wanglab/gogpt-training-data huggingface dataset:
Protein: Class II major histocompatibility complex transactivator (A0A0B4J1S1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRCLAPRPAGSYLSEPQGSSQCATMELGPLEGGYLELLNSDADPLCLYHFYDQMDLAGEEEIELYSEPDTDTINCDQFSRLLCDMEGDEETREAYANIAELDQYVFQDSQLEGLSKDIFKHIGPDEVIGESMEMPAEVGQKSQKRPFPEELPADLKHWKPAEPPTVVTGSLLVGPVSDCSTLPCLPLPALFNQEPASGQMRLEKTDQIPMPFSSSSLSCLNLPEGPIQFVPTISTLPHGLWQISEAGTGVSSIFIYHGEVPQASQVPPPSGFTVHGLPTSPDRPGSTSPFAPSATDLPSMPEPALTSRANMTEHKTSPTQCPAAGEVSNKLPKWPEPVEQFYRSLQDTYGAEPAGPDGILVEVDLVQARLERSSSKSLERELATPDWAERQLAQGGLAEVLLAAKEHRRPRETRVIAVLGKAGQGKSYWAGAVSRAWACGRLPQYDFVFSVPCHCLNRPGDAYGLQDLLFSLGPQPLVAADEVFSHILKRPDRVLLILDGFEELEAQDGFLHSTCGPAPAEPCSLRGLLAGLFQKKLLRGCTLLLTARPRGRLVQSLSKADALFELSGFSMEQAQAYVMRYFESSGMTEHQDRALTLLRDRPLLLSHSHSPTLCRAVCQLSEALLELGEDAKLPSTLTGLYVGLLGRAALDSPPGALAELAKLAWELGRRHQSTLQEDQFPSADVRTWAMAKGLVQHPPRAAESELAFPSFLLQCFLGALWLALSGEIKDKELPQYLALTPRKKRPYDNWLEGVPRFLAGLIFQPPARCLGALLGPSAAASVDRKQKVLARYLKRLQPGTLRARQLLELLHCAHEAEEAGIWQHVVQELPGRLSFLGTRLTPPDAHVLGKALEAAGQDFSLDLRSTGICPSGLGSLVGLSCVTRFRAALSDTVALWESLQQHGETKLLQAAEEKFTIEPFKAKSLKDVEDLGKLVQTQRTRSSSEDTAGELPAVRDLKKLEFALGPVSGPQAFPKLVRILTAFSSLQHLDLDALSENKIGDEGVSQLSATFPQLKSLETLNLSQNNITDLGAYKLAEALPSLAASLLRLSLYNNCICDVGAESLARVLPDMVSLRVMDVQYNKFTAAGAQQLAASLRRCPHVETLAMWTPTIPFSVQEHLQQQDSRISLR
Protein: Alpha-methylacyl-CoA racemase (EC 5.1.99.4) (2-methylacyl-CoA racemase) (O09174)
Organism: Mus musculus (Mouse)
Function: Catalyzes the interconversion of (R)- and (S)-stereoisomers of alpha-methyl-branched-chain fatty acyl-CoA esters (By similarity). Acts only on coenzyme A thioesters, not on free fatty acids, and accepts as substrates a wide range of alpha-methylacyl-CoAs, including pristanoyl-CoA, trihydroxycoprostanoyl-CoA (an intermediate in bile acid synthesis), and arylpropionic acids like the anti-inflammatory drug ibuprofen (2-(4-isobutylphenyl)propionic acid) but neither 3-methyl-branched nor linear-chain acyl-CoAs (By similarity).
Subcellular location: Peroxisome {ECO:0000269|PubMed:10770938}. Mitochondrion {ECO:0000269|PubMed:10770938}.
