wanglab/gogpt-training-data huggingface dataset:
Protein: ADP-ribosylation factor-like protein 3A, putative (Q57XJ5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- GMP phosphodiesterase delta subunit domain-containing protein
- Cilia- and flagella-associated protein 36
Sequence:
MGLLTLLRKLRSSDASPRILILGLDNAGKTSILRNLSGEDPTTTQATQGFNIKTVDCEGFKLNVWDIGGQKAIRAYWPNYFDEVDCLVYVVDSADKRRLDETAAELETLLQEEKLREVPFLVLANKCDLATALSPEDISTALNLQNLRDRTWSIQKCSAKTGEGLQEGFMWAIKSIKK
Protein: Contactin-associated protein-like 4 (Cell recognition molecule Caspr4) (Q9C0A0)
Organism: Homo sapiens (Human)
Function: Presynaptic protein involved in both dopaminergic synaptic transmission and GABAergic system, thereby participating in the structural maturation of inhibitory interneuron synapses. Involved in the dopaminergic synaptic transmission by attenuating dopamine release through a presynaptic mechanism. Also participates in the GABAergic system (By similarity).
Subcellular location: Presynaptic cell membrane {ECO:0000250|UniProtKB:Q99P47}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99P47}. Note=Specifically present within the presynaptic compartment of synapses. {ECO:0000250|UniProtKB:Q99P47}.
Interaction partners:
- Contactin-5
- Neuronal cell adhesion molecule
- Amyloid-beta A4 precursor protein-binding family A member 1
- Neural cell adhesion molecule L1-like protein
- Rho guanine nucleotide exchange factor TIAM1
Sequence:
MGSVTGAVLKTLLLLSTQNWNRVEAGNSYDCDDPLVSALPQASFSSSSELSSSHGPGFARLNRRDGAGGWSPLVSNKYQWLQIDLGERMEVTAVATQGGYGSSNWVTSYLLMFSDSGWNWKQYRQEDSIWGFSGNANADSVVYYRLQPSIKARFLRFIPLEWNPKGRIGMRIEVFGCAYRSEVVDLDGKSSLLYRFDQKSLSPIKDIISLKFKTMQSDGILLHREGPNGDHITLQLRRARLFLLINSGEAKLPSTSTLVNLTLGSLLDDQHWHSVLIQRLGKQVNFTVDEHRHHFHARGEFNLMNLDYEISFGGIPAPGKSVSFPHRNFHGCLENLYYNGVDIIDLAKQQKPQIIAMGNVSFSCSQPQSMPVTFLSSRSYLALPDFSGEEEVSATFQFRTWNKAGLLLFSELQLISGGILLFLSDGKLKSNLYQPGKLPSDITAGVELNDGQWHSVSLSAKKNHLSVAVDGQMASAAPLLGPEQIYSGGTYYFGGCPDKSFGSKCKSPLGGFQGCMRLISISGKVVDLISVQQGSLGNFSDLQIDSCGISDRCLPNYCEHGGECSQSWSTFHCNCTNTGYRGATCHNSIYEQSCEAYKHRGNTSGFYYIDSDGSGPLEPFLLYCNMTETAWTIIQHNGSDLTRVRNTNPENPYAGFFEYVASMEQLQATINRAEHCEQEFTYYCKKSRLVNKQDGTPLSWWVGRTNETQTYWGGSSPDLQKCTCGLEGNCIDSQYYCNCDADRNEWTNDTGLLAYKEHLPVTKIVITDTGRLHSEAAYKLGPLLCQGDRSFWNSASFDTEASYLHFPTFHGELSADVSFFFKTTASSGVFLENLGIADFIRIELRSPTVVTFSFDVGNGPFEISVQSPTHFNDNQWHHVRVERNMKEASLQVDQLTPKTQPAPADGHVLLQLNSQLFVGGTATRQRGFLGCIRSLQLNGMTLDLEERAQVTPEVQPGCRGHCSSYGKLCRNGGKCRERPIGFFCDCTFSAYTGPFCSNEISAYFGSGSSVIYNFQENYLLSKNSSSHAASFHGDMKLSREMIKFSFRTTRTPSLLLFVSSFYKEYLSVIIAKNGSLQIRYKLNKYQEPDVVNFDFKNMADGQLHHIMINREEGVVFIEIDDNRRRQVHLSSGTEFSAVKSLVLGRILEHSDVDQDTALAGAQGFTGCLSAVQLSHVAPLKAALHPSHPDPVTVTGHVTESSCMAQPGTDATSRERTHSFADHSGTIDDREPLANAIKSDSAVIGGLIAVVIFILLCITAIAVRIYQQKRLYKRSEAKRSENVDSAEAVLKSELNIQNAVNENQKEYFF
Protein: Structural maintenance of chromosomes protein 2 (DA-box protein SMC2) (P38989)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases.
