wanglab/gogpt-training-data huggingface dataset:
Protein: Inositol-pentakisphosphate 2-kinase (EC 2.7.1.158) (IPK1 homolog) (Inositol-1,3,4,5,6-pentakisphosphate 2-kinase) (Ins(1,3,4,5,6)P5 2-kinase) (InsP5 2-kinase) (Q9H8X2)
Organism: Homo sapiens (Human)
Function: Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form Ins(1,2,3,4,5,6)P6 (InsP6 or phytate). InsP6 is involved in many processes such as mRNA export, non-homologous end-joining, endocytosis, ion channel regulation. It also protects cells from TNF-alpha-induced apoptosis.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Inositol polyphosphate multikinase
- Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1
- Inositol-tetrakisphosphate 1-kinase
- Inositol hexakisphosphate kinase 1
- Inositol hexakisphosphate kinase 2
- Inositol hexakisphosphate kinase 3
- Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2
Sequence:
MEEGKMDENEWGYHGEGNKSLVVAHAQRCVVLRFLKFPPNRKKTSEEIFQHLQNIVDFGKNVMKEFLGENYVHYGEVVQLPLEFVKQLCLKIQSERPESRCDKDLDTLSGYAMCLPNLTRLQTYRFAEHRPILCVEIKPKCGFIPFSSDVTHEMKHKVCRYCMHQHLKVATGKWKQISKYCPLDLYSGNKQRMHFALKSLLQEAQNNLKIFKNGELIYGCKDARSPVADWSELAHHLKPFFFPSNGLASGPHCTRAVIRELVHVITRVLLSGSDKGRAGTLSPGLGPQGPRVCEASPFSRSLRCQGKNTPERSGLPKGCLLYKTLQVQMLDLLDIEGLYPLYNRVERYLEEFPEERKTLQIDGPYDEAFYQKLLDLSTEDDGTVAFALTKVQQYRVAMTAKDCSIMIALSPCLQDASSDQRPVVPSSRSRFAFSVSVLDLDLKPYESIPHQYKLDGKIVNYYSKTVRAKDNAVMSTRFKESEDCTLVLHKV
Protein: Sulfotransferase (EC 2.8.2.-) (Q53X91)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNSELDYYEKFEEVHGILMYKDFVKYWDNVEAFQARPDDLVIATYPKSGTTWVSEIVYMIYKEGDVEKCKEDVIFNRIPFLECRKENLMNGVKQLDEMNSPRIVKTHLPPELLPASFWEKDCKIIYLCRNAKDVAVSFYYFFLMVAGHPNPGSFPEFVEKFMQGQVPYGSWYKHVKSWWEKGKSPRVLFLFYEDLKEDIRKEVIKLIHFLERKPSEELVDRIIHHTSFQEMKNNPSTNYTTLPDEIMNQKLSPFMRKGITGDWKNHFTVALNEKFDKHYEQQMKESTLKFRTEI
Protein: Uncharacterized GPI-anchored protein At5g19240 (Q84VZ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}.
Interaction partners:
- Zinc finger CCCH domain-containing protein 52
- Protein DA1-related 7
- Expansin-A13
- LIM domain-containing protein PLIM2b
- Protein DA1-related 1
- LIM domain-containing protein WLIM1
- LIM domain-containing protein WLIM2a
- Propionyl-CoA carboxylase
- LIM domain-containing protein PLIM2a
- LIM domain protein
Sequence:
MAISKLHLVLFLLSVFLSLHRPVLSNTDGENLLFTVFNQYRESVNLTNLKKNKNAECLADEVVDQLQNQPCTNTTGSASVPGTDPGIPNFPNLLAKCRLNTNVTRDGLILQVCAPKHHSTPDLSSFANVLTKNLNDSKFTGAGVGIDSDGIWLVTVLTTNTPGGSYSNSGAFAFGVNGLVSSSLMFLHVLSHNSLSLFS
Protein: Homeobox protein Meis2a isoform X6 (Meis homeobox 2a) (A0A0H2UKR5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MAQRYDELAHYGGMDGVGMYGDPHAPRPLPQVHHLNHGPPLHASQHYGTHAPHPNVMPTSMGSAVNDVLKRDKDQIYGHPLFPLLALVFEKCELATCTPREPGVAGGDVCSSDSFNEDIAVFAKQVRAEKPLFSSNPELDNLMIQAIQVLRFHLLELEKVHELCDNFCHRYISCLKGKMPIDLVIDERDGSSKSDHEELSGSSTNLADHNPASWRDHDDATSTHSAGTPGPSSGGLASQSGDNSSEQGDGLDNSVASPGTGDDDDPDKDKKRQKKRGIFPKVATNIMRAWLFQHLTHPYPSEEQKKQLAQDTGLTILQVNNWFINARRRIVQPMIDQSNRAVSQGAAYSPEGQPMGSFVLDGQQHMGIRPAGPMSGMGMNMGMDGQWHYM
Protein: Tumor suppressor protein 101 (Tumor susceptibility gene 101) (Q9VVA7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endosome {ECO:0000256|ARBA:ARBA00004177}.
