wanglab/gogpt-training-data huggingface dataset:
Protein: DNA-directed RNA polymerases I, II, and III subunit RPABC3 (Q384M6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- RNA polymerase III subunit Rpc25 domain-containing protein
- DNA-directed RNA polymerase II, putative
- Plastid-encoded RNA polymerase subunit alpha
- DNA-dependent RNA polymerases, putative
- DNA-directed RNA polymerase III subunit RPC6
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit
- Plastid-encoded RNA polymerase subunit alpha
- DNA-directed RNA polymerase I subunit RPA1
- DNA-directed RNA polymerase subunit beta
Sequence:
MASSKVILEDTFTVAAVNEEGTVYSRVSRVRCTGEGGGLIITSDVNTGEFPLHSGDRLTIILTDSIELSEQAGSKHYDQSVYHRSTRLDDCDYAMHGRVYSMEVNESSLDVTVHISCGGLLTQIVGKPQSLKDVHYNSDVYILMKRPGS
Protein: ATPase morc-1 (EC 3.6.1.-) (Q23243)
Organism: Caenorhabditis elegans
Function: Binds non-specifically to DNA and forms static foci which grow by recruiting other morc-1 molecules, and thereby stimulates conformational changes and compaction of DNA, which appears to be enhanced by ATP-binding, but does not require ATP activity. Preferentially binds to long DNAs. Compacts and entraps segments of DNA by sequentially forming loops along the DNA, beginning at the free ends of single- and double-tethered DNA. Does not extrude the DNA loops on compacted double-tethered DNA. Involved in gene silencing. Plays a role in germline RNA interference (RNAi), and in particular, the silencing of endogenous small interfering RNA (endo-siRNA) target genes. May play a role in heterochromatin localization and condensation, and the siRNAi-directed trimethylation of 'Lys-9' of histone H3 in hermaphrodite X chromosomes. Promotes transgenerational epigenetic inheritance and germline immortality.
Subcellular location: Nucleus {ECO:0000269|PubMed:28535375}. Nucleus, nuclear body {ECO:0000269|PubMed:31442422}. Note=Localizes to punctate nuclear bodies in germline stem cells and gonadal meiotic nuclei. {ECO:0000269|PubMed:31442422}.
Interaction partners:
- Remorin_C domain-containing protein
- SET domain-containing protein
- Argonaute protein hrde-1
- Protein hrde-2
- FACT complex subunit
- CDI domain-containing protein
- Histone-lysine N-methyltransferase set-25
- Protein hrde-4
Sequence:
MPNDTNGDDYKKLEKASVNLNFLKSNSHTHIGPLSAIAELVDNAYDADARDLHIDFLDINNEQFLELRDDGLGMAREEALHAITFGHSAKCSYKIGRYGNGLKSGAFHLGRELLLVTKKDGIITALLISHRFHEDQGLTNSVFVPCPSFDLDGIPICQTESEKDRFNLEMKIIGKYAPLGSRTLAELADKITGSTGTIIIIGNLRRSVTGELAINTTKDPTDIIVDSGEENKPWRESLRKYLEFIYLKPRMRIHVRGEQVLPKRISENWIAKKQQLISGDQFTAAYNKILDEKNETVKKCEEEKALVMSEIGGTNYTSVRREDRANQKSLRLRVDTSQKNLDSAIADRDAFKKEGKSEKSFHLNMGIETKDRSNNGIHFYINNRLILWGNKEAKFFSKFANSIGISMFLSLDYSLFSAAQNKQGFDHVKDFQVLVRKCNDALRDYSMYLEKSWIPTHLKNTWNVRIYEGDDVWAVLWGVYGYNNTTSTTCVQTHDSARDQVMWTTCGIWKLCQMCRTWIKASRPNEIVGSNDDFFCCENVNHHGCRTIVAEDNDFSKLPEKYDHILPQKRLTNSAPSSSDSQNSIRSASSCSSSSRLLNVAKIESHERIHSSTGGHRLGESFSTTSVKMEPIPNNAHDSHIAEVQRRHSTGRAISPAVSEISRRAGTAPSSQLDMIMGEESDESQEALTIRAPRQRAKRPIERVSRRNRRDQSDDDSDSENEERYATAPKKSKVKGKAVVRAPKMTREKWLEEMLNQFLTAHGEQPLPKNGQRDFDPTNIVEQTSRRNFKNNQRIVDAQQAIMRQIGSVLDHLKRNPTHNFKIPASGTVEEKLKNIEHQIKGKKK
Protein: Cyclic pyranopterin monophosphate synthase 1 (EC 4.6.1.17) (Molybdenum cofactor biosynthesis protein C 1) (P9WJR9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP) (By similarity). Probably plays a role in host phagosome maturation arrest.
