wanglab/gogpt-training-data huggingface dataset:
Protein: fumarate hydratase (EC 4.2.1.2) (Q8SXM1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVLPLLQRSTLRGVQQMTKPWAAIGSLRLASQEFRVESDTFGELKVPADKYYGAQTMRSQINFPIGGATERMPKPVVQAMGILKKAAAEVNKEFGLDSKVSEAISKAADDVISGKLYDDHFPLVIWQTGSGTQSNMNVNEVISNRAIELLGGKLGSKTPVHPNDHVNKSQSSNDTFPTAIHISVALELNNNLKPAIKTLHDALRAKSEEFKDIIKIGRTHTMDAVPLTLGQEFSGYAQQLAYAQERIDACLPRVYELALGGTAVGTGLNTRKGFAEKCAAKIAELTSLPFVTAPNKFEALAARDAMVEVHGVLNTIAVSLMKIANDIRFLGSGPRCGLGELSLPENEPGSSIMPGKVNPTQCESLTMLSAQVMGNLVAVTIGGSNGHFELNVFKPLIVSNVLRSIRLLSDGSRTFTANCVNGIQANRENIAKIMNESLMLVTALNPHIGYDKAAKIAKTAHKNGTTLKEEAINLGYLTEQQFNDWVRPEQMLGPK
Protein: HMP-PP phosphatase (EC 3.6.1.-) (P46891)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the hydrolysis of 4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate (HMP-PP) to 4-amino-2-methyl-5-hydroxymethylpyrimidine phosphate (HMP-P). Can also hydrolyze other substrates such as MeO-HMP-PP and 4-amino-2-trifluoromethyl 5-hydroxymethylpyrimidine pyrophosphate (CF3-HMP-PP) to give MeO-HMP-P and 4-amino-2-trifluoromethyl-5-hydroxymethylpyrimidine phosphate. This hydrolysis generates resistance to the antibiotics (bacimethrin, CF3-HMP) by reducing the formation of their toxic forms, 2'-methoxythiamin pyrophosphate (MeO-TPP) and CF3-HMP-PP. Also hydrolyzes pyridoxal-phosphate (PLP) and flavin mononucleotide (FMN), and purines (GMP and IMP) as secondary substrates.
Interaction partners:
- 5-amino-6-
- Sugar phosphatase YbiV
Sequence:
MARLAAFDMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGRHALEMQHILGALSLDAYLITGNGTRVHSLEGELLHRDDLPADVAELVLYQQWDTRASMHIFNDDGWFTGKEIPALLQAFVYSGFRYQIIDVKKMPLGSVTKICFCGDHDDLTRLQIQLYEALGERAHLCFSATDCLEVLPVGCNKGAALTVLTQHLGLSLRDCMAFGDAMNDREMLVSVGSGFIMGNAMPQLRAELPHLPVIGHCRNQAVSHYLTHWLDYPHLPYSPE
Protein: Mediator of RNA polymerase II transcription subunit 30 (Mediator complex subunit 30) (dMED20) (dTRAP25) (Q9W0P3)
Organism: Drosophila melanogaster (Fruit fly)
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 {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 11
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 1
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 8
Sequence:
MWKYGQNQGNQGPSSGGGGGGGPNMMPMGGFGMQHGNMQQMHMSPQHQQQQQQMGMMGGPGSMQMNPQGPGGPGGLMPGMSPQHQMQQQQQQQMMQQQMMVPQQGVGVGVGMGGGVGMGGGGVVPQQQQQQPQQNMPQQNIPQQQQQLNPVAGIPPGGAGGSNNMLAISQQNPHKEINIVQLSRLGQETVQDIASRFQEVFASLKGIQPTSHRENSSEKKVQEYFRTIRLLFKRVRIIYEKCNDAGMDYMSAESLIPYRDEPEPRIEPSLCDEYRKVLQENHELIETVKLKNRQLREIIDRTRIIIWEINTMLAMRRS
Protein: Karyopherin subunit alpha 1 (C9J352)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTTPGKENFRLKSYKNKSLNPDEMRRRREEEGLQLRKQKREEQLFKRRNVATAEEETEEEVMSDGGFHEAQISNMEMAPGGVITSDMIEMIFSKSPEQQLSATQKFRKLLSKEPNPPIDEVISTPGVVARFVEFLKRKENCTLQAVWALGNIAGDSTMCRDYVLDCNIL
Protein: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related (SMARCE1-related protein) (BRCA2-associated factor 35) (HMG box-containing protein 20B) (Structural DNA-binding protein BRAF35) (Q9Z104)
Organism: Mus musculus (Mouse)
Function: Required for correct progression through G2 phase of the cell cycle and entry into mitosis. Required for RCOR1/CoREST mediated repression of neuronal specific gene promoters (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}. Chromosome {ECO:0000250}. Note=Localized to condensed chromosomes in mitosis in conjunction with BRCA2. {ECO:0000250}.
