wanglab/gogpt-training-data huggingface dataset:
Protein: Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2 (EC 2.7.4.24) (Diphosphoinositol pentakisphosphate kinase 2) (Histidine acid phosphatase domain-containing protein 1) (InsP6 and PP-IP5 kinase 2) (VIP1 homolog 2) (hsVIP2) (O43314)
Organism: Homo sapiens (Human)
Function: Bifunctional inositol kinase that acts in concert with the IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, exocytosis, insulin signaling and neutrophil activation. Phosphorylates inositol hexakisphosphate (InsP6) at position 1 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively, phosphorylates PP-InsP5 at position 1, produced by IP6Ks from InsP6, to produce (PP)2-InsP4. Required for normal hearing.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:17690096}.
Interaction partners:
- Inositol hexakisphosphate kinase 3
- Inositol hexakisphosphate kinase 1
- Inositol hexakisphosphate kinase 2
- Inositol-pentakisphosphate 2-kinase
- Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1
- Vasoactive intestinal polypeptide receptor 2
- VIP peptides
- Pituitary adenylate cyclase-activating polypeptide
Sequence:
MSEAPRFFVGPEDTEINPGNYRHFFHHADEDDEEEDDSPPERQIVVGICSMAKKSKSKPMKEILERISLFKYITVVVFEEEVILNEPVENWPLCDCLISFHSKGFPLDKAVAYAKLRNPFVINDLNMQYLIQDRREVYSILQAEGILLPRYAILNRDPNNPKECNLIEGEDHVEVNGEVFQKPFVEKPVSAEDHNVYIYYPTSAGGGSQRLFRKIGSRSSVYSPESNVRKTGSYIYEEFMPTDGTDVKVYTVGPDYAHAEARKSPALDGKVERDSEGKEVRYPVILNAREKLIAWKVCLAFKQTVCGFDLLRANGQSYVCDVNGFSFVKNSMKYYDDCAKILGNIVMRELAPQFHIPWSIPLEAEDIPIVPTTSGTMMELRCVIAVIRHGDRTPKQKMKMEVRHQKFFDLFEKCDGYKSGKLKLKKPKQLQEVLDIARQLLMELGQNNDSEIEENKPKLEQLKTVLEMYGHFSGINRKVQLTYLPHGCPKTSSEEEDSRREEPSLLLVLKWGGELTPAGRVQAEELGRAFRCMYPGGQGDYAGFPGCGLLRLHSTYRHDLKIYASDEGRVQMTAAAFAKGLLALEGELTPILVQMVKSANMNGLLDSDSDSLSSCQQRVKARLHEILQKDRDFTAEDYEKLTPSGSISLIKSMHLIKNPVKTCDKVYSLIQSLTSQIRHRMEDPKSSDIQLYHSETLELMLRRWSKLEKDFKTKNGRYDISKIPDIYDCIKYDVQHNGSLKLENTMELYRLSKALADIVIPQEYGITKAEKLEIAKGYCTPLVRKIRSDLQRTQDDDTVNKLHPVYSRGVLSPERHVRTRLYFTSESHVHSLLSILRYGALCNESKDEQWKRAMDYLNVVNELNYMTQIVIMLYEDPNKDLSSEERFHVELHFSPGAKGCEEDKNLPSGYGYRPASRENEGRRPFKIDNDDEPHTSKRDEVDRAVILFKPMVSEPIHIHRKSPLPRSRKTATNDEESPLSVSSPEGTGTWLHYTSGVGTGRRRRRSGEQITSSPVSPKSLAFTSSIFGSWQQVVSENANYLRTPRTLVEQKQNPTVGSHCAGLFSTSVLGGSSSAPNLQDYARTHRKKLTSSGCIDDATRGSAVKRFSISFARHPTNGFELYSMVPSICPLETLHNALSLKQVDEFLASIASPSSDVPRKTAEISSTALRSSPIMRKKVSLNTYTPAKILPTPPATLKSTKASSKPATSGPSSAVVPNTSSRKKNITSKTETHEHKKNTGKKK
Protein: NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit 1) (NDH subunit 1) (NADH-plastoquinone oxidoreductase subunit 1) (P12124)
Organism: Oryza sativa subsp. japonica (Rice)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01350}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01350}.
