wanglab/gogpt-training-data huggingface dataset:
Protein: Hyccin (Down-regulated by CTNNB1 protein A) (Q9BYI3)
Organism: Homo sapiens (Human)
Function: Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. The complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis. HYCC1 plays a key role in oligodendrocytes formation, a cell type with expanded plasma membrane that requires generation of PtdIns(4)P. Its role in oligodendrocytes formation probably explains its importance in myelination of the central and peripheral nervous system. May also have a role in the beta-catenin/Lef signaling pathway (Probable).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:10910037, ECO:0000269|PubMed:26571211}. Cell membrane {ECO:0000269|PubMed:16951682, ECO:0000269|PubMed:26571211}. Note=Localizes to the cytosol and is recruited to the plasma membrane following interaction with other components of the phosphatidylinositol 4-kinase (PI4K) complex. {ECO:0000269|PubMed:26571211}.
Interaction partners:
- Tetratricopeptide repeat protein 7B
- Phosphatidylinositol 4-kinase alpha
- Gap junction gamma-2 protein
- Tetratricopeptide repeat protein 7A
- Aminoacyl tRNA synthase complex-interacting multifunctional protein 1
- Protein EFR3 homolog A
- Protein EFR3 homolog B
Sequence:
MFTSEKGVVEEWLSEFKTLPETSLPNYATNLKDKSSLVSSLYKVIQEPQSELLEPVCHQLFEFYRSGEEQLLQFTLQFLPELIWCYLAVSASRNVHSSGCIEALLLGVYNLEIVDKQGHTKVLSFTIPSLSKPSVYHEPSSIGSMALTESALSQHGLSKVVYSGPHPQREMLTAQNRFEVLTFLLLCYNAALTYMPSVSLQSLCQICSRICVCGYPRQHVRKYKGISSRIPVSSGFMVQMLTGIYFAFYNGEWDLAQKALDDIIYRAQLELYPEPLLVANAIKASLPHGPMKSNKEGTRCIQVEITPTSSRISRNAVTSMSIRGHRWKRHGNTELTGQEELMEISEVDEGFYSRAASSTSQSGLSNSSHNCSNKPSIGKNHRRSGGSKTGGKEKETTGESCKDHFARKQTQRAQSENLELLSLKRLTLTTSQSLPKPSSHGLAKTAATVFSKSFEQVSGVTVPHNPSSAVGCGAGTDANRFSACSLQEEKLIYVSERTELPMKHQSGQQRPPSISITLSTD
Protein: Homeobox protein Hox-A13 (Homeobox protein Hox-1J) (P31271)
Organism: Homo sapiens (Human)
Function: Sequence-specific, AT-rich binding transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein Hox-A10
- Homeobox protein Hox-A11
Sequence:
MTASVLLHPRWIEPTVMFLYDNGGGLVADELNKNMEGAAAAAAAAAAAAAAGAGGGGFPHPAAAAAGGNFSVAAAAAAAAAAAANQCRNLMAHPAPLAPGAASAYSSAPGEAPPSAAAAAAAAAAAAAAAAAASSSGGPGPAGPAGAEAAKQCSPCSAAAQSSSGPAALPYGYFGSGYYPCARMGPHPNAIKSCAQPASAAAAAAFADKYMDTAGPAAEEFSSRAKEFAFYHQGYAAGPYHHHQPMPGYLDMPVVPGLGGPGESRHEPLGLPMESYQPWALPNGWNGQMYCPKEQAQPPHLWKSTLPDVVSHPSDASSYRRGRKKRVPYTKVQLKELEREYATNKFITKDKRRRISATTNLSERQVTIWFQNRRVKEKKVINKLKTTS
Protein: AP-3 complex subunit mu-2 (Adaptor-related protein complex 3 subunit mu-2) (Clathrin assembly protein assembly protein complex 3 mu-2 medium chain) (Clathrin coat assembly protein AP47 homolog 2) (Clathrin coat-associated protein AP47 homolog 2) (Golgi adaptor AP-1 47 kDa protein homolog 2) (HA1 47 kDa subunit homolog 2) (Mu3B-adaptin) (P47B) (P53677)
Organism: Homo sapiens (Human)
Function: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals.