Interaction partners:
- PHD finger protein 21A
- Histone deacetylase 1
- Lysine-specific histone demethylase 1A
- REST corepressor 2
- Histone deacetylase 2
- REST corepressor 1
- Zinc finger protein 217
- Genetic suppressor element 1
- High mobility group protein 20A
- Breast cancer type 2 susceptibility protein homolog
Sequence:
MSHGPRQPGAATAPAGGKTPGQHGAFVVAVKQERSEGSRAGEKGPQEEEPVKKRGWPKGKKRKKILPNGPKAPVTGYVRFLNERREQIRTRHPDLPFPEITKMLGAEWSKLQPAEKQRYLDEAEKEKQQYLKELWAYQQSEAYKVCTEKIQENKIKKEDSSSGLMNTLLNGHKGVDCDGFSTFDVPIFTEEFLDQNKAREAELRRLRKMNVAFEEQNAVLQRHTQSMSSARERLEQELALEERRTLALQQQLQAVRQALTASFASLPVPGTGETPTLGTLDFYMARLHGAIERDPAQHERLIARVKEILARVASEHL
Protein: Small ribosomal subunit protein eS26A (40S ribosomal protein S26-A) (P39938)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein uS2B
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein eL32
- Small ribosomal subunit protein eS6A
- Small ribosomal subunit protein eS28A
- Small ribosomal subunit protein eS17B
- Small ribosomal subunit protein eS28B
- Small ribosomal subunit protein eS19B
- Small ribosomal subunit protein uS10
- Essential nuclear protein 1
Sequence:
MPKKRASNGRNKKGRGHVKPVRCVNCSKSIPKDKAIKRMAIRNIVEAAAVRDLSEASVYPEYALPKTYNKLHYCVSCAIHARIVRVRSREDRKNRAPPQRPRFNRENKVSPADAAKKAL
Protein: Sensor histidine kinase DesK (EC 2.7.13.3) (O34757)
Organism: Bacillus subtilis (strain 168)
Function: Member of the two-component regulatory system DesR/DesK, responsible for cold induction of the des gene coding for the Delta5 acyl-lipid desaturase. Acts as a sensor of the membrane fluidity. Probably activates DesR by phosphorylation.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Transcriptional regulatory protein DesR
- Fatty acid desaturase
- Sensor histidine kinase YvfT
- Uncharacterized transcriptional regulatory protein YvfU
- Transcriptional regulatory protein LiaR
- Transcriptional regulatory protein LnrK
- Transcriptional regulatory protein ComA
- Transcriptional regulatory protein DegU
- Uncharacterized transcriptional regulatory protein YxjL
- Uncharacterized transcriptional regulatory protein YhcZ
Sequence:
MIKNHFTFQKLNGITPYIWTIFFILPFYFIWKSSSTFVIIVGIILTLLFFSVYRFAFVSKGWTIYLWGFLLIGISTASITLFSYIYFAFFIAYFIGNIKERVPFHILYYVHLISAAVAANFSLVLKKEFFLTQIPFVVITLISAILLPFSIKSRKERERLEEKLEDANERIAELVKLEERQRIARDLHDTLGQKLSLIGLKSDLARKLIYKDPEQAARELKSVQQTARTSLNEVRKIVSSMKGIRLKDELINIKQILEAADIMFIYEEEKWPENISLLNENILSMCLKEAVTNVVKHSQAKTCRVDIQQLWKEVVITVSDDGTFKGEENSFSKGHGLLGMRERLEFANGSLHIDTENGTKLTMAIPNNSK
