wanglab/gogpt-training-data huggingface dataset:
Protein: Centrosomal protein of 63 kDa (Cep63) (P0CB05)
Organism: Gallus gallus (Chicken)
Function: Required for normal spindle assembly. Plays a key role in mother-centriole-dependent centriole duplication. Plays a role in DNA damage response. Following DNA damage, such as double-strand breaks (DSBs), is removed from centrosomes; this leads to the inactivation of spindle assembly and delay in mitotic progression.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q96MT8}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:19182792}.
Interaction partners:
- Uncharacterized protein.
- Serine/threonine-protein kinase PLK
- Centromere protein J.
- POLO box domain-containing protein.
- Mitogen-activated protein kinase binding protein 1.
- Coiled-coil domain containing 14.
- Centrosomal protein 135.
- Centrin 3.
- STIL centriolar assembly protein.
- Centrosomal protein 192.
Sequence:
MEALLEGMQRNGQGSSGFLTSCEAELQELMKQIDIMVAHKKAEWEGQTQALEACLGVREQELSSARAALEEKHKEVGKLRQQLEDMEAAKQDLVREYEQQLKKFQEELARLRRSYEKLQKKQLREAREEATKRQGDDQCEMSRLSRKLEEFRQKSLDWEKQRLLYQQQVASLEAQRKALAEQSELIQTQLASRKQILESVELASRSEIQHLTSKLERANDTICANELEVERLNMRVDDLTENNRMILEDQQRVAEELRQSKKMLEVLQDEKMELRATLQSQEDFIDSSKLHQEQLQKELARVTETLHTKEILIRALEERLQEKQLSSPGLEHILLQLDVAQEKEQHLQAEVTHLEDSLVSSNARCVQLSEELAESIKELQSMEEHRAESKVEIKKLKEQLSQAEQIHRGELEGMRKEILRLTQELHQRDITIASAGGSTSDLEQRLRMEIERAERKAVEHRMILVQLETLKLENRHLSEMLEKVELGVLEGKDATLRALSEDYVVELNKLKSENQQLKKDLSEAREKLELTTQSQPEGTAQQLQSEEPEPRDVQHRPTQESQHKQDEQTEKIHHKPDKTTQHHQRWKIQPLPAEIPVAVIPEASVLPTQTSRKSCVESPTLAAGALQGTDSLLLVLDDSKGFPDATSRQSNHEQESVPLCPLPTSSVGSVAARYLEEEELRSQHILECLDAHIEELKKESEKIVRHFGHQE
Protein: Acyl-CoA thioesterase 2 (EC 3.1.2.20) (Thioesterase II) (TEII) (P0AGG2)
Organism: Escherichia coli (strain K12)
Function: Thioesterase that has relatively broad substrate specificity, hydrolyzing primarily medium- and long-chain acyl-CoA substrates to free fatty acids and CoA. Functions in the thioesterase-dependent pathway of beta-oxidation of oleate and conjugated linoleate ((9Z,11E)-octadecadienoate or CLA), which provides all energy and carbon precursors required for the growth of E.coli. Thus, supports growth on oleate or conjugated linoleate as the sole source of carbon by hydrolyzing 3,5-tetradecadienoyl-CoA, the terminal metabolite of oleate beta-oxidation via the alternative thioesterase-dependent pathway, and 3,5-dodecadienoyl-CoA, the end product of CLA beta-oxidation, respectively. Seems to be involved in 3-hydroxyalkanoate production in E.coli.