Interaction partners:
- Peroxisomal acyl-coenzyme A oxidase 2
- Long-chain fatty acid transport protein 5
- Sterol carrier protein 2
- Peroxisomal multifunctional enzyme type 2
- Phytanoyl-CoA dioxygenase, peroxisomal
Sequence:
MVLRGVRVVELAGLAPGPFCGMVLADFGAEVVRVNRLGSTGENFLARGKRSLALDLKRSQGVTVLRRMCARADVLLEPFRCGVMEKLQLGPETLLQDNPKLIYARLSGFGQSGIFSKVAGHDINYLALSGVLSKIGRSGENPYPPLNLLADFGGGGLMCTLGIVLALFERTRSGRGQVIDSSMVEGTAYLSSFLWKTQPMGLWKQPRGQNILDGGAPFYTTYKTADGEFMAVGAIEPQFYALLLKGLGLESEELPSQMSSADWPEMKKKFADVFAKKTKAEWCQIFDGTDACVTPVLTFEEALHHQHNRERASFITDGEQLPSPRPAPLLSRTPAVPSAKRDPSVGEHTVEVLREYGFSQEEILQLHSDRIVESDKLKANL
Protein: Heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) (PEN repeat clone P9) (hnRNP core protein A1-A) (P07909)
Organism: Drosophila melanogaster (Fruit fly)
Function: This protein is a component of ribonucleosomes.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Heterogeneous nuclear ribonucleoprotein K, isoform C
- Heterogeneous nuclear ribonucleoprotein 87F
- LD40489p
- Transportin-1
- LD32469p
- Uncharacterized protein, isoform C
- TAR DNA-binding protein 43
- Purine-rich binding protein-alpha, isoform B
- Importin N-terminal domain-containing protein
- Hephaestus, isoform Y
Sequence:
MVNSNQNQNGNSNGHDDDFPQDSITEPEHMRKLFIGGLDYRTTDENLKAHFEKWGNIVDVVVMKDPRTKRSRGFGFITYSHSSMIDEAQKSRPHKIDGRVVEPKRAVPRQDIDSPNAGATVKKLFVGALKDDHDEQSIRDYFQHFGNIVDINIVIDKETGKKRGFAFVEFDDYDPVDKVVLQKQHQLNGKMVDVKKALPKQNDQQGGGGGRGGPGGRAGGNRGNMGGGNYGNQNGGGNWNNGGNNWGNNRGGNDNWGNNSFGGGGGGGGGYGGGNNSWGNNNPWDNGNGGGNFGGGGNNWNNGGNDFGGYQQNYGGGPQRGGGNFNNNRMQPYQGGGGFKAGGGNQGNYGGNNQGFNNGGNNRRY
Protein: HECT-type E3 ubiquitin transferase (EC 2.3.2.26) (J3QQM4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSNPGGRRNGPVKLRLTGLPDPFAKVVVDGSGQCHSTDTVKNTLDPKWNQHYDLYIGKSDSVTISVWNHKKIHKKQGAGFLGCVRLLSNAINRLKDTGYQRLDLCKLGPNDNDTVRGQIVVSLQSRDRIGTGGQVVDCSRLFDNDLPDGWEERRTASGRIQYLNHITRTTQWERPTRPASEYSSPGRPLSCFVDENTPISGTNGATCGQSSDPRLAERRVRSQRHRNYMSRTHLHTPPDLPEGYEQRTTQQGQVYFLHTQTGVSTWHDPRVPRDLSNINCEELGPLPPGWEIRNTATGRVYFVDHNNRTTQFTDPRLSANLHLVLNRQNQLKDQQQQQVVSLCPDDTECLTVPRYKRDLVQKLKILRQELSQQQPQAGHCRIEVSREEIFEESYRQVMKMRPKDLWKRLMIKFRGEEGLDYGGVAREWLYLLSHEMLNPYYGLFQYSRDDIYTLQINPDSAVNPEHLSYFHFVGRIMGMAVFHGHYIDGGFTLPFYKQLLGKSITLDDMELVDPDLHNSLVWILENDITGVLDHTFCVEHNAYGEIIQHELKPNGKSIPVN
Protein: Calcium-transporting ATPase (EC 7.2.2.10) (A2QQN0)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}. Membrane {ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361146}.