Protein: Nebulin (Q8C3C3)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MNISKTTGSGTEGLGWSPAGSLEVEKAKKATEYASDQKYRQHPSTFQFKKLTDSMDMVLAKQNAHTMNKHLYTIDWNKDKTKIHVMPDTPDILQAKQNQTLYSQKSYRLGWEEALKKGYDLPVDAISVQLAKTSRDIASDFKYKQGYRKQLGHHIGFLSVQDDPKLVLSMNVAKMQSDREYKKDFEKWKTKYTSPVDMLGVVLAKKCQALVSDADYRNYLHQWTCLPDQNDVIQAKKVYELQSENMYKSDLEWLRGIGWSPLGSLEAEKNKRASEIISEKKYRQPPDRNKFTSIPDAMDIVLAKTNAKNRSDRLYREAWDKDKTQIHIMPDTPDIILAKANLINTSDKLYKMGY
Protein: Ribonuclease inhibitor (Ribonuclease/angiogenin inhibitor 1) (A0A140VJT8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSLDIQSLDIQCEELSDARWAELLPLLQQCQVVRLDDCGLTEARCKDISSALRVNPALAELNLRSNELGDVGVHCVLQGLQTPSCKIQKLSLQNCCLTGAGCGVLSSTLRTLPTLQELHLSDNLLGDAGLQLLCEGLLDPQCRLEKLQLEYCSLSAASCEPLASVLRAKPDFKELTVSNNDINEAGVRVLCQGLKDSPCQLEALKLESCGVTSDNCRDLCGIVASKASLRELALGSNKLGDVGMAELCPGLLHPSSRLRTLWIWECGITAKGCGDLCRVLRAKESLKELSLAGNELGDEGARLLCETLLEPGCQLESLWVKSCSFTAACCSHFSSVLAQNRFLLELQISNNRLEDAGVRELCQGLGQPGSVLRVLWLADCDVSDSSCSSLAATLLANHSLRELDLSNNCLGDAGILQLVESVRQPGCLLEQLVLYDIYWSEEMEDRLQALEKDKPSLRVIS
Protein: C2H2-type domain-containing protein (G5EAS8)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- MYB family conidiophore development protein FlbD
- BZIP-type transcription factor
- FlbE
- Protein fluG
- Conidiophore development regulator abaA
- Developmental regulator flbA
- SfgA
- Developmental regulatory protein wetA
- Cell pattern formation-associated protein stuA
Sequence:
MTMVIENQNRQYGGGMGFDSVYQHPHHSQPPQFSDPWTTAHSSSHSTPPVYPASVGIKQDETSRPSHIPMPYSVSVSAPSIVAGSNYSSASTSASYPAPDMMGLPHEIPRTSFDHAPAYTTAPSISSFAPASYAPISYASPVHQDNRRISHADASRVASSQSTSGPTFGDALDASRGMVALSQDLTPRNIYGPRGSRGSGDSYGFPLAHSAGSSISSAGSYPYYSASVASVESSVTDYSSTTSESYENGHLSRTLPRPSTLLTGSAPPGPQSMMSQFSSKMPSNTQKKHKCKVCDKRFTRPSSLQTHMYSHTGEKPFACDVEGCGRHFSVVSNLRRHKKVHKGGKEGGSGDDEE
Protein: Integrin subunit alpha 5 (A0A8I5YCC9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
Interaction partners:
Sequence:
MGSWTPRSPRSPLHAVLLRWGPRRLPPLLPLLLLLWPPPLQVGGFNLDAEAPAVLSGPPGSLFGFSVEFYRPGRDGVSVLVGAPKANTSQPGVLQGGAVYVCPWGTSPIQCSTIQFDSKGSRILESSLYSEEPVEYKSLQWFGATVRAHGSSILACAPLYSWRTEKDPQNDPVGTCYLSTENFTRILEYAPCRSDFGSAAGQGYCQGGFSAEFTKTGRVVLGGPGSYFWQGQILSATQEQISESYYPQYLINPVQGQLQTRQASSVYDDSYLGYSVAVGEFSGDDTEDFVAGVPKGNLTYGYVTVLNGSDIHSLYNVSGEQMASYFGYAVAATDTNGDGLDDLLVGAPLLMERTADGRPQEVGRVYIYLQHPEGIEPTPSLTLTGQDEFGRFGSSLTPLGDLDQDGYNDVAIGAPFGGEAQQGVVFIFPGGPGGLNTKPSQVLQPLWAAGHTPDFFGSALRGGRDLDGNGYPDLIVGSFGVDKALVYRGRPIISASASLTIFPSMFNPEERSCSLEGNPVSCINLSFCLNASGKHVPNSIGFEVELQLDWQKQKGGVRRALFLASKQATLTQTLLIQNGAREDCREMKIYLRNESEFRDKLSPIHIALNFSLDPKAPMDSHGLRPVLHYQSKSRIEDKAQILLDCGEDNICVPDLQLAVYGEKKHVYLGDKNALNLTFLAQNLGEGGAYEAELRVTAPLEAEYSGLVRHPGNFSSLSCDYFAVNQSRQLVCDLGNPMKAGTSIWGGLRFTVPHLQDTKKTIQFDFQILSKNLNNSQSNMVSFPLSVEAQAQVSLNGVSKPEAVIFPVSDWNPQDQPQKEGDLGPAVHHVYELINQGPSSISQGVLEISCPQALEGQQLLYVTKVTGLNNCTSNYTPNSQGLELDPEVSPHHLQRREAPGRSSTTSGTQVLKCPEAKCFRLRCEFGPLHRQESRSLQLHFRVWAKTFLQQEYQPFSLQCEALYEALKMPYQILPRQLPQKKLQVATAVQWTKAEGSNGVPLWIIILAILFGLLLLGLLIYVLYKLGFFKRSLPYGTAMEKAQLKPPATSDA
Protein: 2-hydroxy-7-methoxy-5-methyl-1-naphthoate--CoA ligase (EC 6.2.1.43) (Neocarzinostatin biosynthesis protein B2) (Q84HC5)
Organism: Streptomyces carzinostaticus
Function: Catalyzes the activation of 2-hydroxy-7-methoxy-5-methyl-1-naphthoate in the biosynthesis of the naphthoate moiety of the neocarzinostatin chromophore. Also catalyzes the activation of other 1-naphthoic acid analogs such as 2-hydroxy-5-methyl-1-naphthoate or 2,7-dihydroxy-5-methyl-1-naphthoate in vitro.
Interaction partners:
Sequence:
MHETAAAPAPAGFVPWPDDVAARYTAAGHWEGRSLGTHLAEAARKVPEAVCLVDGPVRMSYSELMARADGAAVRMRGLGIRPADRVVVQLPNCWEHVVVTMACLRLGALPIWALPQYRHRELSGVVTHARASALVVPDVYREFDHQALAHEVAEAQPTVRHVLVAGSDVRPDSVDLRALCEPLDADEAARVAAELDRSAPRGEEVAMLKLSGGTTGLPKLVARTHNDLSYMIKRAAQVCGFGRDTVYLAVLPLGHGFPNTGPGVLGTLLAGGRVVISGSPAPEAAFALMERERVTATSVVPAIVMRWLQYRDERPGADLGSLELMQVGASRLEPEVARQVGPKLGCRLQQVFGMAEGLLCLTRLDDPDDVVHYTQGRPISPDDEIRVVDPEGRTVGVGEPGALLTRGPYTPRGYYDSPSANARAFTPDGWYRTGDLVRRTPDGNLIVVGREKDLINRGGEKINAEEVEGFAVQVDGVLQAAAVGLPDSELGERICLFVVLADGTRVELADVRKVMENAETASFKLPERLITLPSLPTTPMGKIDKKALRAAAGRMSET
Protein: Adenosine 5'-monophosphoramidase HINT3 (EC 3.9.1.-) (HINT-4) (Histidine triad nucleotide-binding protein 3) (HINT-3) (Q9CPS6)
Organism: Mus musculus (Mouse)
Function: Exhibits adenosine 5'-monophosphoramidase activity, hydrolyzing purine nucleotide phosphoramidates with a single phosphate group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP and NH2 (By similarity). Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) generated by lysine tRNA ligase (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9NQE9}. Nucleus {ECO:0000250|UniProtKB:Q9NQE9}.
Interaction partners:
Sequence:
MAEKQAGLVGEPDPEGSSPGTSESWNYDSNCVFCRVAAGQEPKTELFHCENEDLVCFKDIKPAALYHYLVVPKKHIGSCKDLNKDHIEMVESMVAAGKTMLERNNFTDFTDVRMGFHVPPFCSISHLHLHVIAPVKEFGFLSKLVYRQDSYWFVTVDYLLEKLRK
Protein: NCK interacting protein with SH3 domain (D3ZWX4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 2/3 complex subunit 5
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 2
- Actin-related protein 3
- NCK adaptor protein 1.