Interaction partners:
- Vacuolar protein sorting-associated protein 28 homolog
- Multivesicular body subunit 12A
- EG:115C2.5 protein
- LD45836p
- Vacuolar protein-sorting-associated protein 36
- Jak pathway signal transduction adaptor molecule
- Vacuolar protein-sorting-associated protein 25
- Hepatocyte growth factor-regulated tyrosine kinase substrate
- ALG-2 interacting protein X
- vesicle-fusing ATPase
Sequence:
MPAVEETQITKYLSKYKYVAATKKDVVDVVTSFRSLTYDLQRFVFNDGSSKELFTIQGTIPVVYKNNTYYIPICIWLMDTHPQNAPMCFVKPTPTMQIKVSMYVDHNGKVYLPYLHDWQPHSSDLLSLIQVMIVTFGDHPPVYSKPKEQIAAPYPTNSYMPQPGAPGGSNSFLPYPTAGGAGGSNFPPYPTGSNVGPYPPTPAGPAGGSGYPAYPNFIQPTAGGYPPAAGYNPSNPSSTGTITEEHIKASIISAIDDKLRRRVQEKVNQYQAEIETLNRTKQELLEGSAKIDAIIERLEREHIDMQKNISILKDKEQELEKALEDLESAEAINPDEAVTTTAPLYRQLLNAYADEAATEDAIYYLGEGLRGGVIDLETFLKHVRQLSRKQFILRATMQKCRQKAGLAG
Protein: Protein ADP-ribosyltransferase (EC 2.4.2.-) (Sirtuin class M) (SirTM) (P0DN71)
Organism: Streptococcus pyogenes serotype M5 (strain Manfredo)
Function: Catalyzes specifically the mono-ADP-ribosylation of GcvH-L (SpyM50867). This activity is dependent on prior lipoylation of the target protein. May be involved in the modulation of the response to host-derived oxidative stress. In contrast to other sirtuin classes, lacks protein deacylase activity, being unable to catalyze debiotinylation, deacetylation and desuccinylation of proteins.