Interaction partners:
- GTP 3',8-cyclase 2
- GTP 3',8-cyclase 1
- Molybdopterin synthase catalytic subunit 1
- Molybdopterin synthase catalytic subunit 1
- Molybdopterin synthase sulfur carrier subunit
- Molybdopterin synthase catalytic subunit 2
- Putative pterin-4-alpha-carbinolamine dehydratase
- Probable molybdopterin biosynthesis Mog protein
- Possible phosphatase
- CMP/dCMP-type deaminase domain-containing protein
Sequence:
MIDHALALTHIDERGAARMVDVSEKPVTLRVAKASGLVIMKPSTLRMISDGAAAKGDVMAAARIAGIAAAKRTGDLIPLCHPLGLDAVSVTITPCEPDRVKILATTTTLGRTGVEMEALTAVSVAALTIYDMCKAVDRAMEISQIVLQEKSGGRSGVYRRSASDLACQSR
Protein: Sensor histidine kinase TrcS (EC 2.7.13.3) (Tuberculosis regulatory component sensor) (P96368)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Member of the two-component regulatory system TrcS/TrcR. Phosphorylates TrcR. The TrcR-TrcS regulatory system may act as a transition regulatory system involved in adapting to an intracellular environment and transitioning from latency to reactivation.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Transcriptional regulatory protein TrcR
- Transcriptional regulatory protein KdpE
- Probable transcriptional regulatory protein TcrX
- Transcriptional regulatory protein PrrA
- Transcriptional regulatory protein TcrA
- Possible two component system response transcriptional positive regulator PhoP
- DNA-binding response regulator MtrA
- Sensory transduction protein RegX3
- Response regulator MprA
- Probable transcriptional regulatory protein
Sequence:
MIPDRNTRSRKAPCWRPRSLRQQLLLGVLAVVTVVLVAVGVVSVLSLSGYVTAMNDAELVESLHALNHSYTRYRDSAQTSTPTGNLPMSQAVLEFTGQTPGNLIAVLHDGVVIGSAVFSEDGARPAPPDVIRAIEAQVWDGGPPRVESLGSLGAYQVDSSAAGADRLFVGVSLSLANQIIARKKVTTVALVGAALVVTAALTVWVVGYALRPLRRVAATAAEVATMPLTDDDHQISVRVRPGDTDPDNEVGIVGHTLNRLLDNVDGALAHRVDSDLRMRQFITDASHELRTPLAAIQGYAELTRQDSSDLPPTTEYALARIESEARRMTLLVDELLLLSRLSEGEDLETEDLDLTDLVINAVNDAAVAAPTHRWVKNLPDEPVWVNGDHARLHQLVSNLLTNAWVHTQPGVTVTIGITCHRTGPNAPCVELSVTDDGPDIDPEILPHLFDRFVRASKSRSNGSGHGLGLAIVSSIVKAHRGSVTAESGNGQTVFRVRLPMIEQQIATTA
Protein: POU domain protein (D2IYK3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MAGHLASDFAFSPPPGGGGDGPGGPEPGWVDPRTWLSFQGPPGGPGIGPGVGPGSEVWGIPPCPPPYEFCGGMAYCGPQVGVGLVPQGGLETSQPEGEAGVGVESNSDGASPEPCTVTPGAVKLEKEKLEQNPEESQDIKALQKELEQFAKLLKQKRITLGYTQADVGLTLGVLFGKVFSQTTICRFEALQLSFKNMCKLRPLLQKWVEEADNNENLQEICKAETLVQARKRKRTSIENRVRGNLENLFLQCPKPTLQQISHIAQQLGLEKDVVRVWFCNRRQKGKRSSSDYAQREDFEAAGSPFSGGPVSFPLAPGPHFGTPGYGSPHFTALYSSVPFPEGEAFPPVSVTTLGSPMHSN
Protein: CCR4-NOT core ubiquitin-protein ligase subunit (A0A1D8PSH4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- General negative regulator of transcription subunit 3
- General negative regulator of transcription subunit
- General negative regulator of transcription subunit 1
