wanglab/gogpt-training-data huggingface dataset:
Protein: V-maf musculoaponeurotic fibrosarcoma oncogene homolog K (Avian) (Q4V999)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MTTHFKAGKALKVKKEAGENAPALSDDELVAMSVRELNQHLRGLTKEDVVRLKQRRRTLKNRGYAASCRIKRVTQKEELERQKTELQHEVDKLARENASMRLELDALRAKYEALQCFARTVARGPPGKVAATSVITIVKSANHSPSSAPFSAQS
Protein: tRNA(His) guanylyltransferase 1 (EC 2.7.7.79) (F4IRQ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Adds a GMP to the 5'-end of tRNA(His) after transcription and RNase P cleavage.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:20660484}.
Interaction partners:
- Histidine--tRNA ligase, cytoplasmic
- Histidine--tRNA ligase, chloroplastic/mitochondrial
- tRNA-specific adenosine deaminase TAD2
- tRNA-specific adenosine deaminase TAD3
- Proteinaceous RNase P 1, chloroplastic/mitochondrial
- tRNA
- Nucleotidyltransferase
- RNA-binding
Sequence:
MINSVGVVRKEAENCNCLQVFFVSGSFKVDSVEAKKKEENFRETLRDMANSKYEYVKSFELEDEVMLPNLMVVRIDGRDFSRFSQVHEFEKPNDETALNLMNSCSAAVLEEFPDIIFAYGYSDEYSFVFKKTSRFYQRRASKILSLVASFFAAVYVTKWKEFFPQRKLLYAPSFSSKVVSCASAEVLQAYLAWRQQDCHANNQYDTCFWMLVKSGKSVSETQEILKDTQKQQKNELLFQKFGINYKTLPELFRQGSCLFKKKVEETVKHDENGNPVKRLRRKAVFVHSENIAGRSFWNEQPSLYNDLGHFTKDIGKIEPDFIRSFQFENKLLPLTWVVVRIDGCHFHRFSDVHEFEKPNDEQALKLMNSCAVAVLEEFEDIHFAYGVSDEYSFVLKKESELYKRQSSKIISAVASFFTSTYVLQWGEFFPHKELKYPPSFDGRAVCYPTYNILLDYLAWRQVDCHINNQYNTCFWMLVKSGKNKTQSQDYLKGTQTREKNELLSRQFGIEYNSLPVIFRMGSSVFRLKEAENGVVSGKKLEGEVVVDHCNIIERCFWEEHLHILSYS
Protein: L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase (AASD-PPT) (EC 2.7.8.7) (Q10474)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the transfer of a 4'-phosphopantetheine moiety from coenzyme A to a serine residue of acceptor proteins, such as alpha-aminoadipate reductase. Necessary for alpha-aminoadipate reductase activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized protein C14G10.01
- L-2-aminoadipate reductase
- Putative holo-[acyl-carrier-protein] synthase
- Saccharopine dehydrogenase [NAD
- Orotate phosphoribosyltransferase
- Malonyl CoA-acyl carrier protein transacylase, mitochondrial
- Putative acyl carrier protein, mitochondrial
- Saccharopine dehydrogenase [NADP
- Putative 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
Sequence:
MKQKVYRLLIDTQEAWPFERTRIPSFKKLSDSERQQIERYYFDMDAKMALASILIKRHLVSTALECSPNEVQISVTKAGRPYCQSAHCPPIIFDFNVSHYGGIVIVVGAWLPSDPSGMRPINIGVDIVECKPLAFEASWMEDFMSVFTPCEWKLIKSSISSIDVFFLLWTCKEAILKALGIGLSGNPLDIVVTFHKLNELLNSEEVSLRRAATAVYSGYSWDLEIHKLILHSSTFYVSVAFPQDCVIMDLNWETLNDL
Protein: Chemotaxis protein PomA (Flagellar motor protein) (ORF1) (O87126)
Organism: Pseudomonas aeruginosa
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane {ECO:0000256|RuleBase:RU004057}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU004057}.