Interaction partners:
- Thioesterase 1/protease 1/lysophospholipase L1
- Acyl-CoA thioester hydrolase YciA
- Long-chain acyl-CoA thioesterase FadM
- Fatty acid oxidation complex subunit alpha
- Acyl-coenzyme A thioesterase PaaI
- Acyl-CoA thioester hydrolase YbgC
- 1,4-dihydroxy-2-naphthoyl-CoA hydrolase
- Fatty acid oxidation complex subunit alpha
- Glycerol-3-phosphate acyltransferase
Sequence:
MSQALKNLLTLLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSKKPIIYDVETLRDGNSFSARRVAAIQNGKPIFYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETQIAQSLAHLLPPVLKDKFICDRPLEVRPVEFHNPLKGHVAEPHRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGIQIATIDHSMWFHRPFNLNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNHN
Protein: Uncharacterized protein (Q384Q4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MNGEEGKGNGRYPAPVKLAREILDTVTLLQSRQNMWNEEMHRFFATEKQQQDESDSLTQRVQSAEAASREDGAFNDWMSRRAEQGVGKDILQDWYHTEALVSKTPFMAITPCPRGLSSGGRAEMVKAVDALELPRFLVQTVPLHLPLSKLSPTFVSSAFHVPEGERNSKSSLGALSYIGVPCTYGWDVLHLMNDHPMLAAAVDRTPCLFFNDYVPRAKLCIHCAIVGGFCVAAEVACDVQVAATLRLHESDTSERNAKSLISALSFALNTFVKDHLVSTLTGRSFRALIIGTEHTIQHRDLTAREEHLFPNNVSFFLLNLDSVDGSEFECFTQEEILSSARNAAKCRVENIPFDPIMRFLRPPN
Protein: Zinc finger protein 433 (Q8N7K0)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MMFQDSVAFEDVAVTFTQEEWALLDPSQKNLCRDVMQETFRNLASIGKKWKPQNIYVEYENLRRNLRIVGERLFESKEGHQHGEILTQVPDDMLKKTTTGVKSCESSVYGEVGSAHSSLNRHIRDDTGHKAYEYQEYGQKPYKCKYCKKPFNCLSSVQTHERAHSGRKLYVCEECGKTFISHSNLQRHRIMHRGDGPYKCKFCGKALMFLSLYLIHKRTHTGEKPYQCKQCGKAFSHSSSLRIHERTHTGEKPYKCNECGKAFHSSTCLHAHKRTHTGEKPYECKQCGKAFSSSHSFQIHERTHTGEKPYECKECGKAFKCPSSVRRHERTHSRKKPYECKHCGKVLSYLTSFQNHLGMHTGEISHKCKICGKAFYSPSSLQTHEKTHTGEKPYKCNQCGKAFNSSSSFRYHERTHTGEKPYECKQCGKAFRSASLLQTHGRTHTGEKPYACKECGKPFSNFSFFQIHERMHREEKPYECKGYGKTFSLPSLFHRHERTHTGGKTYECKQCGRSFNCSSSFRYHGRTHTGEKPYECKQCGKAFRSASQLQIHGRTHTGEKPYECKQCGKAFGSASHLQMHGRTHTGEKPYECKQCGKSFGCASRLQMHGRTHTGEKPYKCKQCGKAFGCPSNLRRHGRTHTGEKPYKCNQCGKVFRCSSQLQVHGRAHCIDTP
Protein: V-type proton ATPase catalytic subunit A (EC 7.1.2.2) (V-ATPase 69 kDa subunit) (Vacuolar proton pump subunit alpha) (A0A1W2Q641)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000256|ARBA:ARBA00029434}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00029434}.
Interaction partners:
Sequence:
MLLDVLDADTSCTYSWTLGQWSSVLSVVTACDMAGAAMYELVRVGHSELVGEIIRLEGDMATIQVYEETSGVSVGDPVLRTGKPLSVELGPGIMGAIFDGIQRPLSDISSQTQSIYIPRGVNVSALSRDIKWEFIPSKNLRVGSHITGGDIYGIVNENSLIKHKIMLPPRSRGSVTYIAPPGNYDASDVVLELEFEGVKEKLSMVQVWPVRQVRPVTEKLPANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDVIIYVGCGERGNEMSEVLRDFPELTMEVDGKVESIMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGNPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALDEYYDKHFTEFVPLRTKAKEILQEEEDLAEIVQLVGKASLAETDKITLEVAKLIKDDFLQQNGYTPYDRFCPFYKTVGMLSNMISFYDMARRAVETTAQSDNKITWSIIREHMGEILYKLSSMKFKDPVKDGEAKIKADYAQLLEDMQNAFRSLED
Protein: Thiolase (P71855)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MGYPVIVEATRSPIGKRNGWLSGLHATELLGAVQKAVVDKAGIQSGLHAGDVEQVIGGCVTQFGEQSNNISRVAWLTAGLPEHVGATTVDCQCGSGQQANHLIAGLIAAGAIDVGIACGIEAMSRVGLGANAGPDRSLIRAQSWDIDLPNQFEAAERIAKRRGITREDVDVFGLESQRRAQRAWAEGRFDREISPIQAPVLDEQNQPTGERRLVFRDQGLRETTMAGLGELKPVLEGGIHTAGTSSQISDGAAAVLWMDEAVARAHGLTPRARIVAQALVGAEPYYHLDGPVQSTAKVLEKAGMKIGDIDIVEINEAFASVVLSWARVHEPDMDRVNVNGGAIALGHPVGCTGSRLITTALHELERTDQSLALITMCAGGALSTGTIIERI
Protein: Protein CASP (Q13948)
Organism: Homo sapiens (Human)
Function: May be involved in intra-Golgi retrograde transport.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:12429822}; Single-pass type IV membrane protein {ECO:0000269|PubMed:12429822}.
