wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein (Q384D5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDFRLPLCSVLNSEVGRRHKIPHRTLSLPKTSLFVRYLDSDDTRLPVHSLLNIVPQPAEDYETYTGEDDWEKKVDDAAGVVGDCGGIDGNPPRFDEMVQWVIDALKDIEGCGGAASDGVVLCGRWVVADDCSWVVPSRTPILHSPRDVFLAMRNSPKFLRDVHHQILSGDTSSAGMGSTVELTLAKAVGKNPANDFRVFVPYRLVRAEDTFRVTIWEGRVFAGVCQRSTDVCFPSLMSWDLRTHSENYDHVLRHIEGARLLERSIEADPYLRTFLLRKVEANEVEGAASPCSVLLLSVDVVFEGVSLPLYIVSAKVRCFKHDRLRDPLCVSPFIKEEDNNGSEEGVNAVGGGVDGDRSDGIDTKEMLDDSVIFFRLFRDVNNWNFHVTLCLHPDGGEVSGDVDKGVNIVPSPQRDRRFFVIASERSDLVLTKEPILKRGMPLEFLRPELLGDIGEGLPQVWKDRLLRCLSLVQRSQEL
Protein: Phosphate transporter (A0A1D8PF54)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Phosphate transporter
- Pho91p
- Vacuolar transporter chaperone complex subunit 4
- Pho81p
- SPX domain-containing inorganic phosphate transporter
- Bta1p
- Vacuolar transporter chaperone
- DUF202 domain-containing protein
Sequence:
MKYPKVXGKTAFKDYLGKFADVEDPLERRRLALEEIDKAGFGWTQVKMILIAGVGFMTDSYDIFAINLSMNMLQYVYWNGTIPDSTTTLIKVSTSVGTVIGQISFGSIADKVGRKKIYGLELIIMIFATLFQCTLGTSPAINFVAIFSTIRILMGIGIGGDYPLSSIISSEFSTTKWRGAIMAAVFSNQGLGQVFAGIVAMICVAGYKDDLIIANKGSECVGRCRKAADQMWRIIVGFGCVPGCIALYYRLTIAESPRYALDVDEHDDLEKVADAEAAIDVHAQEIAPPKASFKDFCSHFGQWRYGKILLGTAGSWFMLDVAYYGLGLNTTTILQTIGYAGQSNVYEKLYNSAAGNLILVCAGSLPGYWVSAATIDTVGRKPIQMGGFILLTIILCIMGFGYHKIGNHGLLGLFVIAQFFQNFGPNTTTFIVPGECFPTRYRSTAHGLSAAAGKVGAIIAQTCIGTLVNHGCSKENKNCFLPHVLEIFALFMLLGIGLTFLIPETARRTLEEISETCHGEVDTTKLGRDRFATQEEPYDSEEVKN
Protein: Protein MAIN-LIKE 2 (F4IFD0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Maybe required to maintain cell division activity in meristematic cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:24635680}.
Interaction partners:
Sequence:
MDVLANPGPLKDIVLYDQEKHVSSAVWDGQERGALRCHEHTSKLGEWKLKPKQIELVERAGFGFLRRIPAISLDNPLISALVERWRRETNTFHFTVGEMTVTLEDIALLLGLGIDGKPVIGLTYTTCSAVCERYLGKSPASNSASGGMVKLSWLKDNFSECPDDASFEEVERRTRAYLLYLVGSTIFSTTTGNKVPVMYLPLFEDFDDAGTFAWGAAALAFLYRALGNASVKSQSTICGCLTLLQCWSYYHLNIGRPKLNREPIHDQFPFVLKWKGKQNGPTANRDVVFYRKALDVMKPTDVVWLPYENMNGGDMSDRMRKSLLLGRSKTMLISFDKAERHLPDRCRKQFDLFQDIPADVQRWVRKSRGVDGGVDLSNKMESELSEWEMRWENIVPDDVQGVDEADYMRWYLGITRKIVGRPISLSSEFQRTISNVRDILELAENFQIHDLDLERGNMISRIIGLAQDCLRDQVGVTATPETQQQIELGKRMRGKERVRRKGMGKRRKGIDPMEDYGGSEDESQFGPLVEVGQMHLPLSHTNSVYDGTHMYDAVTKVDDMELCDTIPQLPETQDIHKIEGSLLDDTDKFVEESKLQEEFDGEEPTESYDVKKEDKESKVEDDDAAKGFSDVSGEENANREEEDETEMGESVAESSSLDRRGENTVVA
Protein: Methyltransferase small domain-containing protein (A0A0H2UPK7)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MSKMYYAENPDAAHDIHELRVDLLGEKMTFLTDAGVFSKKMVDFGSQLLLKCLDVNQGETVLDVGCGYGPLGLSLVKVYGVQATMVDINTRALDLAQRNAEKNNAKATIFQSNIYARVQGRFDHVISNPPIRAGKQVVHEIIEKSKDFLEIGGDLTIVIQKKQGAPSAKSKMEDVFGNCEILKKDKGYYILRSVKE
Protein: Ferric uptake regulation protein (Q7CQY3)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU364037}.