Interaction partners:
- NAD
- NADH dehydrogenase iron-sulfur protein 2
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial, putative, expressed
- NAD
- NAD
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NAD
- NAD
- NAD
- NAD
Sequence:
MIIDRVQVEAINSFSNLELLKEVYGLIWILPILTLLLGITIEVLVIVWLEREISASIQQRIGPEYAGPLGLLQAIADGTKLLFKEDILPSRGDIPLFSIGPSIAVISILLSFLVIPLGYRFVLADLSIGVFLWIAISSIAPIGLLMAGYSSNNKYSFLGGLRAAAQSISYEIPLTFCVLAISLLSNSLSTVDIVEAQSKYGFFGWNLWRQPIGFLVFLISSLAECERLPFDLPEAEEELVAGYQTEYSGIKYGLFYLVSYLNLLVSSLFVTVLYLGGWNLSIPYISFFGFFQMNKMVGILEMTMSIFITLTKAYLFLFISITIRWTLPRMRMDQLLNLGWKFLLPISLGNLLLTTSFQLVSL
Protein: Heat shock 70 kDa protein 13 (Heat shock protein family A member 13) (Microsomal stress-70 protein ATPase core) (Stress-70 protein chaperone microsome-associated 60 kDa protein) (P48723)
Organism: Homo sapiens (Human)
Function: Has peptide-independent ATPase activity.
Subcellular location: Microsome. Endoplasmic reticulum.
Interaction partners:
- Ubiquilin-2
- Ubiquilin-1
- Heat shock 70 kDa protein 12A
- DnaJ homolog subfamily B member 9
- Ubiquilin-4
- DnaJ homolog subfamily B member 1
- Heat shock 70 kDa protein 12B
- Heat shock 70kDa protein 14 isoform 1 variant 3
- Endoplasmin
- DnaJ homolog subfamily B member 4
Sequence:
MAREMTILGSAVLTLLLAGYLAQQYLPLPTPKVIGIDLGTTYCSVGVFFPGTGKVKVIPDENGHISIPSMVSFTDNDVYVGYESVELADSNPQNTIYDAKRFIGKIFTAEELEAEIGRYPFKVLNKNGMVEFSVTSNETITVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEAANLAGLKILRVINEPTAAAMAYGLHKADVFHVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQYLYKQIYQTYGFVPSRKEEIHRLRQAVEMVKLNLTLHQSAQLSVLLTVEEQDRKEPHSSDTELPKDKLSSADDHRVNSGFGRGLSDKKSGESQVLFETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFFGKDPNTSVDPDLAVVTGVAIQAGIDGGSWPLQVSALEIPNKHLQKTNFN
Protein: Homeobox protein Nkx-6.3 (Q3UHX8)
Organism: Mus musculus (Mouse)
Function: Putative transcription factor, which may be involved in patterning of central nervous system and pancreas.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MESNLQGTFLLNNTQLAQFSEMKAPMCQYSVQNSFYKLSPPGLGPQLAAGTPHGITDILSRPVATPNSSLLSGYPHVAGFGGLSSQGVYYGPQVGSFSKAGNEYPTRTRNCWADTGQDWRGSARPCSNTPDPLSDTIHKKKHTRPTFTGHQIFALEKTFEQTKYLAGPERARLAYSLGMTESQVKVWFQNRRTKWRKKSALEPSSSTPRAPGGASGDRAASENEDDEYNKPLDPDSDDEKIRLLLRKHRAAFSVLSLGAHSV
Protein: Tegument protein VP16 (Alpha trans-inducing protein) (Alpha-TIF) (ICP25) (Vmw65) (P06492)
Organism: Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Function: In the early stage of viral replication, acts as a transcriptional activator of immediate-early (IE) gene products (alpha-genes), which is released by invading virions. Recruits P-TEFb to the viral alpha-gene promoters and overcomes transcriptional inhibition by ICP22 to promote transcription of IE genes. VP16-induced complex represents a regulatory switch: when it is on, it promotes IE-gene expression and thus lytic infection, and when it is off, it limits IE-gene transcription favoring latent infection. Acts as a key activator of lytic infection by initiating the lytic program through the assembly of the transcriptional regulatory VP16-induced complex composed of VP16 and two cellular factors, HCFC1 and POU2F1. This complex recognizes the core motif 'TAATGARAT' in alpha-gene promoters. In the late stage of viral replication, VP16, as a tegument, is involved in viral assembly.
