wanglab/gogpt-training-data huggingface dataset:
Protein: SEC63-like (S. cerevisiae) (SEC63-like protein isoform 1) (A0A0S2Z5M1)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
Sequence:
MAGQQFQYDDSGNTFFYFLTSFVGLIVIPATYYLWPRDQNAEQIRLKNIRKVYGRCMWYRLRLLKPQPNIIPTVKKIVLLAGWALFLFLAYKVSKTDREYQEYNPYEVLNLDPGATVAEIKKQYRLLSLKYHPDKGGDEVMFMRIAKAYAALTDEESRKNWEEFGNPDGPQATSFGIALPAWIVDQKNSILVLLVYGLAFMVILPVVVGSWWYRSIRYSGDQILIRTTQIYTYFVYKTRNMDMKRLIMVLAGASEFDPQYNKDATSRPTDNILIPQLIREIGSINLKKNEPPLTCPYSLKARVLLLSHLARMKIPETLEEDQQFMLKKCPALLQEMVNVICQLIVMARNREEREFRAPTLASLENCMKLSQMAVQGLQQFKSPLLQLPHIEEDNLRRVSNHKKYKIKTIQDLVSLKESDRHTLLHFLEDEKYEEVMAVLGSFPYVTMDIKSQVLDDEDSNNITVGSLVTVLVKLTRQTMAEVFEKEQSICAAEEQPAEDGQGETNKNRTKGGWQQKSKGPKKTAKSKKKKPLKKKPTPVLLPQSKQQKQKQANGVVGNEAAVKEDEEEVSDKGSDSEEEETNRDSQSEKDDGSDRDSDREQDEKQNKDDEAEWQELQQSIQRKERALLETKSKITHPVYSLYFPEEKQEWWWLYIADRKEQTLISMPYHVCTLKDTEEVELKFPAPGKPGNYQYTVFLRSDSYMGLDQIKPLKLEVHEAKPVPENHPQWDTAIEGDEDQEDSEGFEDSFEEEEEEEEDDD
Protein: Zinc finger protein 950 (A0A0U1RPR9)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDAVTYDEVHVNFTQEEWALLDHSQKSLYRDVMLETYKNLTAIGYNWDDHNIEEHCQSSRRHGSRSAFSKSPPNTTN
Protein: NADH-ubiquinone oxidoreductase chain 2 (EC 7.1.1.2) (NADH dehydrogenase subunit 2) (P03892)
Organism: Bos taurus (Bovine)
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:17060615, ECO:0000269|PubMed:25209663}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- NADH dehydrogenase flavoprotein 2, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase 1 beta subcomplex subunit 11, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 3
- NADH-ubiquinone oxidoreductase chain 4L
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 12
- Cytochrome c oxidase subunit 3
- Cytochrome b
- Acyl carrier protein, mitochondrial
Sequence:
MNPIIFIIILLTIMLGTIIVMISSHWLLVWIGFEMNMLAIIPIMMKNHNPRATEASTKYFLTQSTASMLLMMAVIINLMFSGQWTVMKLFNPMASMLMTMALAMKLGMAPFHFWVPEVTQGIPLSSGLILLTWQKLAPMSVLYQIFPSINLNLILTLSVLSILIGGWGGLNQTQLRKIMAYSSIAHMGWMTAVLPYNPTMTLLNLIIYIIMTSTMFTMFMANSTTTTLSLSHTWNKTPIMTVLILATLLSMGGLPPLSGFMPKWMIIQEMTKNNSIILPTFMAITALLNLYFYMRLTYSTTLTMFPSTNNMKMKWQFPLMKKMTFLPTMVVLSTMMLPLTPMLSVLE
Protein: Seripauperin-20 (Q08322)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Seripauperin-10
- Seripauperin-16
- Seripauperin-18
- Seripauperin-14
- Seripauperin-4
- Seripauperin-12
- Seripauperin-24
- Seripauperin-2
- Seripauperin-11
- Seripauperin-3
Sequence:
MVKLTSIAAGVAAIAAGASATTTLAQSDERVNLVELGVYVSDIRAHLAQYYMFQAAHPTETYPVEVAEAVFNYGDFTTMLTGISPDQVTRMITGVPWYSTRLKPAISKALSKDGIYTIAN
Protein: WD repeat-containing protein 7 (TGF-beta resistance-associated protein TRAG) (Q920I9)
Organism: Mus musculus (Mouse)