Interaction partners:
Sequence:
MSDSRSDGHDARQSGTTPLRRERAPTITIDTSAVTSPTDHQEPPQQILPTPSHPSLQVSTENVDAHDMSALLSSGGVSPSSVRSFASSENRDYESRPTSPHNISSPASKMTENMSNSNYLAVPGTRSRGNSLESEDSNNSSTSSYGGDTYVPTASHGSRTDLTQNTIISDEDALKPDPGREAEFEVEDNKFAFAPGHLNKLLNPKSLGAFHALGGLRGIEKGLRTDTRSGLSLDEGDLDGTVSFEDATNTQTSESLPKTASSTPPSPPRTDTGSSKHVENAFGDRSRVYGRNKLPERKAKSFLELAWIAYNDKVLILLTIAAIISLALGIYQSVTATGKEARVQWVEGVAIIVAILIVVVVGAANDWQKERQFVKLNKKKDDRLVKVVRSGKTAEISIHDILVGDVMHLEPGDLIPVDGIFITGHNVKCDESSATGESDVLRKTPAHDVYRAIEQHENISKQDPFIVSGAKVSEGVGTFLVTAVGVNSTYGKTMMSLQDEGQTTPLQSKLNVLAEYIAKLGLASGLLLFVVLFIKFLAQLKDMGGASEKGQAFLQIFIVAVTVIVVAVPEGLPLAVTLALAFATTRMLKDNNLVRLLRACETMGNATTICSDKTGTLTENKMTAVAATLGKNLRFGDKSTETSSRPDGDRGRDPATTLSPSEFASSLSAPAKDLLIKSIVLNSTAFEGEQDGVMTFIGSKTETALLGFARTYLGLGSLSEARDNANLAQMVPFDSGRKCMAVVVKMENGKYRMLVKGASEILVARSTRIVHNATQDLAEGPMSDQDRSNLDNLINRYASRSLRTIGLVYRDFDQWPPRGAPTQEEDRSLAVFDAVFKDMILLGVFGIQDPLRPGVTESVHQCQRAGVFVRMVTGDNIMTAKAIAQECGIFTPGGIAIEGPKFRQLSSRQMTQIIPRLQVLARSSPDDKKILVNQLKKLGETVAVTGDGTNDAQALKTADVGFSMGISGTEVAKEASDIILMDDNFTSIIKAMAWGRTVNDAVKKFLQFQLTVNVTAVVLTFVSAVASGDEESVLTAVQLLWVNLIMDTFAALALATDPPSPHVLDRRPDPKSAPLINLTMWKMIIGQSIYQLVVTLVLNFAGKSIFHYKTADDLDRLETMVFNTFVWMQIFNQWNCRRLDNNFNIFEGMWRNFWFMGIQLIIIGGQILIIFVGGQAFSVKRLDGAQWGVSLVLGVISLPVGVIIRLIPDEFISRLIPRFWQRKKGPELLVSDEDRRFEWNPALEEIRDQLKFLKTVRGGRLRHLKHKLQHPEELLPRSRSGSRSRENSIPGTPVGEHSDSTPTQPPTPDSRSRRRTRSRSNSAFGPAAAMAGVVAGSIAGWSPIERAPGDGEAFKVQTDSPHGGLDKQKGIEIHPDTAADDRILGDYQTTSKTPPSQNPGLLPFFEYAPPERAPSHRSQRSTSRLSRSSQSQA
Protein: D-galactonate dehydratase family member SBI_01856 (EC 4.2.1.-) (D-gluconate dehydratase) (EC 4.2.1.39) (D7BPX0)
Organism: Streptomyces bingchenggensis (strain BCW-1)
Function: Has low D-gluconate dehydratase activity (in vitro), suggesting that it has no significant role in D-gluconate degradation in vivo. Has no detectable activity with a panel of 70 other acid sugars (in vitro).
Interaction partners:
- Mannitol-1-phosphate 5-dehydrogenase
- Mannitol-1-phosphate 5-dehydrogenase
- Mandelate racemase/muconate lactonizing protein
- 2-deoxy-D-gluconate 3-dehydrogenase
- Mandelate racemase/muconate lactonizing protein
- PfkB domain protein
- 2-keto-3-deoxy-gluconate kinase
- 2-oxo-3-deoxygluconate kinase
- 6-phosphogluconate dehydrogenase, decarboxylating
- 6-phosphogluconate dehydrogenase, decarboxylating
Sequence:
MSRPAHKTDTIVAVDVLVTSPGRNFVALKITTEQGLVGWGDATLNGRELAVASYLRDHVAPLLIGRDPARIEDTWQYLYRGAYWRRGPVTMTSIGAVDLALWDIKGKATGQPVYQLLGGAVRDRILTYTHASGWEIPQLLDAVDERREQGFLAVRAQSGIPGLATVYGVSSGEAGYEPADRGAAPAVEVWDTDSYLRHAPRVLAAVREHVGPELKLLHDAHHRLTPGQAARLGRALEEVDLYWLEDVTPAENQEVLRHIRHHTTVPLAIGEVFNTVWECQTLITEQLIDFVRTCVTHAGGISHLRRIAALAEVWQVRLGPHGPSDVSPVALAASLHVGLATPNFAIQEYMGYEPVVHEVFRHAWSYADGHLHPGDQPGLGVEVDEALAARFPYEPAYLPIARRRDGSMTDW