Interaction partners:
Sequence:
MAANVGSMFQYWKRFDLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSDLSGRCAELQVRITEAVATATEQRELIARLEQDLSIIQSIQRPDAEGAAEHRLEKIPEPIKEATALFYGPAAPASGALPEGQVDSLLSIISSQRERFRARNQELEAENRLAQHTLQALQSELDSLRADNIKLFEKIKFLQSYPGRGSGSDDTELRYSSQYEERLDPFSSFSKRERQRKYLSLSPWDKATLSMGRLVLSNKMARTIGFFYTLFLHCLVFLVLYKLAWSESMERDCATFCAKKFADHLHKFHENDNGAAAGDLWQ
Protein: Laminin subunit beta 1 (A0A8I5ZQ25)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
Interaction partners:
Sequence:
MERPLSSLPTFAFSPLYLSRKEDTKKRRAACLPRPPSRAASPRLQGLDMGVLQVFAFGVLALWGTRVCAQEPEFSYGCAEGSCYPATGDLLIGRAQKLSVTSTCGLHKPEPYCIVSHLQEDKKCFICDSRDPYHETLNPDSHLIENVVTTFAPNRLKIWWQSENGVENVTVQLDLEAEFHFTHLIMTFKTFRPAAMLIERSSDFGKTWGVYRYFAYDCESSFPGISTGPMKKVDDIICDSRYSDIEPSTEGEVIFRALDPAFKIEDPYSPRIQNLLKITNLRIKFVKLHTLGDNLLDSRMEIREKYYYAVYDMVVRGNCFCYGHASECAPVDGFNEEVEGMVHGHCMCRHNTKGLNCELCMDFYHDLPWRPAEGRNSNACKKCNCNEHSSSCHFDMAVFLATGNVSGGVCDNCQHNTMGRNCEQCKPFYFQHPERDIRDPNLCEPCTCDPAGSENGGICDGYTDFSVGLIAGQCRCKLHVEGERCDVCKEGFYDLSAEDPFGCKSCACNPLGTIPGGNPCDSETGYCYCKRLVTGQRCDQCLPQHWGLSNDLDGCRPCDCDLGGALNNSCSEDSGQCSCLPHMIGRQCNEVESGYYFTTLDHYIYEAEEANLGPGVVVVERRYIQDRIPSWTGPGFVRVPEGAYLEFFIDNIPHSMEYEILIRYEPQLPDHWEKAVITVQRPGRIPTSSRCGNTVPDDDNQVVSLSPGSRYVVLPRPVCFEKGMNYTVRLELPQYTASGSDVESPYTLIDSLVLMPYCKSLDIFTVGGSGDGEVTNSAWETFQRYRCLENSRSVVKTPMTDVCRNIIFSISALIHQAGLACECDPQGSLSSVCDPNGGQCQCRPNVVGRTCNRCAPGTFGFGPNGCKPCDCHLQGSVSAFCDAVTGQCHCFQGIYARQCDRCLPGFWGFPSCQPCQCNGHAEDCDTVTGECLSCQDYTTGHNCERCLAGYYGDPIIGSGDHCRPCPCPDGPDSGRQFARSCYQDPVTLQLACVCDPGYIGSRCDGCASGYFGNPSDFGGSCQPCQCHHNIDTTDPEACDKETGRCLKCLYHTEGDHCQFCQHGYYGDALRQDCRKCVCNYLGTVREHCNGSDCHCDKTTGQCSCLPNVIGQNCDRCAPHTWQLASGTGCEPCNCNAVHSFGPSCNEFTGQCQCMPGFGGRTCSECQELFWGDPDVECRACDCDPRGIETPQCDQSTGQCVCVEGVEGPRCDKCTRGYSGVFPDCTPCHQCFALWDVIIGELTNRTHKFLEKAKALKISGVIGPYRETVDSVEKKVNEIRDILAQSPAAEPLKNIGILFEEAEKLTKDVTEKMAQVEVKLSDTASRSNSTAGELDALQAEAGSLDKTVNELAEQLEFIKNSDIQGALDSITKYFQISLEAEKRVNASTTDPNSTVEQSALTRDRVEDLMLERESQFKEKQEEQARLLDELAGKLQSLDLSAAAEMTCGTHPGADCSESECGGPNCRTDEGEKKCGGPGCGGLVTVAHSAWQKAMDFDRDVLNALAEVEQLSKMVSEAKVRADEAKQNAQDVLLKTNATREKVDRSNEDLRNLIKQIRDFLTEDSADLDSIEAVANEVLKMEMPSTPQQLQNLTEDIRERVETLSQVEVILQQSAADIARAELLLEEAKRASKSATDVKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKRKAAQNSGEADYIEKVVYSVKQSADEVKKTLDGELDEKYKKVESLIAQKTEESADARRKAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISEKVAVYSTCL
Protein: Neuronal cell adhesion molecule (Nr-CAM) (Ankyrin-binding cell adhesion molecule NrCAM) (Neuronal surface protein Bravo) (rBravo) (NgCAM-related cell adhesion molecule) (Ng-CAM-related) (P97686)
Organism: Rattus norvegicus (Rat)
Function: Cell adhesion protein that is required for normal responses to cell-cell contacts in brain and in the peripheral nervous system. Plays a role in neurite outgrowth in response to contactin binding. Plays a role in mediating cell-cell contacts between Schwann cells and axons (By similarity). Plays a role in the formation and maintenance of the nodes of Ranvier on myelinated axons. Nodes of Ranvier contain clustered sodium channels that are crucial for the saltatory propagation of action potentials along myelinated axons. During development, nodes of Ranvier are formed by the fusion of two heminodes. Required for normal clustering of sodium channels at heminodes; not required for the formation of mature nodes with normal sodium channel clusters. Required, together with GLDN, for maintaining NFASC and sodium channel clusters at mature nodes of Ranvier.
Subcellular location: Cell membrane {ECO:0000305|PubMed:8947556}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q810U4}. Cell projection, axon {ECO:0000269|PubMed:8947556}. Secreted {ECO:0000250|UniProtKB:Q810U4}. Note=Localized to axonal membranes at the node of Ranvier of myelinated axons (PubMed:8947556). {ECO:0000269|PubMed:8947556}.
