wanglab/gogpt-training-data huggingface dataset:
Protein: Type IV inositol polyphosphate 5-phosphatase 7 (At5PTase7) (EC 3.1.3.36) (EC 3.1.3.86) (Protein CVP2 LIKE 1) (Protein CVL1) (Q0WQ41)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Has phosphatase activity toward PtdIns(4,5)P2 and at a lower extent toward PtdIns(3,4,5)P3 but not toward Ins(1,4,5)P3. Acts redundantly with CVP2 for maintaining vascular continuity. Regulates phosphoinositide-dependent VAN3 localization. Functions in salt stress response by regulating reactive oxygen species (ROS) production and stress-responsive genes expression.
Subcellular location: Nucleus. Cell membrane; Peripheral membrane protein {ECO:0000269|PubMed:21677096}.
Interaction partners:
- Phosphoinositide phosphatase SAC6
- Phosphoinositide phosphatase SAC7
- Phosphoinositide phosphatase SAC8
- ADP-ribosylation factor GTPase-activating protein AGD3
- CLAVATA3/ESR
- Phosphatidylinositol 4-phosphate 5-kinase 7
- Phosphatidylinositol 4-phosphate 5-kinase 1
- ADP-ribosylation factor GTPase-activating protein
- Phosphatidylinositol 4-phosphate 5-kinase 2
- Protein BREVIS RADIX
Sequence:
MRDDKTKKSKLSWSKKMVRKWFNIKSKTEKFQADVSLPQGVEVEHRNSFSEREPCTIKKSKTEKLNKNWEQQARQRKMNYENPRIIDVQNHSIFVATWNVAGRSPPEDLNLDEWLHSSAPADIYVLGFQEIVPLNAGNVLGAEDNGPAKKWHSLIRKTLNNLPGASSACHTPSPIPVPIAEIDADFSGSSRQKNETFFNRRSFQTPSVWSMEENDPSISQPRLDRRFSVCDRVFFSHRPSDFDPSFRCGHRPSDYSRRPSDYSRPSDYYSRPSNYSRPSDVSRWGSSDDDNGPGDSPSTFLNSPGSFLGSAANENGYRTPWNSSQYCLVASKQMVGIFLTIWVKSELREHVKNMKVSCVGRGLMGYLGNKGSISISMLLHQTSFCFVCTHLTSGQKEGDELRRNSDVMEILKKTRFPRVQSSADEKSPENILQHDRVIWLGDLNYRIALSYRSAKALVEMQNWRALLENDQLRIEQKRGHVFKGWNEGKIYFPPTYKYSNNSDRYAGGDLHPKEKRRTPAWCDRILWHGEGLHQLSYVRGESRFSDHRPVYGIFSAEVESNHKRSKRTNSHSTARVEAEELLPYARGYTELTFF
Protein: TIA1 cytotoxic granule-associated RNA binding protein (A0A8I6AQH6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
LRQEYVGNLSRDVTEALILQLFSQIGPCKNCKMIMDTAGNDPYCFVEFHEHRHAAAALAAMNGRKIMGKEVKVNWATTPSSQKKDTSNHFHVFVGDLSPEITTEDIKAAFAPFGRISDARVVKDMATGKSKGYGFVSFFNKWDAENAIQQMGGQWLGGRQIRTNWATRKPPAPKSTYESNTKQLSYDEVVSQSSPGNCTVYCGGVTSGLTEQLMRQTFSPFGQIMEIRVFPDKGYSFIRFSSHESAAHAIVSVNGTTIEGHVVKCYWGKETLDMINPVQQQNQIGYPPAYGQWGQWYGNAQQIGQYVPNGWQVPAYGMYGQPWSQQGFNQTQSSAPWMGPNYSVPPPQGQNGGMLPNQPAGYRVAGYETQ
Protein: Stimulated by retinoic acid gene 8 protein (P70278)
Organism: Mus musculus (Mouse)
Function: Meiosis-inducer required for the transition into meiosis for both female and male germ cells. In female germ cells, acts downstream of ZGLP1 as a key effector of the meiotic program: required for premeiotic DNA replication and subsequent events in meiotic prophase. During spermatogenesis, next to its role in meiotic initiation, promotes (but is not required for) spermatogonial differentiation. In complex with MEIOSIN, directly activates the transcription of a subset of critical meiotic genes playing a central role in cell-cycle switching from mitosis to meiosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19805549, ECO:0000269|PubMed:32032549, ECO:0000269|PubMed:8896602}. Nucleus {ECO:0000269|PubMed:19805549, ECO:0000269|PubMed:32032549}. Note=Shuttles between nucleus and cytoplasm (PubMed:19805549). Nuclear export is XPO1-dependent (PubMed:19805549). {ECO:0000269|PubMed:19805549}.