Protein: Na(+)-translocating NADH-quinone reductase subunit A (Na(+)-NQR subunit A) (Na(+)-translocating NQR subunit A) (EC 7.2.1.1) (NQR complex subunit A) (NQR-1 subunit A) (Q56586)
Organism: Vibrio alginolyticus
Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Interaction partners:
- Na
- Na
- Na
- Na
- Na
- NADH:ubiquinone reductase
- FAD:protein FMN transferase
- 
- Electron transport complex subunit RsxG
Sequence:
MITIKKGLDLPIAGTPSQVINDGKTIKKVALLGEEYVGMRPTMHVRVGDEVKKAQVLFEDKKNPGVKFTAPAAGKVIEVNRGAKRVLQSVVIEVAGEEQVTFDKFEAAQLSGLDREVIKTQLVDSGLWTALRTRPFSKVPAIESSTKAIFVTAMDTNPLAAKPELIINEQQEAFIAGLDILSALTEGKVYVCKSGTSLPRSSQSNVEEHVFDGPHPAGLAGTHMHFLYPVNAENVAWSINYQDVIAFGKLFLTGELYTDRVVSLAGPVVNNPRLVRTVIGASLDDLTDNELMPGEVRVISGSVLTGTHATGPHAYLGRYHQQVSVLREGREKELFGWAMPGKNKFSVTRSFLGHVFKGQLFNMTTTTNGSDRSMVPIGNYERVMPLDMEPTLLLRDLCAGDTDSAQALGALELDEEDLALCTFVCPGKYEYGTLLRECLDTIEKEG
Protein: Interferon epsilon (IFN-epsilon) (Interferon epsilon-1) (Interferon tau-1) (Q80ZF2)
Organism: Mus musculus (Mouse)
Function: Type I interferon required for maintaining basal levels of IFN-regulated genes, including 2'-5'-oligoadenylate synthetase, IRF7 and ISG15, in the female reproductive tract. Directly mediates protection against viral, including HSV-2, and bacterial, including Chlamydia muridarum, genital infections.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Interferon alpha/beta receptor 1
- Interferon alpha/beta receptor 2
- Interferon lambda receptor 1
- Interleukin-10 receptor subunit beta
- Interferon gamma receptor 1
- Ifngr2 protein
- Interferon kappa
- Interferon lambda-2
- Granulocyte colony-stimulating factor receptor
- Interleukin-6 receptor subunit beta
Sequence:
MVHRQLPETVLLLLVSSTIFSLEPKRIPFQLWMNRESLQLLKPLPSSSVQQCLAHRKNFLLPQQPVSPHQYQEGQVLAVVHEILQQIFTLLQTHGTMGIWEENHIEKVLAALHRQLEYVESLGGLNAAQKSGGSSAQNLRLQIKAYFRRIHDYLENQRYSSCAWIIVQTEIHRCMFFVFRFTTWLSRQDPDP
Protein: Glucose-1-phosphate adenylyltransferase large subunit 1 (EC 2.7.7.27) (ADP-glucose pyrophosphorylase) (ADP-glucose synthase) (AGPase S) (Alpha-D-glucose-1-phosphate adenyl transferase) (Q00081)
Organism: Solanum tuberosum (Potato)
Function: This protein plays a role in synthesis of starch. It catalyzes the synthesis of the activated glycosyl donor, ADP-glucose from Glc-1-P and ATP.
Subcellular location: Plastid, chloroplast. Plastid, amyloplast. Note=Found in the chloroplast in leaf. Found in the plastid in the developing endosperm.