Interaction partners:
- DmX-like protein 2
- Vacuolar ATPase assembly protein VMA22
- Ras-related protein Rab-3A
- DnaJ homolog subfamily C member 5
- Rab3 GTPase-activating protein catalytic subunit
- Protein rogdi homolog
- V-type proton ATPase subunit C 1
Sequence:
MAGNSLVLPIVLWGRKAPTHCISSILLTDDGGTIVTGCHDGQICLWDVSVELEVNPRALLFGHTASITCLSKACASGDKRYTVSASANGEMCLWDVNDGRCIEFTKLACTHTGIQFYQFSVGNQQEGRLLCHGHYPEILVVDATSLEVLYSLVSKISPDWISSMSIIRSQRTQEDTVVALSVTGILKVWIVTSEMSGMQDTEPIFEEESKPIYCQNCQSISFCAFTQRSLLVVCSKYWRVFDAGDYSLLCSGPSENGQTWTGGDFVSADKVIIWTENGQSYIYKLPASCLPASDSFRSDVGKAVENLIPPVQHSLLDQKDKELVICPPVTRFFYGCKEYLHKLLIQGDSSGRLNIWNIADIAEKQEADEGLKMTTCISLQEAFDKLKPCPAGIIDQLSVIPNSNEPLKVTASVYIPAHGRLVCGREDGSIIIVPATQTAIVQLLQGEHMLRRGWPPHRTLRGHRNKVTCLLYPHQVSARYDQRYLISGGVDFSVIIWDIFSGEMKHIFCVHGGEITQLLVPPENCSARVQHCICSVASDHSVGLLSLREKKCIMLASRHLFPIQVIKWRPSDDYLVVGCTDGSVYVWQMDTGALDRCAMGITAVEILNACDEAVPAAVDSLSHPAVNLKQAMTRRSLAALKNMAHHKLQTLATNLLASEASDKGNLPKYSHNSLMVQAIKTNLTDPDIHVLFFDVEALIIQLLTEEASRPNTALISPENLQKASGSSDKGGSFLTGKRAAVLFQQVKETIKENIKEHLLDEEEDEEEARRQSREDSDPEYRASKSKPLTLLEYNLTMDTAKLFMSCLHAWGLNEVLDEVCLDRLGMLKPHCTVSFGLLSRGGHMSLMLPGYNQAAGKLLHAKAEVGRKLPAAEGVGKGTYTVSRAVTTQHLLSIISLANTLMSMTNATFIGDHMKKGPTRPPRPGTPDLSKARDSPPPSSNIVQGQIKQAAAPVVSARSDADHSGSDSASPALPTCFLVNEGWSQLAAMHCVMLPDLLGLERFRPPLLEMLARRWQDRCLEVREAAQALLLAELRRIEQAGRKETIDTWAPYLPQYMDHVISPGVTAEAMQTMAAAPDASGPEAKVQEEEHDLVDDDITAGCLSSVPQMKKISTSYEERRKQATAIVLLGVIGAEFGAEIEPPKLLTRPRSSSQIPEGFGLTSGGSNYSLARHTCKALTYLLLQPPSPKLPPHSTIRRTATDLIGRGFTVWEPYMDVSAVLMGLLELCADAEKQLANITMGLPLSPAADSARSARHALSLIATARPPAFITTIAKEVHRHTALAANTQSQQSIHTTTLARAKGEILRVIEILIEKMPTDVVDLLVEVMDIIMYCLEGSLVKKKGLQECFPAICRFYMVSYYERSHRIAVGARHGSVALYDIRTGKCQTIHGHKGPITAVSFAPDGRYLATYSNTDSHISFWQMNTSLLGSIGMLNSAPQLRCIKTYQVPPVQPASPGSHNALKLARLIWTSNRNVILMAHDGKEHRFMV
Protein: FGD4 protein (Q49A55)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MVNKIFSNISSINAFHSKFLLPELEKRMQEWETTPRIGDILQKLAPFLKMYGEYVKGFDNAMELVKNMTERIPQFKSVVEEIQKQKICGSLTLQHHMLEPVQRIPRYEMLLKDYLRKLPPDSLDWNDAKKSLEIISTAASHSNSAIRKMENLKKLLEIYEMLGEEEDIVNPSNELIKEGQILKLAARNTSARERYLFLFNNMLLYCVPKFSLVGSKFTVRTRVGIDGMKIVETQNEEYPHTFQVSGKERTLELQASSAQDKEEWIKALQETIDAFHQRHETFRNAIAKDNDIHSEVSTAELGKRAPRWIRDNEVTMCMKCKEPFNALTRRRHHCRACGYVVCWKCSDYKAQLEYDGGKLSKVCKDCYQIISGFTDSEEKKRKGILEIESAEVSGNSVVCSFLQYMEKSKPWQKAWCVIPKQDPLVLYMYGAPQVSKPHLSEGTDALGGKGKRVDSGLKICRTRVQAVSLFH
Protein: Bisphosphoglycerate mutase (BPGM) (EC 5.4.2.4) (2,3-bisphosphoglycerate mutase, erythrocyte) (2,3-bisphosphoglycerate synthase) (EC 5.4.2.11) (BPG-dependent PGAM) (P15327)
Organism: Mus musculus (Mouse)
Function: Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3-bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.11) activity.