Interaction partners:
- Deleted in azoospermia-like
- Spermatogenesis- and oogenesis-specific basic helix-loop-helix-containing protein 1
- Nanos homolog 2
- Synaptonemal complex protein 3
- Meiotic recombination protein REC8 homolog
- ATP-dependent RNA helicase DDX4
- Cytochrome P450 26B1
- Meiotic recombination protein SPO11
- Predicted gene 4969.
- Meiotic recombination protein DMC1/LIM15 homolog
Sequence:
MATPGEGNQPSDDGAPQPLAQLQKLEPRVVRRRLSQARHRATLVGLFNNLRKAVYSQSDITASKWQVLNRTKIHIQEQEESLDKLLKLKASFNLQDGNPNSLEEVKEEYARMYSENDSVFLNSFLQDSPPEWFPSEAVGPDAEEEGEEEGEEEGEEGEEEEEGDEEGEEEEENGEEREVEEYQEEEEEEEEEEKKVDLSHSSSTLLPDLMEFERYLNFYKQTMDLLTMNSIISAHEVTLPIVSAAISHLWQTLSEEKKARLLQVWEQQHSAFADLTEACLELAGVEGSMKDSGVDSQGASCSLESTPEEILFEDAFDVASFLDKSEAQHMSNISAMFATCNSENPEEKFQLYIQIIEFFKSLGCVNTPLNQEPEPPDDDDAMLLKCLETFDDL
Protein: Protein LAZ1 homolog 1 (Lazarus1 homolog 1) (Q94CA0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Accelerated cell death 11
Sequence:
MEWRGILCSLLFIVSVGESSSRFGIMWHPNLGVDSGQYLTWPILSASVFVVIAILLPMYLIFEHLASYNQPEEQKFLIGLILMVPVYAVESFLSLVNSEAAFNCEVIRDCYEAFALYCFERYLIACLDGEERTIEFMEQQTVITQSTPLLEGTCSYGVVEHPFPMNCFVKDWSLGPQFYHAVKIGIVQYMILKMICALLAMILEAFGVYGEGKFAWNYGYPYLAVVLNFSQTWALYCLVQFYNVIKDKLAPIKPLAKFLTFKSIVFLTWWQGIIVAFLFSMGLVKGSLAKELKTRIQDYIICIEMGIAAVVHLYVFPAAPYKRGERCVRNVAVMSDYASIDVPPDPEEVKDSERTTRTRYGRHDDREKRLNFPQSVRDVVLGSGEIIVDDMRFTVSHVVEPVERGIAKINRTFHQISENVKRFEQQKKTTKDDSYVIPLNQWAKEFSDVHENLYDGGSVSDSGLGSTNRHHQSRVSGLWTRMRR
Protein: Serine/threonine-protein kinase Nek10 (EC 2.7.11.1) (Never in mitosis A-related kinase 10) (NimA-related protein kinase 10) (Q6ZWH5)
Organism: Homo sapiens (Human)
Function: Plays a role in the cellular response to UV irradiation. Mediates G2/M cell cycle arrest, MEK autoactivation and ERK1/2-signaling pathway activation in response to UV irradiation. In ciliated cells of airways, it is involved in the regulation of mucociliary transport.
Interaction partners:
- Sodium bicarbonate cotransporter 3
- Cytochrome c oxidase assembly protein COX11
- TOX high mobility group box family member 3
- Lymphocyte-specific protein 1
Sequence:
MPDQDKKVKTTEKSTDKQQEITIRDYSDLKRLRCLLNVQSSKQQLPAINFDSAQNSMTKSEPAIRAGGHRARGQWHESTEAVELENFSINYKNERNFSKHPQRKLFQEIFTALVKNRLISREWVNRAPSIHFLRVLICLRLLMRDPCYQEILHSLGGIENLAQYMEIVANEYLGYGEEQHTVDKLVNMTYIFQKLAAVKDQREWVTTSGAHKTLVNLLGARDTNVLLGSLLALASLAESQECREKISELNIVENLLMILHEYDLLSKRLTAELLRLLCAEPQVKEQVKLYEGIPVLLSLLHSDHLKLLWSIVWILVQVCEDPETSVEIRIWGGIKQLLHILQGDRNFVSDHSSIGSLSSANAAGRIQQLHLSEDLSPREIQENTFSLQAACCAALTELVLNDTNAHQVVQENGVYTIAKLILPNKQKNAAKSNLLQCYAFRALRFLFSMERNRPLFKRLFPTDLFEIFIDIGHYVRDISAYEELVSKLNLLVEDELKQIAENIESINQNKAPLKYIGNYAILDHLGSGAFGCVYKVRKHSGQNLLAMKEVNLHNPAFGKDKKDRDSSVRNIVSELTIIKEQLYHPNIVRYYKTFLENDRLYIVMELIEGAPLGEHFSSLKEKHHHFTEERLWKIFIQLCLALRYLHKEKRIVHRDLTPNNIMLGDKDKVTVTDFGLAKQKQENSKLTSVVGTILYSCPEVLKSEPYGEKADVWAVGCILYQMATLSPPFYSTNMLSLATKIVEAVYEPVPEGIYSEKVTDTISRCLTPDAEARPDIVEVSSMISDVMMKYLDNLSTSQLSLEKKLERERRRTQRYFMEANRNTVTCHHELAVLSHETFEKASLSSSSSGAASLKSELSESADLPPEGFQASYGKDEDRACDEILSDDNFNLENAEKDTYSEVDDELDISDNSSSSSSSPLKESTFNILKRSFSASGGERQSQTRDFTGGTGSRPRPALLPLDLLLKVPPHMLRAHIKEIEAELVTGWQSHSLPAVILRNLKDHGPQMGTFLWQASAGIAVSQRKVRQISDPIQQILIQLHKIIYITQLPPALHHNLKRRVIERFKKSLFSQQSNPCNLKSEIKKLSQGSPEPIEPNFFTADYHLLHRSSGGNSLSPNDPTGLPTSIELEEGITYEQMQTVIEEVLEESGYYNFTSNRYHSYPWGTKNHPTKR
Protein: Pseudin-3 (P83190)
Organism: Pseudis paradoxa (Paradoxical frog)
Function: Possesses antifungal activity against C.albicans and is also active against E.coli and S.aureus.