Subcellular location: Virion tegument {ECO:0000250|UniProtKB:P04486}. Host nucleus {ECO:0000250|UniProtKB:P04486}.
Interaction partners:
Sequence:
MDLLVDELFADMNADGASPPPPRPAGGPKNTPAAPPLYATGRLSQAQLMPSPPMPVPPAALFNRLLDDLGFSAGPALCTMLDTWNEDLFSALPTNADLYRECKFLSTLPSDVVEWGDAYVPERTQIDIRAHGDVAFPTLPATRDGLGLYYEALSRFFHAELRAREESYRTVLANFCSALYRYLRASVRQLHRQAHMRGRDRDLGEMLRATIADRYYRETARLARVLFLHLYLFLTREILWAAYAEQMMRPDLFDCLCCDLESWRQLAGLFQPFMFVNGALTVRGVPIEARRLRELNHIREHLNLPLVRSAATEEPGAPLTTPPTLHGNQARASGYFMVLIRAKLDSYSSFTTSPSEAVMREHAYSRARTKNNYGSTIEGLLDLPDDDAPEEAGLAAPRLSFLPAGHTRRLSTAPPTDVSLGDELHLDGEDVAMAHADALDDFDLDMLGDGDSPGPGFTPHDSAPYGALDMADFEFEQMFTDALGIDEYGG
Protein: At5g57910 (Ribosomal RNA small subunit methyltransferase G) (Q8GW24)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At3g51500
- At4g30630
- RuvB-like helicase
- Actin-related protein 6
- Methyl-CpG-binding domain-containing protein 9
- Zinc finger transcription factor YY1
- DNA-binding protein-like
- Histone-lysine N-methyltransferase ATX5
- Protein EIN6 ENHANCER
- RuvB-like protein 1
Sequence:
MNPTHGDFTPLNSNHFEDPKVRFRHHSLMQDYGELHMETEAMRKRLQAVRERKATLMAEVRFLRRRYRHLRQDQPQEIKKVRRSNGGKKIRVEVSPSNKSEAETKHVSLPDLNHSEKAHDETKTSPKRRVPLFDLNQISGEEEQETEAVDNNQENTRVEESNSCKRLMISSIEMQQKDVKPSSCRNGGNGSNKRKISWQDPVAALRV
Protein: Rab3 GTPase-activating protein catalytic subunit (Q8RWW8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- At3g14910
- Factor of DNA methylation 2
- Factor of DNA methylation 1
- Protein INVOLVED IN DE NOVO 2
- Rab escort protein 1
- At5g50410
- Ras-related protein RABC2a
- Ras-related protein RABC1
- Ras-related protein RABC2b
Sequence:
MASVSKSNHLEEDDDAEEEVQHFDDFTLASSWERFISDIEATCRQWLADGPKNLVEKGAVAVEDSKNLFTVKHELKNVAKSYCMEFYFQIDNNGSQQAGIGNWNSNSHDLQLCFGVKDFLLIAPQSASGVLLDTPESSKLLSAVAIALSNCGSLWPAFVPVHDPSRKAYIGIQNMGTVFTRRFEADRVGSQVPVKLMHLEGLYELFVSKFVYSGVDFSMHTFRVHFMMRLTYQTFPYDEEDEEIDTDEVMGDKSDTAEHYGSESRNKVLWDDDCPWSEWYSAEDPLRGFELVVTWADRTVESTLEMAELENASPHDAEKWILHPILSPYLGDPSHGKRIDFASQLLCLVEALDSSFSAQFMEDFVSVENPSSENLKTSVVIPPPSVLDRVIKDLFREGSKLPDFTKGEHRLSRALKAAPLESLFTQFCLHSLWFGNCNIRAIAFLWIEFVREVRWCWEETQPLPKMPIDGSIDLSSCLINQKLHLLAICIEKKREMNEEFLDCIGSDDSSDASVSMEEHHKVDKRRNTSSEEELRRKRDSSIAEDTSKQLRFERKTERTNSVNQSPTDAIRRGSAGPVGTMMLLKSRQQLHAPFTQDPPLMTEDMHEERLQAVEAFGDSLNVPGQLEKDILLSDMSAFKAANPDAVFEDFIRWHSPGDWESFEPKTTEPSAGPSTEGSKDEWPPRGRLSQRMSDQGNLWRKSWNDAPALPADDQKPLLDPNREGEKIVHYLETVRPHQLLEQMVCTAFRGSADTLNQTNVGNMRQMTSKLEQLYLIMKFTLGALQRNNLPDKAKTVKDLKRLCMVFENVEKLVAVAASIHRKFLDASRLAQVIFSDFYGVYAPTMGMSANDEENKSRTEMEVSRQEVSLRERQVVSNLFSPPSANQSWRKVLSMGNLLNGHEPILREIIFSTGDDVNNGIHYAAAADVAATSDRKGEEIETHRMYVSGTSNDLRVGLSVTSCD