Interaction partners:
- Phosphoglycerate kinase 2
- Phosphoglycerate kinase 1
- Beta-enolase
- Alpha-enolase
- Gamma-enolase
- Glyceraldehyde-3-phosphate dehydrogenase
- Glucose-6-phosphate isomerase
- Enolase 4
- Glyceraldehyde-3-phosphate dehydrogenase, testis-specific
- Multiple inositol polyphosphate phosphatase 1
Sequence:
MSKHKLIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKALNFEFDLVFTSILNRSIHTAWLILEELGQEWVPVESSWRLNERHYGALIGLNREKMALNHGEEQVRLWRRSYNVTPPPIEESHPYFHEIYSDRRYKVCDVPLDQLPRSESLKDVLERLLPYWKERIAPEILKGKSILISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVGPHQFLGNQEAIQAAIKKVDDQGKVKQGKQ
Protein: Polycystin cation channel PKD1/PKD2 domain-containing protein (H2KYK0)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Endosome membrane {ECO:0000256|ARBA:ARBA00004337}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004337}.
Interaction partners:
Sequence:
MSRIFRSQASRSMRLEQIPLESMSRRSTTDRSDFNDNASNASSNASRRPTINFQEIMEDLPHHERETGERLRRHLQFFFMNPMEKWKVRHQLPYKLVLQVLKIVFVTMQLILFAEMRMSHVDFLEDTTTVMRHRFLKEWNDDRDALQYPPAEGRYSVYDDQGLSEHLSFLINSYYSIRNDSFASFSYDVVSHPSGNLGAQISFESIPPIEVLIDRISNVTVNNNTYNFDIREVKDTKRLNLTETEVFQIGQSDDAVRDILATRGITFLPEDALKISTVQFKFRLRTIHYSPTAGDQKPECYKISVSIKFDNSRHTGQVHVTLSTVVSYVNVCNGRIIKGVGWSFDTLLIGGTDIFVLILCILSLILCCRALIKAHLLQIKTSDYFENVLKNKITVTDQLDFLNLWYVMIVVNDALIIIGTVAKISIEFQDFDNSLFTLTSIFLGMGALLVYVGVLRYFGFFSQYNILMLTLKRSAPNIMRFMTCAIVLYAGFLIAGWVIIGPYSMKFRTLAESSEALFSLLNGDDMFATFYTINDSNTVIKVFGTVYIYLFVSLFIYVVLSLFIAIIMDAYEVVKDRYSDGLRAIEKRGCLRDFVESNPPPSELGSPTTRSAYAPSNLLNLVFNHSPTR
Protein: Ciliogenesis-associated TTC17-interacting protein (Q08CH6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays a role in primary ciliogenesis by modulating actin polymerization.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Tubulin polyglutamylase complex subunit 1
- Adenylate kinase 8
- F-box and leucine-rich repeat protein 13.
- Adenylate kinase isoenzyme 5
- cAMP-dependent protein kinase type II regulatory subunit
- Ropporin-1-like protein
Sequence:
MEESELTQNETEELKASVSAVEFIHIAQRDLEQCLFADSLVTVSDSGRELGDFSVSVTKASYNEELCYLLHANSHGTIDDVPCGTSIVAYISRKLEILEENHHEYVKLEKKTVDRKIHIVRQDDQLVVDRVISEREGVKTQTLKFPLSSLDGFVSEASNFLLLRIMARQKIVPENMTFLSLDADSGLSKSVYKALGWQKQMVGEDLVDIFGIERTIYSANLSSATWHCFFMPDGHLASRVQLGSPAVMKLLHLPFLLDGVIKTFFFLVEKDKIPVMEKKPLIWEEDMELYSKFLDRKEELKADYSSYLRQHPELKALLADFLQFLLLRKPQDVFSFARDFFAPFASQSPPGKSQEF
Protein: Mitochondrial genome maintenance protein MGM101 (G8B839)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Function: Plays a role in the replication of the mitochondrial genome and the maintenance of its telomeres. Able to catalyze strand annealing and D-loop formation. Binds a wide variety of DNA substrates. Exhibited the highest affinity for DNA molecules carrying 3' ssDNA overhangs (Y-form, 3' FLAP, 3' overhang) and for substrates with complex structures (X-O and Fork). Forms homogeneous ring-shaped structures at the ssDNA native telomeres ends. Oligomers seem to bind to the ssDNA as a filament until they reach the double-stranded region and induce the formation of bends and loops within the double-stranded part of the molecules.
Subcellular location: Mitochondrion matrix, mitochondrion nucleoid {ECO:0000269|PubMed:26743001}.
