wanglab/gogpt-training-data huggingface dataset:
Protein: Small nuclear ribonucleoprotein Sm D3 (Sm-D3) (snRNP core protein D3) (A0A8I6AKJ4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|RuleBase:RU365050}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365050}. Note=SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes. {ECO:0000256|RuleBase:RU365050}.
Interaction partners:
Sequence:
MSIGVPIKVLHEAEGHIVTCETNTGEVYRGKLIEAEDNMNCQMSNITVTYRDGRVAQLEQVYIRGSKIRFLILPDMLKNAPMLKSMKNKNQGSGAGRGKAAILKAQGRRHGVSGRPA
Protein: Killer cell immunoglobulin-like receptor 2DS2 (CD158 antigen-like family member J) (NK receptor 183 ActI) (Natural killer-associated transcript 5) (NKAT-5) (p58 natural killer cell receptor clone CL-49) (p58 NK receptor CL-49) (CD antigen CD158j) (P43631)
Organism: Homo sapiens (Human)
Function: Receptor on natural killer (NK) cells for HLA-C alleles. Does not inhibit the activity of NK cells.
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
Sequence:
MSLMVVSMACVGFFLLQGAWPHEGVHRKPSLLAHPGPLVKSEETVILQCWSDVRFEHFLLHREGKYKDTLHLIGEHHDGVSKANFSIGPMMQDLAGTYRCYGSVTHSPYQLSAPSDPLDIVITGLYEKPSLSAQPGPTVLAGESVTLSCSSRSSYDMYHLSREGEAHERRFSAGPKVNGTFQADFPLGPATHGGTYRCFGSFRDSPYEWSNSSDPLLVSVTGNPSNSWPSPTEPSSKTGNPRHLHVLIGTSVVKIPFTILLFFLLHRWCSNKKNAAVMDQEPAGNRTVNSEDSDEQDHQEVSYA
Protein: Anion exchange protein (M9PCF0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane {ECO:0000256|RuleBase:RU362035}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362035}.
Interaction partners:
Sequence:
MAEKNEYIELPWTMNSSSGDDEAPKDPRTGGEDFTQQFTENDFEVTPPAQRVQFILGEDVDDGTHVSHPLFSEMGMLVKEGDEIEWKETARWIKFEEDVEEGGNRWSKPHVATLSLHSLFELRRLLVNGSVMLDMEAQNLEVMADLVCDHMVSAGTLPPGVKDKVKDALLRRHRHQHEYAKKTRLPIIRSLADMRNHSSSKIEEHSASILGATTPISLTASEPGPPGSNGNSNLSTAAGAMGRFLTVPSGKPSNRTLEDMVKSPSNQSMARPGSGTELSEQQHKGNTHFMRKIPPGAEASNILVGEVDFLERTLSCFIRLSQAVVLGDLTEVPVPTRFVFILLGPPGSQSNFHEIGRAMATLMSDEIFHEVAYRARKRDHLLSGVDEFLDAVTVLPPGEWDPTIRIEPPAAIPSQEVRKRPPELPKEEVDEEEEEARLREENGLSRTGRLFGGLINDIKRKAPWYISDYKDALSMQCVASWIFLYFACLSPIITFGGLLAEATGKHMAAMESLVSGFVCGMGYGFFSGQPLTILGSTGPVLVFESIIYEFCLKMGWDYMTFRFWIGMWVAGICIVLTAIDASALVCYITRFTEENFATLIAFIFIYKAIENVMVIGKNFPVNQGIYDCVCTPPIGSNASVIDYAKYNWDSCESYNGTLVGGDCGTPPTENVFLMSVVLCAGTFLISTVLKEFKNALFFPSIVRQYISDFSVLIAIFAMSFFDYSLGVPTQKLEVPNELKPTLSTRGWLIPPFVEKNPWWSAIIAVFPALLGTILIFMDQQITAVIVNRKENKLKKGCGYHLDLFILSILIAICSMMGLPWFVAATVLSINHVNSLKLESECSAPGEKPQFLGVREQRVTHILIFLTIGVSVLLTPLLGNIPMPVLFGVFLYMGVASLKGLQFFDRILIMFMPAKYQPDYMFLRQVPIKRVHLFTMIQLACLIILWLIKSFSQTSILFPLMLVVMIGIRKALDLVFTRRELKILDDIMPEMTKRAAADDLHKLDAEVGLLARIFPWGKGSRSRVVTKPPGLDDGIVGSGGAVGAGLITCTTSNANEKEFEAQSSLLKK
Protein: Cytosolic coat protein, putative (Q38CZ1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003827}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003827}.