Interaction partners:
Sequence:
MSNWTTYPQKNLTQAEQLAQLIKEADALVVGIGAGMSAADGFTYIGPRFETAFPDFIAKYQFLDMLQASLFDFEDWQEYWAFQSRFVALNYLDQPVGQSYLDLKEILETKDYHIITTNADNAFWVAGYDPHNIFHIQGEYGLWQCSQHCHQQTYKDDTVIRQMIAEQKNMKVPGQLIPHCPECEAPFEINKRNEEKGMVEDADFHAQKARYEAFLSEHKEGKVLYLEIGVGHTTPQFIKHPFWKRVSENPNALFVTLNHKHYRIPLSIRRQSLELTEHIAQLISATKTIYQKS
Protein: Transcription factor bHLH49 (Basic helix-loop-helix protein 49) (AtbHLH49) (bHLH 49) (Protein ACTIVATOR FOR CELL ELONGATION 1) (Transcription factor EN 82) (bHLH transcription factor bHLH049) (Q9CAA9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator involved in cell elongation. Regulates the expression of a subset of genes involved in cell expansion by binding to the G-box motif.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Transcription factor IBH1
- Transcription factor PRE1
- Transcription factor PRE3
- Transcription factor PRE6
- Transcription factor bHLH150
- F-box/kelch-repeat protein SKIP30
- Transcription factor bHLH147
Sequence:
MDLSAKDEFSAEKRNPDNYDSVNNPSGDWRVDSYPSENLISAGPASCSPSQMMDSFGQTLWYDPTSVQAVGYAGFNGGNASSSSFRGSIDRSLEMGWNLPNLLPPKGNGLFLPNASSFLPPSMAQFPADSGFIERAARFSLFSGGNFSDMVNQPLGNSEAIGLFLQGGGTMQGQCQSNELNVGEPHNDVSVAVKESTVRSSEQAKPNVPGSGNVSEDTQSSGGNGQKGRETSSNTKKRKRNGQKNSEAAQSHRSQQSEEEPDNNGDEKRNDEQSPNSPGKKSNSGKQQGKQSSDPPKDGYIHVRARRGQATNSHSLAERVRREKISERMKFLQDLVPGCNKVTGKAVMLDEIINYVQSLQRQVEFLSMKLATVNPQMDFNLEGLLAKDALQLRAGSSSTTPFPPNMSMAYPPLPHGFMQQTLSSIGRTITSPLSPMNGGFKRQETNGWEGDLQNVIHINYGAGDVTPDPQAAATASLPAANMKVEP
Protein: Nucleolar RNA-binding protein, putative (Q57YF6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- RING-CH-type domain-containing protein
- Ribosome biogenesis protein BOP1 homolog
- MIF4G domain-containing protein
Sequence:
MEGFYGVEVSVGEKVIPEIPEGNVLRLTQIAVPANTSDAVSLVVSLQGKEFTIASLDPVRNVSQMGIDLVIKAEQNIILSATGNGSVHVTGYIQPIENVTDGESSCGGEICSGVPFEKMAPPPFRGVAPACKTSVQSSNNTSESDYDVEGIVSVDDGVEKIGKRGDKGEERPSKIRHEGGVEFHNEQHVDEHRYRRGGYFRYNGEGGYGGVHQGFFRQRGRQRINSTSSQGGFGAIYNEPIHEADQLGMNRGYGRGGYSSRGRGYMGGGYRGQANGEMRRGYTNEERYLYSGGEWQGMSSNLLGRGFAAINRGFHPYSSRNNYPFPPNHHLNDASRTLPPYSGRGGTNAVWNRGGFRGGNSGRGRY
Protein: Elongation factor G, mitochondrial (EF-Gmt) (Elongation factor G 1, mitochondrial) (mEF-G 1) (Elongation factor G1) (dEF-G1) (Protein iconoclast) (Q9VM33)
Organism: Drosophila melanogaster (Fruit fly)
Function: Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity). Essential during development as it acts as a retrograde signal from mitochondria to the nucleus to slow down cell proliferation if mitochondrial energy output is low.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03061, ECO:0000269|PubMed:21364917}.
Interaction partners:
- LD31543p
- GM03767p
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein bS6m
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein uS13
Sequence:
MSLITRLLTGNNTLRLRALKSLGKAGYSSHAKFSEHKPIERIRNIGISAHIDSGKTTLTERILFYTGRIAEMHEVRGKDNVGATMDSMELERQRGITIQSAATYTLWKDTNINIIDTPGHVDFTVEVERALRVLDGAVLVLCAVGGVQSQTLTVNRQMKRYNVPCLAFINKLDRLGSNPYRVLSQMRSKMNHNAAFIQLPIGVESNCKGIVDLVREKAIYFEGEHGMDIRLDEIPQDMRVESLERRQELIEHLSNADETLGELFLEEKPFTEDDIKAALRRTCINRTFTPVLVGTALKNKGVQPLLDAVLDYLPNPGEVENLGFIEKEGQDPEKVVLNPARDGKDPFVGLAFKLEAGRFGQLTYLRCYQGVLRKGDNIFNARTNKKVRIARLVRLHSNQMEDVNEVYAGDIFALFGVDCASGDTFTTNPKNNLSMESIFVPEPVVSMAIKPNNTKDRDNFSKAIARFTKEDPTFHFFFDNDVKETLVSGMGELHLEIYAQRMEREYGCPVTLGKPKVAFRETLVGPCEFDYLHKKQSGGSGQYARIIGVMEPLPPNQNTLLEFVDETVGTNVPKQFVPGVEKGYREMAEKGMLSGHKLSGIRFRLQDGGHHIVDSSELAFMLAAHGAIKEVFQNGSWQILEPIMLVEVTAPEEFQGAVMGHLSKRHGIITGTEGTEGWFTVYAEVPLNDMFGYAGELRSSTQGKGEFTMEYSRYSPCLPDVQDQIVRQYQESQGLAQPDKKKKKN
Protein: Sucrose synthase 2 (AtSUS2) (EC 2.4.1.13) (Sucrose-UDP glucosyltransferase 2) (Q00917)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sucrose-cleaving enzyme that provides UDP-glucose and fructose for various metabolic pathways. Modulates metabolic homeostasis and directs carbon towards starch synthesis in developing seeds.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18701523}. Plastid membrane {ECO:0000269|PubMed:18701523}; Peripheral membrane protein {ECO:0000269|PubMed:18701523}. Note=Associated with plastid membranes during the maturation phase of the seed.
