wanglab/gogpt-training-data huggingface dataset:
Protein: Transport protein particle subunit bet5 (Q9UT70)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May play a role in vesicular transport from endoplasmic reticulum to Golgi.
Subcellular location: Golgi apparatus, cis-Golgi network {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
Interaction partners:
- Transport protein particle subunit trs23
- Transport protein particle subunit bet3
- Transport protein particle subunit trs31
- Transport protein particle subunit trs120
- Uncharacterized protein C13G6.05c
- Uncharacterized protein C15A10.12c
- Transport protein particle 20 kDa subunit
- Uncharacterized protein CC285.14
- GTP-binding protein ypt1
- Transport protein particle subunit trs85-2
Sequence:
MTIYAFYIYSRKCECVFAHRWKPSDRNSMETLVSQLEQNSIEDDMEKLIFGVVFSLRNMVKKITADQDQFMSYTTSKYKLHFYETPTNLRLIFITNPKIDSLTHVLQQIYTTLYVEFVVKHPLYTHVPPSAEEGGINCEIFRITLDRFVRTLSCF
Protein: Mediator of RNA polymerase II transcription subunit 14 (Mediator complex subunit 14) (Mediator of RNA polymerase II complex subunit pmc1) (Q9P7Y4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 22
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 21
- Mediator of RNA polymerase II transcription subunit 19
- Mediator of RNA polymerase II transcription subunit 17
Sequence:
MEPPAIPHITEGFYPLPEIVETFSHHVLQELVSLAEVLPSMSNVEKKKKILDWLLRSRAFTMRLLVLARWVHLSPSVHRCIDVVAFLQGQKFCFQNLVHVLQDIRYQLSFARLRNSDLVTALDILSTGTSLRLANAPTSKLYMLSESPLSTKQILQTLHALNMLIRIRLSLYEIIPTPFQHFTIANGRCTFTVPNEFSVSLTTNSQDPKSTGISFQWIVVDFQFHLPDFSSTPAKYRVFIELHLNEEIAAAFVLQKPILPLIYNILHKFCLYQRLNLLSQQTFQLSRESWLGHLRGVYDEKPPRLRLYYWPQLNVKKEGKPGKIGHYIHIFVNTQPISAFERTLSSKRSSCEYDHFLLLVEWHHDGIVEHVPLDDHMDAQHLLLLITQKHAQLILEQIRKELHPNIFSEHVGGGLKIHVFDNEIIVKVNSVTGRLVLSSSASPLSPPRHLRAAEKNIALNTQPPAQILNRLYFFCIQTQLLEVAQCAELHAVQGYYSFPYLTFSKGKWRKDGDSLWVLAYNVESNSWSVRLLNAAGQTLYTQDVHTTKGTLSIESFSRLSYLLEVQILLFNVQTACQARGMPFEYLPIPPKALIEDDFTTYVQTGCLCIMMPSSNEDMLPVVFVRAHDGQLIFDSRIKGKLPYQSETETEKNCYIDWRTGRITIRVQNFSSFEKTWIGLLKLVALSKTSAFNVDCITLKHVDFTYLDDEKFRATIHDDNTFTLHFFNRHSPFHLISQFLQDTFSDGPSAIQPLRVIMDRTRGVLVAQELGYVVLARSLRQYRIILSKNHGIQVLLNRHGCILQDLSYLSADSRYLEGTQTLTSQWEPCSWLNTVWEGDLGDDELNGQIEAAPEMHLIKMNKTADLTAILKRILAISRKK
Protein: Nucleolin (B8JLQ3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
- Nucleophosmin
- Nucleophosmin 1b.
- rRNA 2'-O-methyltransferase fibrillarin
- Heterogeneous nuclear ribonucleoprotein K
- Nucleophosmin/nucleoplasmin, 2b.
- Adenosine deaminase RNA-specific B2
- Eukaryotic translation initiation factor 3 subunit A
- Pur-alpha
- SECIS-binding protein 2.