- Actin-related protein 2/3 complex subunit 1B
- Actin-related protein 2/3 complex subunit 1A
- Actin-related protein 2/3 complex subunit 5-like protein
Sequence:
MRRNATLTPELGETFLVLERSSTHWWLAARARSGETGYVPPAYLHRLQGMEQDVLQAIDRAIEAVHNTAMRDGGKYSLEQRGVLQKLIHHRKETLSRRGTSAASASVMTPSTSDHHLDTAVSRQPNGVCRTGFERQHSLPSSEHLGTDGALYQVPPQPRRAAPATPPPPVKRRDREALVISGSGGRTAVPSGGSSVSSGSSVSSTSMDTLYTGSSPSELGPSCSPTPPPVPRRSAHTTVSQAQPSPSKAPSPEPPAEEVAAETNSAPDDLEALDALSPETTEEKPATETVVPRTIGAELMELVRRNTGLSHELCRVAIGVVVGHIQASVPASSPVMEQVLLSLVEGKDLSTALPSGQVCHDQQRLEVIFADLARRKDDAQQRSWALYEDEDVIRCYLEELLHILTDADPEVCKKMCKRSDFESVLALVAYYQMEHRASLRLLLLKCFGAMCSLDAAIISTLVSSVLPVELARDMQTDTQDHQKLCYSALVLAMVFSMGEAVPYAHYEHLGTPFAQFLLSIVEDGLPLDATEQLPDLCMNLLLALNLHLTAPDQNVIMAALSKHTNVKIFSEKLLLLLNRGDDPVRIFRHEPQPPHSVLKFLQDVFSSAATASIFYHTDMMALIDITVRQIADLSPGDKLRMEYLSLMHAVVRSTPYLQHRHRLSDLQATLRRILTEEETSPQCQMDRMIVQEMYKEFPDLGEVPS
Protein: Transcription initiation factor TFIID subunit 13 (Function unknown 81 protein) (TAFII-19) (TAFII19) (TBP-associated factor 13) (TBP-associated factor 19 kDa) (P11747)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as a component of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in pre-initiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 4
- Transcription initiation factor TFIID subunit 7
- SAGA complex/transcription factor TFIID complex subunit TAF6
- SAGA complex/transcription factor TFIID complex subunit TAF5
- Transcription initiation factor TFIID subunit 8
- TATA-box-binding protein
- Transcription initiation factor TFIID subunit 11
- SAGA complex/transcription factor TFIID complex subunit TAF9
Sequence:
MSRKLKKTNLFNKDVSSLLYAYGDVPQPLQATVQCLDELVSGYLVDVCTNAFHTAQNSQRNKLRLEDFKFALRKDPIKLGRAEELIATNKLITEAKKQFNETDNQNSLKRYREEDEEGDEMEEDEDEQQVTDDDEEAAGRNSAKQSTDSKATKIRKQGPKNLKKTKK
Protein: Dedicator of cytokinesis protein 2 (Q92608)
Organism: Homo sapiens (Human)
Function: Involved in cytoskeletal rearrangements required for lymphocyte migration in response of chemokines. Activates RAC1 and RAC2, but not CDC42, by functioning as a guanine nucleotide exchange factor (GEF), which exchanges bound GDP for free GTP. May also participate in IL2 transcriptional activation via the activation of RAC2.
Subcellular location: Endomembrane system {ECO:0000269|PubMed:12393632}; Peripheral membrane protein {ECO:0000269|PubMed:12393632}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12393632}. Note=Colocalizes with F-actin.
