wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphatidylinositol 3-kinase catalytic subunit type 3 (PI3-kinase type 3) (PI3K type 3) (PtdIns-3-kinase type 3) (EC 2.7.1.137) (Phosphoinositide-3-kinase class 3) (Q6PF93)
Organism: Mus musculus (Mouse)
Function: Catalytic subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. As part of PI3KC3-C1, promotes endoplasmic reticulum membrane curvature formation prior to vesicle budding. Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2. Involved in the transport of lysosomal enzyme precursors to lysosomes. Required for transport from early to late endosomes (By similarity).
Subcellular location: Midbody {ECO:0000250|UniProtKB:Q8NEB9}. Late endosome {ECO:0000250|UniProtKB:Q8NEB9}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:22493499}. Note=As component of the PI3K complex I localized to pre-autophagosome structures. As component of the PI3K complex II localized predominantly to endosomes (By similarity). Also localizes to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme (PubMed:24089209). {ECO:0000250|UniProtKB:Q8NEB9, ECO:0000269|PubMed:24089209}.
Interaction partners:
- Activating molecule in BECN1-regulated autophagy protein 1
- Nuclear receptor-binding factor 2
- Beclin 1-associated autophagy-related key regulator
- Beclin-1
- Phosphoinositide 3-kinase regulatory subunit 4
- UV radiation resistance-associated protein
- Gamma-aminobutyric acid receptor-associated protein
- RB1-inducible coiled-coil protein 1
- Autophagy-related protein 13
- Serine/threonine-protein kinase ULK2
Sequence:
MGEAEKFHYIYSCDLDINVQLKIGSLEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVTCQVFAEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGSAVPVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTRTPGRTSSTLSEDQMSRLAKLTKAHRQGHMVKVDWLDRLTFREIEMINESEKRSSNFMYLMVEFRCVKCDDKEYGIVYYEKDGDESSPILTSFELVKVPDPQMSMENLVESKHHKLARSLRSGPSDHDLKPNATTRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVEDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKKDSQTSASESLSNSGVSSGDIDSSQIITNPLPPVASPPPASKAKEVSDGENLEQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALLKGDKSVRVMRSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSETGPYGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQYWRK
Protein: Similar to hydroxylamine oxidoreductase (EC 1.7.3.4) (Q1PVE0)
Organism: Kuenenia stuttgartiensis
Interaction partners:
Sequence:
MLTIRRCFEMKKILLGMVAFAVMLPAIVEWTSGQSNVAWATEQKTEEIPPPDLYKDTPAWYQAVYKDNVGLSEGSGPFTKYFKAQMLDMYWQPNRHYEPMENLDHSIFIEQERRDLCVICHEEATPGIVADWRSSGHKHPKSTPYLSSKTAQIEKNVGRVLDEVHCFDCHADTEKNQIRMPTGEVCGGCHRQQFDEFLREREVGRPNHLQSWEANTIVPWYAEAARRGYLYGQHGCDMCHSGAEKCDVCHTRHKFSAVEGRQPEACMTCHMGPDHPDAESYGESKHGKIYEKEEEHYDFTKPLVEVRPGEDYRTPTCQYCHMYEKHGRFIHNPVMKGIWRMGTVPPSNLEYTSSLKDYPYGIKIIADKIDIYSEENVAKRSYWLEVCAKCHSDRFADTYLKSLDQFMFQAHTLADQAQKIVEDLIADGLLYPDAANRDPYPLSDGIVKELSADFLGEPVYNAFKTLQGKFPVVGPILGVYGMFLQMQDNPSDIENMYNRLWFWYKLQGYKGTAHAQQDVSWWWGQAPMMMEMTRIQAEAARLRRLAGIEKTISK
Protein: Growth/differentiation factor 2 (GDF-2) (Bone morphogenetic protein 9) (BMP-9) (Q9UK05)
Organism: Homo sapiens (Human)
Function: Potent circulating inhibitor of angiogenesis. Signals through the type I activin receptor ACVRL1 but not other Alks. Signaling through SMAD1 in endothelial cells requires TGF-beta coreceptor endoglin/ENG.