Subcellular location: Golgi apparatus. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. {ECO:0000250}.
Interaction partners:
- AP-3 complex subunit beta-1
- AP-3 complex subunit delta-1
- AP-3 complex subunit sigma-1
- AP-3 complex subunit sigma-2
- AP-3 complex subunit beta-2
- AP-3 complex subunit mu-1
- AP-2 complex subunit alpha-1
- AP-1 complex subunit sigma-1A
- AP-4 complex subunit epsilon-1
- AP-2 complex subunit sigma
Sequence:
MIHSLFLINSSGDIFLEKHWKSVVSRSVCDYFFEAQERATEAENVPPVIPTPHHYLLSVYRHKIFFVAVIQTEVPPLFVIEFLHRVVDTFQDYFGVCSEPVIKDNVVVVYEVLEEMLDNGFPLATESNILKELIKPPTILRTVVNTITGSTNVGDQLPTGQLSVVPWRRTGVKYTNNEAYFDVIEEIDAIIDKSGSTITAEIQGVIDACVKLTGMPDLTLSFMNPRLLDDVSFHPCVRFKRWESERILSFIPPDGNFRLLSYHVSAQNLVAIPVYVKHNISFRDSSSLGRFEITVGPKQTMGKTIEGVTVTSQMPKGVLNMSLTPSQGTHTFDPVTKMLSWDVGKINPQKLPSLKGTMSLQAGASKPDENPTINLQFKIQQLAISGLKVNRLDMYGEKYKPFKGIKYMTKAGKFQVRT
Protein: Alpha-actinin, sarcomeric (H2L2C8)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MLLLEVISGEPLPKPDRGKMRFHKIANVNKALEYIESKGVKLVSIGAEEIVDGNVKMTLGLIWTIILRFAIQDINVEELSARDGLLLWCQRKTAPYNNVNVQNFHNSWKDGLAFCALIHRHRPDLLDYSQLHKGDPIHNLNLAFDIAEKHLDIPKMLDAEDMANSQPDEKAVMTYVSCYYHYFSGMRKAETAANRICRVLKVNQENEKMMEDYENLASDLLAWINRWMPWLANRSTDDTLQQAQQKLEDYRNYRRREKPPRIEDKGRLETLFNTLQTRLRLSNRPAFLPRDGHLIKDINAAWAGLEDSEKGFEEWLLSEIMRLERLEHLAEKFRRKCALHEEWAHGKEDALRSNDWRSCGLYKIKALRKRHEAFESDLGAHQDRVEQIAAIARELNNLRYPDIGPINARCQAICSQWDRLGQLSSKRRETLEDAERIAERLDSLYLDFAKRAAPFNNWLDGAREDLADLVIVHEMREIEELVNAHDQFKSTLGDADREFSSINQIEHEVEHLVTSHGLDRELLRNPYTDLSASDIRRKWGEVQNSVPRRDSQLQAELKRQQNNERLRTIFAEKANQVGPWLERELEQVLAIGLGGRGRLEDAIQQLRSIQRNVLGYKPNLDELERVHQEMQENFVFENRKSRYSMESLRVGWETLLTSINKTINEFENQVLLRDSKGISEEQIAEFRASFSHFDKERAGLDPEQLRSCLISVGYTIRPGREGDAELHRVLAHVDPNRMGRVPFEAFLDFMTKENSDQDTVEQMIDSFRILASGKTFITADELERELPRDQAAYCMARMAPSREPGAPPRSFDYVTFSRSLYSQ
Protein: Secretoglobin family 3A member 2 (Pneumo secretory protein 1) (PnSP-1) (Uteroglobin-related protein 1) (Q920H1)
Organism: Mus musculus (Mouse)
Function: Secreted cytokine-like protein (By similarity). Binds to the scavenger receptor MARCO (By similarity). Can also bind to pathogens including the Gram-positive bacterium L.monocytogenes, the Gram-negative bacterium P.aeruginosa, and yeast (By similarity). Strongly inhibits phospholipase A2 (PLA2G1B) activity. Seems to have anti-inflammatory effects in respiratory epithelium. Also has anti-fibrotic activity in lung. May play a role in fetal lung development and maturation. Promotes branching morphogenesis during early stages of lung development. In the pituitary, may inhibit production of follicle-stimulating hormone (FSH) and luteinizing hormone (LH).