Interaction partners:
- Engulfment and cell motility protein 1
- Ras-related C3 botulinum toxin substrate 2
- Ras-related C3 botulinum toxin substrate 3
- Ras-related C3 botulinum toxin substrate 1
- Tyrosine-protein kinase Fgr oncogene homolog)
- Tyrosine-protein kinase HCK
- Proto-oncogene tyrosine-protein kinase Src
- Tyrosine-protein kinase Lyn
- Adapter molecule crk
- Phospholipase D2
Sequence:
MAPWRKADKERHGVAIYNFQGSGAPQLSLQIGDVVRIQETCGDWYRGYLIKHKMLQGIFPKSFIHIKEVTVEKRRNTENIIPAEIPLAQEVTTTLWEWGSIWKQLYVASKKERFLQVQSMMYDLMEWRSQLLSGTLPKDELKELKQKVTSKIDYGNKILELDLIVRDEDGNILDPDNTSVISLFHAHEEATDKITERIKEEMSKDQPDYAMYSRISSSPTHSLYVFVRNFVCRIGEDAELFMSLYDPNKQTVISENYLVRWGSRGFPKEIEMLNNLKVVFTDLGNKDLNRDKIYLICQIVRVGKMDLKDTGAKKCTQGLRRPFGVAVMDITDIIKGKAESDEEKQHFIPFHPVTAENDFLHSLLGKVIASKGDSGGQGLWVTMKMLVGDIIQIRKDYPHLVDRTTVVARKLGFPEIIMPGDVRNDIYITLLQGDFDKYNKTTQRNVEVIMCVCAEDGKTLPNAICVGAGDKPMNEYRSVVYYQVKQPRWMETVKVAVPIEDMQRIHLRFMFRHRSSLESKDKGEKNFAMSYVKLMKEDGTTLHDGFHDLVVLKGDSKKMEDASAYLTLPSYRHHVENKGATLSRSSSSVGGLSVSSRDVFSISTLVCSTKLTQNVGLLGLLKWRMKPQLLQENLEKLKIVDGEEVVKFLQDTLDALFNIMMEHSQSDEYDILVFDALIYIIGLIADRKFQHFNTVLEAYIQQHFSATLAYKKLMTVLKTYLDTSSRGEQCEPILRTLKALEYVFKFIVRSRTLFSQLYEGKEQMEFEESMRRLFESINNLMKSQYKTTILLQVAALKYIPSVLHDVEMVFDAKLLSQLLYEFYTCIPPVKLQKQKVQSMNEIVQSNLFKKQECRDILLPVITKELKELLEQKDDMQHQVLERKYCVELLNSILEVLSYQDAAFTYHHIQEIMVQLLRTVNRTVITMGRDHILISHFVACMTAILNQMGDQHYSFYIETFQTSSELVDFLMETFIMFKDLIGKNVYPGDWMAMSMVQNRVFLRAINKFAETMNQKFLEHTNFEFQLWNNYFHLAVAFITQDSLQLEQFSHAKYNKILNKYGDMRRLIGFSIRDMWYKLGQNKICFIPGMVGPILEMTLIPEAELRKATIPIFFDMMLCEYQRSGDFKKFENEIILKLDHEVEGGRGDEQYMQLLESILMECAAEHPTIAKSVENFVNLVKGLLEKLLDYRGVMTDESKDNRMSCTVNLLNFYKDNNREEMYIRYLYKLRDLHLDCDNYTEAAYTLLLHTWLLKWSDEQCASQVMQTGQQHPQTHRQLKETLYETIIGYFDKGKMWEEAISLCKELAEQYEMEIFDYELLSQNLIQQAKFYESIMKILRPKPDYFAVGYYGQGFPSFLRNKVFIYRGKEYERREDFQMQLMTQFPNAEKMNTTSAPGDDVKNAPGQYIQCFTVQPVLDEHPRFKNKPVPDQIINFYKSNYVQRFHYSRPVRRGTVDPENEFASMWIERTSFVTAYKLPGILRWFEVVHMSQTTISPLENAIETMSTANEKILMMINQYQSDETLPINPLSMLLNGIVDPAVMGGFAKYEKAFFTEEYVRDHPEDQDKLTHLKDLIAWQIPFLGAGIKIHEKRVSDNLRPFHDRMEECFKNLKMKVEKEYGVREMPDFDDRRVGRPRSMLRSYRQMSIISLASMNSDCSTPSKPTSESFDLELASPKTPRVEQEEPISPGSTLPEVKLRRSKKRTKRSSVVFADEKAAAESDLKRLSRKHEFMSDTNLSEHAAIPLKASVLSQMSFASQSMPTIPALALSVAGIPGLDEANTSPRLSQTFLQLSDGDKKTLTRKKVNQFFKTMLASKSAEEGKQIPDSLSTDL
Protein: DAP3-binding cell death enhancer 1 (DAP3-binding cell death enhancer 1, long form) (DELE1(L)) (Death ligand signal enhancer) [Cleaved into: DAP3-binding cell death enhancer 1 short form (DELE1(S)) (S-DELE1)] (Q9DCV6)
Organism: Mus musculus (Mouse)
Function: Key activator of the integrated stress response (ISR) following mitochondrial stress. In response to mitochondrial stress, cleaved by the protease OMA1, generating the DAP3-binding cell death enhancer 1 short form (DELE1(S) or S-DELE1), which translocates to the cytosol and activates EIF2AK1/HRI to trigger the ISR. Essential for the induction of death receptor-mediated apoptosis through the regulation of caspase activation.