Interaction partners:
- Granule-bound starch synthase 1, chloroplastic/amyloplastic
- Glucose-1-phosphate adenylyltransferase small subunit, chloroplastic
- Glucose-1-phosphate adenylyltransferase large subunit 3, chloroplastic
- Glucose-1-phosphate adenylyltransferase large subunit 2, chloroplastic
- Probable glucose-1-phosphate adenylyltransferase large subunit, chloroplastic
- Glucose-1-phosphate adenylyltransferase large subunit 1, chloroplastic
- alpha-D-xyloside xylohydrolase
- UTP--glucose-1-phosphate uridylyltransferase 1
- UTP--glucose-1-phosphate uridylyltransferase 2
- Beta-fructofuranosidase, insoluble isoenzyme CWINV2
Sequence:
MPTGRFETMREWVYDAISAQRNELLSLFSRYVAQGKGILQSHQLIDEFLKTVKVDGTLEDLNKSPFMKVLQSAEEAIVLPPFVALAIRPRPGVREYVRVNVYELSVDHLTVSEYLRFKEELVNGHANGDYLLELDFEPFNATLPRPTRSSSIGNGVQFLNRHLSSIMFRNKESMEPLLEFLRTHKHDGRPMMLNDRIQNIPILQGALARAEEFLSKLPLATPYSEFEFELQGMGFERGWGDTAQKVSEMVHLLLDILQAPDPSVLETFLGRIPMVFNVVILSPHGYFGQANVLGLPDTGGQVVYILDQVRALENEMLLRIQKQGLEVIPKILIVTRLLPEAKGTTCNQRLERVSGTEHAHILRIPFRTEKGILRKWISRFDVWPYLETFAEDASNEISAELQGVPNLIIGNYSDGNLVASLLASKLGVIQCNIAHALEKTKYPESDIYWRNHEDKYHFSSQFTADLIAMNNADFIITSTYQEIAGSKNNVGQYESHTAFTMPGLYRVVHGIDVFDPKFNIVSPGADMTIYFPYSDKERRLTALHESIEELLFSAEQNDEHVGLLSDQSKPIIFSMARLDRVKNLTGLVECYAKNSKLRELANLVIVGGYIDENQSRDREEMAEIQKMHSLIEQYDLHGEFRWIAAQMNRARNGELYRYIADTKGVFVQPAFYEAFGLTVVESMTCALPTFATCHGGPAEIIENGVSGFHIDPYHPDQVAATLVSFFETCNTNPNHWVKISEGGLKRIYERYTWKKYSERLLTLAGVYAFWKHVSKLERRETRRYLEMFYSLKFRDLANSIPLATDEN
Protein: Long arms of the bivalent protein 1 (Q17604)
Organism: Caenorhabditis elegans
Function: Involved in sister chromatid cohesion during mitosis and meiosis. In association with the gsp-2 phosphatase, it both restricts the localization and antagonizes the function of the air-2 kinase during meiosis I and mitosis to promote chromatid cohesion and spindle attachment. This in turn, drives germ cell immortality. Furthermore, may play a role in ensuring the timely assembly of the synaptonemal complex during prophase I of meiosis.