Interaction partners:
- Flavodoxin 1
- LexA regulated, putative SOS response
- Hydroxymate-dependent iron transport
Sequence:
MTDNNTALKKAGLKVTLPRLKILEVLQEPDNHHVSAEDLYKRLIDMGEEIGLATVYRVLNQFDDAGIVTRHNFEGGKSVFELTQQHHHDHLICLDCGKVIEFSDDSIEARQREIAAKHGIRLTNHSLYLYGHCAEGDCREDEHAHDDATK
Protein: Integrin beta-like protein E (Q54JA3)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Implicated in cellular adhesion.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Latrophilin receptor-like protein A
Sequence:
MNNLFKFLFVLLAIFCPPISDLVVSHGVPQQHITIIKFTTNFAFRTTFYKTSSSSIVIGEKITLGTLTFGDGSSTSVRASVTSFDTKNDWFFGQFIFTKTYTALTPNNSKQYLAMFTSCCRISTLLNNKDADWNITSSVYLDNKNWPSVNHSPVSGMLPIVQVIANKNNNFRVIASDPNVDDKLSFSFSTVYPMTQPSGMKINSTGHVFFLPTSVGLYSTQIYITDDAVPPAYAVVDFILESITEPGKCDPSCSNGGATCNGNSECKNCANAGSTTSNTCSTTNYPPYFVSPTPQDNQLIPFTVGQPNSITLSCKSDYTTRTVGIQAANVPAGAAIAEGTSSQGTVKNILSWTPVAANVGVYVTSIFCYDSNGLTSSSRSFTIFIAKPECGNGHKDPSTGKCKCDGDKWDPTSNCFDCSTGYYGQNCDPTPPCDKGIPNEGILGDGKCMCINGYSGDKCDVPLSQSCKDLKNSILLSTSVPSFFVNPTKVQLYIESDFALTTSLNIPQKLTKIDVFVLVDVNVASSTLFGVVQSSISTFVTEVSKSICETTQFGIGYFSDASSSGFNFAPGSIIGSNIVNTINGYAVSSYTSTSSGNSLLGATNAASNSNGWNSGSFKAIVVLTDKDHSSNSAAITNFVNTYISNSIAPVVVGFGASSIPNWNSAISTADFGYSTVSAATSIDISAKAVAGLKSVLSNVVYKTDNTTNGASFVKSTPSDVAVSSTADTVKTVSGLVLTKPSATSIVSPVASVSAIGFGQTDFSINYNRPPTPTGTAFSVNQNSFATFKLTGTDPDFNILTFAFTTFLTSDVGVITDSNNKDVSTQKSKYYDSTETFTFTPAINYLLPISVSFVANDGCLNSTTSATVSITINKVNQLPTCQQKTISPTLNVANKFVLSASDFEDATPFIQFTSPTDLTAYGTLTFGGVAVTSTSKIPTSSEITFTQTVNPTNAIDVPVSFQAVDSVGAISTSTCTLTVKLVHTNIKPVSSSTSPISVIPRGSVSLTLVSTDSDSTSAKFTIKSVNKGAKGDFYTCSTNDCTCNSTQTNIYTSISTTTTYTSISYTNKVANKLICFTNGEPSAISNYASISFTSTDNQGLESDSVNVVVNIVGNRTNVAPVVTKIQGYSVYQDYLDSDAHVVTGTDADIDDYNPPNVNNLIAIITTPPSNGILVTLQNGSIAATQGKAPFTHYYRPNPGFKGTDSYSYQVVDTFKAGSSIESTTVTVNPINHKPSVVVSSYSFTSQSGDGETQDLVTSDPDGDSVICSVVSIPSQIGMYDSDGNLIESVPTVLSGTSYSFKLLDPSKITPTPFTSVSSSFAVKCTDVTTKTIPFGTLSTGVVTANVQYTYINTPPTTQGGTVQLDQDTVKVFTFNGSDIETPKDDIKVKILSLPINGQLLINATGVALTTTNIASETYNLNALSYKPNAGLSNWNTIDQQSPLDSISYTVIDQQGLTSDSDIVYFSVRPRNPPVYTGARVIDVLQNTRYPLTITSRIGGGGSEVNIQVIGFTNNGTLSIAHNMGSEGTMDSEITSYPNQQSGSTSYNYAYMPPRNKYGNDFDFIYFKLFDGDLYSELYTVTVNVIHVNQPPTIELVSYKILDGVSSEVLFENTSLINMNINTTVLIKYSGNDIDVDQVTPLISMIPNFPLRGSLYAYNPTASNSSGAPITRNSSNVEQNADGFYYVVFVPSKKTSGESYARITFIMTDNGGLNSPIVGVLINVNTVNIAPFVIIGNKNYTTQTNLTASVMGVQFDDPDSTTNNVSIVVSIVGQKDDKVASLKDIKLSFTQSPMCEYHQTLASITCIGPKKPLNSSIVSISVIASTAGDYRLKLFVDDLGYNAPSAIRAQSHLNATGYVDVKVNAPEATTQTTNNKTVLTGAIAGAAAGTALIAAAAWKLLRKAAPPTDTFFSEAAFLGDGVNANPLYEQSASAAENPLYQSASDNTD