Subcellular location: Secreted {ECO:0000269|PubMed:18309101, ECO:0000269|PubMed:21710321, ECO:0000269|PubMed:25237187}.
Interaction partners:
- Activin receptor type-1-like
- Bone morphogenetic protein receptor type-2
- Activin receptor type-2A
- Activin receptor type-2B
- Endoglin
- Activin receptor type-1
- TGF-beta receptor type-1
- Bone morphogenetic protein receptor type-1A
- Bone morphogenetic protein 10
- Mothers against decapentaplegic homolog 9
Sequence:
MCPGALWVALPLLSLLAGSLQGKPLQSWGRGSAGGNAHSPLGVPGGGLPEHTFNLKMFLENVKVDFLRSLNLSGVPSQDKTRVEPPQYMIDLYNRYTSDKSTTPASNIVRSFSMEDAISITATEDFPFQKHILLFNISIPRHEQITRAELRLYVSCQNHVDPSHDLKGSVVIYDVLDGTDAWDSATETKTFLVSQDIQDEGWETLEVSSAVKRWVRSDSTKSKNKLEVTVESHRKGCDTLDISVPPGSRNLPFFVVFSNDHSSGTKETRLELREMISHEQESVLKKLSKDGSTEAGESSHEEDTDGHVAAGSTLARRKRSAGAGSHCQKTSLRVNFEDIGWDSWIIAPKEYEAYECKGGCFFPLADDVTPTKHAIVQTLVHLKFPTKVGKACCVPTKLSPISVLYKDDMGVPTLKYHYEGMSVAECGCR
Protein: Ricin B-like lectin (F6KMV5)
Organism: Macrolepiota procera (Parasol mushroom)
Interaction partners:
Sequence:
MSTQVSSGQTYKITNVKAGTVIDLSGEDNKSIIGYPYHSGKNQQWTFNWTGKAWTLRSASSGSYLGIEGTPADGTRLVAVNDPFEWHIWRDEANENAFRIFVPFTNYNLDLSGYGDTTPGTPVQLWWTWEGLHQTWTIDRP
Protein: Stanniocalcin-2 (STC-2) (O88452)
Organism: Mus musculus (Mouse)
Function: Has an anti-hypocalcemic action on calcium and phosphate homeostasis.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Pappalysin-1
- Biorientation of chromosomes in cell division protein 1
- Pappalysin 2
Sequence:
MCAERLGQFVTLALVFATLDPAQGTDSTNPPEGPQDRSSQQKGRLSLQNTAEIQHCLVNAGDVGCGVFECFENNSCEIQGLHGICMTFLHNAGKFDAQGKSFIKDALRCKAHALRHKFGCISRKCPAIREMVFQLQRECYLKHDLCSAAQENVGVIVEMIHFKDLLLHEPYVDLVNLLLTCGEDVKEAVTRSVQAQCEQSWGGLCSILSFCTSNIQRPPTAAPEHQPLADRAQLSRPHHRDTDHHLTANRGAKGERGSKSHPNAHARGRTGGQSAQGPSGSSEWEDEQSEYSDIRR
Protein: Uncharacterized protein (Q9A573)
Organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus)
Interaction partners:
Sequence:
MSCRLLLVLATFAALVSPAIAEEQSALNVLDLNKAQNWAEALAACDVTRFLLTDPDVTASTIIAPGEGAPQFLYPPLFTPPNVLYTPSLLRTFEILQARGEVDRKSLADARFRFANAVVPSFQKGDAIAKAVLSDQMKLCNVLTDGVASEAPRK
Protein: Acetylcholine receptor subunit gamma (P07510)
Organism: Homo sapiens (Human)
Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular location: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Acetylcholine receptor subunit alpha
- 43 kDa receptor-associated protein of the synapse
- Acetylcholine receptor subunit delta