Interaction partners:
- ATP-dependent DNA helicase
Sequence:
MLHSTKLVFRATPQALCFPVRSYSRYVRTVPKTASAKTTSKLAPSITTEDEVAEQDPSLQEPQSATSTASFAFHDAPPETRSVLNSSTNNNIDWSDSYHGLGSQPFSREIADILLAPIKDQDIEIKPDGLLYLPEIKYRRILNKAFGPGGWGLVPRTESLITKSQISREYGLICHGRLISIARGEQDYFGGEEKVTTALEGCKSNALMRCCKDLGIASELWDPGFIRKWKAKYCEEVFVEHVVNKKKKKLWKLKSNKKIEYPYKQL
Protein: aminodeoxychorismate synthase (EC 2.6.1.85) (Para-aminobenzoate synthase) (p-aminobenzoic acid synthase) (Q5AYT0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Multifunctional tryptophan biosynthesis protein
- Tryptophan synthase
- tryptophan synthase
- Anthranilate phosphoribosyltransferase, hypothetical
- Chorismate synthase
- Aminodeoxychorismate lyase
- Chorismate mutase
- anthranilate synthase
- Folic acid synthesis protein FOL1
- dihydroneopterin aldolase
Sequence:
MAPLLGDWAASKARRDKEAGQGVRQKSILYVDAYDSFSYNVAAMIEEILGARVTVMMIDAEWPDGNMLECLQHYDAVVLGPGPGDPNVPEDVGIMADIWNIDSSHMLPVLGICLGFQSLCLHYGTPIGRLPEPLHGQVHRITTAERDIFENLQNLEVTLYHSLYAMLDGQAESGSCDGAASPTPALDVLAWLSIQADDLCSSVTQIPMAVRHTEKPFWGVQFHPESCKSDREACSQLLRKWWDMAIKYNKSRHRDGCGSLSIDMIRSSCEDTRLPNVAFTMVNWSVSSSANCASRLFDTCQLDAEGLCELFNDPGVPTVLFQSNGRYSIISVPSPGSWRLEYYSQRHSLSMQRQSVSSSGCNALKDSDMRLEATMSVSQFWDVLRYLMDMKKVESGNYELPFWGGFLGYFSYELGLACLAHPKHESGSIADDHCSQESASADDPPDVSLLWTDRSVVVDNETGRVILQSTREADNLPAGWLDQASKTLERFCCMDILPKPKNSASDDEFLDSVLGRGVIQFPSENAYRNQVEACKDELRAGESYELCLTCETSITLPSPDVPIGRIEFPWKLYKRLRMYNPAAFSAFARLGNSKIVSSSPECFLNWDRHSTLEMKPMKGTVRKSDSMTMERAREILGSTKEMAENLMIADLVRHDLYGICGAGNVHVEKLLKVEDHGRVYQMITHVKGHVDPHRPGYAAKSLPRLQSSNMSGYGLTALQRCLPPGSMTGAPKERSCMHLSSIEGRKRGIYSGVMGFLDLGGGGSFSVLIRTAFTSSNDNDDVQKWRIGAGGAVTMLSSADGEWAEMLTKLQTVCGIFMPSHAK
Protein: DCD domain-containing protein NRP-B (N-rich protein B) (C6TAQ0)
Organism: Glycine max (Soybean) (Glycine hispida)
Function: Involved in stress signaling pathway that mediates cell death in response to endoplasmic reticulum (ER) stress and osmotic stress.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18490446}.
Interaction partners:
Sequence:
MENNNQSFWQFSDQLRLQASNLANLSLNDSIWSNNYISKRRDERINFDIKVGGEINSFKSKDPACDYNDNVNGSLLAMPYNNNNNNNIILGFGGVGLNGGFNKGIYSKPAFANLNNNINLNINPKGHKGKVEDELFHPSKSSKKNNNLNKKHGDNNNNDNNKDSKAAGDKRFKTLPPSESLPRDETIGGYIFVCNNDTMAENLKRQLFGLPPRYRDSVRAITPGLPLFLYNYSTHQLHGIFEAASFGGTNIDPSAWEDKKCPGESRFPAQVRVITRKTCEPLEEDSFRPILHHYDGPKFRLELNVPEALSLLDIFAEQDTFNDAFEALPA
Protein: Glucosidase 2 subunit beta (B1WC34)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Neutral alpha-glucosidase AB
- Translocation protein SEC63 homolog
- Polycystin-2
- Coiled-coil domain-containing protein 167
- Arginine/serine-rich coiled-coil protein 2
- Alpha-1,3-glucosyltransferase
- Flt3-interacting zinc finger protein 1
Sequence:
MLLLLLLLPLCWAVEVKRPRGVSLSNHHFYDESKPFTCLDGTATIPFDQVNDDYCDCKDGSDEPGTAACPNGSFHCTNTGYKPLYILSSRVNDGVCDCCDGTDEYNSGTVCENTCREKGRKEKESLQQLAEVTREGFRLKKILIEEWKTAREEKQSKLLELQAGKKSLEDQVETLRTAKEEAERPEKEAKDQHRKLWEEQQAAAKARREQELAASAFQELDDNMDGLVSLAELQTHPELDTDGDGGLSEEEAQALLSGDTQTDTTSFYDRVWAAIRDKYRSEVPPTDIPVPEVTEPKEEKLPVLPPMEEEEEEEEPEEEEEEEEEEVPGEQPKEVPPPQQPLRPPSPAEDEKMPPYDEETQAIIDAAQEARNKFEEVERSLKEMEESIRSLEQEISFDFGPSGEFAYLYSQCYELTTNEYVYRLCPFKLVSQKPKHGGSPTSLGTWGSWAGPDDDKFSAMKYEQGTGCWQGPNRSTTVRLLCGKETVVTSTTEPSRCEYLMELMTPAACPEPPPEVPTDGDHDEL
Protein: Collagen type VI alpha 2 chain (F1LNH3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Collagen alpha-1
- Collagen alpha-1
- CD44 antigen
- Glycoprotein VI
- Integrin subunit alpha 5
- Collagen alpha-2
- Collagen alpha-1
- Integrin alpha-11
- Collagen alpha-1
- Integrin alpha-8
Sequence:
MATPYCRTSGHMTTTTKMLQGSFSVLLLGGLLGVLHAQQQEAISPDISTTDRNNNCPEKADCPVNVYFVLDTSESVAMQSPTDSLLYHMQQFVPQFISQLQNEFYLEQVALSWRYGGLHFSDQVEVFSPPGSDRASFTKSLQGIRSFRRGTFTDCALANMTQQIRQHVGRGVVNFAVVITDGHVTGNPCGGIKMQAERAREEGIRLFAVAPNRNLNEQGLRDIANTPHELYRNNYATMRPDSTEIDQDTINRIIKVMKHEAYGECYKVSCLEIPGPHGPKGYRGQKGAKGNMGEPGEPGQKGRQGDPGIEGPIGFPGPKGVPGFKGEKGEFGSDGRKGAPGLAGKNGTDGQKGKLGRIGPPGCKGDPGSRGPDGYPGEAGSPGEQGDQGAKGDSGRPGRRGPPGNPGDKGSKGYRGNSGAPGSPGVKGGKGGPGPRGPKGEPGRRGDPGTKGGPGSDGPKGEKGDPGPEGPRGLAGEIGSKGAKGDRGLPGPRGPQGALGEPGKQGSRGDPGDAGPRGDSGQPGPKGDPGRPGFSYPGPRGTPGEKGEPGPPGPEGGRGDFGLKGAPGRKGEKGEPADPGPPGEPGPRGPRGIPGPEGEPGPPGDPGLTECDVMTYVRETCGCCDCEKRCGALDVVFVIDSSESIGYTNFTLEKNFVINVVNRLGAIAKDPKSETGTRVGVVQYSHEGTFEAIRLDDERVNSLSSFKEAVKNLEWIAGGTWTPSALKFAYNQLIKESRRQKTRVFAVVITDGRHDPRDDDLNLRALCDRDVTVTAIGIGDMFHETHESENLYSIACDKPQQVRNMTLFSDLVAEKFIDDMEDVLCPDPQIVCPELPCQTELYVAQCTQRPVDIVFLLDGSERLGEQNFYKARRFVEEVSRRLTLARRDDDPLNARMALLQYGSQNQQQVAFPLTYNVTTIHEALERTTYLNSFSHVGTGIVHAINNVVRGARGGARRHAELSFVFLTDGVTGNDSLEESVHSMRKQNVVPTVVAVGGDVDMDVLTKISLGDRAAIFREKDFDSLAQPSFFDRFIRWIC
Protein: Type IV secretion system protein VirD4 (Q2GI61)
Organism: Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Type IV secretion system protein VirB10
- Type IV secretion system protein
- Type IV secretion system protein VirB8
- Type IV secretion system protein VirB9
- Type IV secretion system protein VirB3
- Type IV secretion system protein virB4
- Type IV secretion system protein VirB4
- Type IV secretion system protein, VirB9
- Type IV secretion system protein VirB6
- Type IV secretion system protein VirB8
Sequence:
MDSVSANHIRNILFLVLGAFFGLEFCFYLSGVLFILMVWGPDYLDFNAINPSFSDFPDRIWPTVFNYVEHWWHNPSSYDAILLVKLISSLCIPIGILSIVLWNLRNILFDWRPFKKKESLHGDSRWATEKDIRKIGLRSRKGILLGKDKRGYLIADGFQHALLFAPTGSGKGVGFVIPNLLFWEDSVIVHDIKLENYDLTSGWRKKRGQEVFVWNPAQPDGVSHCYNPLDWISSKPGQMVDDVQKIANLIMPEQDFWYNEARSLFVGVVLYLLAVPEKVKSFGEVVRTMRSDDVVYNLAVVLDTIGKKIHPVAYMNIAAFLQKADKERSGVVSTMNSSLELWANPLIDTATASSDFNIQEFKRKKVTVYVGLTPDNLTRLRPLMQVFYQQATEFLCRTLPSDDEPYGVLFLMDEFPTLGKMEQFQTGIAYFRGYRVRLFLIIQDTEQLKGIYEEAGMNSFLSNSTYRITFAANNIETANLISQLIGNKTVNQESLNRPKFLDLNPASRSLHISETQRALLLPQEVIMLPRDEQILLIESTYPIKSKKIKYYEDKNFTKKLLKSTFVPTQEPYDPNNVKITKKENEDPIPSIESDIPENKPNNTENNLTEEGAIYNSTETNYEDDEDEDDDFNFDDLDEYIDEDEEYSEQPEEDYDYTDEEDEDEEEDEEDNDYNNSNEDDDYENNNISNSHHENDFDNHNEKPVKDQDIKNDKQ