Protein: Methionine S-methyltransferase (EC 2.1.1.12) (AdoMet:Met S-methyltransferase) (Q9LTB2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the S-methylmethionine (SMM) biosynthesis from adenosyl-L-homocysteine (AdoMet) and methionine. SMM biosynthesis (by MMT1) and degradation (by HMT-1, HMT-2 and HMT-3) constitute the SMM cycle in plants, which is probably required to achieve short term control of AdoMet level. Also able to catalyze the selenium-methylmethionine (SeMM) from AdoMet and selenium-methionine (SeMet). May play a role in phoem sulfur transport; such function is however not essential.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Methionine gamma-lyase
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 2
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 1
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 3, chloroplastic
- Methionine--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, chloroplastic/mitochondrial
- Homocysteine S-methyltransferase 1
- Homocysteine S-methyltransferase 2
- Homocysteine S-methyltransferase 3
- Cystathionine gamma-synthase 1, chloroplastic
Sequence:
MADLSSVDEFLNQCKQSGDAAYGALRSVLERLEDPNTRSKARIFLSDIYKRVGSSETSLQTYHFHIQDIYLDQYEGFQSRKKLTMMVIPSIFIPEDWSFTFYEGLNRHPDTIFKDKTVSELGCGNGWISIAIAAKWLPSKVYGLDINPRAVKISWINLYLNALDDNGEPVYDEEKKTLLDRVEFYESDLLGYCRDNKIQLERIVGCIPQILNPNPEAMSKLITENASEEFLHSLSNYCALQGFVEDQFGLGLIARAVEEGISVIKPAGIMIFNMGGRPGQGVCRRLFERRGVRVTQMWQTKILQAADTDISALVEIERSSPHRFEFFMGLSGDQPICARTAWAYGKAGGRISHALSVYSCQIRQPNLVKIIFDFLKNGFQEISNSLDLSFEDETVADEKIPFLAYLASVLKNSSYFPFEPPAGSKRFCSLIAGFMRTYHRIPINQDNIVVFPSRAVAIESAFRLFSPRLAIVDEHLTRQLPRSWLTSLAIEDTSMDKSDDQITVIESPHQSDLMIELIKKLKPQVVVTGMAPFEVITSSSFLHLLEVTKEIGCRLFLDISDHFELSSLPASNGVLKYLAENQLPSHAAIICGLVKNKVYSDLEVAFVITEVDAIAKALSKTVEVLEGHTAIISQYYYGCLFHELLAFQLADRHAPAERESEKAKSEEIIGFSSSAVSILKDAELSVTEIDETSLIHMDVDQSFLQIPQSVKAAIFESFVRQNISEAEVDINPSIKQFVWSNYGFPTKSSTGFVYADGSLALFNKLVICCAQEGGTLCLPAGTNGNYVAAAKFLKANVVNIPTESSDGFKLTEKTLTKALESVKKPWVCISGPTVSPTGLVYSNEEMDILLSTCAKFGAKVIIDTSFSGLEYSATSWDLKNALSKMDSSLSVSLLGCLSLNLLSGAIKLGFLVLDQSLIDAFHTLPGLSKPHSTVKYAAKKMLALKEEKASDFLDAVSETIKTLEGRSRRLKEVLQNSGWEVIQPSAGISMVAKPKAYLNKKVKLKAGDGQEIVELTDSNMRDVFLSHTGVCLNSGSWTGIPGYCRFSFALEDSEFDKAIESIAQFKSVLAN
Protein: Endoglycoceramidase I (EGCase I) (EC 3.2.1.123) (A0A3S5YBC7)
Organism: Rhodococcus hoagii (strain 103S) (Rhodococcus equi)
Function: Hydrolyzes glycosphingolipids; exhibits broad substrate specificity including monosialodihexosylganglioside (GM3), monosialotetrahexosylganglioside (GM1), fucosyl-GM1, lactosylceramide, globotriosylceramide, globotetraosylceramide, ganglioside GD1a, and ganglioside GD1b. No activity towards glucosylceramide and galactosylceramide.