- Muscle, skeletal receptor tyrosine-protein kinase
- Acetylcholine receptor subunit beta
- Acetylcholine receptor subunit epsilon
Sequence:
MHGGQGPLLLLLLLAVCLGAQGRNQEERLLADLMQNYDPNLRPAERDSDVVNVSLKLTLTNLISLNEREEALTTNVWIEMQWCDYRLRWDPRDYEGLWVLRVPSTMVWRPDIVLENNVDGVFEVALYCNVLVSPDGCIYWLPPAIFRSACSISVTYFPFDWQNCSLIFQSQTYSTNEIDLQLSQEDGQTIEWIFIDPEAFTENGEWAIQHRPAKMLLDPAAPAQEAGHQKVVFYLLIQRKPLFYVINIIAPCVLISSVAILIHFLPAKAGGQKCTVAINVLLAQTVFLFLVAKKVPETSQAVPLISKYLTFLLVVTILIVVNAVVVLNVSLRSPHTHSMARGVRKVFLRLLPQLLRMHVRPLAPAAVQDTQSRLQNGSSGWSITTGEEVALCLPRSELLFQQWQRQGLVAAALEKLEKGPELGLSQFCGSLKQAAPAIQACVEACNLIACARHQQSHFDNGNEEWFLVGRVLDRVCFLAMLSLFICGTAGIFLMAHYNRVPALPFPGDPRPYLPSPD
Protein: Inner membrane protein YqjF (P42619)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Probable HTH-type transcriptional regulator YhaJ
- Pirin-like protein YhaK
- Uncharacterized protein YbiJ
- Quercetin 2,3-dioxygenase
- UPF0382 inner membrane protein YgdD
Sequence:
MKKLEDVGVLVARILMPILFITAGWGKITGYAGTQQYMEAMGVPGFMLPLVILLEFGGGLAILFGFLTRTTALFTAGFTLLTAFLFHSNFAEGVNSLMFMKNLTISGGFLLLAITGPGAYSIDRLLNKKW
Protein: AT5g24690/MXC17_8 (Plant/protein, putative (DUF3411)) (Q93W02)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast membrane {ECO:0000256|ARBA:ARBA00004508}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004508}.
Interaction partners:
- ADP,ATP carrier protein 2, chloroplastic
- Dicarboxylate transporter 2.2, chloroplastic
- Uncharacterized protein At5g13720)
- S-adenosylmethionine carrier 1, chloroplastic/mitochondrial
- Folate transporter 1, chloroplastic
- Protein TRIGALACTOSYLDIACYLGLYCEROL 1, chloroplastic
- Plastidal glycolate/glycerate translocator 1, chloroplastic
- Keratin-associated protein, putative
- Protein ACTIVITY OF BC1 COMPLEX KINASE 8, chloroplastic
- Dicarboxylate transporter 2.1, chloroplastic
Sequence:
MSHMVFQSVVAPKPLSPLKPCLPIPRPLVTLPCKLRRGFVRASSSSFLVDDSVSGLERCLQLPSGVELGTSSSGSFSASTQMCPVMKGKFGSVGAVTLEKGKLDMTQKISETSPEIATGGGGGNIGKSINNGGGDGGDDNGDDDDYFDEFDDGDEGDDDGLFRRRMFLAEIFDRKFVDAVLNEWQKTMMDLPAGLRQAYEMGLVSSAQMVKFLAINARPTTTRMISRALPQGLSRAFVGRMLADPAFLYKLLLEQAATVGCSVWWEVKNRKNRLKEEWDLALINVLTVSACNAAAVWLLAPCRSYGNTFRFDLQNTLQKLPNNLFEMSYPLREFDLQKRFHSLFYKAAELSILGLAAGTLQGSLSNVLAGKKKNRVSVTVPSISTNALGYGAFLGIYANLRYQLLCGFERGVSSHFDVIGVALFFGTALRIMNVQLGEKSRQVWLGVEADPLAQSDDLLAKAYNRPSEEAVAKPSSKWFISKNAIVSGLLGKKQEDSVSDSPPPKARRKRIVRKKVAASAS