- CCR4-NOT core subunit
- CCR4-NOT core DEDD family RNase subunit
- CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4
- CCR4-NOT core subunit
- ATP-dependent RNA helicase DHH1
- CCR4-NOT core subunit
- ATP-dependent RNA helicase
Sequence:
MIQADDTFISDDEEEYCPLCVEEMDISDKNFKPCPCGYQICQFCYNNIRQNPELNGRCPGCRRLYDDESVEYKTVSAEEYKLMQLKKEKRDREKKQKEKEKKEMEMVNKKHLAGLRVVQKNLVYVTGLNPPCNPDDLHSVLRSDKYFGQYGKISKIVINKKTPTTQTSTHHHQNPGLVVYVTFTRKEDALRCITELDGSLCDGRVLRAAHGTTKYCSSYLRGQPCPNPNCMFLHEPGEEADSYTRKDLSTQQGIKMGMTARSHTTSFGEESSNNSQSNQAGSDDDHHEAHKEHLPSTAHWAAAGTTSGSNSPSVNNNIPLANSAAFPTLGEIVRDQKQQQKKETKPRSKTTKSNNTLVPDELDAGDNSVFKFVETTTEQLRGLEDIRNVRFKGFDNGKILPLFSFKGNFSNDTQLEEEKVIARQVIEKFLLRPLKNYHLAYQNHPITQQQAILQRQQQQQQQQQQQQTPALQVAQLQQNKNDEQQKQAQQQLLLLQLQHQQQLQQQQQQRQLQQQQNQPHQLNILKTSDRVNTSTPPPPGLFAGKDVAASSDMSNTGAPLPSSSSQLLTQLMSGKR
Protein: Citrate-sodium symporter (Q79AF8)
Organism: Lactococcus lactis
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MKKLKETKISGISLPLYAFFVAVIIVVTLLGKLPLDMVGLTLLLVTLGHLLYFIGEKFPIMNSYLGGGSVFTLIGATLLSFFHIVPSNVIGAVSNFMGGKFGFLDFYIAALICGSILGMNRNLLVKASKKFIPIALITMVIGFFSVGLVGMLIGNGFADSVMYVSMPMMSGGMGAGITPLSQIYAAGLAHGNQAAIFSQLAPAVTFGNILAIIGALSIAKVFNKSKYNGHGTLVAATKEELAKPKIKLDAQQIGTGMLFAFALLMAGDILNKFFPNIHQYAFMIIIVFILKATNTVPKDLEESVVMFNQVIMTNLTHAVLAGIGLALIDLNTLASAFTWQFVVLCLTSVVVMGLASWFLARLFGLYPVETAIGAGMINNSMGGTGNIAVLSASDRMEMIAFAQMANRLCGAIVLIFGGILIRFFY
Protein: Seminal fluid protein 78E, isoform B (M9PG65)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNIFISLILVVLAILSFADHTVVRVNPYMEYYGSYIYFKADGDRHLNEDLNRATVKKTKYGWQCAGVTCPIKFTASCKVTKVLKPSDLQHTELLILCMDKNDKPMCGITRTRKGVIQEVLDVDENGNTIYDKKEVISENDGTKIPRCPRK
Protein: Homeobox protein PKNOX1 (PBX/knotted homeobox 1) (O70477)
Organism: Mus musculus (Mouse)
Function: Activates transcription in the presence of PBX1A and HOXA1.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Pre-B-cell leukemia transcription factor 1
- Homeobox protein Hox-B1
- Pre-B-cell leukemia transcription factor 2
Sequence:
MMATQTLSIDSYQDGQQMQVVTELKTEQDPNCSDPDAEGVSPPPIESQTPMDADKQAIYRHPLFPLLALLFEKCEQSTQGSEGTTSASFDVDIENFVRKQEKDGKPFFCEDPETDNLMVKAIQVLRIHLLELEKVNELCKDFCSRYIACLKTKMNSETLLSGEPGSPYSPVQSQQIQSAITGTLSPQGIVVPASALQQGNVTMATVAGGTVYQPVTVVTPQGQVVTQALSPGTIRIQNSQLQLQLNQDLSILHQEDGSSKNKRGVLPKHATNVMRSWLFQHIGHPYPTEDEKKQIAAQTNLTLLQVNNWFINARRRILQPMLDSSCSETPKTKKKPAQNRPVQRFWPDSLASGVAQATPSELAMSEGAVVTITTPVNMNVDSLQSLSSDGATLAVQQVMMAGQSEDESVDSTEDEGGALAPTHISGLVLENSDSLQ
Protein: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2 (EC 3.1.4.11) (Phosphoinositide phospholipase C-gamma-2) (Phospholipase C-IV) (PLC-IV) (Phospholipase C-gamma-2) (PLC-gamma-2) (P16885)
Organism: Homo sapiens (Human)
Function: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. It is a crucial enzyme in transmembrane signaling.