Interaction partners:
- Ankyrin-3
- Gliomedin
- Receptor-type tyrosine-protein phosphatase zeta
- Contactin-5
- Contactin-2
- Ankyrin 2
- Ankyrin 1
- Hyaluronan and proteoglycan link protein 2
- Contactin associated protein family member 4
- Semaphorin-6D
Sequence:
MQLKTMPKKKPLSAGRAPLFLFLCQMISALDVPLDPKLLDDLVQPPTITQQSPKDYIIDPRENIVIQCEAKGKPPPSFSWTRNGTHFDIDKDPLVTMKPGSGTLVINIMSEGKAETYEGVYQCTARNERGAAVSNNIVVRPSRSPLWTKERLEPIILRSGQSLVLPCRPPIGLPPAIIFWMDNSFQRLPQSERVSQGLNGDLYFSNVLPEDTREDYICYARFNHTQTIQQKQPISLKVISVDELNDTIAANLSDTEFYGAKSSKERPPTFLTPEGNESHKEELRGNVLSLECIAEGLPTPVIYWIKEDGTLPVNRTFYRNFKKTLQIIHVSEADSGNYQCIAKNALGAVHHTISVTVKAAPYWIVAPHNLVLSPGENGTLICRANGNPKPRISWLTNGVPVEIALDDPSRKIDGDTIMFSNVQESSSAVYQCNASNKYGYLLANAFVNVLAEPPRILTSANTLYQVIANRPALLDCAFFGSPMPTIEWFKGTKGSALHEDIYVLHDNGTLEIPVAQKDSTGTYTCVARNKLGMAKNEVHLEIKDPTRFIKQPGYAVVQRGSKVSFECKVKHDHTLIPTILWLKDNGELPNDERFSVDKDHLVVSDVKDEDGGTYTCAANTTLDSVSASAVLRVVAPTPTPAPIYDVPNPPFDLELTNQLDKSVQLTWTPGDDNNSPITKFIIEYEDAMHEAGLWRHQAEVSGTQTTAQLKLSPYVNYSFRVMAENSIGRSVPSEASEQYLTKAAEPDQNPTAVEGLGTEPDNLVITWKPLNGFQSNGPGLQYKVSWRQKDGDDEWTSVVVANVSKYIVSGTPTFVPYLIKVQALNDVGFAPEPAAVMGHSGEDLPMVAPGNVRVSVVNSTLAEAHWDPVPPKSVRGHLQGYRIYYWKAQSSSKRNRRHIEKKILTFQGSKTHGMLPGLQPYSHYVLNVRVVNGKGEGPASADRGFHTPEGVPSAPSSLKIVNPTLDSLTLEWDPPSHPNGILTEYILKYQPINSTHELGPLVDLKIPANKTRWTLKNLNFSTRYKFYFYAQTSVGSGSQITEEAITTVDEGKKAGILPPDVGAGKAMASRQVDIATQGWFIGLMCAVALLILILLIVCFIRRNKGGKYPVKEKEDAHADPEIQPMKEDDGTFGEYSDAEDHKPLKKGSRTPSDRTVKKEDSDDSLVDYGEGVNGQFNEDGSFIGQYSGKKEKEPAEGNESSEAPSPVNAMNSFV
Protein: Protein LITTLE ZIPPER 1 (F4IG60)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Competitive inhibitor of the HD-ZIPIII transcription factors in shoot apical meristem (SAM) development. Acts by forming non-functional heterodimers. Part of a negative feedback loop. Essential for proper functioning of stem cells in the SAM.
Interaction partners:
- Protein LITTLE ZIPPER 4
- Protein LITTLE ZIPPER 3
Sequence:
MQREHKTHNKLSFIYITPLYISPINQTRLTYLSSSFLLSSSSKMCLSSSETFSDTPTRLVLYLKTQSHVRIPRLSRRRRMWREEKKMEMINLKLYVENQNIIRENEKLKKKALLLHQENKTLFSLLQTKKLSSVHK
Protein: Tryptase 5 (Q80X17)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MELALPAILFTFFPGVLLGSEVLPTDSDSPSTTTGRRSIDLDSVCGRPRTSGRIVSGQDAQLGRWPWQVSVRENGAHVCGGSLIAEDWVLTAAHCFNQGQSLSIYTVLLGTISSYPEDNEPKELRAVAQFIKHPSYSADEHSSGDIALVQLASPISFNDYMLPVCLPKPGDPLDPGTMCWVTGWGHIGTNQPLPPPFTLQELQVPLIDAETCNTYYQENSIPGTEPVILEGMLCAGFQEGKKDACNGDSGGPLVCDINDVWIQAGVVSWGSDCALFKRPGVYTNVSVYISWIQNTMWNLPMEGRGFSPSLSGTPLLGLLTSLSSAFFLLGP
Protein: WD repeat-containing and planar cell polarity effector protein fritz homolog (WD repeat-containing and planar cell polarity effector protein) (Q32NR9)
Organism: Xenopus laevis (African clawed frog)
Function: Probable effector of the planar cell polarity signaling pathway which regulates the septin cytoskeleton in both ciliogenesis and collective cell movements including covergent extension during gastrulation. Controls cell shape but not polarization during convergent extension. Proposed to function as core component of the CPLANE (ciliogenesis and planar polarity effectors) complex involved in the recruitment of peripheral IFT-A proteins to basal bodies.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20671153}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:20671153}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000305|PubMed:27158779}. Note=Also found adjacent to the cilium basal body.