Subcellular location: Nucleus. Cytoplasm. Chromosome. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, condensin associates with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase.
Interaction partners:
- Condensin complex subunit 3
- Structural maintenance of chromosomes protein 4
- Condensin complex subunit 1
- Condensin complex subunit 2
- Kinetochore protein NDC80
- Sister chromatid cohesion protein 1
- DNA topoisomerase 2
- Cohesin subunit SCC3
- Structural maintenance of chromosomes protein 3
- Structural maintenance of chromosomes protein 6
Sequence:
MKVEELIIDGFKSYATRTVITDWDPQFNAITGLNGSGKSNILDAICFVLGIASMSTVRASSLQDLIYKRGQAGVTKASVTIVFDNTDKSNSPIGFTNSPQISVTRQVVLGGTSKYLINGHRAPQQSVLQLFQSVQLNINNPNFLIMQGKITKVLNMKPSEILSLIEEAAGTKMFEDRREKAERTMSKKETKLQENRTLLTEEIEPKLEKLRNEKRMFLEFQSTQTDLEKTERIVVSYEYYNIKHKHTSIRETLENGETRMKMLNEFVKKTSEEIDSLNEDVEEIKLQKEKELHKEGTISKLENKENGLLNEISRLKTSLSIKVENLNDTTEKSKALESEIASSSAKLIEKKSAYANTEKDYKMVQEQLSKQRDLYKRKEELVSTLTTGISSTGAADGGYNAQLAKAKTELNEVSLAIKKSSMKMELLKKELLTIEPKLKEATKDNELNVKHVKQCQETCDKLRARLVEYGFDPSRIKDLKQREDKLKSHYYQTCKNSEYLKRRVTNLEFNYTKPYPNFEASFVHGVVGQLFQIDNDNIRYATALQTCAGGRLFNVVVQDSQTATQLLERGRLRKRVTIIPLDKIYTRPISSQVLDLAKKIAPGKVELAINLIRFDESITKAMEFIFGNSLICEDPETAKKITFHPKIRARSITLQGDVYDPEGTLSGGSRNTSESLLVDIQKYNQIQKQIETIQADLNHVTEELQTQYATSQKTKTIQSDLNLSLHKLDLAKRNLDANPSSQIIARNEEILRDIGECENEIKTKQMSLKKCQEEVSTIEKDMKEYDSDKGSKLNELKKELKLLAKELEEQESESERKYDLFQNLELETEQLSSELDSNKTLLHNHLKSIESLKLENSDLEGKIRGVEDDLVTVQTELNEEKKRLMDIDDELNELETLIKKKQDEKKSSELELQKLVHDLNKYKSNTNNMEKIIEDLRQKHEFLEDFDLVRNIVKQNEGIDLDTYRERSKQLNEKFQELRKKVNPNIMNMIENVEKKEAALKTMIKTIEKDKMKIQETISKLNEYKRETLVKTWEKVTLDFGNIFADLLPNSFAKLVPCEGKDVTQGLEVKVKLGNIWKESLIELSGGQRSLIALSLIMALLQFRPAPMYILDEVDAALDLSHTQNIGHLIKTRFKGSQFIVVSLKEGMFANANRVFRTRFQDGTSVVSIM
Protein: Acetylcholine receptor subunit epsilon (P02715)
Organism: Bos taurus (Bovine)
Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular location: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Secreted LY6/PLAUR domain containing 1
- 43 kDa receptor-associated protein of the synapse
- Acetylcholine receptor subunit alpha
- Docking protein 7.