Subcellular location: Secreted {ECO:0000269|PubMed:28179425}. Membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
Interaction partners:
Sequence:
MRKTVVAFAAAIAACSAVLSSTTTSAAPPATPITTLQADGTHLVDGYGRTVLLHGVNNVDKDAPYLPAGETLTPQDIDILVRHGFNTVRLGTSFDALMPQRGQIDEAYLDRLTGVVDALTARGMHVLLDNHQDGLSKAWGGNGFPEWAIESRPREWEPNPGFPLYYLMPSLNAGWDEVWGNTHGALDHLGTALGALAERVEGKPGVMGIELLNEPWPGSRFLSCFPNGCPDFDRTYQAAMQKLTDAVRAQNPTIPVYWEPNVTWNQMMPSNLFAPPVTPALTTADVVFAPHDYCIPSQLAIYLGLPQALRGLCVPQQDLTWSNIDAITERANVPTVITEFGDGDPTVLKNTLARADERFIGWQYWHFGAGNATDPFLGEVGRQLVRTYPQATAGEPGRMIFDADNGDFAYRFTPRAATRPTEIFVSDLHYPDGYAVQVDGGQVTSAPGARIVTVVADGSGPVTVKINRPGSAGAEVPDGPIETSSSGSSGSS
Protein: Optic atrophy 3 protein homolog (Q505D7)
Organism: Mus musculus (Mouse)
Function: May play some role in mitochondrial processes.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Transmembrane protein 126A
Sequence:
MVVGAFPMAKLFYLGIRQVSKPLANRIKDAARRSEFFKTYICLPPAQLYHWVEMRTKMRIMGFRGTTIKPLNEEAAAELGAELLGEATIFIVGGGCLVLEYWRHQTQQRNKEEEQRAAWNALQDEVGRLALALEALQAQAQAMPSLSALEELREELQEVRGQVCNAHCTSKCQAASSKK
Protein: Short transient receptor potential channel 7 (TrpC7) (Transient receptor protein 7) (TRP-7) (mTRP7) (Q9WVC5)
Organism: Mus musculus (Mouse)
Function: Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Activated by diacylglycerol (DAG). May also be activated by intracellular calcium store depletion.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9HCX4}; Multi-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000250|UniProtKB:Q9HCX4}.
Interaction partners:
- Short transient receptor potential channel 3
Sequence:
MLGSNTFKNMQRRHTTLREKGRRQAIRGPAYMFNEKGTSLTPEEERFLDSAEYGNIPVVRKMLEESKTLNFNCVDYMGQNALQLAVGNEHLEVTELLLKKENLARVGDALLLAISKGYVRIVEAILSHPAFAQGQRLTLSPLEQELRDDDFYAYDEDGTRFSHDITPIILAAHCQEYEIVHILLLKGARIERPHDYFCKCNECTEKQRKDSFSHSRSRMNAYKGLASAAYLSLSSEDPVLTALELSNELARLANIETEFKNDYRKLSMQCKDFVVGVLDLCRDTEEVEAILNGDVNLQVWSDHHRPSLSRIKLAIKYEVKKFVAHPNCQQQLLTMWYENLSGLRQQSIAVKFLAVFGVSIGLPFLAIAYWIAPCSKLGQTLRSPFMKFVAHAVSFTIFLGLLVVNASDRFEGVKTLPNETFTDYPKQIFRVKTTQFSWTEMLIMKWVLGMIWSECKEIWEEGPREYVLHLWNLLDFGMLSIFVASFTARFMAFLKASEAQLYVDQYVQDVTLHNVSLPPEVAYFTYARDKWWPSDPQIISEGLYAIAVVLSFSRIAYILPANESFGPLQISLGRTVKDIFKFMVIFIMVFVAFMIGMFNLYSYYRGAKYNPAFTTVEESFKTLFWSIFGLSEVISVVLKYDHKFIENIGYVLYGVYNVTMVVVLLNMLIAMINNSYQEIEEDADVEWKFARAKLWLSYFDEGRTLPAPFNLVPSPKSFYYLIMRIKMCLIELCQSKAKRCENDLEMGMLNSKFRKTRYQAGMRNSENLTANSTFSKPTRYQKIMKRLIKRYVLKAQVDRENDEVNEGELKEIKQDISSLRYELLEEKSQATGELADLIQQLSEKFGKNLNKDHLRVNQGKDI
Protein: Cilia- and flagella-associated protein 300 (Q57Y38)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000256|ARBA:ARBA00004430}.