Protein: T10F20.8 protein (Translation elongation factor EF1A/initiation factor IF2gamma family protein) (Q9LMS7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Eukaryotic peptide chain release factor subunit 1-1
- Eukaryotic peptide chain release factor subunit 1-2
- Eukaryotic peptide chain release factor subunit 1-3
- Protein SUPPRESSOR OF GENE SILENCING 3
- Regulator of nonsense transcripts 1 homolog
- Protein cereblon
- Protein PELOTA 1
- AT3g13440/MRP15_7
- Small ribosomal subunit protein uS12y
- Small ribosomal subunit protein uS12z
Sequence:
MDLEAEIRALQLESADENNGVVIPEVHNSHEVENLDKAPEDLKDEVQESIPVPDEQEASEDHDEVMLHPVHNPAKAKEKAAQEKAAKEEAEDVAEANKKRHLNVVFIGHVDAGKSTIGGQILFLSGQVDDRQIQKYEKEAKDKSRESWYMAYIMDTNEEERLKGKTVEVGRAHFETESTRFTILDAPGHKSYVPNMISGASQADIGVLVISARKGEFETGYERGGQTREHVQLAKTLGVSKLIVVVNKMDDPTVNWSKERYDEIEQKMVPFLKASGYNTKKDVVFLPISGLMGKNMDQRMGQEICPWWSGPSFFEVLDSIEIPPRDPNGPFRLLTGIDFMNCRMPIIDKFKDMGTVVMGKVESGSIREGDSLVVMPNKEQVKVVAIYCDEDKVKRAGPGENLRVRITGIEDEDILSGFVLSSIVNPVPAVTEFVAQLQILELLDNAIFTAGYKAILHIHAVVEECEIIELKSQIDLKTRKPMKKKVLFVKNGAAVVCRIQVTNSICIEKFSDFPQLGRFTLRTEGKTIAVGKVTELLSSVSSA
Protein: Serine/threonine-protein phosphatase 4 regulatory subunit 3-like central domain-containing protein (Q580Q3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Serine/threonine-protein phosphatase 2A activator
Sequence:
MDNGPHLFTKAKLYTALSDQESWTEMGVGVVFIVMRSVANEGEEGFGEGKGEGRSGDCGRLEQTVGCLEMVDIDNPQELLISTPISLEDIYVVQQETILLWSDVALGRLLSCSFNTKEGCDKIYSEILDYQRSRRPPTEVGGMNNGGDDGGGLVVTGSEAEGYIDGCGGPLALCRNWLVCRENLPIIISVMQTNPQRFGLFVRSHETYIKELVDLFEYCKGDNDQRGMNLIGTITTTLLHQPFCTDGKIISQFIDREVIDRVLQVVQFAIGRCDSQSGFVDIAQRRATFRNPLMLPESTVLKIHELHACSCLKDMLPVSLDEADANPSSLLSNYIMTNKSQLVDDICKSRHILPEAFTRAYDDVKLAFEVTAFLHDMCRTVRSATMSIEYKSSIFGAMIRTSLIPFIRFVLSRALALYEAAPRWQPDQQCLISPNISPGMALLMACDIISNCLTFYPQGRCLLTEEGHSKPDGCLLELLLQCVVVTHCGAELQAAVDAVVSCVTCALLQSPAGVAICAAERRDIIQFWLNGDDGKRRPPLLSLTEGLVNVLGSLERVMRGFHGETRVIHILRVFTVLVDAVDEPLSRPLANLLQQSCLVQCLDNVLQSRARSVANVQSSVASFIASLLNCNKRQLVALPLLYAGGELLDTAVRRYLVCSPNSNSLFRSSLAHLIDSLCRAIRMEKGSALRQTSFCGSANNPFAPSLFASEDESTVISSANGDGADVDVDECNRNMCHNVGNRLWQAYGERMRQHCPALATRLEHSLLETPEEAASAGAETSSVASTVERNGWNGRDSDFELLLAELGVDAQPANNKLQVMGSGVVGYDDPLESHYTTSAQQAPDNSDFASNDDSCNCDSEENEGEENSSSEPPAKRSRSESSSATAVE
Protein: Transcription factor 21 (TCF-21) (Capsulin) (Epicardin) (MyoRa2) (Q32PV5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Involved in epithelial-mesenchymal interactions in kidney and lung morphogenesis that include epithelial differentiation and branching morphogenesis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O43680, ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- T-box transcription factor 18.