Interaction partners:
Sequence:
MDVLSLVGIILAFVAIVGGNFLEGGHAGALLNGPAALIVIGGTLAAALLQTPVNVLKRGLGMLGWVFFPPREDLSGGIDRIVSWSMTARKEGLLGLESIADAEPDPYARKGLQLLVDGAEPEVIRSILEVDLFTQESRDLQAAKVFESMGGYAPTIGIIGAVMGLIHVMGNLANPAQLGSGIAVAFVATIYGVGFANLLLLPIGNKLKTLVLRQSRYREMLLEGLLSIAEGENPRSIELKLQGFMD
Protein: Transcription factor 7 like 2, T cell specific, HMG box (D3YWT3)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPQLNGGGGDDLGANDELISFKDEGEQEEKNSENSSAERDLADVKSSLVNESETNQNSSSDSEAERRPPPRSESFRDKSRESLEEAAKRQDGGLFKGPPYPGYPFIMIPDLTSPYLPNGSLSPTARTYLQMKWPLLDVQAGSLQSRQTLKDARSPSPAHIVSNKVPVVQHPHHVHPLTPLITYSNEHFTPGNPPPHLPADVDPKTGIPRPPHPPDISPYYPLSPGTVGQIPHPLGWLVPQQGQPVYPITTGGFRHPYPTALTVNASMSRFPPHMVPPHHTLHTTGIPHPAIVTPTVKQESSQSDVGSLHSSKHQDSKKEEEKKKPHIKKPLNAFMLYMKEMRAKVVAECTLKESAAINQILGRRWHALSREEQAKYYELARKERQLHMQLYPGWSARDNYGKKKKRKRDKQPGETNGEKKSAFATYKVKAAASAHPLQMEAY
Protein: Galanin receptor type 1 (GAL1-R) (GALR-1) (P56479)
Organism: Mus musculus (Mouse)
Function: Receptor for the hormone galanin. The activity of this receptor is mediated by G proteins that inhibit adenylate cyclase activity.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P47211}; Multi-pass membrane protein.
Interaction partners:
- Galanin peptides
- Galanin receptor type 3
- Galanin receptor type 2
- Galanin-like peptide
- Mu-type opioid receptor
- Somatostatin
- Pro-opiomelanocortin
Sequence:
MELAMVNLSEGNGSDPEPPAPESRPLFGIGVENFITLVVFGLIFAMGVLGNSLVITVLARSKPGKPRSTTNLFILNLSIADLAYLLFCIPFQATVYALPTWVLGAFICKFIHYFFTVSMLVSIFTLAAMSVDRYVAIVHSRRSSSLRVSRNALLGVGFIWALSIAMASPVAYHQRLFHRDSNQTFCWEQWPNKLHKKAYVVCTFVFGYLLPLLLICFCYAKVLNHLHKKLKNMSKKSEASKKKTAQTVLVVVVVFGISWLPHHVVHLWAEFGAFPLTPASFFFRITAHCLAYSNSSVNPIIYAFLSENFRKAYKQVFKCHVCDESPRSETKENKSRMDTPPSTNCTHV
Protein: Mitochondrial carrier protein, putative (Q387M4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004225}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004225}.
Interaction partners:
Sequence:
MHDGNFLKEVTAGSVGGALATIVEYPLDTIKVRLQDDPHRYRGSLSCIIEITRSEGIFGGFFRGLPLPVIGAAVENATLFATYREAIGPAQDLFYRKRCEPDTEPYLAVFTAAAIGGIVVSHVLTPAELIKCKMQVQNTLPEEKRIYKNSAHCVTSIYRSSGIRGLFKGHVSMIMREALGCGMYFSTFQLVIRNMLQEGQVFTDASPFVHFLGGGCAGVVFWTSIYPIDVLKTKVQTNRSEYGNLSITQGLMRLYKIEGMRGLIRGYGVTAIRAFPGNAVLIAAYEQVNRIFEAQGSTNKLLCVCSGLNG
Protein: Proteinase inhibitor PSKP-1 (P83578)
Organism: Phyllomedusa sauvagei (Sauvage's leaf frog)
Function: Has antibacterial activity against Gram-negative bacterium E.coli ATCC 11229. Shows hemagglutinating activity. Inhibits prolyl endopeptidase, but not trypsin, chymotrypsin, V8 protease and proteinase K. May have a role in mucosal defense against microbes by interacting directly with their membranes.