Subcellular location: Membrane raft {ECO:0000250|UniProtKB:Q8CIH5}.
Interaction partners:
- B-cell linker protein
- Tyrosine-protein kinase SYK
- Tyrosine-protein kinase BTK
- Lymphocyte cytosolic protein 2
- Proto-oncogene vav
- Epidermal growth factor receptor
- Receptor tyrosine-protein kinase erbB-2
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Proto-oncogene tyrosine-protein kinase Src
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform
Sequence:
MSTTVNVDSLAEYEKSQIKRALELGTVMTVFSFRKSTPERRTVQVIMETRQVAWSKTADKIEGFLDIMEIKEIRPGKNSKDFERAKAVRQKEDCCFTILYGTQFVLSTLSLAADSKEDAVNWLSGLKILHQEAMNASTPTIIESWLRKQIYSVDQTRRNSISLRELKTILPLINFKVSSAKFLKDKFVEIGAHKDELSFEQFHLFYKKLMFEQQKSILDEFKKDSSVFILGNTDRPDASAVYLHDFQRFLIHEQQEHWAQDLNKVRERMTKFIDDTMRETAEPFLFVDEFLTYLFSRENSIWDEKYDAVDMQDMNNPLSHYWISSSHNTYLTGDQLRSESSPEAYIRCLRMGCRCIELDCWDGPDGKPVIYHGWTRTTKIKFDDVVQAIKDHAFVTSSFPVILSIEEHCSVEQQRHMAKAFKEVFGDLLLTKPTEASADQLPSPSQLREKIIIKHKKLGPRGDVDVNMEDKKDEHKQQGELYMWDSIDQKWTRHYCAIADAKLSFSDDIEQTMEEEVPQDIPPTELHFGEKWFHKKVEKRTSAEKLLQEYCMETGGKDGTFLVRESETFPNDYTLSFWRSGRVQHCRIRSTMEGGTLKYYLTDNLTFSSIYALIQHYRETHLRCAEFELRLTDPVPNPNPHESKPWYYDSLSRGEAEDMLMRIPRDGAFLIRKREGSDSYAITFRARGKVKHCRINRDGRHFVLGTSAYFESLVELVSYYEKHSLYRKMRLRYPVTPELLERYNMERDINSLYDVSRMYVDPSEINPSMPQRTVKALYDYKAKRSDELSFCRGALIHNVSKEPGGWWKGDYGTRIQQYFPSNYVEDISTADFEELEKQIIEDNPLGSLCRGILDLNTYNVVKAPQGKNQKSFVFILEPKQQGDPPVEFATDRVEELFEWFQSIREITWKIDTKENNMKYWEKNQSIAIELSDLVVYCKPTSKTKDNLENPDFREIRSFVETKADSIIRQKPVDLLKYNQKGLTRVYPKGQRVDSSNYDPFRLWLCGSQMVALNFQTADKYMQMNHALFSLNGRTGYVLQPESMRTEKYDPMPPESQRKILMTLTVKVLGARHLPKLGRSIACPFVEVEICGAEYDNNKFKTTVVNDNGLSPIWAPTQEKVTFEIYDPNLAFLRFVVYEEDMFSDPNFLAHATYPIKAVKSGFRSVPLKNGYSEDIELASLLVFCEMRPVLESEEELYSSCRQLRRRQEELNNQLFLYDTHQNLRNANRDALVKEFSVNENQLQLYQEKCNKRLREKRVSNSKFYS
Protein: DDRGK domain-containing protein 1 (Dashurin) (UFM1-binding and PCI domain-containing protein 1) (Q96HY6)
Organism: Homo sapiens (Human)
Function: Substrate adapter for ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to substrate proteins, which plays a key role in reticulophagy (also called ER-phagy). In response to endoplasmic reticulum stress, promotes recruitment of the E3 UFM1-protein ligase UFL1 to the endoplasmic reticulum membrane: in turn, UFL1 mediates ufmylation of proteins such as RPN1 and RPL26/uL24, promoting reticulophagy of endoplasmic reticulum sheets. Ufmylation-dependent reticulophagy inhibits the unfolded protein response (UPR) by regulating ERN1/IRE1-alpha stability. Ufmylation in response to endoplasmic reticulum stress is essential for processes such as hematopoiesis or inflammatory response (By similarity). Required for TRIP4 ufmylation, thereby regulating nuclear receptors-mediated. transcription. May play a role in NF-kappa-B-mediated transcription through regulation of the phosphorylation and the degradation of NFKBIA, the inhibitor of NF-kappa-B. Plays a role in cartilage development through SOX9, inhibiting the ubiquitin-mediated proteasomal degradation of this transcriptional regulator.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20018847, ECO:0000269|PubMed:32160526, ECO:0000269|PubMed:36543799, ECO:0000269|PubMed:38383785, ECO:0000269|PubMed:38383789}; Single-pass membrane protein {ECO:0000305|PubMed:38383785, ECO:0000305|PubMed:38383789}.