Interaction partners:
Sequence:
MSFCLTELYLWSLKNNLHIGDEDVGVHQYHEKKEAALHPDYGFLEEKQQWMESRGFPWILKNKRPEKLRDNLTELEELMQSSECVLSKWKNKYVCQLLFGSGVLVSISLSGPQLEKVVIDRSLVGKLISNPISDAIFTDSFIILSFLKENKLCLIQFTKKINSPDINRQLDKLSLLDLKISYTDIPGPKGRHLVRHLAINSMQDLALCWWPVPVDDVKPWSPVSSEKDRANLVLLSNSSCKLEVLSYIRTEGDLLNACFSINQPYQICTVEHSLNSNKEPMADRFIYECVRNKIQCVSVTRVPLRSRVISCAVNTSEDKLVLGCEDSSLILYESDCKVTLLAQADLLPDLIRWHPNGTIFVVASSQGELQIFDMALSPIRAQILAEEIEPNSTIQVCKQFNVSSTLVEMHWAAPHTLLQNMDMTDIYNLLYLRFDGGPIGVLQLKLGAICRGQLGAMEIISQYIRHDEVDEAVGLLSSMNWNTMGHQCFTSMTAIVNHLLRQRLTPDREAQLEASLGTFYSPTRPLLDTIVLQYRDPISRYARRFFHHLLRYQRFEKAFLLAVDIGARDLFMDIHYLALDKGELALAKVARKKAEEIDAESINSGVEPLLPTDTLADVNEAFVDLSLIPQVEDRILGSFPSTDLGAHNSIQRNANRQLVHIENEIGIEVYAESLDKSLPWNQECFEEDFAEENPEGIGSLKVVHFGLV
Protein: Ankyrin repeat-containing protein YCR051W (P25631)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Uncharacterized protein YIR020C
- Uncharacterized protein YCR022C
- Subtilase-type proteinase RRT12
- 18S rRNA
- Sterol O-acyltransferase 1
- Large ribosomal subunit protein bL19m
- Putative uncharacterized protein YGR176W
Sequence:
MNANIWVAASDGNLDRVEHILRESKGAMTPQSKDINGYTPMHAAAAYGHLDLLKKMCNEYNGDINVLDNDGDTPLHHVEDVATARLIVEELGGDFTIRNVEGQTPYDSFVENGEDGELIEYMRIKSGVADVHGVDGVQGEGVIDSKLLEEFKDNVRYTLENDPEEGADEATLQRRRQLEQIITGDNAEEELERYIRAMVREQMLGQGSMAGSGDEPDSKRRK
Protein: 2-succinylbenzoate--CoA ligase (EC 6.2.1.26) (o-succinylbenzoyl-CoA synthetase) (OSB-CoA synthetase) (P37353)
Organism: Escherichia coli (strain K12)
Function: Converts 2-succinylbenzoate (OSB) to 2-succinylbenzoyl-CoA (OSB-CoA).
Interaction partners:
- o-succinylbenzoate synthase
- 1,4-dihydroxy-2-naphthoyl-CoA synthase
- 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
- 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase
- Isochorismate synthase MenF
- Protein ElaA
- Protein ElaB
- 1,4-dihydroxy-2-naphthoyl-CoA hydrolase
- Enterobactin synthase component F
Sequence:
MIFSDWPWRHWRQVRGETIALRLNDEQLNWRELCARVDELASGFAVQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLTLQFALVPDGENTFPALTSLHIQLVEGAHAATWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAQGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDKQPLEQMLAGCTHASLVPTQLWRLLVNRSSVSLKAVLLGGAAIPVELTEQAREQGIRCFCGYGLTEFASTVCAKEADGLADVGSPLPGREVKIVNNEVWLRAASMAEGYWRNGQLVSLVNDEGWYATRDRGEMHNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVMEYDHESVDLSEWVKDKLARFQQPVRWLTLPPELKNGGIKISRQALKEWVQRQQ
Protein: UvrABC system protein B (Protein UvrB) (Excinuclease ABC subunit B) (P9WFC7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00204}.