Subcellular location: Secreted {ECO:0000269|PubMed:11682631}.
Interaction partners:
- Uteroglobin
- Pulmonary surfactant-associated protein A
- Surfactant protein C
- Secretoglobin family 3A member 1
- Pulmonary surfactant-associated protein B
- Forkhead box protein J1
- Pulmonary surfactant-associated protein D
- Advanced glycosylation end product-specific receptor
- BPI fold-containing family A member 1
- Claudin-18
Sequence:
MKLVSIFLLVTIGICGYSATALLINRLPVVDKLPVPLDDIIPSFDPLKMLLKTLGISVEHLVTGLKKCVDELGPEASEAVKKLLEALSHLV
Protein: Nucleoporin alm1 (Abnormal long morphology protein 1) (Sp8) (Q9UTK5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Maintains the proteasome and its anchor cut8 at the nucleus envelope and is required for kinetochore component proteostasis. Proper kinetochore stoichiometry ensures the correct attachment of kinetochores to spindle microtubules during cytokinesis. Required for the localization of spindle assembly checkpoint (SAC) protein mad2 and bub1 to the nucleus envelope during interphase, but not their localization during mitosis.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:28974540}. Nucleus envelope {ECO:0000269|PubMed:28974540}.
Interaction partners:
- Nucleoporin nup211
- Nuclear envelope protein ndc1
- Nucleoporin nup189
- Nucleoporin nup184
- Nucleoporin seh1
- Nucleoporin nsp1
- Nucleoporin nup107
- Poly
- mRNA export factor mex67
- Nucleoporin-like protein amo1
Sequence:
MSSGGLEDDIQLVHEFLDVSFEDIKPLVSVNGFAVFISAIKTKVKDINALKDQLVLQEVNHEHKENVLTKKINFLEQQLQSSNNQAEESRNLISVLRNENESLKTNLENQNKRFDALTTENQSLRRANSELQEQSKIASEQLSIAKDQIEALQNENSHLGEQVQSAHQALSDIEERKKQHMFASSSSRVKEEILVQEKSALVSDLASLQSDHSKVCEKLEVSSRQVQDLEKKLAGLAQQNTELNEKIQLFEQKRSNYSSDGNISKILETDPTSIKELEEEVETQKRLTALWESKSSELQSEVAALQEKLTSQQSLYNNVTEELNNNKQQLLISENSLRELQEKYDSVVSELQVVKENKNTSVSAGVGLFSPLAQKLSAVQNPEFSFTKVYSDNMKLQQKVSSLKLQLDRLTNKFSSFCEQVKQRIPVVKQQRSEIVRNNIYMNFLSESLETSNNNLTKVQAELLSTKMRQEACYLQLTASRTQCSDLSREVICLMAELDHLNETKSRNVPATVQVALDEYAQNPSTASETLVNKELANFSSIKEAVSKTLELREKVRALECDVEIQKQTVQYQISNAVKENSNTLSEQIKNLESELNSSKIKNESLLNERNLLKEMLATSRSSILSHNSSAGNIDDKMKSIDESTRELEKNYEVYRNEMTAIQESLSKRNQDLLSEMEAIRKELENSKYQQQLSTDRLTNANNDVEAFKKEAKELRSINQNLQDIISRQDQRASKFAEELLHVNSLAERLKGELNASKGEKDLRKRTQERLISENDKLLAERERLMSLVSDLQTFLNQQQLSDAARKVKFESEKESLSLSLQKLKESNEKMSNDLHSLQKSLEKSGIEYSSRIKTLMLEKQSLSEDNRKLLDNQQMMEIKLQELNGVIELEKQRFSTLEAKFTQQKNTSYSEREALLESSLSDLQSKHTSLESQYNYSLRNIEQLQAASKLAEEMVERVKTEYDEYRLQTSESLEKNHLKITSLEQRIVILQDEIASSSLRCENITKDSETRVALLLEENKHLNNELSSHRNAEKQHLEKENDYKQQLLLVTEDLRKTREDYEKELLRHADARSTLQKLREDYTKALEQVEDLNKEIALKAGINESQPFPISEKEDPLRQEVYVLKKQNAMLLTQLQSSNLNFAEITSPSPDLDSVMKLGLSDLQNHVKRISKEMEIISCQRQLLFLENKKLKRTVESSNRVIADLQRGITEKDVSSTSESVGERSNYLNMVALLNESNKSLRENLERNEEVITELREKIETLKTDLANFRLNKEQLESQLQTEKAAVKKLENSNEEYKRHNQEILLSLNSSTSTSSDASRLKNELVSKENLIEELNQEIGHLKSELETVKSKSEDLENERAQNQSKIEQLELKNTKLAAAWRTKYEQVVNKSLEKHNQIRQQLSQKTSELEAKVAECHQLNEQLNKPSATPTATTQSEPSTVSLEEFNSTKEELSSTQRKLSEIMDILNTTKEELEKVRQNSNKSEGTSKDTEIPNEEEMERKKVMQQEVLRLRSRIAKELQKNELLRKQNQVLQDQVKALQETVVSSEEAESASVHADTKDLENLKKTEEMLSVTFQVIFNESISDFSTSTADFTTFVQKEWEKRREILQKDVEEQVAQSHQKQLDNIRKELEMRNKLKLSMLEKNLARVRAELEQSKKKDSPAILSLEASKNTDSNKSNSEVPAAQVKEKKLIAKTHSVDTNSPPKRSSSDAGMDVSNDVKKAK
Protein: Structural maintenance of chromosomes protein 5 (Q7KTV9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAGDRALSSKQLAGRIHSVYCKDFVSYSEITFHPKHYLNVLTGPNGSGKSTIVSAIILGLGGEPILLDRSASVADYIQSNKTSATIIVRVYGRTPNTTETFRRIINSNGLSTFSVNDKDTSKKNFLAAVSSFNIQVSNLCQFLPQDRVQDFSKMNPQELLLNTMSSVCDEDLINSFNSLKQMRTEQANVHANREKEKSDLVKKQKRLEHLQMTVSQYKEREEVKQKLQVYSAKKLWVETQAGEAKAAEMKTQVKNAKTQSDKLKNQHDKLLQSQEQIEKEKESLRKALLEKQNIKKSRRTATECDNLNQLVENKIYELETLNKSRPLIVSELERAKESCAAARGKAMEQYSRRRQLEQKLNDEMIPEITAYKLKIERLRNVKMQKIDEIRAKNPNLVVAMNWLAQNKQRYKLNVYDPMILELTVQNHEDAKFLENVVAQRDLFAFACEDKGDMSDLINELCVKQKLGVNVIYCAPSDRLVYSPKTPIDDLRSFGFRSYLVDLVTGPIPLINKLCASYSIHNIPIGTEAVGNYTSSIPKAIRVYFGGSKKFVVTASRYRSDTILTESSIRAKNQLITVDSQQLALVMKQCSEAVKESDSIKNAITQTDNEFERLQAVAKDEQEKRRKLDQKIAHFNSLKTEIETLQKKLEALRNSDSLDCLETNFCNSLHKDLKKIFDADAELCSCLKAIDRLIIEKNMAQTKVSIYMLQHETQIEALKESEEQSKAATRDFQQLLQCLENQISDVNKRKSAIQGLCHGEIPTSSKFPFKKEFRELENIDLPELREAIHDFQARLECMKSVNSEAISSYQGLQNEVKQLEEGIQESVNQAKSIESGMSNLYDKWEPKLNSLVETISTKFSEFMESIEYVGEVVLSKTDKYDFDSYGIQIMVQFRRGLQLQPLDKFIQSGGERAVSIAIYSLSLQHVTHVPFRCVDEINQGMDATNERHIFDLLLKEATKHGSAQYLFVTPKLLRDLNYNEHLCVSIVHNSKTVCHGMQFPMA
Protein: CLAVATA3/ESR (CLE)-related protein 11 [Cleaved into: CLE11p] (Q3ECU1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Extracellular signal peptide that regulates cell fate. Represses root apical meristem maintenance. Regulates the transition of protophloem cells from proliferation to differentiation, thus impinging on postembryonic growth capacity of the root meristem; this signaling pathway requires CRN and CLV2.