Interaction partners:
- Polyubiquitin, putative
Sequence:
MVQREVFTFEPISKRRLETLMADPFFKEAYRRWGLQHRTKISAFRFERDTTGTNSGTVGTVVSGHFRFFGFHKGLLQEFLASLFDAPEVREKLQLRGEPKGTSSSGGGVEYCELQCRWTTLEPFKRLIDAGIVRCVEDEDKGDEAKGTVMVSEFETPLFDGVRMPIVKRADVYLPHDIVVCDELRALFLLAHNKFASVGCEYDEDDDYMGSGAFTFGSCAGLSLAVLRTVFGDVNERAEFLYHILWRLVAGGGTTNQWDDELTVYLEATRMLYKALVSIRAVPTAAAAGAAATNGADEPDRVVEMKDTPHQSLQPDVVSTVVSVHAVAGLHLFDRDDGASPNNLNYCYVCIDPLLGEVVVWYHSF
Protein: F-actin-capping protein subunit alpha-2 (Beta-actinin subunit I) (CapZ 36/32) (P28497)
Organism: Gallus gallus (Chicken)
Function: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. CapZ may mediate the attachment of the barbed ends of actin filaments to the Z-line.
Subcellular location: Cytoplasm, myofibril, sarcomere, Z line. Note=CapZ is located at the Z line in chicken muscle.
Interaction partners:
- F-actin-capping protein subunit beta isoforms 1 and 2
- F-actin-capping protein subunit alpha-1
- Protein S100-B
- F-actin-capping protein subunit alpha
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- Dynactin subunit 2
- ARP1 actin-related A, centractin alpha
- Dynactin subunit 1
- Dynactin subunit 4
- Actin-related protein 10
Sequence:
MADLEEQLSDEEKVRIAAKFIIHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNLDQFTPVKIDGYDEQVLITEHGDLGNGKFLDPKNKISFKFDHLRKEATDPRPHEVENAIESWRNSVETAMKAYVKEHYPNGVCTVYGKTIDGQQTIIACIESHQFQAKNFWNGRWRSEWKFTISPSTTQVAGILKIQVHYYEDGNVQLVSHKDIQDSLTVSNEAQTAKEFIKIVEAAENEYQTAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA
Protein: Ataxin 2 (A0A5F9ZHH4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSLKPQQQQQQQQQQQQQQQQQQQQQQQPPPAAANVRKPGGSGLLASPAAAPSPSSSSVSSSSATAPSSVVAATSGGGRPGLGRGRNSNKGLPQSTISFDGIYANMRMVHILTSVVGSKCEVQVKNGGIYEGVFKTYSPKCDLVLDAAHEKSTESSSGPKREEIMESILFKCSDFVVVQFKDMDSSYAKRDAFTDSAISAKVNGEHKEKDLEPWDAGELTANEELEALENDVSNGWDPNDMFRYNEENYGVVSTYDSSLSSYTVPLERDNSEEFLKREARANQLAEEIESSAQYKARVALENDDRSEEEKYTAVQRNSSEREGHSINTRENKYIPPGQRNREVISWGSGRQNSPRMGQPGSGSMPSRSTSHTSDFNPNSGSDQRVVNGGPPRMSPKAQRHPRNHRVSAGRGSISSGLEFVSHNPPSEAATPPVARTSPSGGTWSSVVSGVPRLSPKTHRPRSPRQNSIGNTPSGPVLASPQAGIIPTEAVAMPIPAASPTPASPASNRAVTPSSEAKDSRLQDQRQNSPAGNKENIKPNETSPSFSKAENKGISPVVSEHRKQIDDLKKFKNDFRLQPSSTSESMDQLLNKNREGEKSRDLIKDKIEPSAKDSFIENSSSNCTSGSSKPNSPSISPSILSNTEHKRGPEVTSQGVQTSSPACKQEKDDKEEKKDAAEQVRKSTLNPNAKEFNPRSFSQPKPSTTPTSPRPQAQPSPSMVGHQQPTPVYTQPVCFAPNMMYPVPVSPGVQPLYPIPMTPMPVNQAKTYRAVPNMPQQRQDQHHQSAMMHPASAAGPPIAATPPAYSTQYVAYSPQQFPNQPLVQHVPHYQSQHPHVYSPVIQGNARMMAPPTHAQPGLVSSSATQYGAHEQTHAMYVSTGSLAQQYAHPNATLHPHTPHPQPSATPTGQQQSQHGGSHPAPSPVQHHQHQAAQALHLASPQQQSAIYHAGLAPTPPSMTPASNTQSPQNSFPAAQQTVFTIHPSHVQPAYTNPPHMAHVPQAHVQSGMVPSHPTAHAPMMLMTTQPPGGPQAALAQSALQPIPVSTTAHFPYMTHPSVQAHHQQQL
Protein: Flagellar motor switch protein FliG (P23448)
Organism: Bacillus subtilis (strain 168)
Function: One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Bacterial flagellum basal body {ECO:0000250}.