Interaction partners:
- UvrABC system protein C
- UvrABC system protein A
- ATP-dependent DNA helicase UvrD1
- Putative bifunctional exonuclease/endonuclease protein Rv2191
- Protein RecA
- ATP-dependent DNA helicase UvrD2
- Probable multidrug-efflux transporter Rv1634
- DNA repair protein RecN
- Adenine DNA glycosylase
- DNA polymerase I
Sequence:
MAFATEHPVVAHSEYRAVEEIVRAGGHFEVVSPHAPAGDQPAAIDELERRINAGERDVVLLGATGTGKSATTAWLIERLQRPTLVMAPNKTLAAQLANELREMLPHNAVEYFVSYYDYYQPEAYIAQTDTYIEKDSSINDDVERLRHSATSALLSRRDVVVVASVSCIYGLGTPQSYLDRSVELKVGEEVPRDGLLRLLVDVQYTRNDMSFTRGSFRVRGDTVEIIPSYEELAVRIEFFGDEIEALYYLHPLTGEVIRQVDSLRIFPATHYVAGPERMAHAVSAIEEELAERLAELESQGKLLEAQRLRMRTNYDIEMMRQVGFCSGIENYSRHIDGRGPGTPPATLLDYFPEDFLLVIDESHVTVPQIGGMYEGDISRKRNLVEYGFRLPSACDNRPLTWEEFADRIGQTVYLSATPGPYELSQTGGEFVEQVIRPTGLVDPKVVVKPTKGQIDDLIGEIRTRADADQRVLVTTLTKKMAEDLTDYLLEMGIRVRYLHSEVDTLRRVELLRQLRLGDYDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSSRSLIQTIGRAARNVSGEVHMYADKITDSMREAIDETERRRAKQIAYNEANGIDPQPLRKKIADILDQVYREADDTAVVEVGGSGRNASRGRRAQGEPGRAVSAGVFEGRDTSAMPRAELADLIKDLTAQMMAAARDLQFELAARFRDEIADLKRELRGMDAAGLK
Protein: NADH-quinone oxidoreductase subunit C/D (EC 7.1.1.-) (NADH dehydrogenase I subunit C/D) (NDH-1 subunit C/D) (NUO3/NUO4) (P33599)
Organism: Escherichia coli (strain K12)
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16079137}. Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01359, ECO:0000269|PubMed:16079137}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01359, ECO:0000269|PubMed:16079137}.
Interaction partners:
- NADH-quinone oxidoreductase subunit A
- NADH-quinone oxidoreductase subunit E
- NADH-quinone oxidoreductase subunit M
- NADH-quinone oxidoreductase subunit G
- NADH-quinone oxidoreductase subunit I
- NADH-quinone oxidoreductase subunit H
- NADH-quinone oxidoreductase subunit F
- Formate hydrogenlyase subunit 6
- NADH-quinone oxidoreductase subunit J
- NADH-quinone oxidoreductase subunit L
Sequence:
MTDLTAQEPAWQTRDHLDDPVIGELRNRFGPDAFTVQATRTGVPVVWIKREQLLEVGDFLKKLPKPYVMLFDLHGMDERLRTHREGLPAADFSVFYHLISIDRNRDIMLKVALAENDLHVPTFTKLFPNANWYERETWDLFGITFDGHPNLRRIMMPQTWKGHPLRKDYPARATEFSPFELTKAKQDLEMEALTFKPEEWGMKRGTENEDFMFLNLGPNHPSAHGAFRIVLQLDGEEIVDCVPDIGYHHRGAEKMGERQSWHSYIPYTDRIEYLGGCVNEMPYVLAVEKLAGITVPDRVNVIRVMLSELFRINSHLLYISTFIQDVGAMTPVFFAFTDRQKIYDLVEAITGFRMHPAWFRIGGVAHDLPRGWDRLLREFLDWMPKRLASYEKAALQNTILKGRSQGVAAYGAKEALEWGTTGAGLRATGIDFDVRKARPYSGYENFDFEIPVGGGVSDCYTRVMLKVEELRQSLRILEQCLNNMPEGPFKADHPLTTPPPKERTLQHIETLITHFLQVSWGPVMPANESFQMIEATKGINSYYLTSDGSTMSYRTRVRTPSFAHLQQIPAAIRGSLVSDLIVYLGSIDFVMSDVDR
Protein: NAD-dependent protein deacetylase sir-2.4 (EC 2.3.1.286) (Regulatory protein SIR2 homolog 4) (SIR2-like protein 4) (Q95Q89)
Organism: Caenorhabditis elegans
Function: NAD-dependent protein deacetylase.