- Collagen like tail subunit of asymmetric acetylcholinesterase.
- Collagen like tail subunit of asymmetric acetylcholinesterase
- receptor protein-tyrosine kinase
- UDP-N-acetylglucosamine transferase subunit ALG14
Sequence:
MAGALLCALLLLQLLGRGEGKNEELRLYHYLFDTYDPGRRPVQEPEDTVTISLKVTLTNLISLNEKEETLTTSVWIGIDWQDYRLNYSKGDFGGVETLRVPSELVWLPEIVLENNIDGQFGVAYEANVLVSEGGYLSWLPPAIYRSTCAVEVTYFPFDWQNCSLVFRSQTYNAEEVEFVFAVDDEGKTISKIDIDTEAYTENGEWAIDFCPGVIRRHDGDSAGGPGETDVIYSLIIRRKPLFYVINIIVPCVLISGLVLLAYFLPAQAGGQKCTVSINVLLAQTVFLFLIAQKTPETSLSVPLLGRYLIFVMVVATLIVMNCVIVLNVSLRTPTTHAMSPRLRYVLLELLPQLLGSGAPPEIPRAASPPRRASSLGLLLRAEELILKKPRSELVFEQQRHRHGTWTATLCQNLGAAAPEIRCCVDAVNFVASSTRDQEATGEEVSDWVRMGKALDSICFWAALVLFLVGSSLIFLGAYFNRVPQLPYPPCM
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A (Oligosaccharyl transferase subunit STT3A) (STT3-A) (EC 2.4.99.18) (F1PJP5)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Catalytic subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (By similarity). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. This subunit contains the active site and the acceptor peptide and donor lipid-linked oligosaccharide (LLO) binding pockets (By similarity). STT3A is present in the majority of OST complexes and mediates cotranslational N-glycosylation of most sites on target proteins, while STT3B-containing complexes are required for efficient post-translational glycosylation and mediate glycosylation of sites that have been skipped by STT3A.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12887896}; Multi-pass membrane protein {ECO:0000269|PubMed:29519914}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Tumor suppressor candidate 3.
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
- Mannosyl-oligosaccharide glucosidase.
- Magnesium transporter 1.
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit KCP2
- Protein transport protein Sec61 subunit beta
Sequence:
MTKLGFLRLSYEKQDTLLKLLILSMAAVLSFSTRLFAVLRFESVIHEFDPYFNYRTTRFLAEEGFYKFHNWFDDRAWYPLGRIIGGTIYPGLMITSAAIYHVLHFFHITIDIRNVCVFLAPLFSSFTTIVTYHLTKELKDAGAGLLAAAMIAVVPGYISRSVAGSYDNEGIAIFCMLLTYYMWIKAVKTGSIYWAAKCALAYFYMVSSWGGYVFLINLIPLHVLVLMLTGRFSHRIYVAYCTVYCLGTILSMQISFVGFQPVLSSEHMAAFGVFGLCQIHAFVDYLRSKLNPQQFEVLFRSVISLVGFVLLTVGALLMLTGKISPWTGRFYSLLDPSYAKNNIPIIASVSEHQPTTWSSYYFDLQLLVFMFPVGLYYCFSNLSDARIFIIMYGVTSMYFSAVMVRLMLVLAPVMCILSGIGVSQVLSTYMKNLDISRPDKKSKKQQDSTYPIKNEVASGMILVMAFFLITYTFHSTWVTSEAYSSPSIVLSARGGDGSRIIFDDFREAYYWLRHNTPEDAKVMSWWDYGYQITAMANRTILVDNNTWNNTHISRVGQAMASTEEKAYEIMRELDVSYVLVIFGGLTGYSSDDINKFLWMVRIGGSTDTGKHIKEHDYYTPTGEFRVDREGSPVLLNCLMYKMCYYRFGQVYTEAKRPPGFDRVRNAEIGNKDFELDVLEEAYTTEHWLVRIYKVKDLDNRGLSRT
Protein: Hepatocyte nuclear factor 1-beta-A (HNF-1-beta-A) (HNF-1B-A) (Hepatocyte nuclear factor 1-beta-2) (HNF-1B-2) (Transcription factor 2) (TCF-2) (Variant hepatic nuclear factor 1) (vHNF1) (A1L1N5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcription factor that binds to the inverted palindrome 5'-GTTAATNATTAAC-3' (By similarity). Required for induction of rhombomere r5/r6 gene expression in the hindbrain.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Iroquois homeobox 3b.