Subcellular location: Secreted {ECO:0000269|PubMed:11689009}.
Interaction partners:
Sequence:
GINTLKKVIQGLHEVIKLVSNHE
Protein: Chaperonin-containing T-complex member BBS12 (Bardet-Biedl syndrome 12 protein homolog) (Q5SUD9)
Organism: Mus musculus (Mouse)
Function: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Involved in adipogenic differentiation.
Subcellular location: Cell projection, cilium {ECO:0000250|UniProtKB:Q6ZW61}. Note=Located within the basal body of the primary cilium of differentiating preadipocytes. {ECO:0000250|UniProtKB:Q6ZW61}.
Interaction partners:
- BBSome complex assembly protein BBS10
- BBSome complex member BBS7
- Protein PTHB1
- BBSome complex member BBS2
- BBSome complex member BBS4
- BBSome complex member BBS1
- BBSome complex member BBS5
- Tetratricopeptide repeat protein 8
- Leucine zipper transcription factor-like protein 1
- Molecular chaperone MKKS
Sequence:
MEMACRVINRRRHVGLQQLLSFAQTGRSFLGPVKATKFITDAECHESVLISSTVRLLEGLDLTCAVGHLLNEAVQAQNNTYKIGTSTLLFLVGAWSRAVEDCLHLGIPTTVIVSVMSEGLNSCIEAVVSLQVPIHNVFDHMDNTSTVYKLETVNATLCPFLQDPSGSGLLQEKRDFKDATSPLLSTYSLSGRHAESPKFFKPQNNLETEKNTLQVLKNNLYTDSFCKKSALAHSRHFNRTDNSHWISRHDGFLEQLESTPKVLRCNDFGELAVGLSHGDHSSMALAKAAVRLQWQSLCLQQANWMAPFMFDISRLLTCCIPGLPETFSRVGLGYVTFVTMSSITLIKELQDQPFRVILIEGDLTESYRHLGFNKSVNIKTKLDSGELSEDSAEELWTNHVLQVLIQFNVTLILVQGSVSEHLTEKCMHSKRLVIGAVNGSVLQAFAEATRAVPVAYVTQVNEDCVGSGVSVTFWMSPHDINRSNRIAILLTAEGINLITAVLTSPASAQMETKEDRFWSCVYRLYHALKEEKVFLGGGAVEFLCLSHLQILAEQSLNRGNHACLGWLPDSSSWMASSLSVYRPTVLKSLAGGWHEFLSAIMCNTATHPSAVEARTFIQQHVQNAIDSGSPSSYILSEYSKLSSGVFHSGISDNLELVPRVYDTVTPKIEAWRRALDVVLLVLQTDSEIITGLVHTEMNSQELDGVLFL
Protein: Alpha-galactosidase 1 (AtAGAL1) (EC 3.2.1.22) (Alpha-D-galactoside galactohydrolase 1) (Melibiase 1) (Q9FT97)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May regulate leaf (and possibly other organ) development by functioning in cell wall loosening and cell wall expansion.
Subcellular location: Secreted, cell wall {ECO:0000250|UniProtKB:Q8RX86}. Secreted, extracellular space, apoplast {ECO:0000250|UniProtKB:Q8RX86}.
Interaction partners:
- Probable galactinol--sucrose galactosyltransferase 1
- Probable galactinol--sucrose galactosyltransferase 5
- Probable galactinol--sucrose galactosyltransferase 2
- Probable galactinol--sucrose galactosyltransferase 6
- alpha-D-xyloside xylohydrolase
- Probable galactinol--sucrose galactosyltransferase 4
- beta-galactosidase
- Aldose 1-epimerase
- Beta-hexosaminidase 3
- Beta-hexosaminidase 1
Sequence:
MSRRAMVIKMPILMILISSMVMTMVESSRSVNNGHDDSEILRRHLLTNGLGVTPPMGWNSWNHFSCNIDEKMIKETADALVTTGLSKLGYNYVNIDDCWAEISRDSKGSLVPKKSTFPSGIKAVADYVHSKGLKLGIYSDAGYFTCSKTMPGSLGYEEHDAKTFAEWGIDYLKYDNCNSDGSKPTVRYPVMTRALMKSGRPIFHSLCEWGDMHPALWGSPVGNSWRTTNDIKDTWLSMISIADMNEVYAEHARPGGWNDPDMLEVGNGGMTKDEYIVHFSIWAISKAPLLLGCDIRNMTKETMEIVANKEVIAINQDPHGVQAKKVRMEGDLEVWAGPLSGYRVALLLLNRGPSRTSITALWEDIEIPANSIVEARDLWEHQTLKQKFVGNLTATVDSHACKLYVLKPVA
Protein: Ferric uptake regulator, Fur family (D2BRN2)
Organism: Dickeya zeae (strain Ech586) (Dickeya dadantii (strain Ech586))
Interaction partners:
- ABC transporter related protein
Sequence:
MDSTNPDKLVAQAERLCQQRNVRLTPQRQEVLRLMALQPGAISAYDLLDLLRVSEPQAKPPTVYRALDFLLEQGFIHKVESTNSYVLCHHFEEHSHTSALFICDRCGQVTERQTEGVEETLHQLAKQAGFALRHSVVEAHGLCGECQQVESCEHRDSCHHDHSIPVKKR
Protein: Carbonic anhydrase 12 (EC 4.2.1.1) (Carbonate dehydratase XII) (Carbonic anhydrase XII) (CA-XII) (Tumor antigen HOM-RCC-3.1.3) (O43570)
Organism: Homo sapiens (Human)
Function: Reversible hydration of carbon dioxide.
Subcellular location: Membrane; Single-pass type I membrane protein. Cell membrane {ECO:0000269|PubMed:26911677}.
Interaction partners:
- 1,25-dihydroxyvitamin D
- Carbonic anhydrase 9
Sequence:
MPRRSLHAAAVLLLVILKEQPSSPAPVNGSKWTYFGPDGENSWSKKYPSCGGLLQSPIDLHSDILQYDASLTPLEFQGYNLSANKQFLLTNNGHSVKLNLPSDMHIQGLQSRYSATQLHLHWGNPNDPHGSEHTVSGQHFAAELHIVHYNSDLYPDASTASNKSEGLAVLAVLIEMGSFNPSYDKIFSHLQHVKYKGQEAFVPGFNIEELLPERTAEYYRYRGSLTTPPCNPTVLWTVFRNPVQISQEQLLALETALYCTHMDDPSPREMINNFRQVQKFDERLVYTSFSQVQVCTAAGLSLGIILSLALAGILGICIVVVVSIWLFRRKSIKKGDNKGVIYKPATKMETEAHA
Protein: 2-dehydro-3-deoxygluconokinase (EC 2.7.1.45) (2-keto-3-deoxygluconokinase) (3-deoxy-2-oxo-D-gluconate kinase) (KDG kinase) (P45416)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Function: Catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG).