- Wilms tumor protein homolog
- Myosin light chain 2 Mlc2a
- Aldehyde dehydrogenase 1 family, member A2
- Semaphorin-3D
- Periostin
- NK2 homeobox 5.
- WT1 transcription factor b.
- GATA-binding protein 4.
- GATA-binding protein 5
Sequence:
MSTGSISDVDEFHESELLDGLPKFGSGKDPGTSNESTEDSSNCEGASVSECTGKRRKSANMRRSAPNGVAQEGKQVQRNAANARERARMRVLSKAFSRLKTTLPWVPPDTKLSKLDTLRLASSYIAHLRQILANDKYENGYIHPVNLTWPFMVAGKPENELKEMLNSTRLCGTTAS
Protein: Cholinergic receptor nicotinic alpha 1 subunit (E7ENE5)
Organism: Homo sapiens (Human)
Subcellular location: Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00034104}.
Interaction partners:
Sequence:
MEPWPLLLLFSLCSAGLVLGSEHETRLVAKLFKDYSSVVRPVEDHRQVVEVTVGLQLIQLINVDEVNQIVTTNVRLKQQWVDYNLKWNPDDYGGVKKIHIPSEKIWRPDLVLYNNADGDFAIVKFTKVLLQYTGHITWTPPAIFKSYCEIIVTHFPFDEQNCSMKLGTWTYDGSVVAINPESDQPDLSNFMESGEWVIKESRGWKHSVTYSCCPDTPYLDITYHFVMQRLPLYFIVNVIIPCLLFSFLTGLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMVFVIASIIITVIVINTHHRSPSTHVMPNWVRKAAAEWKYVAMVMDHILLGVFMLVCIIGTLAVFAGRLIELNQQG
Protein: Processive diacylglycerol beta-glucosyltransferase (EC 2.4.1.315) (Beta-diglucosyldiacylglycerol synthase) (Beta-DGS) (DGlcDAG synthase) (Glc2-DAG synthase) (Beta-gentiobiosyldiacylglycerol synthase) (Beta-monoglucosyldiacylglycerol synthase) (Beta-MGS) (MGlcDAG synthase) (Diglucosyl diacylglycerol synthase (1,6-linking)) (Glucosyl-beta-1,6-glucosyldiacylglycerol synthase) (UDP glucosyltransferase) (UDP-glucose:1,2-diacylglycerol-3-beta-D-glucosyltransferase) (Q2FZP7)
Organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)
Function: Processive glucosyltransferase involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. Is able to successively transfer two glucosyl residues to diacylglycerol (DAG), thereby catalyzing the formation of beta-monoglucosyl-DAG (3-O-(beta-D-glucopyranosyl)-1,2-diacyl-sn-glycerol) and beta-diglucosyl-DAG (3-O-(beta-D-glucopyranosyl-beta-(1->6)-D-glucopyranosyl)-1,2-diacyl-sn-glycerol). Beta-diglucosyl-DAG is the predominant glycolipid found in Bacillales and is also used as a membrane anchor for lipoteichoic acid (LTA). UgtP can only use UDP-glucose as sugar donor.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01280, ECO:0000269|PubMed:11344159}.
Interaction partners:
- Proton-coupled antiporter flippase LtaA
- Lipoteichoic acid synthase
- Cell division protein FtsZ
- UDP-N-acetylmuramoylalanine--D-glutamate ligase
- Cell division protein FtsA
- UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
- UDP-N-acetylmuramate--L-alanine ligase
Sequence:
MVTQNKKILIITGSFGNGHMQVTQSIVNQLNDMNLDHLSVIEHDLFMEAHPILTSICKKWYINSFKYFRNMYKGFYYSRPDKLDKCFYKYYGLNKLINLLIKEKPDLILLTFPTPVMSVLTEQFNINIPVATVMTDYRLHKNWITPYSTRYYVATKETKQDFIDVGIDPSTVKVTGIPIDNKFETPINQKQWLIDNNLDPDKQTILMSAGAFGVSKGFDTMITDILAKSANAQVVMICGKSKELKRSLTAKFKSNENVLILGYTKHMNEWMASSQLMITKPGGITITEGFARCIPMIFLNPAPGQELENALYFEEKGFGKIADTPEEAIKIVASLTNGNEQLTNMISTMEQDKIKYATQTICRDLLDLIGHSSQPQEIYGKVPLYARFFVK
Protein: Actin remodeling regulator NHS (Congenital cataracts and dental anomalies protein) (Nance-Horan syndrome protein) (Q6T4R5)
Organism: Homo sapiens (Human)
Function: May function in cell morphology by maintaining the integrity of the circumferential actin ring and controlling lamellipod formation. Involved in the regulation eye, tooth, brain and craniofacial development.