- Homeobox protein Hox-B1a
- Hepatocyte nuclear factor 1-beta-B
- Single-minded homolog 1-A
Sequence:
MFANMVSKLTSLQQELLSALLDSGVTKDVLLQALEDLDPSPSAFGVKLDSLQMSPSGSKLSDTDSKPVFHTLTNGHSKGKLSGDEGSEDGDDYDTPPILKELQSQNTEEAAEQRAEIERMLAEDPWRAARMIKGYMQQHNIPQREVVDVTGLNQSHLSQHLNKGTPMKTQKRAALYTWYVRKQREILRQFNQATQGSGATMLDKGNQDQVLLFFSEFSQSGQGMVQPGDDAAIEPACKKLRRNRFKWGPASQQILYQAYERQKNPSKEEREALVEECNRAECLQRGVSPSKAHGLGSNLVTEVRVYNWFANRRKEEAFRQKLAMDAYSGPAHSLNSLLSHSSPHHPQTSSSPPSKMQGVRYSQQGPGEVTSSTTINHHSSNAMSTSQSVLQQVSPGALDPSHSLLSPDAKMISVSGGGLPPVSTLTNIHASHHVHQQTPNLIMPLSGVMAIAQSLNTSQAQTVPVINSVAGSLAALQPVQFSQQLNSQHQQLMQQSSGHMSQQSFMASVSHSHMYPHKQEPPQYSHSSRFPPAMVVTDANSLSTLSSMSSSKQCPLQAW
Protein: LON peptidase N-terminal domain and RING finger protein 2 (Neuroblastoma apoptosis-related protease) (RING finger protein 192) (Q1L5Z9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSPEPVPPPPPPQCPGCDRAEPIAQRLEEGDEAFRAGDYEMAAELFRSMLAGLAQPDRGLCLRLGDALARAGRLPEALGAFRGAARLGALRPEELEELAGGLVRAVGLRDRPLSAENPGGEPEAPGEGGPAPEPRAPRDLLGCPRCRRLLHKPVTLPCGLTVCKRCVEPGPARPQVRRVNVVLSGLLEKCFPAECRLRRLAGQARSLQRQQQPEAALLRCDQALELAPDDNSLLLLRAELYLTMKNYEQALQDASAACQNEPLLIKGHQVKAQALSGLGRSKEVLKEFLYCLALNPECNSVKKEAQKVMCEVLFSATANVHENLTSSIQSRLKAQGHSHMNAQALLEEGDAGSSENSSEKSDMLGNTNSSVLYFILGLHFEEDKKALESILPTAPSAGLKRQFPDDVEDAPDLNAPGKIPKKDLSLQRSPNSETEESQGLSLDVTDFECALCMRLLFEPVTTPCGHTFCLKCLERCLDHAPHCPLCKDKLSELLASRNFNITVLAEELIFRYLPDELSDRKRIYDEEMSELSNLTRDVPIFVCAMAFPTVPCPLHVFEPRYRLMIRRCMETGTKRFGMCLSAEHAGLSEYGCMLEIKDVRTFPDGSSVVDAIGISRFRVLSHRHRDGYNTADIEYLEDEKVEGPEYEELAALHDSVHQQSVSWFASLQDRMKEQILSHFGVMPDREPEPQSNPSGPAWSWWILAVLPLERKAQLAILGMTSLKERLLAIRRILVIITRKMNSRQELANARERNN
Protein: Salutaridine synthase (EC 1.14.19.67) (Cytochrome P450 719B1) (B1NF18)
Organism: Papaver somniferum (Opium poppy)
Function: Catalyzes the formation of the morphinan alkaloid salutaridine by intramolecular phenol oxidation of (R)-reticuline without the incorporation of oxygen into the product. Can also use (R)-norreticuline as substrate.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAPINIEGNDFWMIACTVIIVFALVKFMFSKISFYQSANTTEWPAGPKTLPIIGNLHQLGGGVPLQVALANLAKVYGGAFTIWIGSWVPMIVISDIDNAREVLVNKSADYSARDVPDILKIITANGKNIADCDSGPFWHNLKKGLQSCINPSNVMSLSRLQEKDMQNLIKSMQERASQHNGIIKPLDHAKEASMRLLSRVIFGHDFSNEDLVIGVKDALDEMVRISGLASLADAFKIAKYLPSQRKNIRDMYATRDRVYNLIQPHIVPNLPANSFLYFLTSQDYSDEIIYSMVLEIFGLGVDSTAATAVWALSFLVGEQEIQEKLYREINNRTGGQRPVKVVDLKELPYLQAVMKETLRMKPIAPLAVPHVAAKDTTFKGRRIVKGTKVMVNLYAIHHDPNVFPAPYKFMPERFLKDVNSDGRFGDINTMESSLIPFGAGMRICGGVELAKQMVAFALASMVNEFKWDCVSEGKLPDLSEAISFILYMKNPLEAKITPRTKPFRQ
Protein: PslC (Q9I1N6)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- PslA