Protein: Carboxylesterase type B domain-containing protein (G5EFY3)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MERIYLLLLLFLPRIRSYDVRSVTTSWGMVRGEVVSPEGDDLPPVAQYLGIPYGVAPTGQYRFNMAISAAKWTHMPKDARKVSPVCIQTDMPELSETKRFRAFKHTSAQRFDFNHRLLPHLKKQSEDCLYMNIYVPERLEISRDNYLPVMVIVHGEEYGWGTGNAFNGTTLAAYGHIIVVTLNYRLGVFGFLGRCESSSCSGNSGISDLVSALTMLNVILPSFGGDSKSVTLAGWGSGASLVSLLMASPLTQPGRRLFRRAILLDGSALSPWAISQNPQQYFMQLAEELACAPKNRTSSFNDNVDTIVRCMQVHSSENITKAVLKIDVPTFLSGFAPIVDGQLIPNKPQVSFSTQYGSLFREIDLLVGISSNPSHHMISNEDLKVGISKEKRMRIFRSLVRNLYDFHREEILASIINEYTDWENPRDHPKSIRNGVLNALSDVLYTAPLIETLRSHSADEVRKEANTFMFAFAHETRSWSQEQPNSGIRGSLSGDIVPYIFGYPLAQGDSEERLYSGFNTDDKGISKVMMHYVSNFVKSGDPSKPNPMSKNFPMGDVFHSTAWPQFDQPNREAYLEITDRPRVKNYYRNAQVGFWNNFIPQLHKNGKETEPVGEEHHLLSDHFRKDSYFGKTRHFSSYANLPFPPPPMPPSPPPELTTKPKPSESPTTLQTTTESEKAAAGSFTGKALGGVIFIGCGFLIMNVCLLIAVRREWGKKRRNEKKFQLQYQTYNSNHGGGAEQYNSLNSPLSLMPPPPPPLNGVHDDIFDHRVPHLRNGSTVHGTLPRHSFQEQARV
Protein: RING-type E3 ubiquitin transferase BRCA1 (Q90X96)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTCSRMDIEGICSVISVMQKNLECPICLELMKEPVATKCDHIFCKFCMLQLLSKKKKGTVPCPLCKTEVTRRSLQESHRFKLLVEGQLKIIKAFEFDSGYKFFPSQEHTKGLDSTIEDVLVKEDQSIVHCKGYRNRKKGVFNRKTYEETGMLSVSKAEEQFAKEVTRLIPCRQKKPKKEAALIFSNCVPDSSDGDLLNKENGLRNDCSPLHYEKEDTQIPEMEEMVESDLAECEFAESAGSNLLGFDGPEGIPEISAETSINAAGNCDFYGRKTEQFPNDHHCSFKQNIADAEQNKRNQHCGNVPFAPMGKSNLDEKETVETDFDNQHNDSNPENNDPLGKVTKLMRRSTERVNEWLLKTNQDFSTLSAEEDPILDALALQNKETSDKRSCSSDDSELMPVLHKHAEKGISGGGFDKPAVGVKDKIFCKVYKRERKAMPPNNITCVAEVHHDSALETGKENMTLEYGTGMSHLMSKRKMVYSLNPENTSKKNDLANINGSINVFPDCISDANLELEDKSEADSNSADACQSDIVHSSNTQIKQQCVESLANAGETRKKQELSCERSQEEKDFTQSGALGPKTRSQKSPYGHSELHIESSQISNEPSNVTKQVEVRRSRRLLMLPKGPGNKSNSNAVKEMNEQENIAQIPEFRVKDTNKNNEISDTVPSQLKKKDTYFPPCTSEDTGELENGIPVRKISDQNASLDNPIDPCKDEYSDTLLHVAGDNVQPDYMETEESELETQHIVKMFKTSKRTSFILESKEAENENRVNSAVEISQVETSNELPNVAECRHTSLLSSAKEQSGALLKQGSPSSEPKKTSPIHMLKKTESKHSKMSRNRRGKVKPSSNSAKNTTGQPDNLNNPTQGVTGSLYNKQVMSDFPMRLNVDEEHTNASAKGSQSSVADKSTAHSNVNTDFISDINSATPDGLLHYMDKAEGNSSPWDTTRDKNAALLESCLPSAYGSTGEKTPIPKVQSSEEGSSQGLFNQKPKCSSSGKADQKNSSKNPGKSQCRILSDFSGSSNNGKCSSQEMLSKAAFPSLSQESQCSVSLFSTQSNMSQQSVDEDHKQDVLQDELVSPNKTKRTAISGTEETQISPLRDQYQNPDIDEASECESEASHTGDSSILSSQDELLNTQQRNYMKDSLKKLQQEMAALEAVLGQHGTQKLEAETTCIPSSEHVTEMQEATEEEEEETYQGENLFVKTPPEHVANGSTLIGQSTDNGLQGRNRPVSPSFLCQTRIEKDTPEIVCPAMGISKKSLLTQKELPSQHKQEIRPDLETVNVTPTNPIDAQESLRQSSKNKRGSRMLHNKRSTSNQGSFCLSVEAAESPQIPKQNKAEFGIARKSTSPTFASPARAKVPSVGFKSPVVSSRRNLSFVASGLNQCEMALVQRFSKTTQSILSSRITDSTTHVIMKTDAELVCERTLKYFQGIASRKWVVSYEWVVQSFREGQILDEYDFEVKGDVINGRNHRGPRRSRLGSDGLLLIDFEICFFGSFTDMTLDDLEWMVSECGATVVKKLQFFKKKHNVTSLVIVQPDASTEVRDYTEIRKKHKALVVTREWLMDSVATYRLQKFDAYLA