Interaction partners:
- E3 UFM1-protein ligase 1
- CDK5 regulatory subunit-associated protein 3
- Ubiquitin-fold modifier 1
- Ubiquitin-fold modifier-conjugating enzyme 1
- Ufm1-specific protease 2
- Ubiquitin-like modifier-activating enzyme 5
- Ufm1-specific protease 1
- Signal recognition particle receptor subunit alpha
Sequence:
MVAPVWYLVAAALLVGFILFLTRSRGRAASAGQEPLHNEELAGAGRVAQPGPLEPEEPRAGGRPRRRRDLGSRLQAQRRAQRVAWAEADENEEEAVILAQEEEGVEKPAETHLSGKIGAKKLRKLEEKQARKAQREAEEAEREERKRLESQREAEWKKEEERLRLEEEQKEEEERKAREEQAQREHEEYLKLKEAFVVEEEGVGETMTEEQSQSFLTEFINYIKQSKVVLLEDLASQVGLRTQDTINRIQDLLAEGTITGVIDDRGKFIYITPEELAAVANFIRQRGRVSIAELAQASNSLIAWGRESPAQAPA
Protein: Cell division control protein 48 homolog E (AtCDC48e) (Transitional endoplasmic reticulum ATPase E) (Q9LZF6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably functions in cell division and growth processes. Interacts with certain SNAREs as part of specialized membrane fusion events where vesicles from the same organelle fuse (homotypic fusion) (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000250}. Note=Primarily localized to the nucleus and, during cytokinesis, to the phragmoplast, a site where membrane vesicles are targeted in the deposition of new cell wall materials. {ECO:0000250}.
Interaction partners:
- NPL4-like protein 2
- NPL4-like protein 1
- Plant UBX domain-containing protein 11
- AT2G21270 protein
- Probable ubiquitin conjugation factor E4
- Peptide-N
- Protein OS-9 homolog
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 2
- Plant UBX domain-containing protein 6
- Plant UBX domain-containing protein 5
Sequence:
MSNEPESSDSKTKKDFSTAILERKKSPNRLVVDEAINDDNSVVSLHPTTMEKLQLFRGDTILIKGKKRKDTVCIALADETCEEPKIRMNKVVRSNLRVRLGDVISVHQCPDVKYGKRVHILPVDDTVEGVTGNLFDAYLKPYFLEAYRPVRKGDLFLVRGGMRSVEFKVIETDPAEYCVVAPDTEIFCEGEPVKREDEERLDEVGYDDVGGVRKQMAQIRELVELPLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGESESNLRKAFEEAEKNAPSIIFIDEIDSIAPKREKTNGEVERRIVSQLLTLMDGLKSRAHVIVMGATNRPNSIDPALRRFGRFDREIDIGVPDEIGRLEVLRIHTKNMKLAEDVDLERISKDTHGYVGADLAALCTEAALQCIREKMDVIDLEDDSIDAEILNSMAVSNEHFHTALGNSNPSALRETVVEVPNVSWEDIGGLENVKRELQETVQYPVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVREIFDKARQSAPCVLFFDELDSIATQRGNSAGDAGGAADRVLNQLLTEMDGMNAKKTVFIIGATNRPDIIDSALLRPGRLDQLIYIPLPDEDSRLNIFKACLRKSPVAKDVDVTALAKYTQGFSGADITEICQRACKYAIRENIEKDIENERRRSQNPEAMEEDMVDDEVSEIRAAHFEESMKYARRSVSDADIRKYQAFAQTLQQSRGFGSEFRFDSTAGVGRTTGVAAADPFATSAAAADDDDLYS