Subcellular location: [Isoform 1]: Apical cell membrane; Peripheral membrane protein. Cell projection, lamellipodium. Cell junction, tight junction. Cell junction, focal adhesion. Note=Colocalizes with the tight junction protein TJP1 in epithelial cells. Localizes to the leading edge of lamellipodia in motile cells.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm.
Interaction partners:
- Retinoic acid-induced protein 2
- Nck-associated protein 1
- N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase
- Cyclin-dependent kinase-like 5
Sequence:
MPFAKRIVEPQWLCRQRRPAPGPAVDASGGSAEPPPPLQPPGRRDLDEVEAPGPEEPARAVPAPSGLPPPPPPLPAPADQTQPPHGEASVAGEESTAGIPEAAPAAGEASSAAAAAAVLLMLDLCAVSNAALARVLRQLSDVARHACSLFQELESDIQLTHRRVWALQGKLGGVQRVLSTLDPKQEAVPVSNLDIESKLSVYYRAPWHQQRNIFLPATRPPCVEELHRHARQSLQALRREHRSRSDRREQRAAAPLSIAAPPLPAYPPAHSQRRREFKDRHFLTFNSTRSPSPTECCHMTPWSRKSHPPEDEDTDVMLGQRPKNPIHNIPSTLDKQTNWSKALPLPTPEEKMKQDAQVISSCIIPINVTGVGFDREASIRCSLVHSQSVLQRRRKLRRRKTISGIPRRVQQEIDSDESPVARERNVIVHTNPDPSNTVNRISGTRDSECQTEDILIAAPSRRRIRAQRGQSIAASLSHSAGNISALADKGDTMFTPAVSSRTRSRSLPREGNRGGDAEPKVGAKPSAYEEGESFVGDHERTPNDFSEAPSSPSAQDHQPTLGLACSQHLHSPQHKLSERGRSRLSRMAADSGSCDISSNSDTFGSPIHCISTAGVLLSSHMDQKDDHQSSSGNWSGSSSTCPSQTSETIPPAASPPLTGSSHCDSELSLNTAPHANEDASVFVTEQYNDHLDKVRGHRANSFTSTVADLLDDPNNSNTSDSEWNYLHHHHDASCRQDFSPERPKADSLGCPSFTSMATYDSFLEKSPSDKADTSSHFSVDTEGYYTSMHFDCGLKGNKSYVCHYAALGPENGQGVGASPGLPDCAWQDYLDHKRQGRPSISFRKPKAKPTPPKRSSSLRKSDGNADISEKKEPKISSGQHLPHSSREMKLPLDFANTPSRMENANLPTKQEPSWINQSEQGIKEPQLDASDIPPFKDEVAESTHYADLWLLNDLKTNDPYRSLSNSSTATGTTVIECIKSPESSESQTSQSESRATTPSLPSVDNEFKLASPEKLAGLASPSSGYSSQSETPTSSFPTAFFSGPLSPGGSKRKPKVPERKSSLQQPSLKDGTISLSKDLELPIIPPTHLDLSALHNVLNKPFHHRHPLHVFTHNKQNTVGETLRSNPPPSLAITPTILKSVNLRSINKSEEVKQKEENNTDLPYLEESTLTTAALSPSKIRPHTANKSVSRQYSTEDTILSFLDSSAVEMGPDKLHLEKNSTFDVKNRCDPETITSAGSSLLDSNVTKDQVRTETEPIPENTPTKNCAFPTEGFQRVSAARPNDLDGKIIQYGPGPDETLEQVQKAPSAGLEEVAQPESVDVITSQSDSPTRATDVSNQFKHQFVMSRHHDKVPGTISYESEITSVNSFPEKCSKQENIASGISAKSASDNSKAEETQGNVDEASLKESSPSDDSIISPLSEDSQAEAEGVFVSPNKPRTTEDLFAVIHRSKRKVLGRKDSGDMSVRSKSRAPLSSSSSSASSITSPSSNVTTPNSQRSPGLIYRNAKKSNTSNEEFKLLLLKKGSRSDSSYRMSATEILKSPILPKPPGELTAESPQSTDDAHQGSQGAEALSPLSPCSPRVNAEGFSSKSFATSASARVGRSRAPPAASSSRYSVRCRLYNTPMQAISEGETENSDGSPHDDRSSQSST