Interaction partners:
- Granule-bound starch synthase 1, chloroplastic/amyloplastic
- UTP--glucose-1-phosphate uridylyltransferase
- Phosphoglucomutase, chloroplastic
- Phosphoglucomutase, cytoplasmic
- Soluble starch synthase 3, chloroplastic/amyloplastic
- Soluble starch synthase 1, chloroplastic/amyloplastic
- Sucrose synthase
- Sucrose-phosphate synthase
- Sucrose synthase
- Sucrose synthase
Sequence:
NKIKPGVAYSVITTENDTQTVFVDMPRLERRRANPKDVAAVILGGGEGTKLFPLTSRTATPAVPVGGCYRLIDIPMSNCINSAINKIFVLTQYNSAPLNRHIARTYFGNGVSFGDGFVEVLAATQTPGEAGKKWFQGTADAVRKFIWVFEDAKNKNIENIVVLSGDHLYRMDYMELVQNHIDRNADITLSCAPAEDSRASDFGLVKIDSRGRVVQFAEKPKGFDLKAMQVDTTLVGLSPQDAKKSPYIASMGVYVFKTDVLLKLLKWSYPTSNDFGSEIIPAAIDDYNVQAYIFKDYWEDIGTIKSFYNASLALTQEFPEFQFYDPKTPFYTSPRFLPPTKIDNCKIKDAIISHGCFLRDCSVEHSIVGERSRLDCGVELKDTFMMGADYYQTESEIASLLAEGKVPIGIGENTKIRKCIIDKNAKIGKNVSIINKDGVQEADRPEEGFYIRSGIIIILEKATIRDGTVI
Protein: Telomerase Cajal body protein 1 (WD repeat-containing protein 79) (WD40 repeat-containing protein antisense to TP53 gene homolog) (Q8VC51)
Organism: Mus musculus (Mouse)
Function: RNA chaperone that plays a key role in telomere maintenance and RNA localization to Cajal bodies. Specifically recognizes and binds the Cajal body box (CAB box) present in both small Cajal body RNAs (scaRNAs) and telomerase RNA template component (TERC). Essential component of the telomerase holoenzyme complex, a ribonucleoprotein complex essential for the replication of chromosome termini that elongates telomeres in most eukaryotes (By similarity). In the telomerase holoenzyme complex, required to stimulate the catalytic activity of the complex. Acts by specifically binding the CAB box of the TERC RNA and controlling the folding of the CR4/CR5 region of the TERC RNA, a critical step for telomerase activity (By similarity). In addition, also controls telomerase holoenzyme complex localization to Cajal body (By similarity). During S phase, required for delivery of TERC to telomeres during S phase and for telomerase activity (By similarity). In addition to its role in telomere maintenance, also required for Cajal body formation, probably by mediating localization of scaRNAs to Cajal bodies (By similarity). Also plays a role in DNA repair: phosphorylated by ATM in response to DNA damage and relocalizes to sites of DNA double-strand breaks to promote the repair of DNA double-strand breaks (By similarity). Acts by recruiting the ubiquitin ligase RNF8 to DNA breaks and promote both homologous recombination (HR) and non-homologous end joining (NHEJ) (By similarity).
Subcellular location: Nucleus, Cajal body {ECO:0000250|UniProtKB:Q9BUR4}. Chromosome, telomere {ECO:0000250|UniProtKB:Q9BUR4}. Chromosome {ECO:0000250|UniProtKB:Q9BUR4}. Note=Released from telomerase RNA template component (TERC) in mitotic cells coincident with delocalization from Cajal bodies. In response to DNA damage, localizes to sites of DNA double-strand breaks following phosphorylation by ATM. {ECO:0000250|UniProtKB:Q9BUR4}.
Interaction partners:
- H/ACA ribonucleoprotein complex subunit 2
- H/ACA ribonucleoprotein complex subunit 3
- H/ACA ribonucleoprotein complex subunit DKC1
- Telomerase reverse transcriptase
- H/ACA ribonucleoprotein complex subunit 1
- Regulator of telomere elongation helicase 1
- TERF1-interacting nuclear factor 2
- Telomerase protein component 1
- CST complex subunit CTC1
- Guanine nucleotide-binding protein-like 3-like protein
Sequence:
MKTSEERLLAPDSLPPDLAPAPVPQGSPAEKNTDFEPVPPPCGGDDQPQLATDPVASLVVSQELQQGDSVPLEVEFNTSSELSPGIEEQDVSEHASLPGEETNLPELESGEATEGVSEERAEVDEGDTFWTYSFSQVPRYLSGSWSEFSTRSENFLKGCKWAPDGSCILTNSADNVLRIYNLPPELYSEQEQVDYAEMVPVLRMVEGDTIYDYCWYSLMSSTQPDTSYVASSSRENPIHIWDAFTGELRASFRAYNHLDELTAAHSLCFSPDGSQLFCGFNRTVRVFSTSRPGRDCEVRATFAKKQGQSGIISCIAFSPSQPLYACGSYGRTIGLYAWDDGSPLALLGGHQGGITHLCFHPDGNLFFSGARKDAELLCWDLRQPGHLLWSLSREVTTNQRIYFDLDPSGQFLVSGNTSGVVSVWDISGALSDDSKLEPVVTFLPQKDCTNGVSLHPTLPLLATASGQRVFPEPTNSGDEGELELELPLLSLCHAHPECQLQLWWCGGGPDPSSPVDDQDEKGQRRTEAVGMS
Protein: Transcription regulatory protein PrtN (Pyocin activator protein) (Q06552)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Activates pyocin genes, probably by binding to the sequences conserved in their 5' non-coding regions (P box).