Subcellular location: [DAP3-binding cell death enhancer 1]: Mitochondrion {ECO:0000250|UniProtKB:Q14154}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q14154}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q14154}. Note=Imported in the mitochondrial matrix in absence of stress, leading to its degradation by LONP1. Localizes at the mitochondrial surface in response to iron deficiency: iron deficiency impairs mitochondrial import, promoting localization at the mitochondrial surface and stabilization. Associates with the mitochondrion inner membrane in response to mitochondrial stress, leading to its proteolytic processing by OMA1, and generation of the AP3-binding cell death enhancer 1 short form (DELE1(S) or S-DELE1). {ECO:0000250|UniProtKB:Q14154}.; SUBCELLULAR LOCATION: [DAP3-binding cell death enhancer 1 short form]: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q14154}. Note=This short form is generated by proteolytic processing by OMA1 in response to mitochondrial stress, leading to translocation to the cytosol. {ECO:0000250|UniProtKB:Q14154}.
Interaction partners:
- Metalloendopeptidase OMA1, mitochondrial
Sequence:
MWRLTGILGRALPRLLGPGFRGITPKPTSSDGSQTTSPTLPLTRLSFDRSGSHGSKRSRDPKCCGWKDAFHWMSAHVSPNTLRDAISWGTLAVLALHLARQIHFHAPLVAGPQPAERSWHSPLYRFLSSSWWHPHSSLRRHVLPRSDCPAPRNTGLREPRQGQEDHPSAPSQCLPSDSSLRSGLLNLPEEEPSDFDFLHASRDFASQAKAAEAHPPGGKNEQDKAKALPLEEAVTSIQQLFQLSVAITFNFLGTENIKTGDYTAAFSYFQKAADRGYSKAQYNVGLCLEHGRGTPRDLSKAILFYHLAAVQGHSLAQYRYARCLLQSPGSLSDPERERAVSLLKQAADSGLTEAQAFLGVLFTKEPHLDEQRAVKYLWLAASNGDSQSRFHLGICYEKGLGAQRNLGEAVKCYQQAAAMGNEPARERLRTLFNVEAAGPSHLATTGLKSFSSPSLCSLNTLLAGASGLPHASSTGNLGLLCRSGHLGASHGAPSRTIPSLERSLVRLGFG
Protein: CDP-diacylglycerol--inositol 3-phosphatidyltransferase (EC 2.7.8.11) (Phosphatidylinositol synthase) (PI synthase) (PtdIns synthase) (Q59RA2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Catalyzes the synthesis of phosphatidylinositol (PtdIns). Required for proper membrane dynamics and cell wall integrity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:35227874, ECO:0000305|PubMed:8740418}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Phosphatidate cytidylyltransferase
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
- 1-phosphatidylinositol 4-kinase
- Phosphatidylinositol 4-kinase PIK1a
- CDP-diacylglycerol--serine O-phosphatidyltransferase
- Phosphatidylinositol 3-kinase VPS34
- Phosphatidylinositol-3-phosphatase
- Cardiolipin synthase
- phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase
- Phosphoinositide phospholipase C
Sequence:
MPSAKSSDLSPTKTNLESTTKQKVSVQDIFLYIPNLIGYLRIITAIISFLCMANHPVATLIFYGISGFLDAFDGYAARKFNQGTRFGAVLDMVTDRCATSSLIVYLGVLYPQYTVFWQILVSLDLSSHYMHMYAMLSAGSTSHKNVDETQSKLLSLYYNNRLVLFFVCLINELFYMAVYLHYYKFFWLGTVMLVASTPIWLFKQIANIIQLKNASLILARMDAHDHSKRD