Subcellular location: [CLE11p]: Secreted, extracellular space {ECO:0000250|UniProtKB:O49519}.
Interaction partners:
- CLAVATA3/ESR
- Putative F-box protein At1g47915
- CLAVATA3/ESR
- CLAVATA3/ESR
- Putative B3 domain-containing protein At1g05615
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
Sequence:
MTKQPKPCSFLFHISLLSALFVFLLISFAFTTSYKLKSGINSLGHKRILASNFDFTPFLKNKDRTQRQRQSPSLTVKENGFWYNDEERVVPSGPNPLHH
Protein: Candida glabrata strain CBS138 chromosome H complete sequence (Q6FRS0)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome F complete sequence
Sequence:
MRAAVVSAVVLGLFSQVLATPPACLLACVAQVSKQSSQCHTLNQVGCFCENENTAIKNCLDSICPNGNSDAAYTAFKNSCGDVGKAVASVSSSMSSSMSSSASSSMSSSMSSSSSSSSSASSSISSVSSSTSSVVTTGSSSAPKVSESTTSTPSSTASSTFTITSSKPSSVSSTKTSQKPSSSHAISTFSAGANAINAGSGLAVIAAAALLI
Protein: Ethanolamine-phosphate phospho-lyase (EC 4.2.3.2) (Alanine--glyoxylate aminotransferase 2-like 1) (Q7SY54)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalyzes the pyridoxal-phosphate-dependent breakdown of phosphoethanolamine, converting it to ammonia, inorganic phosphate and acetaldehyde.
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Phosphoethanolamine methyltransferase.
- ethanolamine kinase
- Ethanolamine kinase 2.
- Phosphate cytidylyltransferase 2, ethanolamine.
- Ethanolamine kinase
- Ethanolamine kinase
- Probable phosphatase phospho1
- Beta-alanine-activating enzyme
- Alcohol dehydrogenase iron-containing 1.
- R3H domain containing-like precursor
Sequence:
MATETLDKQKTIDLRKKHVGPSCKVFFDHDPIKIVRAKGQYMYNEKDEKYLDCINNVAHVGHCHPDVVSAGAKQMELLNTNSRFLHDSLVLYAQRLQATLPEKLSVCYFVNSGSEANDLALRLAWQYTGHKDIITLDNAYHGHVSSLIDISPYKFHQMAGAEPSQHVHVALSPDTYRGKYREDHPDPATAYAENVKEVIEEAHKKGHEIAAFIAESLQSCGGQVIPPMGYFQKVAQHVRNAGGIFIADEVQVGFGRVGTHFWGFQLQGEDFVPDIVTMGKPIGNGHPMSCVITSREIAESFMSSGMEYFNTFGGNPVSCAIGLAVLNVIEKEDLQGNALHVGGYLTQLLEDLKKRHPLVGDVRGRGLFVGLELVRNQSKRTPATAEAQEVIYRLKEQRILLSADGPHRNVLKFKPPMCFSREDAEFAVEKIDQILTDLEKAMVLQRPEAAILETGHIKRKDASDENGLVHPSNGNSHKHTSTIPLSKKTKRN
Protein: Tricarboxylate transport protein, mitochondrial (Citrate transport protein) (CTP) (Solute carrier family 25 member 1) (Tricarboxylate carrier protein) (P79110)
Organism: Bos taurus (Bovine)