Protein: 4-aminobutyrate aminotransferase (EC 2.6.1.19) (E0SIE8)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Interaction partners:
- Bifunctional aspartokinase/homoserine dehydrogenase
- Bifunctional aspartokinase/homoserine dehydrogenase
- Aspartate-semialdehyde dehydrogenase
Sequence:
MLSLSISQGVKTMSETQFAVTDHVQRTNADYLERQGWFESNVRSYPRKLPLVIQKAQGVWVTDVDGNQYLDCLAGAGTLALGHNHPEVVSSIQEFLASGLPMHTLDLTTPLKDAFCETLLAQLPGGENQYCLQFCGPSGADAVEAALKLAKTYTGRGGIISFSGGYHGMTHGALAVTGNTGPKDAVQNLMPGVQFLPYPHEYRCPLGIGGDAGVQALSHYFTAFIEDVERGMSLPAAVIVEAVQGEGGVNPAPASWLQTLREVTRRHGILLIVDEVQAGFARTGTLFAFEQAGIEPDIIVMSKAVGGGLPMAVLGIRREFDVWKPGTHTGTFRGNQMAMATGKTTIDILLRDKLAAQAAARGDWLKQQFTQLQTRFPCLGQVRGRGLMLGIEIVDERQPAQTGGAYPLDAELALAIQQHCFRQGLLLERGGRQGNVVRLLPPLIITEEQCRSVVERFERALIEAVAQIRHP
Protein: Transporter (A0A0G2KAA8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MLLARMKPQVQPELGGADQLPEQPLRPCKTADLLVVKEHNGVQCLLASQDGDAQPRETWGKKIDFLLSVVGFAVDLANVWRFPYLCYKNGGGAFLIPYTLFLIIAGMPLFYMELALGQFNREGAATVWKICPFFKGVGYAVILIALYVGFYYNVIIAWSLYYLFASFTLNLPWTNCGHAWNSPNCTDPKLLNASVLGDHTKYSKYKFTPAAEFYERGVLHLHESSGIHDIGLPQWQLLLCLMVVIVVLYFSLWKGVKTSGKVVWITATLPYFVLFVLLVHGVTLPGASNGINAYLHIDFYRLKEATVNGQWFLGRGGRVMWTVSSSLSLSTRDALLTSTINCVTSFISGFAIFSILGYMAHEHKVKIEDVATEGAGLVFVLYPEAISTLSGSTFWAVLFFLMLLALGLDSSMGGMEAVITGLADDFQVLKRHRKLFTCAVTLGTFLLAMFCITKGGIYVLTLLDTFAAGTSILFAVLMEAIGVSWFYGVDRFSNDIQQMMGFKPGLYWRLCWKFVSPAFLLFVVVVSIINFKPLTYDDYVYPPWANWVGWGIALSSMILVPAYVIYKFFSIRGSLWERVAYGITPENEHHLVAQRDVRQFQLRHWLAI
Protein: Acyl-protein thioesterase 1 (EC 3.1.2.-) (Palmitoyl-protein hydrolase) (EC 3.1.2.22) (Q12354)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Hydrolyzes fatty acids from S-acylated cysteine residues in proteins with a strong preference for palmitoylated G-alpha proteins over other acyl substrates. Mediates the deacylation of G-alpha proteins such as GPA1 in vivo, but has weak or no activity toward palmitoylated Ras proteins. Has weak lysophospholipase activity in vitro; however such activity may not exist in vivo.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- NADPH--cytochrome P450 reductase
Sequence:
MNGLRVAAKIQPARQTIIFLHGLGDTGSGWGFLAQYLQQRDPAAFQHTNFVFPNAPELHVTANGGALMPAWFDILEWDPSFSKVDSDGFMNSLNSIEKTVKQEIDKGIKPEQIIIGGFSQGAALALATSVTLPWKIGGIVALSGFCSIPGILKQHKNGINVKTPIFHGHGDMDPVVPIGLGIKAKQFYQDSCEIQNYEFKVYKGMAHSTVPDELEDLASFIKKSLSS