Interaction partners:
- GOLD domain-containing protein
- Cytosolic coat protein, putative
- GOLD domain-containing protein
- GOLD domain-containing protein
- GOLD domain-containing protein
- Coatomer subunit delta
- Coatomer subunit beta'
- GPI inositol-deacylase
- Coatomer subunit gamma
- ER lumen protein-retaining receptor
Sequence:
MERIASGHRMSMLLLGVGLLCLYGSLLVNGFAFDLPANQKRCFSEEVPSGTELRISYAALPGYAQFVDAYVVGPAGKMYMTTVGQDRGSMVEYITKGGEFTLCLLSRVATGVKQSEGMARSVSVDFRLGSGKNDYANLTGKEKLRPIEVELRVLEDAVRSLHTECLYYREKEAEMRNANESVIAKVAFCAAAIITFFIIFSLWEMWHLKRYFRKKRLID
Protein: Ras-related protein Rab-14 (EC 3.6.5.2) (O18336)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Early endosome membrane {ECO:0000256|ARBA:ARBA00004438}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004438}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004438}. Golgi apparatus, trans-Golgi network membrane {ECO:0000256|ARBA:ARBA00004387}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004387}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004387}.
Interaction partners:
Sequence:
MTAAPYNYNYIFKYIIIGDMGVGKSCLLHQFTEKKFMANCPHTIGVEFGTRIIEVDDKKIKLQIWDTAGQERFRAVTRSYYRGAAGALMVYDITRRSTYNHLSSWLTDTRNLTNPSTVIFLIGNKSDLESTREVTYEEAKEFADENGLMFLEASAMTGQNVEEAFLETARKIYQNIQEGRLDLNASESGVQHRPSQPSRTSLSSEATGAKDQCSC
Protein: Chromosome 6 open reading frame 130, isoform CRA_a (O-acyl-ADP-ribose deacylase 1) (C9J5P1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASSLNEDPEGSRITYVKGDLFACPKTDSLAHCISEDCRMGAGIAVLFKKKFGGVQELLNQQKKSGEVAVLKRDGRYIYYLDWMWS
Protein: Sulfotransferase 1B1 (ST1B1) (EC 2.8.2.1) (Sulfotransferase family cytosolic 1B member 1) (Q8JG30)
Organism: Gallus gallus (Chicken)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of dopamine, small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3'-diiodothyronine, triidothyronine (T3) and reverse triiodothyronine (rT3).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O43704}.
Interaction partners:
- Sulfotransferase
Sequence:
MGTVDAYLRQPWSTVHAIPMVSAFAQNWERVDNFQSRPDDIVVATFPKSGTTWISEIVDMILQGGDPKKCKRDAIVNRVPMLEFAAPGQMPAGTEQLENMPSPRIIKTHIPADILPKSFWDKSCKMIYVGRNAKDVAVSYYHFDLMNKLHPHPGTWDQYLEAFMAGKVAYGSWFDHVRGYWERRQEHPILYLFYEDMKEDLRREVAKVAQFLGRELTEVALDAIAHHTSFEAMRDNPSTNYSVVPSQLMDHGISPFMRKGITGDWKNHFTVAQSAHFDQYYAQKMAGTDLRFRTHI
Protein: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2 (G protein subunit beta-2) (Transducin beta chain 2) (P62880)
Organism: Mus musculus (Mouse)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P62879}. Cell membrane {ECO:0000250|UniProtKB:P62879}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Phosducin-like protein
Sequence:
MSELEQLRQEAEQLRNQIRDARKACGDSTLTQITAGLDPVGRIQMRTRRTLRGHLAKIYAMHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNFVACGGLDNICSIYSLKTREGNVRVSRELPGHTGYLSCCRFLDDNQIITSSGDTTCALWDIETGQQTVGFAGHSGDVMSLSLAPDGRTFVSGACDASIKLWDVRDSMCRQTFIGHESDINAVAFFPNGYAFTTGSDDATCRLFDLRADQELLMYSHDNIICGITSVAFSRSGRLLLAGYDDFNCNIWDAMKGDRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN
Protein: Patatin-like phospholipase domain-containing protein 6 (EC 3.1.1.5) (Neuropathy target esterase) (Q8IY17)
Organism: Homo sapiens (Human)
Function: Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of PtdCho. Catalyzes the hydrolysis of several naturally occurring membrane-associated lipids. Hydrolyzes lysophospholipids and monoacylglycerols, preferring the 1-acyl to the 2-acyl isomer. Does not catalyze hydrolysis of di- or triacylglycerols or fatty acid amides.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15044461}; Single-pass type III membrane protein {ECO:0000269|PubMed:15044461}.