- Nucleolar protein 58
Sequence:
MVKLAKAAKKDAPPKKKAPPPPKEVEEESSEEDSDDDEEEEAPPVKAVAKKNAAPVKAVKNGKAAAKQESEDEDDDDEDDESEEEAPPPKKAAKAPAKAAAPAKKAAPAEESSEEDDDDDDDDESEEEAPPPKKAPAKATPAKATPAKKAAPVKKAAPAEESEDDDDDDESEEEEAPPPKKAAAAAKPAAKAPAAKEESDEEEDDDEEEDDSEEEEMDTTPAPKAKKAGMVKAKEESEEEDDDDEEDDDDEEEEETPATPAKRKAETKKEKGTPPAKKAKTDGEGFSLFLGNLNNNKDFDELKSAISKFFSKEGLEIQDVRLGGTKKFGYVDFASEEELQKALELNGKKLLGQPVKLDKARSKENSQENKKERDARTLFVKNLPYSITQDDLREIFDQAVDIRVPMGNTGTSRGIAYIEFKTEAIAEKALEEAQGSDVQGRSIIVDFTGDKSRQGGRGAPSASKVLVVNNLAFSASEDSLQSVFEKAVSIRIPQNNGRPKGYAFVEFENVEDSKEALENCNNTDIEGRSIRLEYSQNDRERGGGGRGNSGPTKTLFVKGLSDDTTDQTLKDSFDGAIAARIATDRDTGSSKGFGFVDFDNEQDCKAAKEAMDDGEIDGNKVTLDYAKPKGEGGRGGFGGGRGGFGGRGGGRGGFGGRGGGGRGGGFRGGRGGRGGGGGFRGGRGGGGRGGFGDRPQGKKIKFDD
Protein: Syntrophin-like 1, isoform E (Q9VNY4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
Interaction partners:
Sequence:
MVESSSLGRTPPAAQQPIPQQHSPSPSGLRCGNMETRVRGAWYRVLVTLETDFLAVSLDESCEAAQPSNDGQSTTLNGTLGNHSGGGGGGAGGGGTGGGGQNGTLPNSASLQGMNIQDTELDGSASNDNGDRDPCLNNNNNAGDGGGMDMCDVPDHVANQKRHVRIIKSDNNGLGISIKGGRENRMPILISKIFRGMAADQAKGLYVGDAILTVNGEELRDATHDEAVRALKRSGRVVDLEVKFLREVTPYFRKASIISEVGWELQRAFLCPLGPGVPTSPPAPKTTPRADTRYIPLQLTHLARNLKYIDPENRCFELHSPDGVHSCILRAADSAEALVWFNALHSAMGTSTQRALAEANRALTNLIGELKHIGWLSKRMSGGGSSGSAGGGAASGGSGTSNSVVAGELPSGRSSSESSDESDKWLPIFVAVTEREFRIYESAPWSVEAWSRPLEIYALATTRLAGAGNNSSLNGQQTTVFCVRCGTARGVLVYWLRSETHRDMAAWARSLVQGSHQAVNYQREFSFRCLFQGRQCQLVVHINRGFFLYDCGGFAPTTPTVATAKTQLWQFAFDKLKGSADDGARMLYLDFGEDGEIELDMECCPKPVVFVVHNCLSAKVHNIA
Protein: Ecto-ADP-ribosyltransferase 3 (EC 2.4.2.31) (ADP-ribosyltransferase C2 and C3 toxin-like 3) (ARTC3) (Mono(ADP-ribosyl)transferase 3) (NAD(P)(+)--arginine ADP-ribosyltransferase 3) (Q13508)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Lipoyl amidotransferase LIPT1, mitochondrial
- Uncharacterized protein C17orf47
- Poly
- Potassium voltage-gated channel subfamily E member 3
- Octanoyl-[acyl-carrier-protein]:protein N-octanoyltransferase LIPT2, mitochondrial
Sequence:
MKTGHFEIVTMLLATMILVDIFQVKAEVLDMADNAFDDEYLKCTDRMEIKYVPQLLKEEKASHQQLDTVWENAKAKWAARKTQIFLPMNFKDNHGIALMAYISEAQEQTPFYHLFSEAVKMAGQSREDYIYGFQFKAFHFYLTRALQLLRKPCEASSKTVVYRTSQGTSFTFGGLNQARFGHFTLAYSAKPQAANDQLTVLSIYTCLGVDIENFLDKESERITLIPLNEVFQVSQEGAGNNLILQSINKTCSHYECAFLGGLKTENCIENLEYFQPIYVYNPGEKNQKLEDHSEKNWKLEDHGEKNQKLEDHGVKILEPTQIPGMKIPEPFPLPEDKSQGNINNPTPGPVPVPGPKSHPSASSGKLLLPQFGMVIILISVSAINLFVAL