Protein: Mediator of RNA polymerase II transcription subunit 7 (hMED7) (Activator-recruited cofactor 34 kDa component) (ARC34) (Cofactor required for Sp1 transcriptional activation subunit 9) (CRSP complex subunit 9) (Mediator complex subunit 7) (RNA polymerase transcriptional regulation mediator subunit 7 homolog) (Transcriptional coactivator CRSP33) (O43513)
Organism: Homo sapiens (Human)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular location: Nucleus.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 19
- Mediator of RNA polymerase II transcription subunit 9
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 8
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 11
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 15
- Mediator of RNA polymerase II transcription subunit 21
- Mediator of RNA polymerase II transcription subunit 10
Sequence:
MGEPQQVSALPPPPMQYIKEYTDENIQEGLAPKPPPPIKDSYMMFGNQFQCDDLIIRPLESQGIERLHPMQFDHKKELRKLNMSILINFLDLLDILIRSPGSIKREEKLEDLKLLFVHVHHLINEYRPHQARETLRVMMEVQKRQRLETAERFQKHLERVIEMIQNCLASLPDDLPHSEAGMRVKTEPMDADDSNNCTGQNEHQRENSGHRRDQIIEKDAALCVLIDEMNERP
Protein: Hamartin (Tuberous sclerosis 1 protein homolog) (Q9EP53)
Organism: Mus musculus (Mouse)
Function: In complex with TSC2, inhibits the nutrient-mediated or growth factor-stimulated phosphorylation of S6K1 and EIF4EBP1 by negatively regulating mTORC1 signaling (By similarity). Implicated as a tumor suppressor. Involved in microtubule-mediated protein transport, but this seems to be due to unregulated mTOR signaling. Acts as a co-chaperone for HSP90AA1 facilitating HSP90AA1 chaperoning of protein clients such as kinases, TSC2 and glucocorticoid receptor NR3C1. Increases ATP binding to HSP90AA1 and inhibits HSP90AA1 ATPase activity. Competes with the activating co-chaperone AHSA1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (By similarity). Recruits TSC2 to HSP90AA1 and stabilizes TSC2 by preventing the interaction between TSC2 and ubiquitin ligase HERC1 (By similarity).
Subcellular location: Lysosome membrane {ECO:0000250|UniProtKB:Q92574}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q92574}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q92574}. Note=Recruited to lysosomal membranes in a RHEB-dependent process in absence of nutrients. In response to nutrients, the complex dissociates from lysosomal membranes and relocalizes to the cytosol. {ECO:0000250|UniProtKB:Q92574}.