Interaction partners:
- 2-dehydro-3-deoxy-phosphogluconate aldolase
- Mannonate dehydratase
- 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase
- Starvation sensing protein rspA
- Altronate hydrolase
- Ribulose-phosphate 3-epimerase
- Ribulokinase
- Uncharacterized protein
- Probable tautomerase K2
Sequence:
MTTKNIAIIGECMIELSQKGADLNRGFGGDTLNTAVYISRQVKPDALDVHYVTALGTDSFSSEMMASWQKEGVKTDLIQRLDNKLPGLYFIETDATGERTFYYWRNDAAARYWLESPDADTISQQLAQFDYIYLSGISLAILNQASRARLLTVLRACRANGGKVIFDNNYRPRLWQSKEETRQAYSDMLACTDIAFLTLDDEDMLWGELPVDEVLKRTHGAGVMEVVIKRGADACLVSIQGEALLEVPAIKLPKEKVVDTTAAGDSFSAGYLSVRLNGGSAQDAAKRGHLTASTVIQYRGAIIPLEAMPA
Protein: Eukaryotic translation initiation factor 2 subunit 2 (Eukaryotic translation initiation factor 2 subunit beta) (eIF2-beta) (P41375)
Organism: Drosophila melanogaster (Fruit fly)
Function: eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This preinitiation complex mediates ribosomal recognition of a start codon during the scanning process of the leader region.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P56329}.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit 3
- Eukaryotic translation initiation factor 5
- Eukaryotic translation initiation factor 2 subunit 1
- Translation initiation factor eIF2B subunit gamma
- Translation initiation factor eIF2B subunit epsilon
- Eukaryotic translation initiation factor 4C
- Translation initiation factor eIF2B subunit delta
- Eukaryotic translation initiation factor eIF1
- Translation initiation factor eIF2B subunit alpha
- Eukaryotic translation initiation factor 3 subunit A
Sequence:
MDAEDGFDPTLLKKKKKKKTTFDLDAALGLEDDTKKEDPQDEASAEGGAAAEEDNLDLESFGKKKKKKKKPFNMDEIEAAIPSFGGDDVAASEEPEEEEINLDMDFSMAKKKKKSKKKELDELFADQADDDKSEDKENDEDNSSTWFGSDRDYTYDELLKRVFEIILDKNPDMAAGRKPKFVMRPPQVLRVGTKKTSFANFMDIAKTLHRLPKHLLDFLLAELGTSGSMDGNQQLIIKGRFQPKQIENVLRRYIKEYVTCHTCRSPETILQKDTRLFFLQCESCGSRCSVASIKSGFQAVTGKRAAIRAKTT
Protein: Thiosulfate sulfurtransferase GlpE (EC 2.8.1.1) (P0A6V5)
Organism: Escherichia coli (strain K12)
Function: Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide. The relatively low affinity of GlpE for both thiosulfate and cyanide suggests that these compounds are not the physiological substrates. Thioredoxin 1 or related dithiol proteins could instead be the physiological sulfur-acceptor substrate. Possible association with the metabolism of glycerol-phosphate remains to be elucidated.
Subcellular location: Cytoplasm.
Interaction partners:
- Rhomboid protease GlpG
- 3-mercaptopyruvate sulfurtransferase
- Sulfite reductase flavoprotein alpha-component
- Sulfite reductase hemoprotein beta-component
- Alkanesulfonate monooxygenase
- Putative cytochrome YdhU
- Phosphoadenosine 5'-phosphosulfate reductase
- Alpha-ketoglutarate-dependent taurine dioxygenase
- Glycogen phosphorylase
- Maltodextrin phosphorylase
Sequence:
MDQFECINVADAHQKLQEKEAVLVDIRDPQSFAMGHAVQAFHLTNDTLGAFMRDNDFDTPVMVMCYHGNSSKGAAQYLLQQGYDVVYSIDGGFEAWQRQFPAEVAYGA
Protein: Methionine aminopeptidase 1B, chloroplastic (MAP 1B) (MetAP 1B) (EC 3.4.11.18) (Peptidase M 1B) (Q9FV52)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Subcellular location: Plastid, chloroplast {ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:11060042}.
Interaction partners:
- Methionine aminopeptidase 2A
- Peptide deformylase 1B, chloroplastic/mitochondrial
- F-box/LRR-repeat protein At1g48400
- Replication factor C large subunit
- Putative F-box protein At1g47300
- Peptide deformylase 1A, chloroplastic/mitochondrial
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein uL18z
- Large ribosomal subunit protein uL23y
- Large ribosomal subunit protein uL23z
Sequence:
MASSVFLSSFSSSSSLQLCSSFHGEYLAPSRCFLGAPVTSSSLSLSGKKNSYSPRQFHVSAKKVSGLEEAIRIRKMRELETKSKVRRNPPLRRGRVSPRLLVPDHIPRPPYVESGVLPDISSEFQIPGPEGIAKMRAACELAARVLNYAGTLVKPSVTTNEIDKAVHDMIIEAGAYPSPLGYGGFPKSVCTSVNECMCHGIPDSRQLQSGDIINIDVTVYLDGYHGDTSRTFFCGEVDEGFKRLVKVTEECLERGIAVCKDGASFKKIGKRISEHAEKFGYNVVERFVGHGVGPVFHSEPLIYHYRNDEPGLMVEGQTFTIEPILTIGTTECVTWPDNWTTLTADGGVAAQFEHTILITRTGSEILTKC
Protein: Flagellar biosynthetic protein FliP (P0AC05)
Organism: Escherichia coli (strain K12)
Function: Plays a role in the flagellum-specific transport system.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}. Bacterial flagellum basal body {ECO:0000269|PubMed:15919996}.