Subcellular location: Secreted {ECO:0000269|PubMed:15153102}.
Interaction partners:
Sequence:
VIEPKCYKYEGKKCPPDINPVCGTDKRTYYNECALCVFIRQSTKKADKAIKIKKWGKC
Protein: Mitogen-activated protein kinase 9 (MAP kinase 9) (MAPK 9) (EC 2.7.11.24) (JNK-55) (Stress-activated protein kinase 1a) (SAPK1a) (Stress-activated protein kinase JNK2) (c-Jun N-terminal kinase 2) (P45984)
Organism: Homo sapiens (Human)
Function: Serine/threonine-protein kinase involved in various processes such as cell proliferation, differentiation, migration, transformation and programmed cell death. Extracellular stimuli such as pro-inflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK9/JNK2. In turn, MAPK9/JNK2 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity. In response to oxidative or ribotoxic stresses, inhibits rRNA synthesis by phosphorylating and inactivating the RNA polymerase 1-specific transcription initiation factor RRN3. Promotes stressed cell apoptosis by phosphorylating key regulatory factors including TP53 and YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Upon T-cell receptor (TCR) stimulation, is activated by CARMA1, BCL10, MAP2K7 and MAP3K7/TAK1 to regulate JUN protein levels. Plays an important role in the osmotic stress-induced epithelial tight-junctions disruption. When activated, promotes beta-catenin/CTNNB1 degradation and inhibits the canonical Wnt signaling pathway. Participates also in neurite growth in spiral ganglion neurons. Phosphorylates the CLOCK-BMAL1 heterodimer and plays a role in the regulation of the circadian clock. Phosphorylates POU5F1, which results in the inhibition of POU5F1's transcriptional activity and enhances its proteosomal degradation (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19675674}. Nucleus {ECO:0000269|PubMed:19675674}. Note=Colocalizes with POU5F1 in the nucleus. {ECO:0000250|UniProtKB:Q9WTU6}.
Interaction partners:
- Transcription factor Jun
- Dual specificity mitogen-activated protein kinase kinase 4
- Mitogen-activated protein kinase 8
- C-Jun-amino-terminal kinase-interacting protein 1
- Transcription factor JunD
- Dual specificity protein phosphatase 16
- Cellular tumor antigen p53
- Dual specificity protein phosphatase 10
- Transcription factor JunB
- C-Jun-amino-terminal kinase-interacting protein 3
Sequence:
MSDSKCDSQFYSVQVADSTFTVLKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGCVIFQGTDHIDQWNKVIEQLGTPSAEFMKKLQPTVRNYVENRPKYPGIKFEELFPDWIFPSESERDKIKTSQARDLLSKMLVIDPDKRISVDEALRHPYITVWYDPAEAEAPPPQIYDAQLEEREHAIEEWKELIYKEVMDWEERSKNGVVKDQPSDAAVSSNATPSQSSSINDISSMSTEQTLASDTDSSLDASTGPLEGCR
Protein: Ribonuclease J1 (RNase J1) (EC 3.1.-.-) (Q45493)
Organism: Bacillus subtilis (strain 168)
Function: An RNase that has endonuclease and 5'-3' exonuclease activity, playing a role in both rRNA and mRNA stability and degradation. Endonuclease activity can cleave within 4 nucleotides of the 5'-end of a triphosphorylated RNA. Endonuclease digestion by the RNase J1/J2 complex occurs at a different site and in some cases more efficiently than J1 or J2 alone. The exonuclease activity of the J1/J2 complex is highly processive on substrates longer than 5 nucleotides, on shorter substrates is distributive. Preferentially cleaves ssRNA, possibly in AU-rich regions. The 5'-exonuclease activity acts on 5'-hydroxyl and 5'-monophosphate but not 5'-triphosphate ends; it can digest through stem-loop structures if they are not too stable. Required for maturation of 16S rRNA. Acts preferentially on 16S rRNA precursors after association of the 30S and 50S ribosomal subunits. Plays a role in the secondary pathway of 23S rRNA 5' end maturation. Probably also participates in processing of pre-scRNA (the precursor of the signal recognition particle RNA). Major RNase that degrades both RNAs of the type I toxin-antitoxin system BsrE/SR5.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01491, ECO:0000269|PubMed:15831787, ECO:0000269|PubMed:17005971}. Note=Colocalizes with ribosomes.