Interaction partners:
- HTH-type transcriptional regulator PrtR
- Repressor, PtrB
- Protein RecA
- Phage tail protein
- Pyocin S5
Sequence:
MQPSIAPSTPIPRQETVELVYRIFGDVLVPLEQVRERWFRNLNKENFSKALACGRIALPVTTLDDSHKAMQFVALDHLAAYVDQRANQAGSARRAQPGADSIAS
Protein: Ermin (Juxtanodin) (JN) (Q5EBJ4)
Organism: Mus musculus (Mouse)
Function: Plays a role in cytoskeletal rearrangements during the late wrapping and/or compaction phases of myelinogenesis as well as in maintenance and stability of myelin sheath in the adult. May play an important role in late-stage oligodendroglia maturation, myelin/Ranvier node formation during CNS development, and in the maintenance and plasticity of related structures in the mature CNS (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16421295}.
Interaction partners:
- E3 ubiquitin-protein ligase listerin
- Opalin
- Myelin-associated oligodendrocyte basic protein
- Hyaluronan and proteoglycan link protein 2
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein uL5
- Cullin-7
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL2m
Sequence:
MTDTPETLSGTECNGDRPPENGQQPSSQTRQETTDADETQAYYKVEPSLEDLPAKENQEETGNTKGNILPKGPEDEKILNENPEENLFVVHQAIKDLSLQEISAEDMAFREGHPWKKIPPNSSNLEVSRQKERTAQQQLEQRGDASTTEIEWLGFQKSRPVDILHSKCDEEEEEEEEVWNEEINEEDVDECAEEEDEVRVIEFKRKHREGSPLKEESLAREDSPLGSPGSQPGTPDEQPVFGKKGDIARNSYSRYNTISYRKIRKGNTKQRIDEFESMMHL
Protein: FK506-binding protein 15 (FKBP-15) (133 kDa FK506-binding protein) (133 kDa FKBP) (FKBP-133) (WASP- and FKBP-like protein) (WAFL) (Q5T1M5)
Organism: Homo sapiens (Human)
Function: May be involved in the cytoskeletal organization of neuronal growth cones. Seems to be inactive as a PPIase (By similarity). Involved in the transport of early endosomes at the level of transition between microfilament-based and microtubule-based movement.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q6P9Q6}. Cell projection, axon {ECO:0000250|UniProtKB:Q6P9Q6}. Early endosome {ECO:0000269|PubMed:19121306}. Note=Present in axons and neuronal growth cones. {ECO:0000250|UniProtKB:Q6P9Q6}.
Interaction partners:
- WASH complex subunit 2C
- WASH complex subunit 5
- WASH complex subunit 4
- Vacuolar protein sorting-associated protein 29
- Vacuolar protein sorting-associated protein 35
- TBC1 domain family member 5
Sequence:
MFGAGDEDDTDFLSPSGGARLASLFGLDQAAAGHGNEFFQYTAPKQPKKGQGTAATGNQATPKTAPATMSTPTILVATAVHAYRYTNGQYVKQGKFGAAVLGNHTAREYRILLYISQQQPVTVARIHVNFELMVRPNNYSTFYDDQRQNWSIMFESEKAAVEFNKQVCIAKCNSTSSLDAVLSQDLIVADGPAVEVGDSLEVAYTGWLFQNHVLGQVFDSTANKDKLLRLKLGSGKVIKGWEDGMLGMKKGGKRLLIVPPACAVGSEGVIGWTQATDSILVFEVEVRRVKFARDSGSDGHSVSSRDSAAPSPIPGADNLSADPVVSPPTSIPFKSGEPALRTKSNSLSEQLAINTSPDAVKAKLISRMAKMGQPMLPILPPQLDSNDSEIEDVNTLQGGGQPVVTPSVQPSLHPAHPALPQMTSQAPQPSVTGLQAPSAALMQVSSLDSHSAVSGNAQSFQPYAGMQAYAYPQASAVTSQLQPVRPLYPAPLSQPPHFQGSGDMASFLMTEARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMLIPSMSVTMETSMIMSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFELEESYNGRTILGTIMNTIKMVTLQLLNQQEQEKEESSSEEEEEKAEERPRRPSQEQSASASSGQPQAPLNRERPESPMVPSEQVVEEAVPLPPQALTTSQDGHRRKGDSEAEALSEIKDGSLPPELSCIPSHRVLGPPTSIPPEPLGPVSMDSECEESLAASPMAAKPDNPSGKVCVREVAPDGPLQESSTRLSLTSDPEEGDPLALGPESPGEPQPPQLKKDDVTSSTGPHKELSSTEAGSTVAGAALRPSHHSQRSSLSGDEEDELFKGATLKALRPKAQPEEEDEDEVSMKGRPPPTPLFGDDDDDDDIDWLG
Protein: Glycosyltransferase BC10 (EC 2.4.-.-) (Protein BRITTLE CULM 10) (Protein FRAGILE CULM 116) (Q65XS5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Glycosyltransferase required for the regulation of cellulose biosynthesis in the cell wall. Required for the biosynthesis of hexoses (glucose, mannose and galactose) in both cellulosic and non-cellulosic (pectins and hemicelluloses) components of cell walls. Required for the formation of arabinogalactan proteins which contribute to the strengthening of cell walls. Possesses low glycosyltransferase activity.