Interaction partners:
- Tuberin
- TBC1 domain family member 7
- GTP-binding protein Rheb
- RAC-alpha serine/threonine-protein kinase
- Serine/threonine-protein kinase mTOR
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- Regulatory-associated protein of mTOR
- Glycogen synthase kinase-3 beta
- DNA damage-inducible transcript 4 protein
- Ribosomal protein S6 kinase alpha-1
Sequence:
MAQLANIGELLSMLDSSTLGVRDDVTAIFKESLNSERGPMLVNTLVDYYLETNSQPVLHILTTLQEPHDKHLLDKINEYVGKAATRLSILSLLGHVVRLQPSWKHKLSQAPLLPSLLKCLKMDTDVVVLTTGVLVLITMLPMIPQSGKQHLLDFFDIFGRLSSWCLKKPGHVTEVYLVHLHASVYALFHRLYGMYPCNFVSFLRSHYSMKENVETFEEVVKPMMEHVRIHPELVTGSKDHELDPRRWKTLETHDVVIECAKISLDPTEASYEDGYSVSHQLSACFPYRSADVTTSPYVDTQNSYGGSTSTPSSSSRLMLFSPPGQLPQSLSSPSTRLLPEPLQASLWSPSAVCGMTTPPTSPGNVPADLSHPYSKAFGTTAGGKGTPSGTPATSPPPAPPCPQDDCVHGSAAQASATAPRKEERADSSRPYLHRQSNDRGLEDPPGSKGSVTLRNLPDFLGDLASEEDSIEKDKEEAAISKELSEITTAEADPVVPRGGFDSPFYRDSLSGSQRKTHSAASGTQGSSVNPEPLHSSLDKHGPDTPKQAFTPIDPPSGSADVSPAGDRDRQTSLETSILTPSPCKIPPQRGVSFGSGQLPPYDHLFEVALPKTACHFVSKKTEELLKKVKGNPEEDCVPSTSPMEVLDRLIEQGAGAHSKELSRLSLPSKSVDWTHFGGSPPSDELRTLRDQLLLLHNQLLYERFKRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQSKHPDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRLEKDGRLRKLEEDRAEAAEAAEERLDCCSDGCTDSLVGHNEEASGHNGETRTSRPGGTRASCGGRVTGGSSSSSSELSTPEKPPSQRFSSRWEPALGEPSSSIPTTVGSLPSSKSFLGMKARELFRNKSESQCDEDSVTMSSSSLSETLKTELGKDSGTENKTSLSLDAPHPSSPNSDNVGQLHIMDYNETHPEHS
Protein: Quinohemoprotein alcohol dehydrogenase ADH-IIG (ADH IIG) (EC 1.1.9.1) (Alcohol dehydrogenase (azurin)) (Q4W6G0)
Organism: Pseudomonas putida (Arthrobacter siderocapsulatus)
Function: Catalyzes the dye-linked oxidation of primary alcohols to the corresponding aldehydes and the (subsequent) oxidation of the aldehydes to carboxylic acids. Active with primary alcohols, glycerol, 1,2-propanediol, 1,3-propanediol but not with methanol or sugar alcohols such as D-sorbitol.
Subcellular location: Periplasm {ECO:0000305|PubMed:16061256}.
Interaction partners:
Sequence:
MRQTGLASLPLKSLAVAVLLSLAGTPALAADIPANVDGARIIAADKEPGNWMSTGRTYDEQRYSPLKQISDQNVGQLGLAWSYKLDLDRGVEATPIVVDGAMYTTGPFSVVYALDARDGRLIWKYDPQSDRHRAGEACCDAVNRGVAVWKGKVYVGVLDGRLEAIDAKTGQRAWSVDTRADHKRSYTITGAPRVVNGKVVIGNGGAEFGVRGYVTAYDAETGKEAWRFYTVPGDPKLPPEGKGMEIAAKTWFGDAYVEQGGGGTAWDSFAYDPELNLLYIGVGNGSLWDPKWRSQAKGDNLFLSSIVAVNADTGEYVWHYQTTPGDAWDYTATQHMILAELPIDGKPRKVLMQAPKNGFFYVIDRATGELLSAKGIVPQSWTKGMDMKTGRPILDEENAAYWKNGKRNLVTPAFWGAHDWQPMSYNPDTGLVYIPAHIMSAYYEHIPEAPKRNPFKSMYQLGLRTGMMPEGAEGLLEMAKSWSGKLIAWDPVKQQAAWEVPYVTIFNGGTLSTAGNLVFEGSADGRVIAYAADTGEKLWEQPAASGVMAAPVTYSVDGEQYVTFMAGWGGAFSTFAGALSLRAGVQPYAQVLTYKLGGTAKLQEPAPRPDTPKPPALSNDTASIEAGAKLYDGYCSQCHGIHAVSGGVLPDLRKLTPEKHQMFLGILFGGRVPDGMPSFADAFTPEQVDQIHQYLIKRAHDLHQEGDTWKQFSAKSSH
Protein: S-methyl-5'-thioadenosine phosphorylase (EC 2.4.2.28) (5'-methylthioadenosine phosphorylase) (MTA phosphorylase) (MTAP) (MTAPase) (A0A0G2K583)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03155}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03155}.