Interaction partners:
- Phospholipase B1, membrane-associated
- Lysosomal phospholipase A and acyltransferase
- Acyl-protein thioesterase 1
- Glycerophosphocholine phosphodiesterase GPCPD1
- Phospholipase A and acyltransferase 3
- Patatin-like phospholipase domain-containing protein 7
- Acyl-protein thioesterase 2
- Membrane-bound glycerophospholipid O-acyltransferase 2
- Phosphatidylcholine-sterol acyltransferase
- Lysophospholipid acyltransferase 5
Sequence:
MEAPLQTGMMGTSSHGLATNSSGAKVAERDGFQDVLAPGEGSAGRICGAQPVPFVPQVLGVMIGAGVAVVVTAVLILLVVRRLRVPKTPAPDGPRYRFRKRDKVLFYGRKIMRKVSQSTSSLVDTSVSATSRPRMRKKLKMLNIAKKILRIQKETPTLQRKEPPPAVLEADLTEGDLANSHLPSEVLYMLKNVRVLGHFEKPLFLELCRHMVFQRLGQGDYVFRPGQPDASIYVVQDGLLELCLPGPDGKECVVKEVVPGDSVNSLLSILDVITGHQHPQRTVSARAARDSTVLRLPVEAFSAVFTKYPESLVRVVQIIMVRLQRVTFLALHNYLGLTNELFSHEIQPLRLFPSPGLPTRTSPVRGSKRMVSTSATDEPRETPGRPPDPTGAPLPGPTGDPVKPTSLETPSAPLLSRCVSMPGDISGLQGGPRSDFDMAYERGRISVSLQEEASGGSLAAPARTPTQEPREQPAGACEYSYCEDESATGGCPFGPYQGRQTSSIFEAAKQELAKLMRIEDPSLLNSRVLLHHAKAGTIIARQGDQDVSLHFVLWGCLHVYQRMIDKAEDVCLFVAQPGELVGQLAVLTGEPLIFTLRAQRDCTFLRISKSDFYEIMRAQPSVVLSAAHTVAARMSPFVRQMDFAIDWTAVEAGRALYRQGDRSDCTYIVLNGRLRSVIQRGSGKKELVGEYGRGDLIGVVEALTRQPRATTVHAVRDTELAKLPEGTLGHIKRRYPQVVTRLIHLLSQKILGNLQQLQGPFPAGSGLGVPPHSELTNPASNLATVAILPVCAEVPMVAFTLELQHALQAIGPTLLLNSDIIRARLGASALDSIQEFRLSGWLAQQEDAHRIVLYQTDASLTPWTVRCLRQADCILIVGLGDQEPTLGQLEQMLENTAVRALKQLVLLHREEGAGPTRTVEWLNMRSWCSGHLHLRCPRRLFSRRSPAKLHELYEKVFSRRADRHSDFSRLARVLTGNTIALVLGGGGARGCSHIGVLKALEEAGVPVDLVGGTSIGSFIGALYAEERSASRTKQRAREWAKSMTSVLEPVLDLTYPVTSMFTGSAFNRSIHRVFQDKQIEDLWLPYFNVTTDITASAMRVHKDGSLWRYVRASMTLSGYLPPLCDPKDGHLLMDGGYINNLPADIARSMGAKTVIAIDVGSQDETDLSTYGDSLSGWWLLWKRLNPWADKVKVPDMAEIQSRLAYVSCVRQLEVVKSSSYCEYLRPPIDCFKTMDFGKFDQIYDVGYQYGKAVFGGWSRGNVIEKMLTDRRSTDLNESRRADVLAFPSSGFTDLAEIVSRIEPPTSYVSDGCADGEESDCLTEYEEDAGPDCSRDEGGSPEGASPSTASEMEEEKSILRQRRCLPQEPPGSATDA
Protein: Mitotic checkpoint protein BUB3 (xbub3) (WD repeat protein Bub3) (Q9YGY3)
Organism: Xenopus laevis (African clawed frog)
Function: Has a dual function in spindle-assembly checkpoint signaling and in promoting the establishment of correct kinetochore-microtubule (K-MT) attachments. Plays a role in the kinetochore-mediated mitotic checkpoint, which delays anaphase onset until all chromosomes have attached properly to the mitotic spindle. Required to establish and maintain spindle checkpoint arrest in eggs.