- Alginate biosynthesis protein AlgA
- PslE
- PslD
- PslF
- PslH
- PslI
- PslJ
- PslG
- PslL
Sequence:
MRCALVIPTRNAGAHLDRLLPALAAQRRQPDSILVVDSRSSDDTVERFRAFGARVEVIEPASFNHGGTRRWASQQVEADALIYLTQDAIPASPDSFANLLDELYAEADIGVAYGRQLPHPGAGLLGAQARRFNYPPESRSKRLADASELGIKTCFSSDSFSAYRSDALAAVGDFPEDVIGSEDAYVAARLLQAGYAVRYAASAEVYHSHDYRLLEEFRRYFDIGVFYGRERWIRAAFGGAGGEGKRYVLAEIQALRAAGALYRVPEIALRSAFKLLGYRLGQLERHLPVALKRRISMFPGYWK
Protein: Endonuclease ALBA3 (PfAlba3) (EC 3.1.-.-) (DNA/RNA-binding protein Alba 3) (Q8IJX8)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Nucleus {ECO:0000269|PubMed:22006844, ECO:0000269|PubMed:36947546}. Chromosome {ECO:0000269|PubMed:22006844}. Chromosome, telomere {ECO:0000269|PubMed:22006844}. Cytoplasm {ECO:0000269|PubMed:22006844}.
Interaction partners:
Sequence:
MASTEEVSQERSENSIQVSMTKKPTFYARIGKRMFTGNEEKNPFDEVIITGLGNATKIAIGAASIMEKEDIGQIVKVQTAYFSSDRINRRIPKITIVLKKHPDFVAN
Protein: RE03780p (Q9VNP6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKLFTAVLAICLVAFAAAQSADPAAALEPSSEYLPPVGEAEAAQLSENGYKYRTVRRLKLRHRREVPNQEYLPPVENAPSQEYLPPVDAAAIGDTKVADDGYRYKTVRKLKFRARHRRDVSEIAEPSGEYLPPVQVELAPELKTILGDDGYKYKTVRRLKFRRHRREAVAEEAAAESAPNGEYLPPAEAAAAAPAAAEAEPKSAEEGTELAKDGYRYKTVRRLRYRYRH
Protein: Arf3p (A0A1D8PJ64)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- ADP-ribosylation factor
- ADP-ribosylation factor
- Rga2p
- Arf family guanine nucleotide exchange factor
- Rab family GTPase
- Age3p
- Lrg1p
Sequence:
MGGLVSKLFKNREMRILMLGLDNAGKTTILYKLKLGKTSKTVPTVGFNVETVKHKNVSFAVWDCGGQERIRPLWRHYFTGTNALIYVVDSSDVDRLEESKQELFRIVTDKELTNCLLVVLANKQDVDGAVKPKDLIERFQLNKLTGEHTWSVIPTIAIDGTGLVETLNWISSHSK
Protein: Zinc finger and BTB domain-containing protein 8A (BTB/POZ and zinc-finger domain-containing factor) (BTB/POZ and zinc-finger domains factor on chromosome 1) (BOZ-F1) (Q96BR9)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MEISSHQSHLLQQLNEQRRQDVFCDCSILVEGKVFKAHRNVLFASSGYFKMLLSQNSKETSQPTTATFQAFSPDTFTVILDFVYSGKLSLTGQNVIEVMSAASFLQMTDVISVCKTFIKSSLDISEKEKDRYFSLSDKDANSNGVERSSFYSGGWQEGSSSPRSHLSPEQGTGIISGKSWNKYNYHPASQKNTQQPLAKHEPRKESIKKTKHLRLSQPSEVTHYKSSKREVRTSDSSSHVSQSEEQAQIDAEMDSTPVGYQYGQGSDVTSKSFPDDLPRMRFKCPYCTHVVKRKADLKRHLRCHTGERPYPCQACGKRFSRLDHLSSHFRTIHQACKLICRKCKRHVTDLTGQVVQEGTRRYRLCNECLAEFGIDSLPIDLEAEQHLMSPSDGDKDSRWHLSEDENRSYVEIVEDGSADLVIQQVDDSEEEEEKEIKPNIR
Protein: Phosphatidate cytidylyltransferase 2 (EC 2.7.7.41) (CDP-DAG synthase 2) (CDP-DG synthase 2) (CDP-diacylglycerol synthase 2) (CDS 2) (CDP-diglyceride pyrophosphorylase 2) (CDP-diglyceride synthase 2) (CTP:phosphatidate cytidylyltransferase 2) (O95674)
Organism: Homo sapiens (Human)