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (Q4QJ67)
Organism: Leishmania major
Interaction partners:
- rRNA 2'-O-methyltransferase fibrillarin
- Putative peroxin 13
- peptidylprolyl isomerase
- Putative fibrillarin
- Small-subunit processome Utp21 domain-containing protein
- Periodic tryptophan protein 2-like protein
- RNA cytidine acetyltransferase
- Putative beta propeller protein
- HEAT repeat-containing protein 1
- U3 small nucleolar RNA-associated protein 6 N-terminal domain-containing protein
Sequence:
MRAVAVVAVVLCALSFLNVAAEPEVTSKVYFDVMMDSEPLGRITIGLFGKDAPLTTENFRQLCTGEHGFGYKDSIFHRVIPNFMIQGGDFTNFDGTGGKSIYGEKFADENLKIKHFVGALSMANAGPNTNGSQFFITTAPTPWLDGRHVVFGKVLDGMDVVLRIEKAKTNSHDRPVKPVKIVASGDL
Protein: sulfate adenylyltransferase (EC 2.7.7.4) (Q54F74)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- FAD synthase
- 3'
- 3'
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Sulfite oxidase
- Uncharacterized protein
- Pyruvate kinase
- Elongation factor 1-alpha
- Elongation factor 1-alpha
- HBS1-like protein
Sequence:
MVSPDILTTNNSKLYGSIPHGGELINLILEGEELVELKQRSISLPSLLLTKKQLCDIELLMNGGFSPLSTFMDETIYNNVVETMTIDGDKDEGLLFPMPIVLDISKECLDTVLATDSKQMALRDEEGNLIAVLTVSNYYTPNKENEAKKTMGSIDPYHPGVSTIFNTKEYYVSGKLEGAQLPVHYDYNGLRRTPIQVRELFKTKGWENVIAFQTRNPMHRAHRELTVRAAELNANCHLLIQPVVGMTKPGDIDYHTRVKCYKEIMDSYPEGLATLSLLPLAMRMGGPREAVWHAIIRKNFGCNHFIVGRDHAGPGEDKQGNLFYQPYEAQELALKLANRLSIKILPFQMMVYVPAHDKYYPVDEVPEGLETANISGTKLRHLLRTGGEIPNWFTYEKVVKILRDSCPPRSKQGFTVFFTGFSGSGKSTIANALNEALLEDGSRSITLLDGDVVRTFLSSELGFSKEHRDLNIKRIGFVASEISKAGGIAICAPIAPYAGARKFARDLITPNGGFIEIHISTPIETCEKRDRKGLYAKVRSGQLKGFTGIDDPYETPENPELRIDTTHTSVKDAILLILNHLRTEGYIN
Protein: Rho guanine nucleotide exchange factor 5 (E9Q7D5)
Organism: Mus musculus (Mouse)
Function: Guanine nucleotide exchange factor which activates Rho GTPases. Strongly activates RHOA. Also strongly activates RHOB, weakly activates RHOC and RHOG and shows no effect on RHOD, RHOV, RHOQ or RAC1. Involved in regulation of cell shape and actin cytoskeletal organization. Plays a role in actin organization by generating a loss of actin stress fibers and the formation of membrane ruffles and filopodia (By similarity). Required for SRC-induced podosome formation. Involved in positive regulation of immature dendritic cell migration.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q12774}. Cytoplasm {ECO:0000250|UniProtKB:Q12774}. Cell projection, podosome {ECO:0000269|PubMed:21525037}.