Subcellular location: Nucleus. Chromosome, centromere, kinetochore. Note=Aurora B controls the kinetochore localization. Kinetochore localization starts in early prophase and maintains the localization until the metaphase-anaphase transition. Diffusively localized to the nucleus during interphase and telophase.
Interaction partners:
Sequence:
MNTQTDMTGSNEFKLNQAPEDGISAVKFSPNTSQFLLVSSWDSSVRLYDVPANTMRLKYQHAGPVLDCAFYDPTHAWSGGLDHQLKMHDLNTDGDTVVGSHDAPIRCVEYCPEVNVIVTGSWDQTVKLWDPRTPCNAGTFSQPDKVYTLSVSGDRLIVGTAGRRVLVWDLRNMGYVQQRRESSLKYQTRCIRAFPNKQGYVLSSIEGRVAVEYLDPSLEVQKKKYAFKCHRLKENNIEQIYPVNAVSFHNLHNTFATGGSDGFVNIWDPFNKKRLCQFHRYPTSIASLAFSNDGSTLAIAASYMYEMDDIDHPEDAIYIRQVTDAETKPK
Protein: ubiquitinyl hydrolase 1 (EC 3.4.19.12) (E9PJH5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLVYRLQTQEKPNTTVQVPAFLQELVDRDNSKFEEWCIEMAEMRKQSVDKGKAKHEEVKELYQRLPAGAEPYEFVSLEWLQKWLDESTPTKPIDNHACLCSHDKLHPDKISIMKRISEYAADIFYSRYGGGPRLT
Protein: Protein HIR2 (Histone transcription regulator 2) (P32480)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the HIR complex, which cooperates with ASF1 to promote replication-independent chromatin assembly. The HIR complex is also required for the periodic repression of three of the four histone gene loci during the cell cycle as well as for autogenous regulation of the HTA1-HTB1 locus by H2A and H2B. DNA-binding by the HIR complex may repress transcription by inhibiting nucleosome remodeling by the SWI/SNF complex. The HIR complex may also be required for transcriptional silencing of centromeric, telomeric and mating-type loci in the absence of CAF-1.
Subcellular location: Nucleus {ECO:0000269|PubMed:8417331}. Chromosome {ECO:0000269|PubMed:19683497}. Note=Localizes to the promoter region of histones HTA1-HTB1. {ECO:0000269|PubMed:19683497}.