Protein: Hepatocyte growth factor-regulated tyrosine kinase substrate (Q17796)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Signal transducing adapter molecule 1
- Tumor susceptibility gene 101 protein
- Vacuolar protein sorting-associated protein 28 homolog
- Charged multivesicular body protein 2a
- Vacuolar protein-sorting-associated protein 36
- Charged multivesicular body protein 6
- Vacuolar protein-sorting-associated protein 25
- EHS-1
- Charged multivesicular body protein 3
- VPS37 C-terminal domain-containing protein
Sequence:
MATKFQRVLDQATDSTLVEPNWEGIILCTDMIRSGEVPAKPSLQAIRKRMQHENPHVVNHTLLVLDACVKNCGHKVHAEVATREFMEDFKNLVTENKYDEVKNKSLEMLQCWATAFANKPEYKMVVDTHNLMKLAGFDFPSLKEADAMFMAQVAPEWADGPECYRCRSVFSVFTRKHHCRACGQIFCDKCSSRELALPQFGIEKEVRVCETCYEKKVAEVKERYPAVKKQLDAAHGRKGDSEADKAAKEKLLREKEEEDLALAIAISQSEAEAKEKEKQNNLYSMYNGIKPEVDGYKGAAEPVTAPPPDDSSSDPLARYLNRDYWQQKKEGKVEDWSSRSSALSATAPPPSEPSIAPSICSTLMGPDDNSLNADIAAMSLGGTNGLNGTVSDDAKLQADDTMKWCQSIREQVSVMDNRIRSNLARGRPVFNDSAIQDLFTKLTELHSHVLSRMHTLDEQRGYYESLQDHLANIGEARQAIDEMREEHERKRQERMAEEQRLRQAQMQQTLEMMRMKKHAMLMEQREQALQRFQQQQQEMAMRRHQQQAYYNPQQMGYGAPPPSGPQQPPQQSYYGYQQGPQSQAPPPSSQYQQSHASTQQQQQQYYQHYQANQTVTQPVQQAQQQYQQQYQGYYQQQQPYQQQAGYQNPQQHQNYQNGTTNENGQYQQQQSSEVKQEHQNHGYQQQQAQHPPASVASNGHNGYGNVDQNAHHHQQQQPQIAEQPLISFD
Protein: GM06687p (Q95S76)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSKYHKERKYAKFRYYMEKYYVLPLELKNDIIYCQRSLRDFLKVHALVSEVFDEQADADPVQMRRILDELEEEVYEINAEQQFLLLRLNDSLQEFSVKLKENNIMFLPDIAHEYVSAQVVPLIVDPNYKIMPQSVMARDTEEMLIRKHFLLSQDDDSGMPPLKLSELDENIPLMLAPPVRGLGQQIAAVKPEPEWLQGDEATVSVPPPPPQSKSKLMKGSLDSTPAKRENISRSSPPPLAPITQTVVAELSQVPPSPQAESPPVNFHVVAQSRKNLQQALRRARKTKQQPRLFDDEEDLEITSLQNDRNKNRTSDGKGTPPSLEPTNAAANQAAKKTIPQMSSQGTAKNITAKSKNTCRKSSPTPTSSGQSQPAVSSSGSSDDSSAELQQEQQRRVASAAQWRDEPRESRTQPEEYGQETFLGLFELYSPEVLKKLSQRHSKRKRRTVQNASGVDFHYGQQLNAVDALVMGVRGQKKTKEKSEFLLSPTEKRLQANSKRTYTRKSKSPDEITEKSSAGGGSGTSGTVSSPACQHKDGGASKCRKCRECRECKRRVETEAMYCHLCSGLYHMDCHEFTKNRQLMQLQNSRCPPCLREKDKLEK
Protein: Short coiled-coil domain-containing protein UNC-69 splice variant T07A5.6b (Short coiled-coil protein) (G5EDQ5)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255}. Golgi apparatus, trans-Golgi network {ECO:0000256|ARBA:ARBA00004601}.