Interaction partners:
- Flagellar motor switch protein FliN
- Flagellar motor switch protein FliG
- Flagellar motor switch protein FliM
- Flagellar biosynthetic protein FliR
- Flagellar biosynthetic protein FlhB
- Flagellum-specific ATP synthase
- Flagellar biosynthetic protein FliQ
- Flagellar assembly protein FliH
- Flagellar biosynthesis protein FlhA
- Flagellar M-ring protein
Sequence:
MRRLLSVAPVLLWLITPLAFAQLPGITSQPLPGGGQSWSLPVQTLVFITSLTFIPAILLMMTSFTRIIIVFGLLRNALGTPSAPPNQVLLGLALFLTFFIMSPVIDKIYVDAYQPFSEEKISMQEALEKGAQPLREFMLRQTREADLGLFARLANTGPLQGPEAVPMRILLPAYVTSELKTAFQIGFTIFIPFLIIDLVIASVLMALGMMMVPPATIALPFKLMLFVLVDGWQLLVGSLAQSFYS
Protein: Uncharacterized protein (Q54NE5)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MDQHVNPFSGFNPISLSFRDDDNLLNNFNHHLSTEFGNLDEFGLGSNRSNNDQFLSRFSNVSDKVNLNNVGNGFLDDTRVGSSSGGGGGGSSGGNRVENYSYVGNITDNDSRNHRNQSVLFDSRVPDNNGINNNHHNNNNGNNGNNNFGDSFRNSALHKQNSFISSIKNLHNQRLSQDSFINKHLSRYQQSPSHQNSQQPQLQQQTQNQPNQNFQNSLPFDNFNGDDNILRDTTFSFNVSNPNIDINDVDFYGSQNNRFNKDFINNHNNNPNIDNIGNTRQNGSNQFTDINGQSVIDTSLMYSPATNYQGDDDDDDDDHNNNNNNINNDGYQNSINNKSQNYNNSYNNYSYQHQYQEPHVEVYEDDQYLDNNDNDNNHNDNNNNNNGNDNYKDDQMNHQSLNNSNQAFIQDNGEAKTPGTYFQYKSPHMGRLSGTGSGIEFGETINDDDHYERNKNENNNDNNELNFSRNQSMNDPTADNNNNIINNNNSINQTFGNSGNQSMNGGGGGGGYQNTPNGTTPNHNSGHNQSMNGGVSGRMNNYVSPILTNISGDVSNRTGQNDTTFASIGVPNDPSHVGYTPTRGNLDYDTYQRLKERYLNPKQQQQQPSQPQLQPQLQHQHQQPQQSKQQPQPSQIQPKSPKIKNNSFLISSLINNSQYQQKMQQQEQEQEQPNRPKTPQHQQQQRPRTPQQQQQQQQHIEDINEENYDDGIIKYPMVVIEKRIDLGKCELEWILSRDIIVTNPHSKPVTLSNINIFGLDKDAFRIIVSDKTNNNNNTPSNNGLKQGELAPFPPIIIIQPLSHIFLKVEYIPNVDNLPKPESNGIHYANLVLTCSGTVPLNLNDSETEDEFRIQYIPQSGVYNLSIPINATPTADILNHEDLFYSYNNWDMGECNSNDTLTSNLSLKSQNGQKLTYEINGEGFSFEKLSNDQISLKFNLPEKQIYNANATIIDQLTGQKKLIKLSATITNNHHNNNNIDNNNNNSKTPTSQKPLIIDPSPTQSPSTLLSQQQKLEKIEKSKSFTPKFILKKEKLNDDSSSIGSSSDDNDNEDYENIDNNSRVPLSISNYVLENGIKLVYEERKKIYPIETLSMYCNFNSYNKINNNNNELIDIECISTQPDVFSISPSIFSVEPNSMIPLQIKYQPNNNIQLQRAAIIISTPSITKEKIKIDVIGITVPLDSTLYMPSSPPSPTYQSKRFNNIRKDNYYQDSNKLLPSTKIISDDQDNLNNINNSSVIFHNDDDDDDNNNNLPPSLYCNRKVVNFGGVKLGDTKSVLITLTSTLPHALHLNATFKQNDHSGSSSSNNSHSFFSIGNGEQLLISPHSKTEVEIIYTPLSISPHGSVVVFSSLNKQLSFSIPVLGYGGSAKMEVASSARNLDSIDNTSGSNNNNNNNIVLYVNKQSTDGKSVYCKFTVKNTGQRSGFVRAISFYPNSKSTIKPDRVSIGVGEQVDFRLEIHPNSSSGGGSINNLLSQLNGSLMNSTISPGKVKLYFGDEISRQRKIRSVHNRLENLKTDSMDSTSKEVSFDDEFLFDFKFKEEEIQDIQFKETFINENSQQINDSNSQNHNFDLDDYDDVELFFNNLSSIKITPIIGNPPTKQNNNINNNNNNNNNKMNNNNNNNNNNNNNNNNDIFSNLPPSTKKTTTSTTTTTTTATPINGREFELSEMDLNNTPFKATINLPFPTNSVLNANTTSFNAATTNIPPTTSASNNTNLKSILKKPQPSVYNNTNNNNNNNENNLFNTFENTLRFNPTVTTTTDGIKKSEEVRHYHIHQFEPDQQPPPQQQRKQQQQQQQPPQQQQPKQHTNGILFFYDNKITFGIVQIGQSSTNKVSISNASNATLNVRLSLPSPSPFILNHHTITLNPKTTTKVPIIFKPKEIGTFSQSLKVESIPKTLNDPILSDTCELISESKSIPF
Protein: Methyl-CpG-binding domain protein 4 (EC 3.2.2.-) (Methyl-CpG-binding protein MBD4) (Mismatch-specific DNA N-glycosylase) (Q9Z2D7)
Organism: Mus musculus (Mouse)
Function: Mismatch-specific DNA N-glycosylase involved in DNA repair. Has thymine glycosylase activity and is specific for G:T mismatches within methylated and unmethylated CpG sites. Can also remove uracil or 5-fluorouracil in G:U mismatches. Has no lyase activity. Was first identified as methyl-CpG-binding protein.
Subcellular location: Nucleus {ECO:0000269|PubMed:9774669}. Note=Nuclear, in discrete foci.
Interaction partners:
- G/T mismatch-specific thymine DNA glycosylase
- DNA
- Single-strand selective monofunctional uracil DNA glycosylase
- DNA
- DNA
Sequence:
MESPNLGDNRVRGESLVPDPPWDRCKEDIAVGLGGVGEDGKDLVISSERSSLLQEPTASTLSSTTATEGHKPVPCGWERVVKQRLSGKTAGKFDVYFISPQGLKFRSKRSLANYLLKNGETFLKPEDFNFTVLPKGSINPGYKHQSLAALTSLQPNETDVSKQNLKTRSKWKTDVLPLPSGTSESPESSGLSNSNSACLLLREHRDIQDVDSEKRRKSKRKVTVLKGTASQKTKQKCRKSLLESTQRNRKRASVVQKVGADRELVPQESQLNRTLCPADACARETVGLAGEEKSPSPGLDLCFIQVTSGTTNKFHSTEAAGEANREQTFLESEEIRSKGDRKGEAHLHTGVLQDGSEMPSCSQAKKHFTSETFQEDSIPRTQVEKRKTSLYFSSKYNKEALSPPRRKSFKKWTPPRSPFNLVQEILFHDPWKLLIATIFLNRTSGKMAIPVLWEFLEKYPSAEVARAADWRDVSELLKPLGLYDLRAKTIIKFSDEYLTKQWRYPIELHGIGKYGNDSYRIFCVNEWKQVHPEDHKLNKYHDWLWENHEKLSLS
Protein: Pentatricopeptide repeat-containing protein At1g79490, mitochondrial (Protein EMBRYO DEFECTIVE 2217) (Q9SAK0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Pentatricopeptide repeat-containing protein At2g17033
- Protein-S-isoprenylcysteine O-methyltransferase A
- Jacalin-related lectin 33
Sequence:
MIRGRTAKVIPRNVIFTLSRSSISESPLISPSRINPKLAGSFSFNIRLLSYFTVRNGFCPDCSVPRDPNFVGLTTQCRSIVRRFCSEKIGSSESSGWTEEVEYLDESGSVLHSGKGIRSVEPGLDDHVMVGGLKKPYMNASSVAKIVEVVQRWKWGPELETQLDKLQFVPNMVHITQSLKIVKEVDAALSLFRWAKKQPWYLPSDECYVVLFDGLNQGRDFVGIQSLFEEMVQDSSSHGDLSFNAYNQVIQYLAKAEKLEVAFCCFKKAQESGCKIDTQTYNNLMMLFLNKGLPYKAFEIYESMEKTDSLLDGSTYELIIPSLAKSGRLDAAFKLFQQMKERKLRPSFSVFSSLVDSMGKAGRLDTSMKVYMEMQGFGHRPSATMFVSLIDSYAKAGKLDTALRLWDEMKKSGFRPNFGLYTMIIESHAKSGKLEVAMTVFKDMEKAGFLPTPSTYSCLLEMHAGSGQVDSAMKIYNSMTNAGLRPGLSSYISLLTLLANKRLVDVAGKILLEMKAMGYSVDVCASDVLMIYIKDASVDLALKWLRFMGSSGIKTNNFIIRQLFESCMKNGLYDSARPLLETLVHSAGKVDLVLYTSILAHLVRCQDEDKERQLMSILSATKHKAHAFMCGLFTGPEQRKQPVLTFVREFYQGIDYELEEGAARYFVNVLLNYLVLMGQINRARCVWKVAYENKLFPKAIVFDQHIAWSLDVRNLSVGAALIAVVHTLHRFRKRMLYYGVVPRRIKLVTGPTLKIVIAQMLSSVESPFEVSKVVLRAPGELVMEWFKKPIVQQFLLNEIPSRSDILMHKMNVMFPSSAPELRSMSPPKPLMSSKAF
Protein: Endoglucanase 10 (EC 3.2.1.4) (Endo-1,4-beta glucanase 10) (Q8LCP6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Beta-glucosidase 7
- KH domain-containing protein At4g18375
- Cellulose synthase-like protein B4
- Uncharacterized protein At5g48480
- GDSL esterase/lipase CPRD49
- Cytochrome P450 71B26
Sequence:
