTKVEQVQAHLGTVSLLGVGGSPVKLGLRRVALHPRYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNATKPDILQKASVGIIEQKMCGALYNFSLTDRMLCAGFLEGRVDSCQGDSGGPLACEETPGVFYLAGIVSWGIGCAQAKKPGVYARITRLKDWILKAMSSDPSSMARPHTSSTRLIPSEPPKTTAAGLIIPEATTSRLATPRATIRVTTRPLNTTLSARSTTTRGQTAAPSAPGTTIHSHLPDCGLAPPGALTRIVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDIYGDPMQWAAFLGTPFLSSTEGQLERVARIYRHPFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGPARPPDGARCVITGWGSLREGGSMARQLQKAAVRVLSEQTCRRFYPVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPSGQWVLTGVTSWGYGCGRPHFPGVYTRVAAVLGWIGQNIQE
Protein: AMP-binding domain-containing protein (O18693)
Organism: Caenorhabditis elegans
Interaction partners:
- Fatty acid synthase
- Trifunctional enzyme subunit alpha, mitochondrial
- Fatty acid synthase
- carnitine O-palmitoyltransferase
- Choline/carnitine acyltransferase domain-containing protein
- Nsp1_C domain-containing protein
- 3-hydroxyacyl-CoA dehydrogenase
- Bifunctional glyoxylate cycle protein
- Nuclear hormone receptor family member nhr-49
- Delta
Sequence:
MRSILVSRRFAHVLTSTHAAPSTSNIPTTDSHHLTHPSVHRQHTNSYIHGTSNIPLRNETLGQTLRNTTERVPDKEFCVFSKYPIRKTYEEFYHDVRQMAASLYTLGLEKGDRVGVWGPNYYEWVVLQYACAFAGVIQVNVNPHYLHEELRFVMRKTGMKVLFAPKRHKHSNYVHTMLEAMPEMRRGQPGVGHIKSHDIPELRHIVLYGDDVPVHGAWVYSDLIHAAGSAERAKLEDMDRKLRPDEPVNMQFTSGTTGHPKGATLTHFGLNNNAYFAGIRLGWDREDHRICIPNPLYHCFGCAVGVINAVNHGQTVVFPSKSYHVPDIFEAIQNEKCTTMFGTPTMFIDVLKSPLMKQFDISSLRGGVIGGAPCPMALCEKMVKEMRMTDFSVIYGSTETSPLVTMSELHVDPFERIKSVGSVMPHQELAIVDEFGVPVPTGAKGELWSRGYSTMLGYWADHDKTNLAITRDRWYKSGDTATMNEDGTINIVGRTRDMIVKGGENVYPTEIEQFLHKLDYVADAHVVGVPDDRYGENICAWVRLRVEDEGKITAEHIKKACKRGMAHYKVPKYVLIKKESEFPLTISGKVKKFEIQKISKELLGLGTVKSHFTEAVDN
Protein: beta-fructofuranosidase (EC 3.2.1.26) (D5FW81)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Vacuole lumen {ECO:0000256|ARBA:ARBA00004410}.
Interaction partners:
- fructokinase
- fructokinase
- fructokinase
- fructokinase
- fructokinase
- fructokinase
- Phosphotransferase
- Phosphotransferase
- Phosphotransferase
- Phosphotransferase
Sequence:
MEASYDPEQNPPLHAPLLDRSSPRTRRFAAIFACLVSLLLLLALIINQAQQPFEKVQPRGVAEGVSAKSNPSLLNQVPFNWTNAMFSWQRSAYHFQPQKNWMNDPNGPLYHKGWYHLFYQYNPYSAIWGNITWGHAVSRDLIHWLYLPLALVPDHWYDIKGVWTGSATILADGQIIMLYTGETNESVQVQNLAYPANVSDPLLLHWLKYPGNPVMVPPPGVKPDDFRDPTTAWLGPDGTWRLTMGSKFDTTIGISLVYHTTNFRDYELLDGVLHAVPGTGMWECVDFYPVAINGSVALDTSSLGPGIKHVLKASLDNTKVDHYAIGTYDPITDKWTPDNPEEDVGIGLKVDYGRYYASKTFFDQHKQRRVLWGWINETDTETADLKKGWASLQTIPRTVLYDNKTGTNLLQWPVEEVESLRLNSTMFKEVLVEPGSVVPLDIGTTTQLDILAEFEIEPLIPSTTNEIDNCGDGAVDRSTYGPFGLLVIADASLSELTPIYFRPLNASDGSLKTYFCSDETRSSKASDVFKQVYGGKVPVLDDENYNMRVLVDHSIVESFAQGGRTVISSRIYPTEAIYGAARLFLFNNATGVNVKATLKIWELNSAFIRPFPFERDSV
Protein: Transcriptional regulator URE2 (Disulfide reductase) (EC 1.8.4.-) (Glutathione peroxidase) (EC 1.11.1.9) (P23202)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Plays an important role in nitrogen catabolite repression. Down-regulates the expression of many genes involved in nitrogen utilization by inhibiting the GATA transcriptional activators GLN3 and GAT1. Under good nitrogen conditions, binds to the phosphorylated forms of GLN3 and GAT1 and sequesters them in the cytoplasm, preventing transcription of genes expressed upon nitrogen limitation. Is also an atypical glutaredoxin without a catalytical cysteine residue. Has glutathione peroxidase and thiol:disulfide oxidoreductase activities in both native and fibrillar form. Also shows insulin disulfide reductase and dehydroascorbic acid reductase (DHAR) activities.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10604478}.
Interaction partners:
- Nitrogen regulatory protein GLN3
- Eukaryotic peptide chain release factor GTP-binding subunit
- [PIN+] prion protein RNQ1
- Mitochondrial protein import protein MAS5
- Glutathione reductase
- Glutathione hydrolase proenzyme
- Transcriptional regulatory protein GAT1
- Nitrogen regulatory protein DAL80
- Peroxiredoxin PRX1, mitochondrial
- Heat shock protein 104
Sequence:
MMNNNGNQVSNLSNALRQVNIGNRNSNTTTDQSNINFEFSTGVNNNNNNNSSSNNNNVQNNNSGRNGSQNNDNENNIKNTLEQHRQQQQAFSDMSHVEYSRITKFFQEQPLEGYTLFSHRSAPNGFKVAIVLSELGFHYNTIFLDFNLGEHRAPEFVSVNPNARVPALIDHGMDNLSIWESGAILLHLVNKYYKETGNPLLWSDDLADQSQINAWLFFQTSGHAPMIGQALHFRYFHSQKIASAVERYTDEVRRVYGVVEMALAERREALVMELDTENAAAYSAGTTPMSQSRFFDYPVWLVGDKLTIADLAFVPWNNVVDRIGINIKIEFPEVYKWTKHMMRRPAVIKALRGE
Protein: Cilia and flagella associated protein 68 (E9PMC1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000256|ARBA:ARBA00004611}.
Interaction partners:
Sequence:
MVIWVILSLLGELGKPGLLTSLKNMEQPSKDFCDSHKKSSKSSTYSASSYSSSGKRQNLACFLTNPHCGSLVNADGHGEVWTDWNNMSKFFQYGWRCTTNENTYSNRTLMGNWNQERYDLRNIVQPKPLPSQFGHYFETTYDTSYNNKMPLSTHRFKREPHWFPGHQPELDPPRYKCTEKSTYMNSYSKP