Subcellular location: Chromosome {ECO:0000269|PubMed:18923084, ECO:0000269|PubMed:22927794, ECO:0000269|PubMed:29483514, ECO:0000269|PubMed:30921322}. Nucleus {ECO:0000269|PubMed:30921322}. Note=Recruited to chromosomes by smc-3 which is a component of the cohesin complex, and the proteins htp-1, htp-2 and htp-3 (PubMed:22927794, PubMed:29483514). Localizes to chromosomes in the mid-pachytene phase of prophase I to the end of meiosis I (PubMed:18923084, PubMed:30921322). Localizes to the long arms of chromosomes during diakinesis phase of prophase I of meiosis (PubMed:18923084, PubMed:30921322). Does not localize to chromosomes in meiosis II (PubMed:18923084). Localizes to chromosomes in prophase of mitosis in the first embryonic division and subsequently from late prophase to anaphase during early embryonic division (PubMed:18923084). {ECO:0000269|PubMed:18923084, ECO:0000269|PubMed:22927794, ECO:0000269|PubMed:29483514, ECO:0000269|PubMed:30921322}.
Interaction partners:
- HORMA domain-containing protein
- Serine/threonine-protein phosphatase PP1-beta
- HORMA domain-containing protein
- Biogenesis of lysosome-related organelles complex 1 subunit 1
- Aurora/IPL1-related protein kinase 2
- HORMA domain-containing protein
- Shugoshin
- Long Arms of the Bivalent protein
- Meiotic recombination protein rec-8
- HORMA domain-containing protein
Sequence:
MVSHKKNDRPRPLWILKIHKRLSLFEFKRYATGIGKDDGQDISWVLKGNAKNNVYQVTVETMENCETDECKKVIWVPDELAESTGTMFEDFKEDQPQESVSSISNNEANWGSSVNELDENYEKMQKEETFDPYDSDSDTSEDSDFDEDFEDSDKTMCSGQS
Protein: Prdm2 protein (Q80VF3)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
RNFVCNVCASPFLSIKDLTKHLSVHAEEWPFKCEFCVQLFKGKTDLSEHRFLLHGVGNIFVCSVCKKEFAFLCNLQQHQRDLHPDELCTHHEFESGTLRPQNFTDPSKAHVEHMPSLPEEPAEASREEELNDSSEELYTTIKIMASGIKTKEPDVRLGLNQHYPSFKPPPFQYHHRNPMGIGVTATNFTTHNIPQTFTTAIRCTKCGKSVDNMPELHKHILACASASDKKRYTPKKNPVPLRQTVQPKNGVLVLDNSGKNAFRRMGQPKRLSFNVELSKMSPNKLKLNALKKKNQLVQKAILQKNRSAKQKADLRDTSEASSHICPYCDREFTYIGSLNKHAAFSCPKKPLSPSKRKVSHSSKKGGHTSSASSDRNSSSNPRRRTADTEIKMQSMQAPLGKTRARSTGPAQASLPSSSFRSRQNVKFAASVKSKKASSSSLRNSSPVRMAKITHVEGKKSKAVAKSHSTQLSSKASRSLHVKVQKSKAVLQSKTALASKKRTDRFIVKSRERSGGPITRSLQLAAAADLSESRREDSSARHELKDLR
Protein: Tubulin beta chain (Q5JP53)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MFWEVISDEHGIDPTGTYHGDSDLQLDRISVYYNEATGGKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQVFDAKNMMAACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEEDFGEEAEEEA
Protein: Bm2195, isoform b (Bm2196, isoform b) (Small heat shock protein 12.6) (A0A1P6BU67)
Organism: Brugia malayi (Filarial nematode worm)
Interaction partners:
Sequence:
MEEKVVELTHNWSAEQWDWPLQHNDEVIKVTNTNDKFEVGLDASFFTPKEIEVKVAGDNLVIHCRHESRAEHYGEIKREISRTYKLPSDVDTKTLTSNLTKRGHLVIAAKKKA
Protein: Electrogenic sodium bicarbonate cotransporter 1 (Sodium bicarbonate cotransporter) (Solute carrier family 4 member 4) (Q9GL77)
Organism: Bos taurus (Bovine)
Function: Electrogenic sodium/bicarbonate cotransporter with a Na(+):HCO3(-) stoichiometry varying from 1:2 to 1:3. May regulate bicarbonate influx/efflux at the basolateral membrane of cells and regulate intracellular pH.