MEEKSKSRGWCGWFIAIIVLASVILAVVYTVKLRTKKSGDDDGGGPVPGPPGAIDKKYADALKLALQFFDIQKSGKLENNKIPWRGDSGLKDGSEDNLDLSKGLYDAGDHIKFGFPMAFTATVLSWSILEYGDQMNAVNQLDPAKDSLRWITDYLIKAHPSDNVLYIQVGDPKVDHPCWERPEDMKEKRPLTKIDVDTPGTEVAAETAAAMASASLVFKDSDPTYSATLLKHAKQLFNFADTKRGSYSVNIPEVQKFYNSTGYGDELLWAASWLYHATEDKTYLDYVSNHGKEFASFGNPTWFSWDNKLAGTQVLLSRLLFFKKDLSGSKGLGNYRNTAKAVMCGLLPKSPTSTASRTNGGLIWVSEWNSMQQSVSSAFLASLFSDYMLTSRIHKISCDGKIFKATELRDFAKSQADYMLGKNPLGTSFVVGYGDKYPQFVHHRGASIPADATTGCLDGFKWFNSTKPNPNIAYGALVGGPFFNETFTDSRENPMQNEPTTYNNALLVGLLSSLVTTSSTLQSLK
Protein: Complement C8 gamma chain (A0A8I6A491)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MWTSGLCFLWHWTVDSDLEQCTPPPPCPITYCHRTAMLSPGAVLFFTLILMASSLGQRTRKPYGSTSPISTIQAQANFNAQQFAGTWLLVAVGSACRFLQEQGHRAEATTLHIAPQGAAMAASTFRKLDGICWQVRQLYGITGVPGRFLLQAPRARGPVHVVVAETDYQSFAILYLEQARRLSVKLYTRTLPVSDSALNAFEERVRGANLTEDQIFFFPKYVSGGVVCPRSGRQHLQERAPAFAAFLYHAVQAERQQ
Protein: Candida glabrata strain CBS138 chromosome E complete sequence (Q6FVI2)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Transcription factor
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
Sequence:
MSHEEVHDEFIAEDVTPNRPDETRGENGAPRRMLVREHRKIGRGAFGTVVQAYLTQDEQTWYGPFAIKKVPAQTEYKSRELQILRLTDHPNIVKLEYFFTHTSPKDNKVYQHLAMECLPETLQIEINRYTSNNLQLAIKHVKLYSYQIARGMLYLHALGICHRDIKPSNILVDPKTGVLKICDFGSAKRLEPNQPSISYICSRFYRAPELILGSTQYTTQVDIWGLGCVIGEMLIGRAIFQGQDPLLQLREIAKLLGPPDKKFIFFSNPRYTGPLYSTPLFNGTSLERFQKYFGHAGPDGIDLLMKVLKYEPELRFSPRRIMAHPFFDDLRNEKYFFPREQTQPVLLPELFNFNEFELQVIGELLQQIKPHSEEH
Protein: Pathogenesis-related thaumatin-like protein 3.4 (allergen Cry j 3.4) (Q5DWG2)
Organism: Cryptomeria japonica (Japanese cedar) (Cupressus japonica)
Function: May be involved in disease resistance.
Interaction partners:
Sequence:
MARAILWVLLTVMAVSLLLHAGVEGVNFDIENQCPYTVWAAGTPFGGGIELKRGQSWRVNVPGGARGRFWGRTGCSFDGNGRGRCNTGDCGGLLNCQGSGGVPSTLLEYALNQYQNLDFYDISLVDGFNLRMTVVLSNTNCKRIACNSDINSKCPGELKVVDGCRSACAAFNTPAYCCTGSFLDNCPPTGYSQFFKRECPLAYSYAKDDPTSTFTCPGGSDYKIIFCGNGDSQSNSTSTSSGSLYAVE
Protein: Erythrocyte membrane protein band 4.1 like 3 (A0A0J9YY18)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XTPEKKAEEERDEEEDKRRKGEEVTPISAIRHEGKTDSERTDTAADGETTATEELEKTQDDLMKHQTNISELKRTFLETSTDTAVTNEWEKRLSTSPVRLAARQEDAPMIEPLVPEETKQSSGEKLMDGSEIFSLLESARKPTEFIGGVTSTSQSWVQKMETKTESSGIETEPTVHHLPLSTEKVVQETVLVEERRVVHASGDASYSAGDSGDAAAQPAFTGIKGKEGSALTEGAKEEGGEEVAKAVLEQEETAAASRERQEEQSAAIHISETLEQKPHFESSTVKTETISFGSVSPGGVKLEISTKEVPVVHTETKTITYESSQ