Interaction partners:
- Histone promoter control protein 2
- Histone chaperone ASF1
- Protein HIR1
- Histone transcription regulator 3
- Histone H2A.1
- Histone H3
- Histone chaperone RTT106
- Histone H2B.1
- Histone-binding protein MSI1
- Protein SPT10
Sequence:
MRLLKYPLDIHNEQVNALAALGPYIILAGSGGHVMAWRQQQLVDTAFDRVMIKDLKPEVSFQVDQDTTGDIFFITGDLETLYIGSEHRLWGYSGWLCRDTNNINSVEKMNSKLLFECKSPSTITDVKYDINLGILFVLLSNENKILLFRHKTFDKLSEITIDKASKPITGIIDPTGQTFTVMTSDRSILVYQINKTGTHKLINKLTQHVQMYPLHYRISMSPQADILPVINSVKGVPNNATSCTALLDRNNNYKVTKTLVTPSSNGCRVLVYSPAFYEKPNLKKGTSTRYNLIATSGSTDGTILVWNTKRMKPLFNALQVSSTAINDMSWSQDGFTLFAISNDATLYTFAFQEKDLGVALPQTEIKSLQEVNKKLPKLEEPLAEQIPKSFPENIKLEESASAAPIPNDIGRSAVGKKPTKKKTANNQTNGIKTIQSTSMEFNTPSYTVPRDLKRKPKEATPSNIAPGSKKQKKELQPIDFLDTGLLLPNTSFSRIRLATPKIRSTFKYSPINNPNLILDVKNGSGNEQRPTIVKLTSKVLDQDQVLFQDFIPKLITICTAGDTFWSFCSEDGSIYIYSDSGRKLMAPLVLGVSISFLEACGTYLLCLTSIGELYCWNIEQKKLAFPTNTIYPLLNPSLRYSDDILTRAENITLCSITKKGVPLVTLSNGDGYLFDKNMETWLLVSDGWWAYGSQYWDTTNTTGLSSSKANTDSFNGSESNINEIVSDIKNDNQSIINFLECKTNDELNRKGRIKNLQRFARTILMKEGFENMEEIVTLSHLENKILISIRLEEPEEFSKLMMVYCIRLSELGYMDRLNDVFQWLYDDLPISGTGSAFADKDFKRNLLKKILIACGDIRQVQRVTTRYAKEMNIIS
Protein: BCL-W (Bcl2-like 2) (O88996)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004325}.
Interaction partners:
- Bcl-2-like protein 11
- Phorbol-12-myristate-13-acetate-induced protein 1
- Bcl2-interacting killer, isoform CRA_a.
- Bcl-2-modifying factor
- BCL2-antagonist/killer 1, isoform CRA_b.
- Caspase-9
- Beclin-1
- Bcl-2-like protein 1
- Cellular tumor antigen p53
- Apoptotic protease-activating factor 1
Sequence:
MATPASTPDTRALVADFVGYKLRQKGYVCGAGPGEGPAADPLHQAMRAAGDEFETRFRRTFSDLAAQLHVTPGSAQQRFTQVSDELFQGGPNWGRLVAFFVFGAALCAESVNKEMEPLVGQVQDWMVTYLETRLADWIHSSGGWAEFTALYGDGALEEARRLREGNWASVRTVLTGAVALGALVTVGAFFASK
Protein: Catabolic 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10) (Q59087)
Organism: Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Function: Involved in the biosynthesis of protocatechuate. Catalyzes the catabolic dehydration of 3-dehydroquinate (DHQ) to yield 3-dehydroshikimate.
Interaction partners:
- 3-dehydroshikimate dehydratase
- Quinate/shikimate dehydrogenase
- 3-dehydroquinate synthase
- Shikimate dehydrogenase
- 3-dehydroquinate dehydratase
- isochorismate synthase
- Protocatechuate 3,4-dioxygenase alpha chain
- 4-carboxymuconolactone decarboxylase
- Shikimate kinase
Sequence:
MSLPILSTTYAAENTVPASKSTYVVKNLNIGDLPVKTLVPITAKTREQALAQAKVIAENKDADIAEFRIDLLEFASDTKKVIALGQELNQILKDKPLLATIRTSNEGGKLKVTDQEYEKIYSEYLKKPFMQLLDIEMFRDQAAVAKLTKLAHQKKVLVVMSNHDFDKTPSEQEIVSRLLKQDQMGADILKIAVMPKSKQDVFTLMNATLKVSEQSTKPLLTMSMGRLGTISRIATANMGGSLSFGMIGEASAPGQIDVTALKQFLKTVQPTP
Protein: Methyl-CpG-binding protein 2 (MeCp-2 protein) (MeCp2) (Q7T2T7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR038006}. Note=Colocalized with methyl-CpG in the genome. {ECO:0000256|PIRNR:PIRNR038006}.
Interaction partners:
- DNA
- Cyclin-dependent kinase-like 5
- Histone deacetylase 1
- Paired amphipathic helix protein Sin3a
- Brain-derived neurotrophic factor
- FMRP translational regulator 1.