Subcellular location: Basolateral cell membrane {ECO:0000269|PubMed:11029313}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q9Y6R1}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Carbonic anhydrase 2
- Sodium/hydrogen exchanger 1
Sequence:
MEDEAVLDRGASFLKHVCDEEEVEGHHTIYIGVHVPKSYRRRRRHKRKTGHREKKEKERISENYSDKSDVENADESSSSILKPLISPAAERIRFILGEEDDSPAPPQLFTELDELLAVDGQEMEWKETARWIKFEEKVEQGGERWSKPHVATLSLHSLFELRTCMEKGSIMLDREASSLPQLVEMIVDHQIETGLLKPDLKDKVTYTLLRKHRHQTKKSNLRSLADIGKTVSSASRMFTNPDNGSPAMTHRNLTSSSLNDISDKPEKDQLKNKFMKKLPRDAEASNVLVGEVDFLDSPFIAFVRLQQAVMLGALTEVPVPTRFLFILLGPKGKAKSYHEIGRAIATLMSDEVFHDIAYKAKDRQDLIAGIDEFLDEVIVLPPGEWDPAIRIEPPKSLPSSDKRKNMYSGGENVQMNGDTPPDGGHGGGGHADCEELQRTGRFCGGLIKDIKRKAPFFASDFYDALNIQALSAILFIYLATVTNAITFGGLLGDATDNMQGVLESFLGTAVSGAIFCLFAGQPLTILSSTGPVLVFERLLFNFSKDHNFDYLEFRLWIGLWSAFLCLILVATDASFLVQYFTRFTEEGFSSLISFIFIYDAFKKMIKLADYYPINSNFKVGYNTQFSCVCMPPDPVNISVSNDTTLAPEDLPTISSSNMYHNATFDWAFLTTKECLKYGGKLVGNNCGFVPDITLMSFILFLGTYTSSMALKKFKTSPYFPTTARKLISDFAIILPILIFCVIDALVGVDTPKLIVPSEFKPTSPNRGWFVAPFGGNPWWVYLAAAIPALLVTILIFMDQQITAVIVNRKEHKLKKGAGYHLDLFWVAILMVVCSFMALPWYVAATVISIAHIDSLKMETETSAPGEQPKFLGVREQRVTGTLVFILTGLSVFMAPILKFIPMPVLYGVFLYMGVASLNGVQFMDRLKLLLMPLKHQPDFIYLRHVPLRRVHLFTFLQVLCLALLWILKSTVAAIIFPVMILALVAVRKGMDYLFSQHDLSFLDDVIPEKDKKKKEDEKKKKKKKGSVDSDNDDSDCPYSEKVPSIKIPMDIMEQQPFLSDSKPSDRERSPTFLERHTSC
Protein: Transcription factor MYC3 (Basic helix-loop-helix protein 5) (AtbHLH5) (bHLH 5) (Protein ALTERED TRYPTOPHAN REGULATION 2) (Transcription factor ATR2) (Transcription factor EN 36) (bHLH transcription factor bHLH005) (Q9FIP9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor involved in tryptophan, jasmonic acid (JA) and other stress-responsive gene regulation. With MYC2 and MYC4, controls additively subsets of JA-dependent responses. Can form complexes with all known glucosinolate-related MYBs to regulate glucosinolate biosynthesis. Binds to the G-box (5'-CACGTG-3') of promoters. Activates multiple TIFY/JAZ promoters.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:21242320, ECO:0000269|PubMed:21321051, ECO:0000269|PubMed:21335373}.