Function: Catalyzes the conversion of phosphatidic acid (PA) to CDP-diacylglycerol (CDP-DAG), an essential intermediate in the synthesis of phosphatidylglycerol, cardiolipin and phosphatidylinositol. Exhibits specificity for the nature of the acyl chains at the sn-1 and sn-2 positions in the substrate, PA and the preferred acyl chain composition is 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid. Plays an important role in regulating the growth and maturation of lipid droplets which are storage organelles at the center of lipid and energy homeostasis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:25375833, ECO:0000269|PubMed:26946540, ECO:0000269|PubMed:31548309}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial
- Cardiolipin synthase
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Phosphatidate cytidylyltransferase, mitochondrial
- 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
- 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
- Phosphatidate cytidylyltransferase 1
- Phospholipase D1
- Membrane-bound glycerophospholipid O-acyltransferase 2
- Phospholipid phosphatase 2
Sequence:
MTELRQRVAHEPVAPPEDKESESEAKVDGETASDSESRAESAPLPVSADDTPEVLNRALSNLSSRWKNWWVRGILTLAMIAFFFIIIYLGPMVLMIIVMCVQIKCFHEIITIGYNVYHSYDLPWFRTLSWYFLLCVNYFFYGETVTDYFFTLVQREEPLRILSKYHRFISFTLYLIGFCMFVLSLVKKHYRLQFYMFGWTHVTLLIVVTQSHLVIHNLFEGMIWFIVPISCVICNDIMAYMFGFFFGRTPLIKLSPKKTWEGFIGGFFATVVFGLLLSYVMSGYRCFVCPVEYNNDTNSFTVDCEPSDLFRLQEYNIPGVIQSVIGWKTVRMYPFQIHSIALSTFASLIGPFGGFFASGFKRAFKIKDFANTIPGHGGIMDRFDCQYLMATFVNVYIASFIRGPNPSKLIQQFLTLRPDQQLHIFNTLRSHLIDKGMLTSTTEDE
Protein: DNA-directed RNA polymerases I, II, and III subunit RPABC5 (Q57XV8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA-dependent RNA polymerases, putative
- DNA-direcetd RNA polymerase II, subunit 9, putative
- Plastid-encoded RNA polymerase subunit alpha
- DNA-directed RNA polymerase II, putative
- RNA polymerase III subunit Rpc25 domain-containing protein
- Nitroreductase, putative
- Plastid-encoded RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase I subunit RPA1
Sequence:
MLIPVRCYSCGKVVGHLYELYQELLNQDHTEAEALNALRLSRMCCRRMILSHIDLADDLLPYSVPVVGSMPLINPVQGPVPRRQ
Protein: AP-1 complex subunit mu (AP-1 adaptor complex mu1 subunit) (Adaptor protein complex AP-1 subunit mu) (Adaptor-related protein complex 1 subunit mu) (Clathrin-adaptor medium chain Apm1) (Mu1-adaptin) (Q54HS9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the trans-Golgi network (TGN) and endosomes. The AP complexes mediate the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. Also involved in early steps of phagocytosis and macropinocytosis.