Interaction partners:
Sequence:
MSQKTEQDDIPLADDDDTVTIISGGKTPRAAQPLPKEEPPEDPEEKARMITQVLELQNTLDDLSQRVESVKEESLKLRSENQVLGQYIQNLMSSSSVFQSSQPSRPKQDDSVHDDDFGEYEY
Protein: Chromatin structure-remodeling complex protein RSC3 (Remodel the structure of chromatin complex subunit 3) (Q06639)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is required for transcription of ribosomal protein genes and genes involved in the integrity of the cell wall, and also for proper metaphase progression. Together with HTL1, LDB7, NPL6, RSC30 components, defines a fungal-specific module within the RSC complex that plays a role in many cellular functions including the maintenance of cell wall integrity.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:12697820}. Note=Localizes to centromeric and flanking chromatin. Association with these loci is dependent on STH1.
Interaction partners:
- Chromatin structure-remodeling complex protein RSC6
- Chromatin structure-remodeling complex protein RSC8
- Chromatin structure-remodeling complex subunit RSC4
- Chromatin structure-remodeling complex subunit RSC9
- Chromatin structure-remodeling complex protein RSC58
- Nuclear protein STH1/NPS1
- Chromatin structure-remodeling complex subunit RSC2
- Actin-related protein 7
- Chromatin structure-remodeling complex protein RSC30
- Actin-like protein ARP9
Sequence:
MDIRGRKMKKPPACVQCRKRKIGCDRVKPICGNCMKHNKMDCFYPDVPGQYVPSSSSSSNTRQVANGPYLNSYYASRRVSKETAALLQKNPELASLEQIREYNTRLQLLNAQNQLNNRSSAANATLNQQHTQYIPKSVPSLESKPVTSANESSTPLNWVQGPAIFHMLTSPYTQDEIINHEMNFLKGRLLELQEITGKKITGVNLDLKQDSSAQMQSSHSNRNQEEFLTIKKRKLSEDGVTDGDGKPIPESERRPHLNEFKDLDPQFLDTNKVFNVFNSAISEEGRNRLWLLPKNINKSSIFQIQYLIERDPFLFKFFNDLNILIETQFNGPLHDLVASRNSIERNSGISQILKFPSQSITQTLINKYLSTITETNSILPILKPKRLLPIVEQLFPSNTINKPNSKDFETIFQVFSVTNDQLLNLGFITLCLLILFESLNSTVLIPLRDDEHLQLFNVLFNYLPLLKSNLTTLRFEIEKRSMCNIETLRFISLWKYYQFVMDTSSSSSFVIDYDEDMHMACLLSLNHETQNQSHILTWNFIFKNYCWRHLFLGQLPLLMSEPFTNSTPIIDPLLNNDFELIDFEVNLMKYLQSKDQQLSIDKIIQLIKLLKNKNIEVSQGCLTTPSIINNIMDSLIYRNSMLYLNFYLLLQFETLKNYAKFNEILEDFLELSRETLFFVFSNLANIKFAGHEFTFINKSIVVLQTLVLMLLALYQRSFDSSKRTNDANEISEQTDIHSNNDNSKRIKNKNVIHLIINKIAMLLSDYTKNCKKQNKLIENLIIKIKTISKYIKNLEENKVTTSADSNYSINNGFSGISAEQLIKLNHELSKISESLIKTDFYEQRKNSTVSNGVLGAAAPVDSDANSDTFGLTKENFNEVFEAIRS
Protein: Ras-related protein Rab-2 (EC 3.6.5.2) (O18333)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Vesicle {ECO:0000269|PubMed:33822845}. Cytoplasmic vesicle {ECO:0000269|PubMed:33822845}. Cell projection, axon {ECO:0000269|PubMed:33822845}. Presynapse {ECO:0000269|PubMed:33822845}. Presynaptic active zone {ECO:0000269|PubMed:33822845}. Golgi apparatus {ECO:0000269|PubMed:33822845}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:33822845}. Perikaryon {ECO:0000269|PubMed:33822845}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:28063257}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Autolysosome membrane {ECO:0000269|PubMed:28483915}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Autophagosome localization is not dependent on Rab7, Syx17 or Vps39 (PubMed:28063257). Associated with autolysosomes in its active GTP-bound form (PubMed:28483915). {ECO:0000269|PubMed:28063257, ECO:0000269|PubMed:28483915}.