Interaction partners:
- Protein TIFY 7
- Protein TIFY 10A
- Protein TIFY 9
- Transcription factor MYB24
- Transcription factor MYB29
- Mediator of RNA polymerase II transcription subunit 25
- Transcription factor MYB21
- Protein TIFY 11B
- Protein TIFY 10B
- Protein TIFY 11A
Sequence:
MNGTTSSINFLTSDDDASAAAMEAFIGTNHHSSLFPPPPQQPPQPQFNEDTLQQRLQALIESAGENWTYAIFWQISHDFDSSTGDNTVILGWGDGYYKGEEDKEKKKNNTNTAEQEHRKRVIRELNSLISGGIGVSDESNDEEVTDTEWFFLVSMTQSFVNGVGLPGESFLNSRVIWLSGSGALTGSGCERAGQGQIYGLKTMVCIATQNGVVELGSSEVISQSSDLMHKVNNLFNFNNGGGNNGVEASSWGFNLNPDQGENDPALWISEPTNTGIESPARVNNGNNSNSNSKSDSHQISKLEKNDISSVENQNRQSSCLVEKDLTFQGGLLKSNETLSFCGNESSKKRTSVSKGSNNDEGMLSFSTVVRSAANDSDHSDLEASVVKEAIVVEPPEKKPRKRGRKPANGREEPLNHVEAERQRREKLNQRFYSLRAVVPNVSKMDKASLLGDAISYINELKSKLQQAESDKEEIQKKLDGMSKEGNNGKGCGSRAKERKSSNQDSTASSIEMEIDVKIIGWDVMIRVQCGKKDHPGARFMEALKELDLEVNHASLSVVNDLMIQQATVKMGSQFFNHDQLKVALMTKVGENY
Protein: Ras-related protein Rab-39A (Rab-39) (Q8BHD0)
Organism: Mus musculus (Mouse)
Function: Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. Plays a role in vesicular trafficking. Plays a role in the fusion of phagosomes with lysosomes. Negatively regulates LPS-induced autophagosome formation in macrophages possibly by implicating PI3K (By similarity). May be involved in multiple neurite formation.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, phagosome {ECO:0000250}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Lysosome {ECO:0000250|UniProtKB:Q14964}. Note=Recruited to phagosomes containing S.aureus or Mycobacterium. {ECO:0000250}.
Interaction partners:
- Geranylgeranyl transferase type-2 subunit alpha
Sequence:
METIWIYQFRLIVIGDSTVGKSCLLHRFTQGRFPGLHSPACDPTVGVDFFSRLLEIEPGKRIKLQLWDTAGQERFRSITRSYYRNSVGGFLVFDITNRRSFEHVKDWLEEAKMHVQPFQIVFLLVGHKCDLASQRQVSREEAERLSTDCGMKYIETSAKDATNVEESFTILTRDIYELIKKGEICIQDGWEGVKSGFVPNTVHSSEEAVKPRKECFC
Protein: Protein odd-skipped-related 2-A (XOsr2) (Q32NK7)
Organism: Xenopus laevis (African clawed frog)
Function: Transcriptional repressor. Required for pronephric kidney development.
Subcellular location: Nucleus {ECO:0000269|PubMed:17011543, ECO:0000305}.
Interaction partners:
Sequence:
MGSKALPAPVPLHPSLQLTNYSFLQAVNTFPAAVDHLQGLYGLSAVQTMHMNHWTLGYPNLHGLTRSTITEMAAAQGLMDARFSFPALPFATHLFHPKQGTIAHVIPALHKDRPRFDFANLAIAATQEDPPKIGDLSKLSPGLGSPISEISKLSPDRKPSRGRLPSKTKKEFICKFCGRHFTKSYNLLIHERTHTDERPYTCDICHKAFRRQDHLRDHRYIHSKEKPFKCQECGKGFCQSRTLAVHKTLHMQTSSPTVVSSAEKFSGEIAI
Protein: Protein disulfide isomerase-like 1-2 (AtPDIL1-2) (EC 5.3.4.1) (Protein disulfide-isomerase 2) (PDI 2) (Protein disulfide-isomerase 6) (AtPDI6) (Q9SRG3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a protein-folding catalyst that interacts with nascent polypeptides to catalyze the formation, isomerization, and reduction or oxidation of disulfide bonds.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000305}.