Protein: ATP synthase subunit b' (ATP synthase F(0) sector subunit b') (ATPase subunit II) (F-type ATPase subunit b') (F-ATPase subunit b') (P27183)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular location: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01399}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01399}.
Interaction partners:
- ATP synthase gamma chain
- ATP synthase subunit delta
- ATP synthase epsilon chain
- ATP synthase subunit alpha
- ATP synthase subunit c
- ATP synthase subunit a
- ATP synthase subunit beta
- ATP synthase subunit b
- ATP synthase protein I
- Inorganic pyrophosphatase
Sequence:
MFDFDATLPLMALQFVVLAFLLNAIFYKPMNKVLDERADYIRTNEEDARERLAKAKAITQEYEQQITDARRQSQAVIADAQAEARRLAAEKIAEAQRESQRQKETAAQEIEAQRQSALSSLEQEVAALSNQILHKLLGPELIK
Protein: Rho-related GTP-binding protein RhoH (GTP-binding protein TTF) (Translocation three four protein) (Q15669)
Organism: Homo sapiens (Human)
Function: Negative regulator of hematopoietic progenitor cell proliferation, survival and migration. Critical regulator of thymocyte development and T-cell antigen receptor (TCR) signaling by mediating recruitment and activation of ZAP70. Required for phosphorylation of CD3Z, membrane translocation of ZAP70 and subsequent activation of the ZAP70-mediated pathways. Essential for efficient beta-selection and positive selection by promoting the ZAP70-dependent phosphorylation of the LAT signalosome during pre-TCR and TCR signaling. Crucial for thymocyte maturation during DN3 to DN4 transition and during positive selection. Plays critical roles in mast cell function by facilitating phosphorylation of SYK in Fc epsilon RI-mediated signal transduction. Essential for the phosphorylation of LAT, LCP2, PLCG1 and PLCG2 and for Ca(2+) mobilization in mast cells (By similarity). Binds GTP but lacks intrinsic GTPase activity and is resistant to Rho-specific GTPase-activating proteins. Inhibits the activation of NF-kappa-B by TNF and IKKB and the activation of CRK/p38 by TNF. Inhibits activities of RAC1, RHOA and CDC42. Negatively regulates leukotriene production in neutrophils.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11809807, ECO:0000269|PubMed:19414807}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Colocalizes together with ZAP70 in the immunological synapse. {ECO:0000250}.