Interaction partners:
Sequence:
MEAEEPEYGVSTEVPDIEELKTIPEGIMRSSQIPALDPEAQEDRDPSYKWTDGHRPVMNQSKVLRDMGDHTPNSMAIFFKKESSDMETSQEILLAEACNTPDQQEAVIQSLKDRLSRTIAAPELLACAVQEEWLDIPSKLDNRVGAELQSELMSLTLAVSKEKEEEETSPDTSIPRGSWPPCKTHPGETEQTQGSGSELLRQGKQLQLEATQENQGQEGFLQSQEAQGLEEQEGQEVEIQEEGTLNEGICFGGLLGEQEEVEEGFNGNEEEQKQGQIQSYMLLGGQWENEGLSGELEGLNYSERGQENRERRVWVLRDSEEEGQDQESREVEERRVATQYTENQRLVEKSEIVKRKQRDHDQTGKVMPVRDQKEVVDSGDRVQGNGDSGGQTAVEGSRPGEDSKPSLPVASVDPEVLSPGTLFPGISSSVADIPQIQKEPVCEELSPQAPALEPTEWSHQPISPPASFAPEESLDNRTHNSQQEEFRLRKGIEVVSASTSVAPSGTRDSPPFSPPNVFSSTATLSPVSSSVILPEETPTASASADTPHHCGPCETPPLPAKSSRYPCATSDTANPHSPLSSYTGVTQHLRSNSFPGSHRTEQTPDSLGMSLSFSHLELPQRPPKPAIYGSLTPRRNRRSRDGIVFSDSSTALFALKQDSEEFTSNPERPSSPHGSPTWGSPQNSAFAIGSPANVSSPPTVSMDMTIREALLPIPPEKRHSYSHIVERDGLLHEVASTLKRHSHPPPLTLSSGLHRSSKGSFSLVPDSTVARQHRPLPSTPESPNHTQTSIPSRLRYNKPLPPTPDMPEFYHPSISSSYISRMYRPLPPVPIIDPSSEPPPLPPKSRGRSKSIQGGVIHSGGQAKPRPNNQDWTASTLSVGRTSWPPATGRSTESLPLTSRCNNEVSPGLAFSNMTNLLSPSSPTTPWIPDLQRPTTKDESGLTEESEPPVRGSFRRSAPQEEFNNTRRSALGSRKNSEKPLHHQLEKASSWPHRRDPARTSESSSEQVVLGQVPNKQKGWNRQGLRRPSILPESSSDLRNPAAGRLPGSSDSVVFREKKPKEGMGGFSRRCSKLISSQLLYQEYSDVVLNKEIQSQQRLDSLAEPHGLSSPRHRRKALVSSDSYLQRLSMASSGSLWQEIPVVRNSTVLLSMTHEDQKLQEAKFELIVSEASYLRSLNIAVDHFQHSAQLRGTLSNQDHQWLFSRLQDVRDVSTTFLSDLEENFENNIFSFQVCDVVLNHAADFHRVYLPYVTNQTYQERTFQSLMNSNSSFREVLEKLESDPICQRLSLKSFLILPFQRITRLKLLLQNILKRTQPGSSEEAEATKAHHALEKLIRDCNSNVQRMRRTEELIYLSQKIEFECKIFPLISQSRWLVKSGELTALEFSVSPGLRRKLTTRPVHLHLFNDCLLLSRPREGSRFLVFDHAPFSSIRGEKCEMKLHGPHKNLFRLFLLHNAQGTQVEFLFRTETQSEKLRWISALAMPREELDLLECYDSPQVQCLRAYKPRENDELALEKADVVMVTQQSSDGWLEGVRLSDGEQGWFPVQQVEFISNPEVRAQNLKEAHRVKTAKLQLVEQQV
Protein: Uncharacterized protein (Q385W7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSLSNQLPRCATPLFYQLAENSDQFESINDMVIILQQQFVRLFKTPDTPMGAQKSTASSIASKEEEKLLAVRAVHALHTVGAVRHGDFFRSELYHTNAAFFIQEMLGCLVGDRRNWYRQLQVESLRGCLAVVQAVGYGNTRLCLPGIVSACTKYLVRAHHGTDAADVRVAAVNLMRVALTVSLVQQQDNEGWLRETVDHLGRGMGRLLAPEELVGTEIGLPVMKAMLRLVVDLLALQSLNTLVSTQLVRELLVGYFVLENLVHLEGENTRDEMNCVPSSLLENEEVVSMLHGRLKALQKVELLHYSSSLLRCEGTRTIVFSEETQFQCVMGQCIRVAGTQMGMEEFCGVRGSASRICSIVDGFIECLAYNVHLVALGPLRLATFIDECEATLSDWDLYALHPPTIYVLTRLIVWQFKTPMWVVGASADGAVDGTAKRDLPVEDLILSGTFEHLWSVVAKPHLWNITEDEDLCTYKQLQHRRIVAATILRFLEITAQTLRGIPSGRSAKRRRALRRLNVLMLYLVLEKAVIAGIVHDVAMRVIDAFSEASSQSDTLLFFLESSDFIADEAARAVTEEELRISAANVLHGGVNFIRSRLFAVSRRDVIASNTKESRRWVQVIKGSDVAITASESIVSKVADFVTSSIKVASDGCRRATLQEDAAGARAAVILLTSCFELSALLNRSVPQLGFDEDRDTVTTAAHPRVQILQLAVLEAVQMLLAYCARNDGVSPYVVRAVGCGLTVFLTTPKAAAWEHEDDTGDEGRLPCVFPWEVDVPPVLSRHHLRTVYRAYLVFLAILAEPVATITAPNAAKQRSAAERRVLEGVRPKPGVLAALDGLETLFTLSTEFLSQRMVEEVLPAVLTWYERGALSRIPTGTEEKLKLAVKKFVESVCDIEPSITQNLHEACAQLLPHTLFSTLLE