Function: Mitochondrial electroneutral antiporter that exports citrate from the mitochondria into the cytosol in exchange for malate. Also able to mediate the exchange of citrate for isocitrate, phosphoenolpyruvate, cis-aconitate and to a lesser extend cis-aconitate, maleate and succinate. In the cytoplasm citrate is important in the regulation of glycolysis through a feedback mechanism and in the production of acetyl-CoA which is needed for the synthesis of fatty acids, sterols, prostaglandins, dolichol and coenzyme Q (CoQ). Required for proper neuromuscular junction formation (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q8JZU2}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:2549027}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Citrate synthase, mitochondrial
- ATP-citrate synthase
- Ethanolamine-phosphate cytidylyltransferase
- Citrate synthase
- DNA polymerase epsilon subunit 2
- Progranulin
- STING ER exit protein
- Enoyl-CoA hydratase, mitochondrial
Sequence:
MAAARAPRALTSASPGSGKAKLTHPGKAILAGGLAGGIEICITFPTEYVKTQLQLDERSHPPRYRGIGDCVRQTVRSHGLLGLYRGLSSLLYGSIPKAAVRFGTFEFLSNHMRDAQGRLDSTRGLLCGLGAGVPEAVVVVCPMETIKVKFIHDQTSASPKYRGFFHGVREIVREQGLKGTYQGLTATVLKQGSNQGIRFFVMTSLRNWYRGDNPNKPMNPLITGVFGAIAGAASVFGNTPLDVIKTRMQGLEAHKYRNTLDCGLQILRNEGLKAFYKGTVPRLGRVCLDVAIVFIIYDEVVKLLNKVWKAD
Protein: Bone morphogenetic protein 7 (Q9R228)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
TQGPPLASLQDSHFLTDADMVMSFVNLVEHDKEFFHPRYHHREFRFDLSKIPEGEAVTAAEFRIYKDYIRERFDNETFQITVYQVLQEHSGRESDLFLLDSRTIWASEEGWLVFDITATSNHWVVNPRHNLGLQLSVETLDGQSINPKLAGLIGRHGPQNKQPFMVAFFKATEVHLRSIRSTGGKQRSQNRSKTPKNQEALRMASVAENSSSDQRQACKKHEPYVSFRDLGWQDWIIAPEGYAAYYCEGECAFPLNSYMNATNHAIVQTLVHFINPDTVPKPCCAPTQLNAISVLYFDDSSNRIPA
Protein: MARVEL domain-containing protein (Q18550)
Organism: Caenorhabditis elegans
Interaction partners:
- G-protein coupled receptors family 1 profile domain-containing protein
- Nuclear Hormone Receptor family
- Amine oxidase domain-containing protein
- Peptidase_M13_N domain-containing protein
Sequence:
MTERSRQAQSVASAQPIRIPRIAIAPPSATLSGAHYLSPHASTLPRSNDVLTSPTYITDHLPSRRLSEIDSPMYLPNLLSSTADRPLRNYAPISGYSTTPLRIRTDVSALPRFVDTSTDYGNIGRDYSRDYVRERPITSENPRDDFIRLSEYPATSAVIGLQPPRLITPVLDADESKSMNQLVPETTADVDRLALYNNSSLGYQRLCFLLSRYPAIAMTIIATWMLWGRGLGLSSVKSNENVCYIVSFVAGAFILSSQVVLTTAHGNSYKKEKILANLYHFSNTVAILISITVIVFAAISFQDVNKVNHKTDTCTWMSAPLNLGGIPEFYCFTPQERQTFLSILIGASGLVIILYIFSGIYGCVGQSLMKKKRQDEFKQYAEAHDNAAFRF
Protein: VQ motif-containing protein 31 (AtVQ31) (MPK3/6-targeted VQ-motif-containing protein 6) (Q9FNP0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May modulate WRKY transcription factor activities.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9M9F0}.