Interaction partners:
- Ribonuclease Y
- Polyribonucleotide nucleotidyltransferase
- DEAD-box ATP-dependent RNA helicase CshA
- Ribonuclease J2
- Ribonuclease 3
- Ribonuclease R
- Mini-ribonuclease 3
- 3'-5' exoribonuclease YhaM
- ATP-dependent 6-phosphofructokinase
- Ribonuclease Z
Sequence:
MKFVKNDQTAVFALGGLGEIGKNTYAVQFQDEIVLIDAGIKFPEDELLGIDYVIPDYTYLVKNEDKIKGLFITHGHEDHIGGIPYLLRQVNIPVYGGKLAIGLLRNKLEEHGLLRQTKLNIIGEDDIVKFRKTAVSFFRTTHSIPDSYGIVVKTPPGNIVHTGDFKFDFTPVGEPANLTKMAEIGKEGVLCLLSDSTNSENPEFTMSERRVGESIHDIFRKVDGRIIFATFASNIHRLQQVIEAAVQNGRKVAVFGRSMESAIEIGQTLGYINCPKNTFIEHNEINRMPANKVTILCTGSQGEPMAALSRIANGTHRQISINPGDTVVFSSSPIPGNTISVSRTINQLYRAGAEVIHGPLNDIHTSGHGGQEEQKLMLRLIKPKFFMPIHGEYRMQKMHVKLATDCGIPEENCFIMDNGEVLALKGDEASVAGKIPSGSVYIDGSGIGDIGNIVLRDRRILSEEGLVIVVVSIDMDDFKISAGPDLISRGFVYMRESGDLINDAQELISNHLQKVMERKTTQWSEIKNEITDTLAPFLYEKTKRRPMILPIIMEV
Protein: Kunitz-type serine protease inhibitor (Oh11-1) (Venom chymotrypsin inhibitor) (P82966)
Organism: Ophiophagus hannah (King cobra) (Naja hannah)
Function: Serine protease inhibitor that inhibits chymotrypsin (Ki=3520 nM).
Subcellular location: Secreted {ECO:0000269|PubMed:11350064}.
Interaction partners:
Sequence:
MSSGRLLLLLGLLTLWAELTPVSGLGRPKFCELPPEPGLCNARKTFFYYSLHSHACQKFIYGGCGGNANKFKTIDECHRTCVG
Protein: Serine and arginine rich splicing factor 10 (A0A8I6A795)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSRYLRPPNTSLFVRNVADDTRSEDLRREFGRYGPIVDVYVPLDFYTRRPRGFAYVQFEDVRDAEDALHNLDRKWICGRQIEIQFAQGDRKTPNQMKAKEGRNVYSSSRYDDYDRYRRSRSRSYERRRSRSRSFDYNYRRSYSPRNRPTGRPRRSRSHSDNDRFKHRNRSFSRSKSNSRSRSKSQPKKEMKAKSRSRSASHTKTRGTSKTDSKTHYKSGSRYEKESRKKEPPRSKSQSRSQSRSRSKSRSRSWTSPKSSGH
Protein: Calcium channel, voltage-dependent, T type, alpha 1G subunit (Q5SUF8)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MDEEEDGAGAEESGQPRSFTQLNDLSGAGGRQGPGSTEKDPGSADSEAEGLPYPALAPVVFFYLSQDSRPRSWCLRTVCNPWFERVSMLVILLNCVTLGMFRPCEDIACDSQRCRILQAFDDFIFAFFAVEMVVKMVALGIFGKKCYLGDTWNRLDFFIVIAGMLEYSLDLQNVSFSAVRTVRVLRPLRAINRVPSMRILVTLLLDTLPMLGNVLLLCFFVFFIFGIVGVQLWAGLLRNRCFLPENFSLPLSVDLEPYYQTENEDESPFICSQPRENGMRSCRSVPTLRGEGGGGPPCGLDYEAYNSSSNTTCVNWNQYYTNCSAGEHNPFKGAINFDNIGYAWIAIFQVITLEGWVDIMYFVMDAHSFYNFIYFILLIIVGSFFMINLCLVVIATQFSETKQRESQLMREQRVRFLSNASTLASFSEPGSCYEELLKYLVYILRKAARRLAQVSRAVGVRAGLLSSPVARGGQEPQPSGSCSRSHRRLSVHHLVHHHHHHHHHYHLGNGTLRVPRASPEIQDRDANGSRWLMLPPPSTPTPSGGPPRGAESVHSFYHADCHLEPVRCQAPPPRSPSEASGRTVGSGKVYPTVHTSPPPEMLKDKALVEVAPSPGPPTLTSFNIPPGPFSSMHKLLETQSTGACHSSCKISSPCSKADSGACGPDSCPYCARTGAGEPESADHEMPDSDSEAVYEFTQDAQHSDLRDPHRRRRPSLGPDAEPSSVLAFWRLICDTFRKIVDSKYFGRGIMIAILVNTLSMGIEYHEQPEELTNALEISNIVFTSLFALEMLLKLLVYGPFGYIKNPYNIFDGVIVVISVWEIVGQQGGGLSVLRTFRLMRVLKLVRFLPALQRQLVVLMKTMDNVATFCMLLMLFIFIFSILGMHLFGCKFASERDGDTLPDRKNFDSLLWAIVTVFQILTQEDWNKVLYNGMASTSSWAALYFIALMTFGNYVLFNLLVAILVEGFQAEGDATKSESEPDFFSPSVDGDGDRKKRLALVALGEHSELRKSLLPPLIIHTAATPMSLPKSSSTGVGEALGSGSRRTSSSGSAEPGTAHHEMKSPPSARSSPHSPWSAASSWTSRRSSRNSLGRAPSLKRRSPSGERRSLLSGEGQESQDEEESSEEDRASPAGSDHRHRGSLEREAKSSFDLPDTLQVPGLHRTASGRSSASEHQDCNGKSASGRLARTLRADDPPLDGDDGDDEGNLSKGERLRAWVRARLPACCRERDSWSAYIFPPQSRFRLLCHRIITHKMFDHVVLVIIFLNCITIAMERPKIDPHSAERIFLTLSNYIFTAVFLAEMTVKVVALGWCFGEQAYLRSSWNVLDGLLVLISVIDILVSMVSDSGTKILGMLRVLRLLRTLRPLRVISRAQGLKLVVETLMSSLKPIGNIVVICCAFFIIFGILGVQLFKGKFFVCQGEDTRNITNKSDCAEASYRWVRHKYNFDNLGQALMSLFVLASKDGWVDIMYDGLDAVGVDQQPIMNHNPWMLLYFISFLLIVAFFVLNMFVGVVVENFHKCRQHQEEEEARRREEKRLKRLEKKRRSKEKQMAEAQCKPYYSDYSRFRLLVHHLCTSHYLDLFITGVIGLNVVTMAMEHYQQPQILDEALKICNYIFTVIFVLESVFKLVAFGFRRFFQDRWNQLDLAIVLLSIMGITLEEIEVNASLPINPTIIRIMRVLRIARVLKLLKMAVGMRALLDTVMQALPQVGNLGLLFMLLFFIFAALGVELFGDLECDETHPCEGLGRHATFRNFGMAFLTLFRVSTGDNWNGIMKDTLRDCDQESTCYNTVISPIYFVSFVLTAQFVLVNVVIAVLMKHLEESNKEAKEEAELEAELELEMKTLSPQPHSPLGSPFLWPGVEGVNSPDSPKPGAPHTTAHIGAASSGFSLEHPTMVPHTEEGPVPLGPDLLTVRKSGVSRTHSLPNDSYMCRNGSTAERSLGHRGWGLPKAQSGSILSVHSQPADTSCILQLPKDAHYLLQPHGAPTWGAIPKLPPPGRSPLAQRPLRRQAAIRTDSLDVQGLGSREDLLSEVSGPSCPLTRSSSFWGGSSIQVQQRSGSQSKVSKHIRLPAPCPGLEPSWAKDPQETRSSLELDTELSWISGDLLPSSQEEPLSPRDLKKCYSVEAQSCRRRPGSWLDEQRRHSIAVSCLDSGSQPRLCPSPSSLGGQPLGGPGSRPKKKLSPPSISIDPPESQGPRPPCSPGVCLRRRAPASDSKDPSASSPLDSTAASPSPKKDALSLSGLSSDPTDLDP
Protein: Transposon Ty1-DR2 Gag polyprotein (Gag-p49) (Transposon Ty1 protein A) (TY1A) (TYA) (p58) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Gag-p4] (Q03964)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MESQQLSQHSPISHGSACASVTSKEVQTTQDPLDISASKTEECEKVFTQANSQQPTTPPSAAVPENHHHASPQAAQVPLPQNGPYPQQRMMTPQQANISGWPVYGHPSLMPYPPYQMSPMYAPPGAQSQFTQYPQYVGTHLNTPSPESGNSFPDSSSAKSNMTSTNQHVRPPPILTSPNDFLNWVKIYIKFLQNSNLGDIIPTATRKAVRQMTDDELTFLCHTFQLFALSQFLPTWVKDILSVDYTDIMKILSKSINKMQSDTQEVNDITTLANLHYNGSTPADAFEAEVTNILDRLKNNGIPINNKVACQFIMRGLSGEYKFLRYARHRYIHMTVADLFSDIHSMYEEQQESKRNKSTYRRSPSDEKKDSRTYTNTTKPKSITRNSQKPNNSQSRTARAHNVSTSNNFPGPDNDLIRGSTTEPIQLKNKHDLHLRPGTY