Interaction partners:
- Flagellar M-ring protein
- Flagellar motor switch phosphatase FliY
- Flagellum-specific ATP synthase
- Flagellar motor switch protein FliM
- Flagellar basal-body rod protein FlgC
- Probable flagellar hook-length control protein
- Flagellar basal body rod protein FlgB
- Flagellar hook-basal body complex protein FliE
- Motility protein B
- Probable flagellar assembly protein FliH
Sequence:
MARRDQDKLTGKQKAAILMISLGLDVSASVYKHLTDEEIERLTLEISGVRSVDHQKKDEIIEEFHNIAIAQDYISQGGLSYARQVLEKALGEDKAENILNRLTSSLQVKPFDFARKAEPEQILNFIQQEHPQTMALILSYLDPVQAGQILSELNPEVQAEVARRIAVMDRTSPEIINEVERILEQKLSSAFTQDYTQTGGIEAVVEVLNGVDRGTEKTILDSLEIQDPDLAEEIKKRMFVFEDIVTLDNRAIQRVIRDVENDDLLLSLKVASEEVKEIVFNNMSQRMVETFKEEMEFMGPVRLKDVEEAQSRIVSIVRKLEEAGEIVIARGGGDDIIV
Protein: Actin-related protein 2/3 complex subunit 4 (Arp2/3 complex 20 kDa subunit) (p20-ARC) (P59998)
Organism: Homo sapiens (Human)
Function: Actin-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA. The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9359840}. Cell projection {ECO:0000269|PubMed:9359840}. Nucleus {ECO:0000269|PubMed:29925947}.
Interaction partners:
- Actin-related protein 2/3 complex subunit 5-like protein
- Actin-related protein 2/3 complex subunit 5
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 1A
- Actin-related protein 2/3 complex subunit 2
- Actin-related protein 2/3 complex subunit 1B
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 3
- Actin nucleation-promoting factor WASL
- NCK-interacting protein with SH3 domain
Sequence:
MTATLRPYLSAVRATLQAALCLENFSSQVVERHNKPEVEVRSSKELLLQPVTISRNEKEKVLIEGSINSVRVSIAVKQADEIEKILCHKFMRFMMMRAENFFILRRKPVEGYDISFLITNFHTEQMYKHKLVDFVIHFMEEIDKEISEMKLSVNARARIVAEEFLKNF
Protein: Secretion system chaparone (H9L426)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Interaction partners:
- SPI-2 type 3 secretion system translocon protein SctB
- Secreted effector protein SseB
- SPI-2 type 3 secretion system translocon protein SctE
- Secretion system chaparone
- Secretion system apparatus lipoprotein SsaJ
- Type III secretion system chaperone SseA
- Secretion system effector
- Virulence protein YscR
- Type 3 secretion system secretin
- Secretion system apparatus protein SsaL
Sequence:
MKKDPTLQQAHDTMRFFRRGGSLRMLLDDDVTQPLNTLYRYATQLMEVKEFAGAARLFQLLTIYDAWSFDYWFRLGECCQAQKHWGEAIYAYGRAAQIKIDAPQAPWAAAECYLACDNVCYAIKALKAVVRICGEVSEHQILRQRAEKMLQQLSDRS
Protein: Synembryn (Protein Ric-8) (B7WPL0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cell cortex {ECO:0000256|ARBA:ARBA00004544}.
Interaction partners:
Sequence:
MDEERALYIVRAGEAGAIERVLRDYSDKHRATFKFESTDEDKRKKLCEGIFKVLIKDIPTTCQVSCLEVLRILSRDKKVLVPVTTKENMQILLRLAKLNELDDSLEKVSEFPVIVESLKCLCNIVFNSQMAQQLSLELNLAAKLCNLLRKCKDRKFINDIKCFDLRLLFLLSLLHTDIRSQLRYELQGLPLLTQILESAFSIKWTDEYESAIDHNGPPLSPQETDCAIEALKALFNVTVDSWKVHKESDSHQFRVMAAVLRHCLLIVGPTEDKTEELHSNAVNLLSNVPVSCLDVLICPLTHEETAQEATTLDELPSNKTAEKETVLKNNTMVYNGMNMEAIHVLLNFMEKRIDKGSSYREGLTPVLSLLTECSRAHRNIRKFLKDQVLPPLRDVTNRPEVGSTVRNKLVRLMTHVDLGVKQIAAEFLFVLCKERVDSLLKYTGYGNAAGLLAARGLLAGGRGDNWYSEDEDTDTEEYKNAKPNINLITGHLEEPMPNPIDEMTEEQKEYEAMKLVNMLDKLSREELLKPMGLKPDGTITPLEEALNQYSVIEETSSDTD
Protein: Metal-response element-binding transcription factor 2 (Metal regulatory transcription factor 2) (Metal-response element DNA-binding protein M96) (Polycomb-like protein 2) (hPCl2) (Q9Y483)
Organism: Homo sapiens (Human)
Function: Polycomb group (PcG) protein that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex, thus enhancing PRC2 H3K27me3 methylation activity. Regulates the transcriptional networks during embryonic stem cell self-renewal and differentiation (By similarity). Promotes recruitment of the PRC2 complex to the inactive X chromosome in differentiating XX ES cells and PRC2 recruitment to target genes in undifferentiated ES cells (By similarity). Required to repress Hox genes by enhancing H3K27me3 methylation of the PRC2 complex (By similarity). In some conditions may act as an inhibitor of PRC2 activity: able to activate the CDKN2A gene and promote cellular senescence by suppressing the catalytic activity of the PRC2 complex locally (By similarity). Binds to the metal-regulating-element (MRE) of MT1A gene promoter (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:31959557}. Note=Localizes to chromatin as part of the PRC2 complex. {ECO:0000269|PubMed:31959557}.