Interaction partners:
- NAD-dependent protein deacylase sir-2.2
- Glutamine-dependent NAD
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Nicotinamide-nucleotide adenylyltransferase
- Purine nucleoside phosphorylase
- NAD-capped RNA hydrolase ndx-9
- NAD
- NAD kinase 2, mitochondrial
- NAD
- Nicotinamide N-methyltransferase-like
Sequence:
MTSVYESLLSDYPDKGVIGKPEIRDTETEIIEKLRTLYNHFVQAKQTGKPIFVLIGAGVSTGSKLPDFRGKQGVWTLQAEGKHAEGVDFQVARPGVSHKSILALHKAGYIKTIITQNVDGLDRKVGIPVEDLIEVHGNLFLEVCQSCFSEYVREEIVMSVGLCPTGRNCEGNKRTGRSCRGKLRDATLDWDTEISLNHLDRIRKAWKQTSHLLCIGTSLEIIPMGSLPLDAKSKGIKTTTINYQETAHEKIVETAIHADVKLILYSLCNALGVNVDLGDDLPDEVPIPLKIS
Protein: GH16214p (Myosin binding subunit, isoform E) (Q9VUX7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSFRSRSRTQAPLSSRRRSLSSSSRMAPSSGGSGAYNYNGSSYSSSGSTGRPLSTGYFPSSSSASSYQSPYASVYSSRESLYGGGGAGRSSYGSGGGGYDSSRYNPSSYSSAGSSYSTSDRYVSPYSSSYDKGVTTASLTFKSPGLSSSNSFKSSRLLKTKSLSASNSSLNGAYGGPSSNGVTSAGATVAAIAATRSNSLREQERKSRNRTRSKSAAQRSISASSEKSEGYESGSERTSRSRLGSTASTATTSESKSSSSNDKTENGDGIDYKALWEAEKLENDKLRQMLKQKDDEAVQTRATLERFANATTKNSLSELEKRERRAMERKLSELEEELKLLQKLKTENDRLRAENRALTRVVSKLTTSAQSQLAKSK
Protein: MARCKS-related protein (Brain protein F52) (MARCKS-like protein 1) (Macrophage myristoylated alanine-rich C kinase substrate) (Mac-MARCKS) (MacMARCKS) (Q9EPH2)
Organism: Rattus norvegicus (Rat)
Function: Controls cell movement by regulating actin cytoskeleton homeostasis and filopodium and lamellipodium formation. When unphosphorylated, induces cell migration. When phosphorylated by MAPK8, induces actin bundles formation and stabilization, thereby reducing actin plasticity, hence restricting cell movement, including neuronal migration. May be involved in coupling the protein kinase C and calmodulin signal transduction systems.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P28667}. Cell membrane {ECO:0000250|UniProtKB:P28667}; Lipid-anchor {ECO:0000250|UniProtKB:P28667}. Note=Associates with the membrane via the insertion of the N-terminal N-myristoyl chain and the partial insertion of the effector domain. Association of the effector domain with membranes may be regulated by Ca(2+)/calmodulin. Colocalizes with F-actin at the leading edge of migrating cells. {ECO:0000250|UniProtKB:P28667, ECO:0000250|UniProtKB:P49006}.
Interaction partners:
- Myristoylated alanine-rich C-kinase substrate
- Protein kinase C delta type
- Protein kinase C epsilon type
- Calmodulin-like protein 4
Sequence:
MGSQSSKAPRGDVTAEEAAGASPAKANGQENGHVKSNGDLTPKGEGESPPVNGADEAAGATGDAIEPAPPSQEAEAKGEVAPKETPKKKKKFSFKKPFKLSGLSFKRNRKEGGGDSSASSPTEEEQEQGEISACSDEGTAQEGKAAATPESQEPQAKGAEASAVSKGGDAEEEAGPQAAEPSTPSGPESGPASASAENE