- Paired amphipathic helix protein Sin3b
- Paired amphipathic helix protein Sin3a
- Ubiquitin-protein ligase E3A
- E3 ubiquitin-protein ligase UHRF1
Sequence:
MAAAESGEERLRGEDKNEDQEGSKDKTQKHKKSKKERHDVEKLETTVSVPPPPSLFTQRDVGQQAEAGKSEPIDPEVGAALSAPESSASAKQRRSVIRDRGPMYEDPSLPQGWTRKLKQRKSGRSAGKFDVYLINPEGKAFRSKVELMAYFQKVGDTITDPNDFDFTVTGRGSPSRREKRPPKKPKMVKPSGRGRGRPKGSGKVRQATEGVAVKRVIEKSPGKLLVKMPFVAPKTEPGAPLGQAPVAKARRGRKRKSEQDPPSTPKKRGRKPATVSQSTVGTGSAAAYAAAAILTAEAKKKALKESSAKPVQERALPIKKRKTRETLEELEASTTSATETFEKRLTASTVTPTGEEAETGQKPHKHPSRKHKEADPGSSSSGTTASGVAPKSHKKRDQRGQHFKHHHHHHHHHHQHQHLQASTPSTYTPQAHQLSLGHSTHGGLENEPQDLSTSRPKAEHVACREEARTGSSSSRDSQNASKMASMTVTGESKELRDIVPPSAVPRPSREETVESRTPVSEPVS
Protein: Protein CLAVATA 3 [Cleaved into: MCLV3] (Q9XF04)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Extracellular signal that regulates meristem maintenance. Acts with CLV1 as a ligand-receptor pair in a signal transduction pathway coordinating growth between adjacent meristematic regions and controlling the balance between meristem cell proliferation and differentiation.
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:19525968}.
Interaction partners:
- Receptor-like protein CLAVATA2
- Receptor protein kinase CLAVATA1
- LRR receptor-like serine/threonine-protein kinase RPK2
- Protein WUSCHEL
- CLAVATA3/ESR
- Serine/threonine-protein kinase-like protein ACR4
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- WUSCHEL-related homeobox 5
Sequence:
MDSKSFLLLLLLFCFLFLHDASDLTQAHAHVQGLSNRKMMMMKMESEWVGANGEAEKAKTKGLGLHEELRTVPSGPDPLHHHVNPPRQPRNNFQLP
Protein: P2Y purinoceptor 6 (P2Y6) (Q15077)
Organism: Homo sapiens (Human)
Function: Receptor for extracellular UDP > UTP > ATP. The activity of this receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- P2X purinoceptor 2
- P2X purinoceptor 1
- P2Y purinoceptor 2
- P2X purinoceptor 4
- P2X purinoceptor 3
- P2X purinoceptor 5
- P2X purinoceptor 6
- P2Y purinoceptor 11
- P2X purinoceptor 7
Sequence:
MEWDNGTGQALGLPPTTCVYRENFKQLLLPPVYSAVLAAGLPLNICVITQICTSRRALTRTAVYTLNLALADLLYACSLPLLIYNYAQGDHWPFGDFACRLVRFLFYANLHGSILFLTCISFQRYLGICHPLAPWHKRGGRRAAWLVCVAVWLAVTTQCLPTAIFAATGIQRNRTVCYDLSPPALATHYMPYGMALTVIGFLLPFAALLACYCLLACRLCRQDGPAEPVAQERRGKAARMAVVVAAAFAISFLPFHITKTAYLAVRSTPGVPCTVLEAFAAAYKGTRPFASANSVLDPILFYFTQKKFRRRPHELLQKLTAKWQRQGR
Protein: Amino acid transporter, putative (Q38AV6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MVVNSDGVLKDNYTDDQTSEEDPNGDNIRTNRSSDDGPRRGIMRFTEPLFSRVIPHGGTLSNTFTFASATLGGSIVALPWAFHAVGIVMGTVYLFLMTLVTAYTVTIIGFVMKKSRFSGFEQMSLVVLGRGAAYLMSVVMGASCLGAAVAYVIAVRTLLEPLLQQSPLTSNFFGTTAGVRLTTFFVWLLGMLPLVLPKQINSLRYFSAIGVVCVVYFSVAIIAHATMAGVPKRGDVSMFQGGNIAVEGFGIFIFAYLCHCVAFQTYYEMRIPSVRKLFISTTIAMIFCSVLYWFAGVFAYLEFGPEVKDSVLYMYDPISDPMMFVAYVGLVAKLCVSYAMNMLPLRNTVYFLLQWEIQQLPYWKHTAVVTVMSILVLICGIFFPKISTVFGFVGSVCGGLIGFIYPALFYMYSGNWSLATVGWFHYIMTYCVLMLGVASVVFGTAATIYAIIN
Protein: Tyrosine-protein phosphatase non-receptor type 22 (EC 3.1.3.48) (Hematopoietic cell protein-tyrosine phosphatase 70Z-PEP) (PEST-domain phosphatase) (PEP) (P29352)
Organism: Mus musculus (Mouse)