Interaction partners:
- Polycomb protein SUZ12
- Protein Jumonji
- Histone-lysine N-methyltransferase EZH2
- Elongin BC and Polycomb repressive complex 2-associated protein
- Histone-binding protein RBBP7
- PHD finger protein 19
- Histone-binding protein RBBP4
- Zinc finger protein AEBP2
- Histone-lysine N-methyltransferase EZH1
- PHD finger protein 1
Sequence:
MRDSTGAGNSLVHKRSPLRRNQKTPTSLTKLSLQDGHKAKKPACKFEEGQDVLARWSDGLFYLGTIKKINILKQSCFIIFEDSSKSWVLWKDIQTGATGSGEMVCTICQEEYSEAPNEMVICDKCGQGYHQLCHTPHIDSSVIDSDEKWLCRQCVFATTTKRGGALKKGPNAKALQVMKQTLPYSVADLEWDAGHKTNVQQCYCYCGGPGDWYLKMLQCCKCKQWFHEACVQCLQKPMLFGDRFYTFICSVCSSGPEYLKRLPLQWVDIAHLCLYNLSVIHKKKYFDSELELMTYINENWDRLHPGELADTPKSERYEHVLEALNDYKTMFMSGKEIKKKKHLFGLRIRVPPVPPNVAFKAEKEPEGTSHEFKIKGRKASKPISDSREVSNGIEKKGKKKSVGRPPGPYTRKMIQKTAEPLLDKESISENPTLDLPCSIGRTEGTAHSSNTSDVDFTGASSAKETTSSSISRHYGLSDSRKRTRTGRSWPAAIPHLRRRRGRLPRRALQTQNSEIVKDDEGKEDYQFDELNTEILNNLADQELQLNHLKNSITSYFGAAGRIACGEKYRVLARRVTLDGKVQYLVEWEGATAS
Protein: LD36178p (Q7K0T0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
LFLGPRLGITGCTHSAPQLHRPPPLQGPTMNSKDKSKFKLFLKSLPAGYVGERTLRPEFERELRPEQPVAQRCRMLKELGDTQLHNFNLDESAITILFNLTNDLIVPNKPAETRQIALSFYKRLIHTQYKNLTIMREKFFLVIQNHEAREDLRHLLELLDTLTDNGKDITNFEEKIGKFMLLWIPAITEANLLTPYLDILVNLIKFNAAHLDKDILVGIVQNACDLSCSVTVNEIGLQCLTILEMVIGYTIFPSEPLPQCITTLCRTVNHAPYCPSSFKIMKNLLGTQLGYHSMKMMCSILNDRALYDDAHLLRGAVFHLNMNIFGSNIIFQVSPMTYATNVLTAFLRALDSRQVIVTFEVILSVRMVITKRQLSEIIWDLICDIMSSIVSNIEYYEEVNINKDRLHHLQINFHENIDCIEKLLQQDRSQILGNVERIYDLIERVADRRPEASVLALIEYRSRRVTATRPDWLQVLAQFVRRYYRMSNVNVRIKTIEALVQIMDQNRACYEEEILSRVVLVHLSHIHLESSVQVRVAVARALSNFATHCDTKRCMDLLDILEALINRPFEHTRHGSSSGEGTLAEVTFGLVNNESEISDIIAAVDGLVKVFAIKLHRLPGIHALKIFNILMDHLELHYERPKIFEHISVVRYKIFAWLLKARANGSYHIGYPEGSTEVVKFSPYLGIDSPLLPQAHPTAISIRRVCKLIVRCLEHDTDYQVFQLVIRELPKVLQNKALVQGNDIEELANTLLKINLVSNNKFKRPTDEFHALVLPAIASLVIYHESLQPQQHYGIITALNSRVLTGIASVCINTMTILILEMPEALMRKLPDVLLQMSKMSDTNALATPVLEFLSLLIHLSKHLFANFTSMHNMYVFAITLPYTKPHRYDHYTVSLAHHVIAGWFLKCKLELRRNCVNYIKSSIQSNAKMLSSDIVNLNSLNEDSSNRKRSTSLTERGSRNNANAWNDLEMRPQMNNGLRNFHAELAETCFDFLARHTYSPCPSMPKRLPAAEFLLKDGVSQTWLVGNNLVTITTSGCPSAPARSGLCERCAQLGKAPSISLNSKSLSDAAPPLSPERERRYTKVSLQHSSGNESAGSTELTSSSSSNSAAAGGHPHRQISNSSTASLDALSRRGSNPEALGSALGEGAHTGSNTSLLGNSLSQSSVSMSPSSGSVVQQPVCVRACTGWAEVLVRRPTGNVSWITRIQNPITNDCFGQELPFNNVVSLFLPTAHGGVFGPDNTIQAPPHTLADPEPEPEAEVNAATAPQASALRSRMVAKARALQRQEEIHSVGGNGNGNGNGNGSGNAPSTGGAAAIPIPRVPASGKRGKEAALCGSVSDGEADDDSLAFEDAQSRARNPVRRVNSSPEMSSSWRQSFLTNKPTPLSQEPVKTTADEPQSLLTLKKKTVQYSTKDMRVSCEAIPEEIAGSTPPSQAAALALQPESGTLPPKQHSADDVSSHVAGGSNLQAGGSTLKLGKPPLSPGQPPLLGTGRVTSFGGTSVPQPGALAKSSSSGSNGTNVGVITSDYDNGNNGNGDMMRGRSKTISVVREVNNGNTRPPPASSFRNFGAAKPPINTKLCMNPSFIFMQLYTTGQLGVTDEPLKVGPENSSAVSLIDLVPPFETHKIGVLYVGQGQCNNEVEILRNSHGSARYVEFLRNIGTLVSLKEAEQNNLFIMLDRNGADGKFAYIWKDDILQVTFHVATLMPTNLQDDPNCNEKKSHIGNDFVKIIYNESGEEYNLNTISGQFNYACVIVEPLDLNSNRVYVKARSEISKFVCHAEYRIVSDRSAPLLARQMALHANLASLVYQSVQKKHPYASNWLERLRKLKRLRSKLIEGLNSQQKSGSASSGIGINASAIGSDMDDQRGDFIKYT
Protein: ATP-dependent RNA helicase dbp7 (EC 3.6.4.13) (O60173)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- AdoMet-dependent rRNA methyltransferase spb1
- ATP-dependent RNA helicase rok1
- ATP-dependent RNA helicase dbp4
- rRNA biogenesis protein rrp5
- Multiple RNA-binding domain-containing protein 1
- ATP-dependent RNA helicase dbp3
- Ribosome biogenesis protein erb1
- Probable U3 small nucleolar RNA-associated protein 18
- ATP-dependent RNA helicase dbp9
- Nucleolar protein 12
Sequence:
MADEPLLLNFVVDNAQSRKPEALKSSRRWTDRARDRKRQKRNSNESSKSTVKRNSGTNGASTDYKNSQKEKVINPVFDPRKPAHELKGNKRDNTFVTSLFTGDDSEHFSQDVGQNLEDNQISNIGTTKEASNAPIKTTNFAGVQLDTQLADHLNNKMNISAPTAIQSCCLPALLNTDDKDAFIEAQTGSGKTLAYLLPIVQRLIRLPKNLHTRTSGIYAVIMAPTRELCQQIYNVANKLNNNPLSHWIVSCNVIGGEKKKSEKARIRKGVNILIGTPGRLADHLENTEALDVSQVRWVVLDEGDRLMDMGFEETLTKILSYLESQSSIIKKDLSIPSRKVTMLCSATMKDTVKRLSDSALKDALYLKSSIVEETNDGYSQAPEQLLQRYVVVPPKLRLVSLVALLRSHVRSYKKIIIFLSCSDSVDFHFEAFRCAINADEMEEAVKEKPDSEGDIISNAPALRIDGKSNVYRLHGSLSQQIRTSTLNLFSSSEDSGSHILLCTDVAARGLDLPNVDLVVQYDAPFSTDDYLHRIGRTARAGHNGAAIMFLLPKESEYINLLKSSVSANILEQPNGPSGLLSAGFSQGKTNTNDWQDRATEWQLELERFILENEPMRNIAKRAFTSYVRAYATHLSSERSIFNMRDLHLGHIAKSFALREAPGKISGANSSKPRKQGGSVDKGKSKSSKDIAALMHRKAMEHYSTEHNIG