Interaction partners:
- Endoplasmic reticulum oxidoreductin-1
- Heat shock 70 kDa protein BIP1
- Transcription factor MEE8
- Heat shock 70 kDa protein BIP2
- Endoplasmic reticulum oxidoreductin-2
- Heat shock 70 kDa protein BIP3
- Calreticulin-2
- Calreticulin-1
- Calnexin homolog 1
- Calnexin homolog 2
Sequence:
MAFKGFACFSILLLLSLFVSSIRSEETKEFVLTLDHSNFTETISKHDFIVVEFYAPWCGHCQKLAPEYEKAASELSSHNPPLALAKIDASEEANKEFANEYKIQGFPTLKILRNGGKSVQDYNGPREAEGIVTYLKKQSGPASVEIKSADSATEVVGEKNVVAVGVFPKLSGDEFDSFMALAEKLRADYDFAHTLDAKFLPRGESVEGPAVRLFKPFDELFVDSKDFNGEALEKFVKESSIPLVTVFDSDPNNHPYVAKFFESPATKAMMFVNFTGATAEALKSKYREVATSNKDQSLAFLVGDAESSQGAFQYFGLEESQVPLIIIQTPDNKKYLKVNVEVDQIESWFKDFQDGKVAVHKKSQPIPAENNEPVKVVVAESLDDIVFKSGKNVLIEFYAPWCGHCQKLAPILDEVALSFQNDPSVIIAKLDATANDIPSDTFDVKGFPTIYFRSASGNVVVYEGDRTKEDFINFVEKNSEKKPTSHGEESTKSEEPKKTEETAAKDEL
Protein: Chaperonin containing TCP1 subunit 6 (GH13725p) (Q9VXQ5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit gamma
- Phosducin-like protein 2
- Uncharacterized protein
- Heat shock protein 83
Sequence:
MASISLLNPKAEFARAAQALAINISAAKGLQDVMRTNLGPKGTVKMLVSGAGDIKITKDGNVLLHEMQIQHPTASMIARASTAQDDSTGDGTTTTVMLIGELLKQADIYLSEGLHPRIMTDGFEKARDKALEVLDQVKVPVEINKKNLVEVANTSLKTKVHPALADLLTDVCVNAVLTIASADKTKPVDLHMVELMEMQHKSDTDTQLVRGLVMDHGARHPDMPKRLENAYILTANVSLEYEKAEVNSGFFYKTAEEREAFVRAEREFIDQRVKKVIELKRSVCDGTDKTFVLINQKGIDPISLDALAKEGILALRRAKRRNMERLSLACGGTAMNSFDDLQEEHLGYAGVVYEHVLGENKYTFVEDCKNPLSVTILIKGPNKHTITQIKDAIRDGLRAINNTIADKALVPGAGAFEVRAYNELVAFKDTIKGKSRLAVQAFADALLVIPKTLAVNSGYDAQDTIVKLTVEDRLSPELVGLDLATGEPMKPVDLGVYDNYIVKKQILNSCSIIASNLLLVDEVMRAGMTSLKG
Protein: Adenosine kinase (EC 2.7.1.20) (P78825)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Adenylate kinase
- Adenine phosphoribosyltransferase
- Adenine deaminase
- AMP deaminase
- Putative purine nucleoside phosphorylase
- Uncharacterized deaminase C1683.02
- Adenylosuccinate lyase
- 3',5'-cyclic-nucleotide phosphodiesterase
- Adenylate kinase isoenzyme 6 homolog
- Golgi apyrase
Sequence:
MSSYILFGLENPLLDYYVGGETATLEKYGLKSNDAVLASESQMGIYKEPCVSYSAGGAAQNSCRAAQYVLPPNSTVFAGCVGQDKFADMLLESNEKAGLRSEFSVDPTTPTGVCAVVLSNNNKNRSLCTNLGAANNYKLKDLQQPNVWKFVEEAKVIYVGGFHLTVSPESMLCLAQHANENNKPYIMNLSAPFLSQFFKEQMDSVIPYCDYVIGNEAEILSYGENHGIKSTDVQEIALALSSVEKVNKKRTRVVVITQGADATIVAKDGKVTTYKPNRVPSEEIVDTNGAGDAFAGGFIAALSQGQGIDYAVTLGHWLGQECIKVSGTTLPLPKKQFPLP