Interaction partners:
- VQ motif-containing protein 10
- VQ motif-containing protein 25
- VQ motif-containing protein 20
- VQ motif-containing protein 9
- VQ motif-containing protein 1
- VQ motif-containing protein 8, chloroplastic
- VQ motif-containing protein 5
- VQ motif-containing protein 29
- VQ motif-containing protein
- VQ motif-containing protein
Sequence:
MNSKGSQNVATTCKPVTTFVQTDTNTFREIVQRLTGPTENNAAAATPEATVIKTAIQKRPTSKLHERRQCMRPKLEIVKPPLSFKPTGTTPSSKSGNTNLLTSPVGTPSSLFSNLSLIEGEPDSCTTNIEEEEKAIKERRFYLHPSPRSKPGYTEPELLTLFPLTSPNSSGKP
Protein: Cell division protein kinase 5 (A0A0S2Z355)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQKYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLHDVLHSDKKLTLVFEFCDQDLKKYFDSCNGDLDPEIVKNGELKLADFGLARAFGIPVRCYSAEVVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAGRPLFPGNDVDDQLKRIFRLLGTPTEEQWPSMTKLPDYKPYPMYPATTSLVNVVPKLNATGRDLLQNLLKCNPVQRISAEEALQHPYFSDFCPP
Protein: UDP-N-acetylglucosamine diphosphorylase (EC 2.7.7.23) (Q9Y0Z0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Phosphoacetylglucosamine mutase
- chitin synthase
- chitin synthase
- glutamine--fructose-6-phosphate transaminase
- Probable glucosamine 6-phosphate N-acetyltransferase
- Probable galactose-1-phosphate uridylyltransferase
- glutamine--fructose-6-phosphate transaminase
- Major facilitator superfamily transporter 16, isoform B
- RE30121p
- Glucose-6-phosphate isomerase
Sequence:
MGRSNFSSHHQQTHVRRHRNAGGATSKSPNAAKTSPTMTDYLSLHSRLAQVGQEHLLKFWPELTNDERIDLVRDIEELNLDEIKLYFDRATVSMNENGIKLDDRLQPLPEGKLISIARAPLEKLDAYRDEGLLQISNGHVAVLLMAGGQGTRLGFDHPKGMYDVGLQSRKTLFRIQAERILKLEELAQEANGKRGHITWYIMTSEHTVQPTYDYFVANNFFGLKAENVLLFEQGSLPCFEYDGRIILDEKHRVARAPDGNGGIYRAMKRQGILDDMQKRGVLYLHAHSVDNILIKVADPVFIGYCVQEKADCAAKVVEKAAPNEAVGVVAIVDGKYQVVEYSEISAKTAEMRNSDGRLTFSAGNICNHFFSSNFLQKIGSTYEQELKLHVAKKKIPFVDNAGKRLTPDKPNGIKIEKFVFDVFEFAQKFVAMEVPRDEEFSALKNSDAAGKDCPSTARSDLHRLHKKYIEGAGGIVHGEVCEISPFVTYAGENLASHVEGKSFTSPVYLRDSRDPLHGHL
Protein: Ecotin-like protein 2 (Q57ZQ7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Serine peptidase, putative serine peptidase, Clan SC, Family S9D
Sequence:
MTDRPPTLADFKAPYPEPGPDQTCCIILLEEKPDEEENYRVELIPGRVMEDGLATGTVSGVVREEVIHGWGYSYYVVEMEPLVTTRRSIRSFHRPTRFVPVPTKHFIRYNSQLPVVVYLPHNTELRYRVWTPIDMQKVEPTEPEGLLKIEERAG
Protein: Immunoglobulin kappa variable 1-12 (A0A0C4DH73)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MDMRVPAQLLGLLLLWFPGSRCDIQMTQSPSSVSASVGDRVTITCRASQGISSWLAWYQQKPGKAPKLLIYAASSLQSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQANSFP
Protein: Chloride channel protein (Q8IQN2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endosome membrane {ECO:0000256|ARBA:ARBA00004337}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004337}. Membrane {ECO:0000256|RuleBase:RU361221}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361221}.