Subcellular location: Golgi apparatus, trans-Golgi network. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250}.
Interaction partners:
- AP-1 complex subunit gamma
- AP-1 complex subunit beta
- AP-2 complex subunit alpha-2
- AP-3 complex subunit delta
- AP-4 complex subunit epsilon
- AP-2 complex subunit sigma
- Clathrin heavy chain
- AP-4 complex subunit beta
- Clathrin light chain
- AP-1 complex subunit sigma-2
Sequence:
MAASAIFLMDSKGKVLISRNYRGDVPMSVASKFISKILEEEDLNLKPIIQEDGISYIYVKHNNLFLLATTERNANAATILLFLYKMIEVFNEYFKELEEESIRDNFVVIYELMDEMMDFGYPQSTEPKILQEYITQEGYKLERGARGMVLPAAITGAVSWRKEGIKYNKNEVFLDVVESINLLVSANGTVLRSEIVGAVKMKSKLSGMPELRLGLNDKILFENSAKTGAPKGKGVELEDVKFHQCVRLSKFENDRTISFIPPDGEFELMSYRLNTTVKPLIWVECISDTHAHSRVEYMVKAKSQFKGKSIANNVEIIVPVPPDADTPKFRCTVGTCKYAPEKDAIIWTIKQFPGGGREFLMRAHFGLPSISDEKPATKPPIMVKFEIPYYTVSGIQVRYLKIIEKSGYQALPWVRYVCLSGDYQFRTS
Protein: Probable succinate transporter subunit YjjP (P0ADD5)
Organism: Escherichia coli (strain K12)
Function: Involved in succinate export with YjjB. Both proteins are required for export. Contributes to succinate production under both aerobic and anaerobic conditions.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Probable succinate transporter subunit YjjB
- Anaerobic C4-dicarboxylate transporter DcuC
Sequence:
MQTEQQRAVTRLCIQCGLFLLQHGAESALVDELSSRLGRALGMDSVESSISSNAIVLTTIKDGQCLTSTRKNHDRGINMHVVTEVQHIVILAEHHLLDYKGVEKRFSQIQPLRYPRWLVALMVGLSCACFCKLNNGGWDGAVITFFASTTAMYIRQLLAQRHLHPQINFCLTAFAATTISGLLLQLPTFSNTPTIAMAASVLLLVPGFPLINAVADMFKGHINTGLARWAIASLLTLATCVGVVMALTIWGLRGWV
Protein: Tachykinin-like peptide-VIII (P.nigriventer tachykinin peptides VIII) (PnTkP-VIII) (U29-ctenitoxin-Pn1h) (U29-CNTX-Pn1h) (P86305)
Organism: Phoneutria nigriventer (Brazilian armed spider) (Ctenus nigriventer)
Subcellular location: Secreted {ECO:0000269|PubMed:15573368}.