Interaction partners:
- GH05665p
- Vacuolar protein sorting-associated protein 39 homolog
- GH23156p
- Golgi microtubule-associated protein, isoform D
- FI04457p
- non-specific serine/threonine protein kinase
- Grasp65
- GRIP and coiled-coil domain containing 88 kDa
- Vacuolar protein sorting-associated protein 16 homolog
- ADP-ribosylation factor-like protein 8
Sequence:
MSYAYLFKYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGVEFGARMITIDGKQIKLQIWDTAGQEAFRSITRSYYRGAAGALLVYDITRRETFNHLTTWLEDARQHSNSNMVIMLIGNKSDLDSRREVKKEEGEAFAREHGLVFMETSARTAANVEEAFINTAKEIYEKIQEGVFDINNEANGIKIGQQHSPTNPSLPGAGGAAGAANSGCC
Protein: Anaphase spindle elongation protein (P50275)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for anaphase spindle elongation.
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:7559759}.
Interaction partners:
- Kinesin-like protein CIN8
- Kinesin-like protein KIP1
- Cell cycle serine/threonine-protein kinase CDC5/MSD2
- Kinesin-like protein KIP3
- G2/mitotic-specific cyclin-2
- Kinesin-like protein KIP2
- Securin
- Kinesin-like protein KAR3
- Protein BIM1
- Filament protein FIN1
Sequence:
METATSSPLPIKSRRNSENSGSTTVIPHMNPSLATPLTVSTMVNQSNSKEFMKLTPVRIRDFGSPLKNVSTNYHFLDSENGKGNTMDNMYRENFILISKDLEKLLENLNVIYQNIGYSNTEIITKEKIIFTTISNSIKQFFEQADEELKRLSAENGIEQDILNNILERINDPSGIKTIPDLYIRNAILLQESKTVPQSPKKPLSLLSKKAALDTAKKFVLGSFLPRLRDYLKSLITLKHLIQSVKENLPGLTEADNEAIAEFPELSTLTAYLLQIENGKGDIGLSMKFIIDNRKDILKGSAFKTINEESVKHMNEVIKIYEEEYERRFKSVLTKKVSISSICEQLGTPLATLIGEDFEQDLRSYGEEENSTSEIPNFHPVDRERMSKIDITLEKLQAIHKERADKKRLLMEQCQKLWTRLKISQEYIKTFMRNNSSLSTESLGRISKEVMRLEAMKKKLIKKLISDSWDKIQELWRTLQYSEESRSKFIIVFEELRNSATTLQEDELLLETCENELKRLEEKLTLYKPILKLISDFESLQEDQEFLERSSKDSSRLLSRNSHKILLTEEKMRKRITRHFPRVINDLRIKLEEADGLFDQPFLFKGKPLSEAIDIQQQEIEAKYPRCRVRMQRSKKGKCGANKENKVIKNTFKATESSIRVPIGLNLNDANITYKTPSKKTIQGLTKNDLSQENSLARHMQGTTKLSSPNRRATRLLAPTVISRNSKGNIERPTLNRNRSSDLSSSPRINHTHGEHAVKPRQLFPIPLNKVDTKGSHIPQLTKEKALELLKRSTGTTGKENVRSPERKSSLEDYAQKLSSPYKEPEHSIYKLSMSPEGKFQLNIQQKDIESGFDDTSMMEDENDKDFITWKNEQVSKLNGFSFTDI
Protein: Tyrosine-protein kinase (EC 2.7.10.2) (A0A0G2K134)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- B-cell linker protein
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
- Lymphocyte cytosolic protein 2