Interaction partners:
Sequence:
MIDITPRSSPGDVIGGGGGGGSSSGYHRETATESDTERDFGHSGGNGGGNHHNQRTMHQHVPTHSAFGDPMDGALSFYGSSDVQDDIPGIGQYEDFHTIDWQRDIARDRMRHRYIVKKRQDSLWDLIKGSIDAGSGWLCVLLVGIAAGCVAGMVDIGASWMSDLKHGICPPAFWFNREQCCYPAKQSVFEEGNCSTWKTWPEIFGLDRNGTGPYIVAYIWYVLWALLFASLSASLVRMFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKSVGLMLSVSAGLTLGKEGPMVHIASCIGNIFSHVFPKYGRNEAKKREILSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALIAAFVLRSLTPFGNEHSVLFFVEYNKPWIFFELIPFVFLGIMGGVIGTFFIKANLWWCRYRKFSKLGQYPVMEVLFVTLVTAIICYPNPFTRMNMNELIFLLVSKCSPGDVTNPLCDYKRMNITSGNSFIEVTEPGPGVYSSIWLLMLTFILKLALTIFTFGMKVPAGLFIPSLLLGAIMGRIVGIGVEQFAYSYPNIWFFTGECADSNLITPGLYAVVGAAAVLGGVTRMTVSLVVIMFELTGGVRYIVPLMAAAMASKWVGDALGRQGIYDAHIALNGYPFLDSKEEFAHTTLAADVMQPKRNETLNVITQDSMTVDDVENLLKETEHNGYPVVVSRENQYLVGFVLRRDLNLAIGNAKRLIEGISSSSIVLFTSSQPIQNLGPQPLKLKKILDMAPITVTDQTPMETVVDMFRKLGLRQTLVTHNGRLLGVITKKDVLRHVKQMDNEDPNTVLFN
Protein: OTU domain-containing protein 3 (EC 3.4.19.12) (Q5T2D3)
Organism: Homo sapiens (Human)
Function: Deubiquitinating enzyme that hydrolyzes 'Lys-6'- and 'Lys-11'-linked polyubiquitin. Also hydrolyzes heterotypic (mixed and branched) and homotypic chains. Important regulator of energy metabolism. Glucose and fatty acids trigger its nuclear translocation by CBP-dependent acetylation. In the nucleus, deubiquitinates and stabilizes the nuclear receptor PPARD regulating the expression of various genes involved in glucose and lipid metabolism and oxidative phosphorylation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:35675826}. Nucleus {ECO:0000269|PubMed:35675826}. Note=Glucose or fatty acid promote nuclear translocation upon acetylation. {ECO:0000269|PubMed:35675826}.
Interaction partners:
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Small ribosomal subunit protein bS6m
- Large ribosomal subunit protein bL32m
- Large ribosomal subunit protein bL20m
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein uL14
Sequence:
MSRKQAAKSRPGSGSRKAEAERKRDERAARRALAKERRNRPESGGGGGCEEEFVSFANQLQALGLKLREVPGDGNCLFRALGDQLEGHSRNHLKHRQETVDYMIKQREDFEPFVEDDIPFEKHVASLAKPGTFAGNDAIVAFARNHQLNVVIHQLNAPLWQIRGTEKSSVRELHIAYRYGEHYDSVRRINDNSEAPAHLQTDFQMLHQDESNKREKIKTKGMDSEDDLRDEVEDAVQKVCNATGCSDFNLIVQNLEAENYNIESAIIAVLRMNQGKRNNAEENLEPSGRVLKQCGPLWEEGGSGARIFGNQGLNEGRTENNKAQASPSEENKANKNQLAKVTNKQRREQQWMEKKKRQEERHRHKALESRGSHRDNNRSEAEANTQVTLVKTFAALNI
Protein: Expansin-A16 (AtEXPA16) (Alpha-expansin-16) (At-EXP16) (AtEx16) (Ath-ExpAlpha-1.7) (Q9M2S9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Causes loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found (By similarity).
Subcellular location: Secreted, cell wall. Membrane; Peripheral membrane protein.
Interaction partners:
- Pectin lyase-like superfamily protein
Sequence:
MAINPLILLTIFPLFLLLSFTDAGIPRVFSGGSWQTAHATFYGGNDASGTMGGACGYGNLYSQGYGTNTAALSTSLFNSGQSCGACFEIKCVNDPKWCHPGNPSVFVTATNFCPPNLAQPSDNGGWCNPPRSHFDLAMPVFLKIAEYRAGIVPISYRRVACRKSGGIRFTINGHRYFNLVLITNVAGAGDIARTSVKGSKTGWMSLTRNWGQNWQSNAVLVGQSLSFRVTSSDRRTSTSWNIAPSNWQFGQTFVGKNFRV