Subcellular location: Membrane {ECO:0000269|PubMed:18939965}; Single-pass type II membrane protein {ECO:0000269|PubMed:18939965}. Note=Localizes in punctuate patterns. {ECO:0000269|PubMed:18939965}.
Interaction partners:
Sequence:
MKPPRRWMYGRGGGKGKPAGLLLLGVFLCLSVVLLLLLHGSSPSLEGEGRKPEAVEAAGGGGEEEEVAVARAEVEEAPLPPGNARLAFLFIARNRLPLDLVWDAFFRGDKEGRFSIFVHSRPGFVLTRATTRSGFFYNRQVNNSVQVDWGEASMIEAERVLLAHALKDPLNERFVFVSDSCVPLYNFNYTYDYIMSSSTSFVDSFADTKAGRYNPRMDPIIPVENWRKGSQWAVLTRKHAEVVVEDEEVLPEFQKHCRRRPLPEFWRDWDRPIPAEAWKAHNCIPDEHYVQTLLAQHGLEEELTRRSVTHSAWDLSSSKDRERRGWHPVTYKISDATPALVKSIKDIDNIYYETENRKEWCTSNGKPAPCFLFARKFTRAAGLKLLDLSLIAANGASTM
Protein: Thioredoxin like 4A (K7ES07)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSYMLPHLHNGWQVDQAILSEEDRVVVIRFGHDWDPTCMKMDEVLYSIAEKVKNFAVIYLVDITEVPDFNKMYELYDPCTVMFFFRYVILKLLLKLNIVSLEA
Protein: Ste:CG33242 (Q7KV18)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Casein kinase II subunit alpha
- Casein kinase II subunit beta
- Segment polarity protein dishevelled
- Stellate protein CG33246
- Stellate protein CG33243
- Stellate protein CG33239/CG33241
- Stellate protein CG33236/CG33240/CG33244/CG33245
- Stellate protein CG33237
- Stellate protein CG33238
- Stellate protein CG33247
Sequence:
MSSSTTTAAGSIGSSGSRATSSSCRVPTDYVQDTFNQMGLEYFSEILDVILKPVIDSSSGLLYGDEKKWYGMIHARYIRSERGLIAMHRKYMRGDFGSCPNISCDRQNTLPVGLSAVWGKSTVKIHCPRCKSNFHPKSDTQLDGAMFGPSFPDIFFSMLPNLTSPLDDPRT
Protein: Protein BRE4 (Brefeldin A-sensitivity protein 4) (Q07660)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in intracellular vesicle transport.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- SAGA complex subunit SPT3
- SAGA complex subunit NGG1
- SAGA complex/NuA4 acetyltransferase complex subunit TRA1
- SAGA complex subunit SGF29
- SAGA complex subunit SGF11
- SAGA complex/transcription factor TFIID complex subunit TAF9
- SAGA complex/transcription factor TFIID complex subunit TAF12
- SAGA complex/transcription factor TFIID complex subunit TAF10
- SAGA complex subunit ADA2
- tRNA
Sequence:
MKRYERDRSPTPDPDIVKGSYSQTSLRSLHELNYKNPAGISGLSFAGSPQQSVASLSQMRLENLVKDKHWEEVEDFGLEELRDGFFDAAFTKPDSKARSPNSDIDDDNGAARKKLQSGFTKLSEYVWTAIYRPIIHFPRDIRKNGVSIFKFFIAYFIAIVICVIRPSGRWIGHEFRYFLPIAVLIHHPVRNIGVQLEMTISSIIGASFGLGWSALAWYISTATKPTANYQGGILFQSLTMALLFAIWLRSVYRRFFYFTTSFSISIIFTHTVRLASSKFDLKWQIFWDFGISYLFGLLLSLLVCVCVSPHSGNAELMEHYNKCLQTTKTFLMALVDTELIKSKEQIYLAQVKMVKTLNIDLSQGFRDFVNQLTISRFDLQSLKSLRNSLTAMETSLRVLPIAPKIFNDDELKKMYEELEKYRSDSATLSKEASASPQSSGIPTRENTPSAFKPIGPGLLKNEIYINALKASFSKSIFNLILEMIFVLENLSRVLKKYESPNQKNNLDECVKILSHSHSKLKRKIYKLDVCYRDFVNSSFFSQELLNDEESVDIFLFLRYLRNSARQLVTVIHDCQVLGENIHWRIALPSYPLSRALTRLPKQCVLDEGAGNVLHYFEAKRDVDEIFERVYNTYTSRHKYNKGEEEALRLDSQGGDEKSQNRKNHTISIRAIDHNDFNFHTTQNPWRFKLWKLSRILSGDECKWTLKITFCMIFLCLPTWLPESYHWYQEFHCWWAPLTFYLLAHRRYSGNWALVMRRLICGIVGIFWGWAANQSRHFGSPYVVCTFAGLIVVPFSINFLVYRNTKSSFTALMCFTIIALEPYSKPNRHYNLTTAGIWKSTWVTGLALIIGILVSIPINWIVWPFRARTELRDSMSSLLAHLGQSYQTVADRYLYRDADDAPTDLTFAFSHIREVRLTQSLEAIRELLKKARHEPIIISNFNPEKYASLINSCQFLLSKIIEARISGAFFEIWDQDFDIETTRALLSLRRDSVSSVIFVFYILSNCFRSKNKIPRYLPNPIMSRKKLYHFIKKFSEMKDQSHSNLNSGGNSMEKNLFKKIYQQKASSSGQQQLPLPSVANSSEIDSEKMHWTEVHGIAFARAFTDISEALFQVESCAKDILGEENF
Protein: E3 ubiquitin-protein ligase TRIM35 (EC 2.3.2.27) (Hemopoietic lineage switch protein 5) (Q9UPQ4)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that participates in multiple biological processes including cell death, glucose metabolism, and in particular, the innate immune response. Mediates 'Lys-63'-linked polyubiquitination of TRAF3 thereby promoting type I interferon production via RIG-I signaling pathway. Can also catalyze 'Lys-48'-linked polyubiquitination and proteasomal degradation of viral proteins such as influenza virus PB2. Acts as a negative feedback regulator of TLR7- and TLR9-triggered signaling. Mechanistically, promotes the 'Lys-48'-linked ubiquitination of IRF7 and induces its degradation via a proteasome-dependent pathway. Reduces FGFR1-dependent tyrosine phosphorylation of PKM, inhibiting PKM-dependent lactate production, glucose metabolism, and cell growth.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25263439}. Nucleus {ECO:0000250}. Note=Found predominantly in cytoplasm with a granular distribution. Found in punctuate nuclear bodies (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MERSPDVSPGPSRSFKEELLCAVCYDPFRDAVTLRCGHNFCRGCVSRCWEVQVSPTCPVCKDRASPADLRTNHTLNNLVEKLLREEAEGARWTSYRFSRVCRLHRGQLSLFCLEDKELLCCSCQADPRHQGHRVQPVKDTAHDFRAKCRNMEHALREKAKAFWAMRRSYEAIAKHNQVEAAWLEGRIRQEFDKLREFLRVEEQAILDAMAEETRQKQLLADEKMKQLTEETEVLAHEIERLQMEMKEDDVSFLMKHKSRKRRLFCTMEPEPVQPGMLIDVCKYLGSLQYRVWKKMLASVESVPFSFDPNTAAGWLSVSDDLTSVTNHGYRVQVENPERFSSAPCLLGSRVFSQGSHAWEVALGGLQSWRVGVVRVRQDSGAEGHSHSCYHDTRSGFWYVCRTQGVEGDHCVTSDPATSPLVLAIPRRLRVELECEEGELSFYDAERHCHLYTFHARFGEVRPYFYLGGARGAGPPEPLRICPLHISVKEELDG