Protein: Ubiquitin system component Cue domain containing protein (Q554F5)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MFFFIKKEEMKISPYEKEQKINQVLSMFPLLSRDHFLYSTLERNNWSLDASLTILQRRHEYLEAEQYQIERKLEENRLKKEREQRERERELRLIAQVRDIFGSKFTDHQIQRALYDNRNNVESTINHFMREIDQEQYRERQRRQQRLDEEDRLQRQRERDEYERRERNKKRVNDLLLEIKYSSPEQKRQLAQSKLFQDVLKDFDHLTVFDQPPPPQIKTIYVPVPQPIPQPRYVNNFPTTPTMPSFSPPDYNSSMFNNGNKPPTTTTTTTSNQPFQNLDPFNNTAITPFSTNPFFVDQNVSQGLMKTRPEEESARKLKELFPNTSDEVVRYVLLSTDNNMSLAIQNLLDITIKVENSKNASN
Protein: Tetratricopeptide repeat (TPR)-like superfamily protein (Q9LKU3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- ATPase E1
- DExH-box ATP-dependent RNA helicase DExH12
- Pre-mRNA-processing-splicing factor 8A
- AT3G18790 protein
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
- Cell division cycle 5-like protein
- Pre-mRNA-splicing factor SYF2
- Pre-mRNA-splicing factor SPF27 homolog
- U2 small nuclear ribonucleoprotein A'
- Pre-mRNA-processing factor 19 homolog 1
Sequence:
MAISKDLYPSQEDLLYEEELLRNQFSLKLWWRYLIAKAESPFKKRFIIYERALKALPGSYKLWYAYLRERLDIVRNLPVTHPQYDSLNNTFERGLVTMHKMPRIWVMYLQTLTVQQLITRTRRTFDRALCALPVTQHDRIWEPYLVFVSQNGIPIETSLRVYRRYLMYDPSHIEEFIEFLVKSERWQESAERLASVLNDDKFYSIKGKTKHKLWLELCELLVHHANVISGLNVDAIIRGGIRKFTDEVGMLWTSLADYYIRKNLLEKARDIYEEGMMKVVTVRDFSVIFDVYSRFEESTVAKKMEMMSSSDEEDENEENGVEDDEEDVRLNFNLSVKELQRKILNGFWLNDDNDVDLRLARLEELMNRRPALANSVLLRQNPHNVEQWHRRVKIFEGNAAKQILTYTEAVRTVDPMKAVGKPHTLWVAFAKLYENHKDLVNTRVIFDKAVQVNYKTVDHLASVWCEWAEMELRHKNFKGALELMRRATAVPTVEVRRRVAADGNEPVQMKLHRSLRLWSFYVDLEESLGTLESTRAVYEKILDLRIATPQIIMNYAFLLEENKYFEDAFKVYERGVKIFKYPHVKDIWVTYLTKFVKRYGKTKLERARELFEHAVSMAPSDAVRTLYLQYAKLEEDYGLAKRAMKVYEEATKKVPEGQKLEMYEIYISRAAEIFGVPRTREIYEQAIESGLPHKDVKIMCIKFAELERSLGEIDRARALYKYSSQFADPRSDPEFWNKWHEFEVQHGNEDTYREMLRIKRSVSASYSQTHFILPENMMQKDKLLDVEDAKGELKRAGLPEDEMAALERQLLSTTTPTEPAKDGGRRVGFVSAGVISQSGENEGKPVTGNGEDIELPDESDDESDGDDHVEISQKEVPAAVFGGLARKRDEDGEEAGEDGAAQKLGALERIKRQKLNQ
Protein: Signal recognition particle subunit SRP72 (Q5BHY9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|PIRNR:PIRNR038922}. Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
Sequence:
MSKDANPKEALIKAAYADVNKFGNNQEFDKAVKAVNRILGVAPDDPTALHCKVVCLVQLSKFEEAYKFIEKNRLSSLFFEKAYCEYQLNKHQQALKTIDDAGLQPLPPNLKELRTQVLYRLERYDECLDSYRDIIKNTSDEYEEERRTNLSAVAANLAVDQTKEVPEVPEDTYEQYFNSACIQANRQKYAEAERKLRTSEKLCLEDECASEEEIIEEVDVIRVQLAYVLQLQGKTKEASSIYADCLRHKPKDAALVAVASNNLVVVNKDQNVFDSKKKIRAALADACESRLTSRQKQVIALNNCLLALYTNAGDQVQQLSQKLAQTYPQVEFEALLIRCTQLAKDRKHKEAIEQLQKFAAAHKSHEFVSKFAIIQLQLLQGNRKDAIETLLSLGEAKYKPGVVSALVSLYLGTDNKTAASALLKSAVDWYKKNEVSSGDLSDMWRQAAEFHLRGGASETAASSLEELLKLNPNDTKVLAQLVIAYAQFQPKRALELSRKLPKLETLTTASEIDALEAANWVMSAKAAKKTANTKVEPSPSTPLEKKKNRNRKRKGKLPKNYNAEVAPDPERWLPKYERTGFRKKRGGARGKDVIKGSQGMASGAADQYDMSSRVNLTKNSPATPVYQETAPGPRQQHRKGGHKKKKGGRF
Protein: Three prime repair exonuclease 2 (EC 3.1.11.2) (3'-5' exonuclease TREX2) (Q9BQ50)
Organism: Homo sapiens (Human)
Function: Exonuclease with a preference for double-stranded DNA with mismatched 3' termini. May play a role in DNA repair.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MSEAPRAETFVFLDLEATGLPSVEPEIAELSLFAVHRSSLENPEHDESGALVLPRVLDKLTLCMCPERPFTAKASEITGLSSEGLARCRKAGFDGAVVRTLQAFLSRQAGPICLVAHNGFDYDFPLLCAELRRLGARLPRDTVCLDTLPALRGLDRAHSHGTRARGRQGYSLGSLFHRYFRAEPSAAHSAEGDVHTLLLIFLHRAAELLAWADEQARGWAHIEPMYLPPDDPSLEA
Protein: Sporulation-specific glucan 1,3-beta-glucosidase (EC 3.2.1.58) (Exo-1,3-beta-glucanase) (P32603)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probably involved in the processes of spore formation and contributes to ascospore thermoresistance by participating in the morphogenesis of ascospore walls. The enzyme may do this by modifying glucan linkages in the developing ascospore wall, thus strengthening it or lending it plasticity.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Glucan 1,3-beta-glucosidase I/II
- Glucan 1,3-beta-glucosidase
- 1,3-beta-glucan synthase component FKS3
- Glucan 1,3-beta-glucosidase 2
- Invertase 2
- 1,3-beta-glucan synthase component GSC2
- 1,3-beta-glucan synthase component FKS1
- Ergosteryl-beta-glucosidase
Sequence:
MVSFRGLTTLTLLFTKLVNCNPVSTKNRDSIQFIYKEKDSIYSAINNQAINEKIHGVNLGGWLVLEPYITPSLFETFRTNPYNDDGIPVDEYHFCEKLGYEKAKERLYSHWSTFYKEEDFAKIASQGFNLVRIPIGYWAFTTLSHDPYVTAEQEYFLDRAIDWARKYGLKVWIDLHGAAGSQNGFDNSGLRDSYKFLEDENLSATMKALTYILSKYSTDVYLDTVIGIELLNEPLGPVIDMERLKNLLLKPAYDYLRNKINSNQIIVIHDAFQPYHYWDGFLNDEKNEYGVIIDHHHYQVFSQVELTRKMNERIKIACQWGKDAVSEKHWSVAGEFSAALTDCTKWLNGVGLGARYDGSWTKDNEKSHYINTCANNENIALWPEERKQNTRKFIEAQLDAFEMTGGWIMWCYKTENSIEWDVEKLIQLNIFPQPINDRKYPNQCH