- Tyrosine-protein kinase Lyn
- phosphatidylinositol-4,5-bisphosphate 3-kinase
- Proto-oncogene vav
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
- Tyrosine-protein phosphatase non-receptor type 6
Sequence:
MAAVILESIFLKRSQQKKKTSPLNFKKRLFLLTVHKLSYYEYDFERGRRGSKKGSIDVEKITCVETVVPEKNPPPERQIPVPRRGEESSEMEQISIIERFPYPFQVVYDEGPLYVFSPTEELRKRWIHQLKNVIRYNSDLVQKYHPCFWIDGQYLCCSQTAKNAMGCQILENRNGSLKPGSSHRKTKKPLPPTPEEDQILKKPLPPEPTAAPISTSELKKVVALYDYMPMNANDLQLRKGEEYFILEESNLPWWRARDKNGQEGYIPSNYVTEAEDSIEMYEWYSKHMTRSQAEQLLKQEGKEGGFIVRDSSKAGKYTVSVFAKSTGEPQGVIRHYVVCSTPQSQYYLAEKHLFSTIPELINYHQHNSAGLISRLKYPVSKQNKNAPSTAGLGYGSWEIDPKDLTFLKELGTGQFGVVKYGKWRGQYDVAIKMIREGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNYLREMRHRFQTQQLLEMCKDVCEAMEYLESKHLHGVYVLDDEYTSSVGSKFPVRWSPPEVLMYSKFSSKSDIWAFGVLMWEIYSLGKIPYERFTNSETAEHIAQGLRLYRPHLASDRVYTIMYSCWHEKADERPSFKILLSNILDVMDEES
Protein: Transaldolase NQM1 (EC 2.2.1.2) (Non-quiescent mutant protein 1) (P53228)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Interaction partners:
- Transketolase 1
- Transketolase 2
- Glucose-6-phosphate isomerase
- Fructose-bisphosphate aldolase
- Triosephosphate isomerase
- 6-phosphogluconate dehydrogenase, decarboxylating 2
- Fructose-1,6-bisphosphatase
- Transaldolase
- Glyceraldehyde-3-phosphate dehydrogenase 1
- Glyceraldehyde-3-phosphate dehydrogenase 2
Sequence:
MSEPSEKKQKVATSSLEQLKKAGTHVVADSGDFEAISKYEPQDSTTNPSLILAASKLEKYARFIDAAVEYGRKHGKTDHEKIENAMDKILVEFGTQILKVVPGRVSTEVDARLSFDKKATVKKALHIIKLYKDAGVPKERVLIKIASTWEGIQAARELEVKHGIHCNMTLLFSFTQAVACAEANVTLISPFVGRIMDFYKALSGKDYTAETDPGVLSVKKIYSYYKRHGYATEVMAASFRNLDELKALAGIDNMTLPLNLLEQLYESTDPIENKLNSESAKEEGVEKVSFINDEPHFRYVLNEDQMATEKLSDGIRKFSADIEALYKLVEEKM
Protein: BTB/POZ domain-containing protein 10 (Glucose metabolism-related protein 1) (Q9BSF8)
Organism: Homo sapiens (Human)
Function: Plays a major role as an activator of AKT family members by inhibiting PPP2CA-mediated dephosphorylation, thereby keeping AKTs activated. Plays a role in preventing motor neuronal death and accelerating the growth of pancreatic beta cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:15556295}. Cytoplasm {ECO:0000250|UniProtKB:Q80X66}. Note=Colocalizes with KCTD20 in filamentous structures. {ECO:0000250|UniProtKB:Q80X66}.