Interaction partners:
Sequence:
QKKDKKDRFY
Protein: Sushi-repeat-containing protein, X-linked (A0A8I6AL59)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGSPGLRPTLLLPQVLLLLLALLHVPPSQGFPEKRCPTLTMPANGGFKCVDGAYFNSRCEYYCSPGYTLKGERTVTCMDNKAWSGRPASCVDMEPPRIKCPSVKERIAEPNKLTVRVSWETPEGRDTADGILTDVILRGLPPGSNFPEGDHKIEYTVYDRAENKGTCKFRVKVRVRRCGKLNAPENGYMKCSSDGDNYGATCEFSCIGGYELQGSPARVCQSNLAWSGTEPSCAAMNVNVGVRTAAALLDQFYEKRRLLIVSTPTARNLLYRLQLGMLQQAQCGLDLRHITVVELVGVFPTLIGRIRAKIMPPALALQLRLLLRIPLYSFSMVLVDKHGMDKERYVSLVTPMALFNLIDTFPLRKEEMILQAEMGQSCNT
Protein: Apoptotic protease-activating factor 1 (APAF-1) (O14727)
Organism: Homo sapiens (Human)
Function: Oligomeric Apaf-1 mediates the cytochrome c-dependent autocatalytic activation of pro-caspase-9 (Apaf-3), leading to the activation of caspase-3 and apoptosis. This activation requires ATP. Isoform 6 is less effective in inducing apoptosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12804598}.
Interaction partners:
- Cytochrome c
- Caspase-3
- Caspase-9
- Heat shock 70 kDa protein 4
- Bcl-2-like protein 1
- Heat shock protein HSP 90-alpha
- Apoptosis regulator Bcl-2
- Diablo IAP-binding mitochondrial protein
- Cell death regulator Aven
- Heat shock protein HSP 90-beta
Sequence:
MDAKARNCLLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNALLHEGYKDLAALLHDGIPVVSSSSGKDSVSGITSYVRTVLCEGGVPQRPVVFVTRKKLVNAIQQKLSKLKGEPGWVTIHGMAGCGKSVLAAEAVRDHSLLEGCFPGGVHWVSVGKQDKSGLLMKLQNLCTRLDQDESFSQRLPLNIEEAKDRLRILMLRKHPRSLLILDDVWDSWVLKAFDSQCQILLTTRDKSVTDSVMGPKYVVPVESSLGKEKGLEILSLFVNMKKADLPEQAHSIIKECKGSPLVVSLIGALLRDFPNRWEYYLKQLQNKQFKRIRKSSSYDYEALDEAMSISVEMLREDIKDYYTDLSILQKDVKVPTKVLCILWDMETEEVEDILQEFVNKSLLFCDRNGKSFRYYLHDLQVDFLTEKNCSQLQDLHKKIITQFQRYHQPHTLSPDQEDCMYWYNFLAYHMASAKMHKELCALMFSLDWIKAKTELVGPAHLIHEFVEYRHILDEKDCAVSENFQEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQAKQEVDNGMLYLEWINKKNITNLSRLVVRPHTDAVYHACFSEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKIWNSMTGELVHTYDEHSEQVNCCHFTNSSHHLLLATGSSDCFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKLWDATSANERKSINVKQFFLNLEDPQEDMEVIVKCCSWSADGARIMVAAKNKIFLFDIHTSGLLGEIHTGHHSTIQYCDFSPQNHLAVVALSQYCVELWNTDSRSKVADCRGHLSWVHGVMFSPDGSSFLTSSDDQTIRLWETKKVCKNSAVMLKQEVDVVFQENEVMVLAVDHIRRLQLINGRTGQIDYLTEAQVSCCCLSPHLQYIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDDAEIQVWNWQLDKCIFLRGHQETVKDFRLLKNSRLLSWSFDGTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTAKIWSFDLLLPLHELRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWNVSNGELLHLCAPLSEEGAATHGGWVTDLCFSPDGKMLISAGGYIKWWNVVTGESSQTFYTNGTNLKKIHVSPDFKTYVTVDNLGILYILQTLE
Protein: ADP-ribosylation factor (B5X3Q1)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Golgi apparatus {ECO:0000256|ARBA:ARBA00004555, ECO:0000256|RuleBase:RU369003}.
Interaction partners:
- ADP-ribosylation factor 6
- ADP-ribosylation factor 6
- ADP-ribosylation factor
- ADP-ribosylation factor
- Intersectin-2-like
- AP complex subunit beta
- AP complex subunit beta
- Cell surface glycoprotein 1-like isoform X1
- Intersectin-1
- Intersectin-1
Sequence:
MGNMFAGLFKNLFGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELTRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRQRNWYIQATCATSGDGLYEGLDWLSNQLKNAK