Interaction partners:
- Tyrosine-protein kinase Lck
- Rho-related GTP-binding protein RhoB
- Tyrosine-protein kinase ZAP-70
- Rho GDP-dissociation inhibitor 1
- Paired box protein Pax-5
- Rho GDP-dissociation inhibitor 2
- Serine/threonine-protein kinase PAK 6
- Rho GDP-dissociation inhibitor 3
- B-cell lymphoma 6 protein
- Single-stranded DNA cytosine deaminase
Sequence:
MLSSIKCVLVGDSAVGKTSLLVRFTSETFPEAYKPTVYENTGVDVFMDGIQISLGLWDTAGNDAFRSIRPLSYQQADVVLMCYSVANHNSFLNLKNKWIGEIRSNLPCTPVLVVATQTDQREMGPHRASCVNAMEGKKLAQDVRAKGYLECSALSNRGVQQVFECAVRTAVNQARRRNRRRLFSINECKIF
Protein: Large ribosomal subunit protein eL22 (60S ribosomal protein L22) (Heparin-binding protein HBp15) (P67985)
Organism: Sus scrofa (Pig)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P35268}.
Interaction partners:
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein eL38
- Uncharacterized protein.
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein eL34
- Ribosomal protein L24.
- Large ribosomal subunit protein eL27
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein eL36
Sequence:
MAPVKKLVAKGGKKKKQVLKFTLDCTHPVEDGIMDAANFEQFLQERIKVNGKAGNLGGGVVTIERSKSKITVTSEVPFSKRYLKYLTKKYLKKNNLRDWLRVVANSKESYELRYFQINQDEEEEEDED
Protein: Outer membrane protein (Q87AV4)
Organism: Xylella fastidiosa (strain Temecula1 / ATCC 700964)
Subcellular location: Cell outer membrane {ECO:0000256|ARBA:ARBA00004571}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004571}.
Interaction partners:
Sequence:
MPCSFLYPLTQGAVMKKKILTAALLGGIAIIQVASAQEFDDRWYLAGSTGFNFQDKRRLTNDAPFFALGIGKFINPVWSIDGTLNYQNPQFKRNKDLNWSQYGFSVDFRRHFIQDNRGWNPYLLLGAGYQRSEEEFDNTPNVNSPGERKKGGFAAKVGAGLQTTFRSRVAVRAEVAYRGDHDKDSVRQPVAGVAAPSSKKWFGDTLASIGVVIPFGPAASSPTPPPAPPAPTPPPPPPAPSCAELDSDGDGVNDCDDKCPNSQPGQTIGPDGCPVPVSIDLKGVNFDFDKSKLRPDAVAVLKEATEILRRYPDLHVEVAGHTDSTGPAAYNKKLSERRAKVVYDYLRNNGIDASRLIGPVGYGETHPIDTNKTPAGRAKNRRTELNVQN
Protein: Calcium-binding protein 39 (MO25alpha) (Protein Mo25) (Q06138)
Organism: Mus musculus (Mouse)
Function: Component of a complex that binds and activates STK11/LKB1. In the complex, required to stabilize the interaction between CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta) and STK11/LKB1 (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Serine/threonine-protein kinase STK11
- STE20-related kinase adapter protein alpha
- STE20-related kinase adapter protein beta
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- Serine/threonine-protein kinase 25
- Calcium-binding protein 39-like
- Serine/threonine-protein kinase 26
- Serine/threonine-protein kinase 24
- STE20/SPS1-related proline-alanine-rich protein kinase
Sequence:
MPFPFGKSHKSPADIVKNLKESMAVLEKQDISDKKAEKATEEVSKNLVAMKEILYGTNEKEPQTEAVAQLAQELYNSGLLGTLVADLQLIDFEGKKDVAQIFNNILRRQIGTRTPTVEYICTQQNILFMLLKGYESPEIALNCGIMLRECIRHEPLAKIILWSEQFYDFFRYVEMSTFDIASDAFATFKDLLTRHKLLSAEFLEQHYDRFFSEYEKLLHSENYVTKRQSLKLLGELLLDRHNFTIMTKYISKPENLKLMMNLLRDKSRNIQFEAFHVFKVFVANPNKTQPILDILLKNQTKLIEFLSKFQNDRTEDEQFNDEKTYLVKQIRDLKRAAQQEA
Protein: Phospholipid phosphatase 2 (K7EMK9)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MQRRWVFVLLDVLCLLVGFSSPPASLPFAILTLVNAPYKRGFYCGDDSIRYPYRPDTITHGLMAGVTITATVILVSAGEAYLVYTDRLYSRSDFNNYVAAVYKVLGTFLFGAAVSQSLTDLAKYMIGRLRPNFLAVCDPDWSRVNCSVYVQLEKVCRGNPADVTEARLSFYSGHSSFG
Protein: Ataxin-3 (EC 3.4.19.12) (Machado-Joseph disease protein 1 homolog) (Q9CVD2)
Organism: Mus musculus (Mouse)
Function: Deubiquitinating enzyme involved in protein homeostasis maintenance, transcription, cytoskeleton regulation, myogenesis and degradation of misfolded chaperone substrates (By similarity). Binds long polyubiquitin chains and trims them, while it has weak or no activity against chains of 4 or less ubiquitins (By similarity). Involved in degradation of misfolded chaperone substrates via its interaction with STUB1/CHIP: recruited to monoubiquitinated STUB1/CHIP, and restricts the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Interacts with key regulators of transcription and represses transcription: acts as a histone-binding protein that regulates transcription (By similarity). Regulates autophagy via the deubiquitination of 'Lys-402' of BECN1 leading to the stabilization of BECN1.
Subcellular location: Nucleus matrix {ECO:0000250|UniProtKB:P54252}. Nucleus {ECO:0000250|UniProtKB:P54252}. Lysosome membrane {ECO:0000250|UniProtKB:P54252}; Peripheral membrane protein {ECO:0000250|UniProtKB:P54252}. Note=Predominantly nuclear, but not exclusively, inner nuclear matrix. Recruited to lysosomal membrane in response to amino acid deprivation by the RagA/RRAGA-RagB/RRAGB complex. {ECO:0000250|UniProtKB:P54252}.
Interaction partners:
- Transitional endoplasmic reticulum ATPase
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- E3 ubiquitin-protein ligase parkin
- Beclin-1
- Ataxin-2
- Forkhead box protein O4
- UV excision repair protein RAD23 homolog A
- E3 ubiquitin-protein ligase CHIP
- Ataxin-2-like protein
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
Sequence:
MESIFHEKQEGSLCAQHCLNNLLQGEYFSPVELSSIAHQLDEEERLRMAEGGVTSEDYRTFLQQPSGNMDDSGFFSIQVISNALKVWGLELILFNSPEYQRLRIDPINERSFICNYKEHWFTVRKLGKQWFNLNSLLTGPELISDTYLALFLAQLQQEGYSIFVVKGDLPDCEADQLLQMIKVQQMHRPKLIGEELAHLKEQSALKADLERVLEAADGSGIFDEDEDDLQRALAISRQEIDMEDEEADLRRAIQLSMQGSSRSMCENSPQTSSPDLSSEELRRRREAYFEKQQQQQQEVDRPGPLSYPRERPTTSSGGRRSDQGGDAVSEEDMLRAAVTMSLETAKDNLKAERKK