Interaction partners:
- Cullin-3
Sequence:
MAGRPHPYDGNSSDPENWDRKLHSRPRKLYKHSSTSSRIAKGGVDHTKMSLHGASGGHERSRDRRRSSDRSRDSSHERTESQLTPCIRNVTSPTRQHHVEREKDHSSSRPSSPRPQKASPNGSISSAGNSSRNSSQSSSDGSCKTAGEMVFVYENAKEGARNIRTSERVTLIVDNTRFVVDPSIFTAQPNTMLGRMFGSGREHNFTRPNEKGEYEVAEGIGSTVFRAILDYYKTGIIRCPDGISIPELREACDYLCISFEYSTIKCRDLSALMHELSNDGARRQFEFYLEEMILPLMVASAQSGERECHIVVLTDDDVVDWDEEYPPQMGEEYSQIIYSTKLYRFFKYIENRDVAKSVLKERGLKKIRLGIEGYPTYKEKVKKRPGGRPEVIYNYVQRPFIRMSWEKEEGKSRHVDFQCVKSKSITNLAAAAADIPQDQLVVMHPTPQVDELDILPIHPPSGNSDLDPDAQNPML
Protein: Angiopoietin-related protein 4 (Angiopoietin-like protein 4) (Hepatic fibrinogen/angiopoietin-related protein) (HFARP) [Cleaved into: ANGPTL4 N-terminal chain; ANGPTL4 C-terminal chain] (Q6TMA8)
Organism: Rattus norvegicus (Rat)
Function: Mediates inactivation of the lipoprotein lipase LPL, and thereby plays a role in the regulation of triglyceride clearance from the blood serum and in lipid metabolism. May also play a role in regulating glucose homeostasis and insulin sensitivity. Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage (By similarity). Upon heterologous expression, inhibits the adhesion of endothelial cell to the extracellular matrix (ECM), and inhibits the reorganization of the actin cytoskeleton, formation of actin stress fibers and focal adhesions in endothelial cells that have adhered to ANGPTL4-containing ECM (in vitro) (By similarity). Depending on context, may modulate tumor-related angiogenesis (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:14570927}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q9BY76}. Note=The unprocessed form interacts with the extracellular matrix. This may constitute a dynamic reservoir, a regulatory mechanism of the bioavailability of ANGPTL4. {ECO:0000250|UniProtKB:Q9BY76}.
Interaction partners:
- Lipoprotein lipase
- Angiopoietin-like 8
- Glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1
- Angiopoietin-related protein 3
- Claudin-5
- [Pyruvate dehydrogenase
- Perilipin
- Peroxisome proliferator-activated receptor gamma
- Cadherin-5
- Platelet glycoprotein 4
Sequence:
MRCAPTAGAALVLCAATAGLLSAQGRPAQPEPPRFASWDEMNLLAHGLLQLGHGLREHVERTRGQLGALERRMAACGNACQGPKGTDPKDRVPEGQAPETLQSLQTQLKAQNSKIQQLFQKVAQQQRYLSKQNLRIQNLQSQIDLLTPTHLDNGVDKTSRGKRLPKMAQLIGLTPNATRLHRPPRDCQELFQEGERHSGLFQIQPLGSPPFLVNCEMTSDGGWTVIQRRLNGSVDFNQSWEAYKDGFGDPQGEFWLGLEKMHSITGDRGSQLAVQLQDWDGNAKLLQFPIHLGGEDTAYSLQLTEPTANELGATNVSPNGLSLPFSTWDQDHDLRGDLNCAKSLSGGWWFGTCSHSNLNGQYFHSIPRQRQQRKKGIFWKTWKGRYYPLQATTLLIQPMEATAAS
Protein: Thrombopoietin (C-MPL ligand) (ML) (Megakaryocyte colony-stimulating factor) (Megakaryocyte growth and development factor) (MGDF) (P42706)
Organism: Sus scrofa (Pig)
Function: Lineage-specific cytokine affecting the proliferation and maturation of megakaryocytes from their committed progenitor cells. It acts at a late stage of megakaryocyte development. It may be the major physiological regulator of circulating platelets.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P40225}.