Interaction partners:
Sequence:
MASGSACTAVKIGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRHHTIMPSKVNYQANIWALKEEGCTHVIVTTACGSLREEIQPGDMVIIDQFIDRTSLRPQTFYDGSHCSARGVCHIPMAEPFCPKTREVLIEMAKKLGLRCHSKGTIVTIEGPRFSSRAESFIFRTWGADVINMTTVPEVVLAKEAGLCYASIAMATDYDCWKEHEEAVSVDGVLKTMKENANKAKSLLLTTIPQIGSMEWSETLRNLKNMAQSSVLPPRH
Protein: Mitochondrial import receptor subunit TOM9-2 (Mitochondrial import receptor subunit TOM22 homolog 2) (Translocase of outer membrane 22 kDa subunit homolog 2) (Translocase of outer membrane 9 kDa subunit TOM9-2) (Q9FNC9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Central component of the receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM20 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the translocation pore (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:14730085, ECO:0000269|Ref.6}; Single-pass type II membrane protein {ECO:0000269|PubMed:14730085, ECO:0000269|Ref.6}.
Interaction partners:
- Mitochondrial import receptor subunit TOM40-1
- Probable mitochondrial import receptor subunit TOM40-2
- Mitochondrial import receptor subunit TOM20-3
- Mitochondrial import receptor subunit TOM20-2
- Outer membrane OMP85 family protein
- Probable mitochondrial import inner membrane translocase subunit TIM21
- Outer membrane OMP85 family protein
- Mitochondrial import inner membrane translocase subunit TIM23-2
- Mitochondrial import inner membrane translocase subunit TIM50
- Mitochondrial import receptor subunit TOM20-4
Sequence:
MAAKRIGAGKSGGGDPNILARISNSEIVSQGRRAAGDAVEVSKKLLRSTGKAAWIAGTTFLILVVPLIIEMDREAQINEIELQQASLLGAPPSPMQRGL
Protein: Propionyl-CoA carboxylase alpha chain, mitochondrial (PCCase subunit alpha) (EC 6.4.1.3) (Propanoyl-CoA:carbon dioxide ligase subunit alpha) (P14882)
Organism: Rattus norvegicus (Rat)
Function: This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the catabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and other metabolites. Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA (By similarity). Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then transfers the carboxyl group from carboxylated biotin to propionyl-CoA (By similarity). Propionyl-CoA carboxylase also significantly acts on butyryl-CoA/butanoyl-CoA, which is converted to ethylmalonyl-CoA/(2S)-ethylmalonyl-CoA (By similarity). Other alternative minor substrates include (2E)-butenoyl-CoA/crotonoyl-CoA (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P05165}.
Interaction partners:
- Propionyl-CoA carboxylase beta chain, mitochondrial
- Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
- Holocarboxylase synthetase
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- Pyruvate carboxylase, mitochondrial
- Methylmalonyl-CoA epimerase, mitochondrial
- Isovaleryl-CoA dehydrogenase, mitochondrial
- 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- Hydroxymethylglutaryl-CoA lyase, mitochondrial
- Negative elongation factor complex member B
Sequence:
MAGLWVRTVALLAARRHWRRSSQQLLWTLKRAPRSSQQLLWTLKRAPVYSQQCLVVSRSLSSVEYEPKEKTFDKILIANRGEIACRVIKTCRKMGIRTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTGAQAVHPGYGFLSENKEFAKCLAAEDVTFIGPDTHAIQAMGDKIESKLLAKRAKVNTIPGFDGVLKDADEAVRIAREIGYPVMIKASAGGGGKGMRIPWDDEETRDGFRFSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAPSIFLDPETRRAMGEQAVAWPKAVKYSSAGTVEFLVDSQKNFYFLEMNTRLQVEHPVTECITGLDLVQEMILVAKGYPLRHKQEDIPISGWAVECRVYAEDPYKSFGLPSIGRLSQYQEPIHLPGVRVDSGIQPGSDISIYHDPMISKLVTYGSDRAEALKRMEDALDSYVIRGVTHNIPLLREVIINTRFVKGDISTKFLSDVYPDGFKGHMLTPSERDQLLAIASSLFVASQLRAQRFQEHSRVPVIRPDVAKWELSVKLHDEDHTVVASNNGPTFNVEVDGSKLNVTSTWNLASPLLSVNVDGTQRTVQCLSPDAGGNMSIQFLGTVYKVHILTKLAAELNKFMLEKVPKDTSSVLRSPKPGVVVAVSVKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKVKLVHCKAGDTVGEGDLLVELE
Protein: Caerin-1.10 (P86502)
Organism: Litoria rothii (Roth's tree frog) (Hyla rothii)
Function: Antibacterial peptide with wide spectrum of activity.