Function: Acts as negative regulator of T-cell receptor (TCR) signaling by direct dephosphorylation of the Src family kinases LCK and FYN, ITAMs of the TCRz/CD3 complex, as well as ZAP70, VAV, VCP and other key signaling molecules (By similarity). Associates with and probably dephosphorylates CBL (By similarity). Dephosphorylates LCK at its activating 'Tyr-394' residue (By similarity). Dephosphorylates ZAP70 at its activating 'Tyr-492' residue (By similarity). Dephosphorylates the immune system activator SKAP2 (By similarity). Positively regulates toll-like receptor (TLR)-induced type 1 interferon production. Promotes host antiviral responses mediated by type 1 interferon. Regulates NOD2-induced pro-inflammatory cytokine secretion and autophagy. Acts as an activator of NLRP3 inflammasome assembly by mediating dephosphorylation of 'Tyr-861' of NLRP3. Dephosphorylates phospho-anandamide (p-AEA), an endocannabinoid to anandamide (also called N-arachidonoylethanolamide).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8890164}.
Interaction partners:
- Tyrosine-protein kinase CSK
- Tyrosine-protein kinase ZAP-70
- Tyrosine-protein kinase JAK1
- Proto-oncogene tyrosine-protein kinase LCK
- T-cell surface glycoprotein CD4
- T-cell surface glycoprotein CD3 zeta chain
- Cytotoxic T-lymphocyte protein 4
Sequence:
MDQREILQQLLKEAQKKKLNSEEFASEFLKLKRQSTKYKADKIYPTTVAQRPKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWAEPGETQLQFGPFSISCEAEKKKSDYKIRTLKAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPICIHCSAGCGRTGVICAVDYTWMLLKDGIIPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLELFKRHMDVISDNHLGREIQAQCSIPEQSLTVEADSCPLDLPKNAMRDVKTTNQHSKQGAEAESTGGSSLGLRTSTMNAEEELVLHSAKSSPSFNCLELNCGCNNKAVITRNGQARASPVVGEPLQKYQSLDFGSMLFGSCPSALPINTADRYHNSKGPVKRTKSTPFELIQQRKTNDLAVGDGFSCLESQLHEHYSLRELQVQRVAHVSSEELNYSLPGACDASCVPRHSPGALRVHLYTSLAEDPYFSSSPPNSADSKMSFDLPEKQDGATSPGALLPASSTTSFFYSNPHDSLVMNTLTSFSPPLNQETAVEAPSRRTDDEIPPPLPERTPESFIVVEEAGEPSPRVTESLPLVVTFGASPECSGTSEMKSHDSVGFTPSKNVKLRSPKSDRHQDGSPPPPLPERTLESFFLADEDCIQAQAVQTSSTSYPETTENSTSSKQTLRTPGKSFTRSKSLKIFRNMKKSVCNSSSPSKPTERVQPKNSSSFLNFGFGNRFSKPKGPRNPPSAWNM
Protein: Ras-related GTP-binding protein (Q54PK6)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
- Ras-related GTP-binding protein A
- Protein raptor homolog
- UPF0171 family protein
- NPR2 family protein
- GATOR2 complex protein WDR24
- DEP domain-containing protein DDB_G0279099
- Ragulator complex protein LAMTOR5 homolog
- GATOR2 complex protein MIOS
- Folliculin
- Roadblock/LAMTOR2 domain-containing protein
Sequence:
MEDNYEEYDNAFVGNLGDMGYGEDTQAAGEPASQIENKPKIFLMGLKRSGKSSIQKVVFHKMLPNETLFLESTSKVVKNDISNSSFVQFQIWDFPGQLDFFDPSFDYEYILNNCGAIVFVIDAQDEIIEALQKLHQTIAKVYQINPNIHFEVFIHKSDGLSDDHKIDRQRDIQQKTTEELADANINVHPSFYVTSIYDHSIFEAFSKVIQKLIPQLPTLENLLDVFISRSRIEKAFLVDVVSKIYVATDNSPVDMQTYELCSDMIDVVIDVSCIYGLKEEEEGLGYDQESHSVIKLNNGMVLYLKEVNKYLALVCLLRESNFDKHGLIDYNFICFKKAIEEVFSRKTTKAGAKKTIKKAN
Protein: Probable enoyl-CoA hydratase 2, mitochondrial (EC 4.2.1.17) (F4JML5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate.