Interaction partners:
- Thrombopoietin receptor
- Granulocyte colony-stimulating factor
- Erythropoietin
- Leptin
- Prolactin
- Somatotropin
- Kit ligand
- Erythropoietin receptor
- CD34 molecule
- Granulocyte colony-stimulating factor receptor
Sequence:
SPAPPACDPRLLNKLLRDDHVLHGRL
Protein: Microtubule-associated tyrosine carboxypeptidase 1 (EC 3.4.17.17) (Q810A5)
Organism: Mus musculus (Mouse)
Function: Tyrosine carboxypeptidase that removes the C-terminal tyrosine residue of alpha-tubulin, thereby regulating microtubule dynamics and function. Also able to remove the C-terminal phenylalanine residue of alpha-tubulin TUBA8. Recognizes adjacent tubulin dimers along the same protofilament (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q68EN5}. Note=Associates with microtubules. {ECO:0000250|UniProtKB:Q68EN5}.
Interaction partners:
Sequence:
MVLDSGTQVYEQAPPRPPAGSPSQHHKLKPSNGNGPPLYPWPESLGMPLALAVPSALQQQTMWQTFSKLHLEQSSHMRRSESTYSVNSTGRRGRGKAPIGRGCDPGGTLRPAASLPHIAKIRKDVGSSSSKSPCMLVALRPTNMDQEREKFFQSHYTYNPQFEYQEPMPMSVLEKYQEASAQFMNQAVGIIEAVLEKFGTYENFEAATGGQLLTKCQIWSTVRKYMQKEGCVGEIVVQLSEDLLSQAVMMVENSRPTLAINLTGARQYWLEGMLRHEIGTHYLRGVNNSRQPWHSTEGRLQYGLQPANPTEEGLASLHSVLFRKQPFLWRAALLYYTIHQAAHMSFRQLFQDLAQYVQDEGVRWEYCVRAKRGQTDTSQPGCFSKDQVYLDGILRILRHRHTIDFQLLTSLGKVSYEDVEQLRPYGVLDNTRVPHFMKDLERYRQQLEHIMTTNRLDEAELGRLLPD
Protein: Interleukin 1 receptor associated kinase 1 (H7C1F0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
PGPGEPAAPGAQHFLYEVPPWVMCRFYKVMDALEPADWCQFAALIVRDQTELRLCERSGQRTASVLWPWINRNARVADLVHILTHLQLLRARDIITAWHPPAPLPSPGTTAPRPSSIPAPAEAEAWSPRKLPSSASTFLSPAFPGSQTHSGPELGLVPSPASLWPPPPSPAPSSTKQDPVSKRKTLGKVKYGCKSHGSVLARSENSEILQKVEQHPPPTSGQCLQALLGTCELA
Protein: Non-structural maintenance of chromosome element 3 (Non-SMC element 3) (Q05541)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14690591}. Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Non-structural maintenance of chromosome element 4
- Structural maintenance of chromosomes protein 6
- Non-structural maintenance of chromosomes element 1
- E3 SUMO-protein ligase MMS21
- Structural maintenance of chromosomes protein 5
- DNA repair protein KRE29
- Non-structural maintenance of chromosome element 5
- Structural maintenance of chromosomes protein 3
- SUMO-conjugating enzyme UBC9
Sequence:
MSSIDNDSDVDLTEDLAVAKIVKENPVARKMVRYILSRGESQNSIITRNKLQSVIHEAAREENIAKPSFSKMFMDINAILYNVYGFELQGLPSKNNMNAGGNGSNSNTNKSMPEPLGHRAQKFILLNNVPHSKNFDDFKILQSAHTYEELIVTGEYIGDDIASGTSNTLESKLSTDRDLVYKGVLSVILCIVFFSKNNILHQELIKFLETFGIPSDGSKIAILNITIEDLIKSLEKREYIVRLEEKSDTDGEVISYRIGRRTQAELGLESLEKLVQEIMGLEKEQTKSLHDDIIKSIGDSYSI
Protein: Uncharacterized protein (Q57XG2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGCGGSAPANKNRHVGADPPKPSEHSEHSKPSDPSDPADATRIHKICTLPLHDKDKPVAAAAIRVTDPKCISDILPPEFLEGKKVHNEFCAITLSFDDGKPEDEGLFEKLKELEGTSIELKPTHIVMNEKVAAIGVCNNDEFPCQDAHPHILVATAPDATQEDIDDVTKKGKIKIFCARKLPDLPPDITIPGEFRFMHW