Protein: Mitochondrial import inner membrane translocase subunit TIM8 (P57744)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIM8-TIM13 complex is non essential and only mediates the import of few proteins under precise conditions, while the predominant TIM9-TIM10 70 kDa complex is crucial and mediates the import of much more proteins. Strictly required for import of TIM23 in some conditions, when a low membrane potential exists in the mitochondria.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:10397776, ECO:0000269|PubMed:10469659, ECO:0000269|PubMed:16823961}; Peripheral membrane protein {ECO:0000269|PubMed:10397776, ECO:0000269|PubMed:10469659, ECO:0000269|PubMed:16823961}; Intermembrane side {ECO:0000269|PubMed:10397776, ECO:0000269|PubMed:10469659}. Mitochondrion intermembrane space {ECO:0000269|PubMed:22984289}. Note=Import into inner membrane protein requires TIM5 function.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit TIM13
- Mitochondrial import inner membrane translocase subunit TIM10
- Mitochondrial import inner membrane translocase subunit TIM9
- Mitochondrial import inner membrane translocase subunit TIM12
- Mitochondrial intermembrane space import and assembly protein 40
- Mitochondrial import receptor subunit TOM40
- Mitochondrial import inner membrane translocase subunit TIM23
- Mitochondrial import receptor subunit TOM22
- Mitochondrial import inner membrane translocase subunit TIM17
- Mitochondrial import inner membrane translocase subunit TIM54
Sequence:
MSSLSTSDLASLDDTSKKEIATFLEGENSKQKVQMSIHQFTNICFKKCVESVNDSNLSSQEEQCLSNCVNRFLDTNIRIVNGLQNTR
Protein: Citrate synthase 1 (EC 2.3.3.16) (P9WPD5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Aconitate hydratase A
- Malate dehydrogenase
- Malate synthase G
- Multifunctional 2-oxoglutarate metabolism enzyme
- Acetyl-coenzyme A synthetase
- Fumarate hydratase class II
- Probable malate:quinone oxidoreductase
- Pyruvate carboxylase
- Putative citrate synthase 2
- Dihydrolipoyllysine-residue acyltransferase component of branched-chain alpha-ketoacid dehydrogenase complex
Sequence:
MADTDDTATLRYPGGEIDLQIVHATEGADGIALGPLLAKTGHTTFDVGFANTAAAKSSITYIDGDAGILRYRGYPIDQLAEKSTFIEVCYLLIYGELPDTDQLAQFTGRIQRHTMLHEDLKRFFDGFPRNAHPMPVLSSVVNALSAYYQDALDPMDNGQVELSTIRLLAKLPTIAAYAYKKSVGQPFLYPDNSLTLVENFLRLTFGFPAEPYQADPEVVRALDMLFILHADHEQNCSTSTVRLVGSSRANLFTSISGGINALWGPLHGGANQAVLEMLEGIRDSGDDVSEFVRKVKNREAGVKLMGFGHRVYKNYDPRARIVKEQADKILAKLGGDDSLLGIAKELEEAALTDDYFIERKLYPNVDFYTGLIYRALGFPTRMFTVLFALGRLPGWIAHWREMHDEGDSKIGRPRQIYTGYTERDYVTIDAR