Subcellular location: Secreted {ECO:0000269|PubMed:16124032}.
Interaction partners:
Sequence:
GLLSVLGSVAKHVLPHVVPVIAEKL
Protein: Large ribosomal subunit protein eL36 (60S ribosomal protein L36) (Protein minute(1)1B) (P49630)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the large ribosomal subunit.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y3U8}. Cytoplasm {ECO:0000305|PubMed:23636399}. Note=Detected on cytosolic polysomes. {ECO:0000250|UniProtKB:Q9Y3U8}.
Interaction partners:
- Small ribosomal subunit protein eS28
- Large ribosomal subunit protein eL15
- 40S ribosomal protein S24
- Large ribosomal subunit protein eL34
- Small ribosomal subunit protein eS4
- Large ribosomal subunit protein P2
- Ubiquitin-ribosomal protein eS31 fusion protein
- Small ribosomal subunit protein uS12
- Large ribosomal subunit protein uL22
- Ubiquitin-ribosomal protein eL40 fusion protein
Sequence:
MAVRYELAIGLNKGHKTSKIRNVKYTGDKKVKGLRGSRLKNIQTRHTKFMRDLVREVVGHAPYEKRTMELLKVSKDKRALKFLKRRLGTHIRAKRKREELSNILTQLRKAQTHAK
Protein: UvrABC system protein A (UvrA protein) (Excinuclease ABC subunit A) (Q8NQQ0)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|HAMAP-Rule:MF_00205}.
Interaction partners:
- UvrABC system protein B
- UvrABC system protein C
- Transcription-repair-coupling factor
- Holliday junction branch migration complex subunit RuvA
- LexA repressor
- UvrD-like helicase ATP-binding domain-containing protein
- DNA repair protein RadA
- DNA polymerase IV
Sequence:
MADRLVVRGAREHNLKGVDIDLPRDSMVVFTGLSGSGKSSLAFDTIFAEGQRRYVESLSSYARMFLGQMDKPDVDLIDGLSPAVSIDQKSTNRNPRSTVGTITEVYDYLRLLYARAGTAHCPVCDARVERQTPQQMVDQILGMEEGLKFQILAPVVRTRKGEFVDLFADLASQGYSRVRVDGEVHQLSDPPKLEKQIKHDIDVVVDRLQVKASQKQRLTDSMETALRLADGVAVLEFVGLEEDDPNRLRRFSEKMSCPNGHALTVDELEPRAFSFNSPYGACPACDGLGVRTEVDIDLIIPDPDAPATKAVQPWNSSPNHSYFEKLIEGLAKALGFDPETPYSELTAAQKKALVYGSKEEVSVRYKNRYGRVRSWTAPFEGVMGYFDRKLEQTDSETQKDRLLGYTREVPCPTCKGARLKPEILAVRLDSGSHGALSIAGLTALSVHEAFEFLDNLTLGKREEMIAGAVLKEIHARLKFLLDVGLSYLTLDRAAGTLSGGEAQRIRLATQIGSGLAGVLYVLDEPSIGLHQRDNQRLITTLEHLRDIGNTLIVVEHDEDTIRRADWLVDIGPRAGEFGGEVVYQGEPKGILDCEESLTGAYLSGRRTLGVPDTRREIDKERQLKVVGARENNLQGIDVKIPLGVLCCITGVSGSGKSTLVNQILAKVLANKLNRARQVPGRAKRVEGLEHLDKLVQVDQSPIGRTPRSNPATYTGVFDKVRNLFAETTEAKVRGYKPGRFSFNIKGGRCEACQGDGTLKIEMNFLPDVYVPCEVCDGQRYNRETLEVKYKGKNIAEVLGMPISEAADFFEPITSIHRYLATLVDVGLGYVRLGQAATTLSGGEAQRVKLAAELQKRSNGRTVYILDEPTTGLHFEDIRKLMMVIEGLVDKGNSVIIIEHNLDVIKAADWIVDMGPEGGSGGGTVVAEGTPEQVAEVAGSYTGQFLKELL