Protein: Transcription factor-like protein EUC1 (Enriches ubiquitin on chromatin protein 1) (Q04461)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transcription factor-like protein that binds to specific DNA motifs called ub-HS-motif associated with several locations where proteins other than histone H2B are ubiquitinated (ub-hotspots). Ubiquitination at these sites depends on the SUMO-targeted ubiquitin ligase (STUbL) complex SLX5/SLX8 and protein turnover on the CDC48 segregase. UBC9, SIZ1, or SIZ2 sumoylate DNA-bound EUC1 to stabilize its DNA-binding. Sumoylated EUC1 acts a cofactor required for the recruitment of the SLX5/SLX8 STUbL complex via specific contacts between EUC1 and SLX5, as well as an additional SUMO-mediated interaction. SLX5/SLX8 then ubiquitinates EUC1 and presumably other targets at ub-hotspots, and the CDC48/UFD1/NPL4 complex, together with UBX4 and UBX5, removes Lys-48-linked ubiquitinated proteins from chromatin. Ubiquitinated proteins could be either degraded by the proteasome or recycled by deubiquitination. EUC1 itself does not seem to underlie extensive turnover, as it is a very stable protein. EUC1 is able to act as a transcription factor, but its function at ub-hotspots does not seem to depend on this ability. EUC1-mediated ub-hotspots are crucial during stress responses when gene expression control is impaired.
Subcellular location: Chromosome {ECO:0000269|PubMed:31015336}. Note=Localizes to few distinct genomic hotspots where proteins other than histone H2B are ubiquitinated (ub-hotspots). {ECO:0000269|PubMed:31015336}.
Interaction partners:
- E3 ubiquitin-protein ligase complex SLX5-SLX8 subunit SLX5
Sequence:
MPAREYNYVEGFGGYGSLDDDDSDRDSERRNHDLGQRTITTSPTGVSRHAALNRYMIPGRINPLFRPTDAAQPPIVSTSTSASATEPTNRIGPGRIKETPETNFNAFLIAQLTRMEEQNANLKEEISLMKKEQELFFLENQKKLEKGFKDINKYVEDVSAMKEVFKEVVGIMTGERIRFIDHTGENVTPQEAARVGNPSTSTQAHQSQSRSTNWQEYSMHASILAGDPRIKPEPGLSDFENGEYDGNESDENATTRNLPLNNPDSVSNADDSNNQLDGTGNENDIRNRRGCVGTSYKLNRAIQNVTDAAREYFEGLPGQPSVLSLERRYGSTWRRSAKERTLFTKRMTIIKRIIDIKDDPSKYGLSLPENKISRNQAIKVVENIRLGNNTFKGHHCRLSMSQLYEYFSKKMDKLEDYSLTLKRRGKPRRIFLLEEREARLSLQQPHSIPNSSTGTPEHDQDT
Protein: Cys-loop ligand-gated ion channel (ELIC) (P0C7B7)
Organism: Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi)
Function: Mediates cation-selective currents but does not discriminate between different monovalent cations.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
APADNAADARPVDVSVSIFINKIYGVNTLEQTYKVDGYIVAQWTGKPRKTPGDKPLIVENTQIERWINNGLWVPALEFINVVGSPDTGNKRLMLFPDGRVIYNARFLGSFSNDMDFRLFPFDRQQFVLELEPFSYNNQQLRFSDIQVYTENIDNEEIDEWWIRKASTHISDIRYDHLSSVQPNQNEFSRITVRIDAVRNPSYYLWSFILPLGLIIAASWSVFWLESFSERLQTSFTLMLTVVAYAFYTSNILPRLPYTTVIDQMIIAGYGSIFAAILLIIFAHHRQAMGVEDDLLIQRCRLAFPLGFLAIGCVLVIRGITL