Subcellular location: Mitochondrion {ECO:0000255}.
Interaction partners:
- Hydroxymethylglutaryl-CoA lyase, mitochondrial
- 3-hydroxyacyl-CoA dehydrogenase family protein
- Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
- Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
- Hydroxymethylglutaryl-CoA synthase
- Isovaleryl-CoA dehydrogenase, mitochondrial
- 3-ketoacyl-CoA thiolase 1, peroxisomal
- 3-ketoacyl-CoA thiolase 5, peroxisomal
- 3-ketoacyl-CoA thiolase 2, peroxisomal
- Ketose-bisphosphate aldolase class-II family protein
Sequence:
MSFVKYLRRDNLLQLAGKPSLSRNYILQTCRTLIIETSPPEFVKLNRLSGSDSGIIEVNLDRPVTKNAINKEMLKSLQNAFESIHQDNSARVVMIRSLVPGVFCAGADLKERRTMSPSEVHTYVNSLRYMFSFIEALSIPTIAAIEGAALGGGLEMALACDLRICGENAVFGLPETGLAIIPGAGGTQRLSRLVGRSVSKELIFTGRKIDAIEAANKGLVNICVTAGEAHEKAIEMAQQINEKGPLAIKMAKKAIDEGIETNMASGLEVEEMCYQKLLNTQDRLEGLAAFAEKRKPLYTGN
Protein: SET domain-containing protein (Q38A07)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSVCLGTDPSPQLFASWAKKQGIFLHPDVAFLVPTKTMGAGVFARRQLPKETVIVSCPFSSSISPYAGPSTVEAPCVKALNDTQVKDNVLYVTLRFMAEVLRPSSPWVPWLKTCPRMLDHLFGNVIDDKAFCSATCTSLGTVSTRWTCLSQQLLEMNVSQRWGLAEEIMKRYPEHWPEDRATFPLFCECLALVLSRNFHRENVEGREGPYLLPGLDMVNHSFEANAILEIRGGGRKHSLTFCLVASKELRRGEQVLLSYGKIGAARFAVEFQFVTDSVVGEDMLRFSVDVIVDIVAAIMASGESTNDTESNVRMLRQRVERLQRLGFLFDEGLYISRLPRTSINRDLDAVGSSCSASTWGAEIAPATVKDVQRFFNVFHLMTVSTGEFDHLIHTINRDWQVKRTDALMTLASRVIAMRAEAAHLQLNLVQEQFSGEEHSSRRRLMETVLNSELQMLDTLQEYVKGMC
Protein: Putative lipid kinase MamU (EC 2.7.-.-) (Q2W8P4)
Organism: Paramagnetospirillum magneticum (strain ATCC 700264 / AMB-1) (Magnetospirillum magneticum)
Function: Might phosphorylate lipids.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:27481925}. Note=Tagged protein forms a diffuse intracellular stain. {ECO:0000269|PubMed:27481925}.
Interaction partners:
- Predicted phosphohydrolase
- Magnetosome protein MamR
Sequence:
MRIAAIINERAGTVACLSPPVVAARLSAIWTSLGHQAHVTLAEGKDMGRAIRKACRDPAVHAVIIGGGDGSLSRSLKHVVGSGKSLGVLPLGTMNYVARQFGVPFDLDRAAVALADAVPTPTDLGRVNDRFFLIRACLGAFPEFIRSRDEARRKGGSFLDGALAGLTGLARGHRLIEAELIGPDVQARIATSFFMVSNNMCRDSDPFQLERERMDGATLGVYIGQGAGPFSLMDLGLQVAMGRWASNEALIRGSLPWLEIRTRQRKPLVSIDGEVEKMEAPFRFDILPGVLPMLVPK