wanglab/gogpt-training-data huggingface dataset:
Protein: Pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH1 (EC 3.6.4.13) (DEAH RNA helicase homolog PRP2) (Protein EMBRYO DEFECTIVE 2733) (Protein ENHANCED SILENCING PHENOTYPE 3) (Q8VY00)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in pre-mRNA splicing.
Interaction partners:
- Pre-mRNA-processing-splicing factor 8A
- DExH-box ATP-dependent RNA helicase DExH12
- At1g31870
- Peptidyl-prolyl cis-trans isomerase CYP57
- THO complex subunit 2
- At4g25020
- Protein MOS2
- Pre-mRNA-processing factor 17
- Transducin/WD40 repeat-like superfamily protein
- Pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH7
Sequence:
MASNDLKTWVSDKLMMLLGYSQAAVVNYLIAMAKKTKSPTELVGELVDYGFSSSGDTRSFAEEIFARVPRKTAGVNLYQKHEAEAAMLVRKQKTYALLDADDDEDEVVVEKKSSVSESRKSDKGKKRFRKKSGQSDESDGEVAVREDSRHVRRKVSEEDDGSESEEERVRDQKEREELEQHLKDRDTARTRKLTEQTLSKKEKEEAVRRANALEKDDLYSLRKVSRQEYLKKREQKKLDELRDEIEDEQYLFGGEKLTETELREFRYKKELYDLVKKRTQDEDNVEEYRIPDAYDQEGGVDQEKRFSVAVQRYRDLDSTEKMNPFAEQEAWEDHQIGKATLKFGAKNKQASDDYQFVFEDQINFIKESVMAGENYEDAMDAKQKSQDLAEKTALEELQEVRRSLPIYTYRDQLLKAVEEHQVLVIVGDTGSGKTTQIPQYLHEAGYTKRGKVGCTQPRRVAAMSVAARVAQEMGVKLGHEVGYSIRFEDCTSDKTVLKYMTDGMLLRELLGEPDLASYSVVIVDEAHERTLSTDILFGLVKDIARFRPDLKLLISSATMDAEKFSDYFDTAPIFSFPGRRYPVEINYTSAPEADYMDAAIVTILTIHVREPLGDILVFFTGQEEIETAEEILKHRIRGLGTKIRELIICPIYANLPSELQAKIFEPTPEGARKVVLATNIAETSLTIDGIKYVVDPGFSKMKSYNPRTGMESLLITPISKASATQRAGRAGRTSPGKCYRLYTAFNYNNDLEENTVPEVQRTNLASVVLALKSLGIHDLINFDFMDPPPAEALVKSLELLFALGALNKLGELTKAGRRMAEFPLDPMLSKMIVVSDKYKCSDEIISIAAMLSIGGSIFYRPKDKQVHADNARMNFHTGNVGDHIALLKVYSSWKETNFSTQWCYENYIQVRSMKRARDIRDQLEGLLERVEIDISSNLNELDSVRKSIVAGFFPHTAKLQKNGSYRTVKHPQTVHIHPNSGLSQVLPRWVVYHELVLTSKEYMRQVTELKPEWLIELAPHYYQLKDVEDAASKKMPKGAGKAAM
Protein: Nuclear pore complex protein Nup107 (107 kDa nucleoporin) (Nucleoporin Nup107) (P57740)
Organism: Homo sapiens (Human)
Function: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. Required for the assembly of peripheral proteins into the NPC. May anchor NUP62 to the NPC. Involved in nephrogenesis.
Subcellular location: Nucleus membrane {ECO:0000269|PubMed:11564755, ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:26411495}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:11564755, ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:26411495}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:11564755}. Note=Located on both the cytoplasmic and nuclear sides of the NPC core structure (PubMed:11564755). During mitosis, localizes to the kinetochores (PubMed:11564755). Dissociates from the dissasembled NPC structure late during prophase of mitosis (PubMed:11564755). {ECO:0000269|PubMed:11564755}.
Interaction partners:
- Nuclear pore complex protein Nup214
- Nucleoporin SEH1
- Nuclear pore complex protein Nup155
- Nuclear pore complex protein Nup205
- Nucleoporin Nup37
- Nuclear pore complex protein Nup93
- Nuclear pore complex protein Nup160
- Nuclear pore complex protein Nup85
- Protein SEC13 homolog
- Nuclear pore complex protein Nup133
Sequence:
MDRSGFGEISSPVIREAEVTRTARKQSAQKRVLLQASQDENFGNTTPRNQVIPRTPSSFRQPFTPTSRSLLRQPDISCILGTGGKSPRLTQSSGFFGNLSMVTNLDDSNWAAAFSSQRSGLFTNTEPHSITEDVTISAVMLREDDPGEAASMSMFSDFLQSFLKHSSSTVFDLVEEYENICGSQVNILSKIVSRATPGLQKFSKTASMLWLLQQEMVTWRLLASLYRDRIQSALEEESVFAVTAVNASEKTVVEALFQRDSLVRQSQLVVDWLESIAKDEIGEFSDNIEFYAKSVYWENTLHTLKQRQLTSYVGSVRPLVTELDPDAPIRQKMPLDDLDREDEVRLLKYLFTLIRAGMTEEAQRLCKRCGQAWRAATLEGWKLYHDPNVNGGTELEPVEGNPYRRIWKISCWRMAEDELFNRYERAIYAALSGNLKQLLPVCDTWEDTVWAYFRVMVDSLVEQEIQTSVATLDETEELPREYLGANWTLEKVFEELQATDKKRVLEENQEHYHIVQKFLILGDIDGLMDEFSKWLSKSRNNLPGHLLRFMTHLILFFRTLGLQTKEEVSIEVLKTYIQLLIREKHTNLIAFYTCHLPQDLAVAQYALFLESVTEFEQRHHCLELAKEADLDVATITKTVVENIRKKDNGEFSHHDLAPALDTGTTEEDRLKIDVIDWLVFDPAQRAEALKQGNAIMRKFLASKKHEAAKEVFVKIPQDSIAEIYNQCEEQGMESPLPAEDDNAIREHLCIRAYLEAHETFNEWFKHMNSVPQKPALIPQPTFTEKVAHEHKEKKYEMDFGIWKGHLDALTADVKEKMYNVLLFVDGGWMVDVREDAKEDHERTHQMVLLRKLCLPMLCFLLHTILHSTGQYQECLQLADMVSSERHKLYLVFSKEELRKLLQKLRESSLMLLDQGLDPLGYEIQL
Protein: Ras-related protein Rab-41 (Q5JT25)
Organism: Homo sapiens (Human)
Function: Required for normal Golgi ribbon organization and ER-to-Golgi trafficking.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23936529}. Note=punctate localization concentrated in ruffled regions at the cell periphery.
Interaction partners:
- Vam6/Vps39-like protein
Sequence:
MSAFGHDEAWMEAGGFGLEAAERTEYQSLCKSKLLFLGEQSVGKTSIISRFMYNSFGCACQATVGIDFLSKTMYLEDQIVQLQLWDTAGQERFHSLIPSYIRDSTIAVVVYDITNINSFKETDKWVEHVRAERGDDVVIMLLGNKIDLDNKRQVTAEQGEEKSRNLNVMFIETSAKTGYNVKKLFRRVASALLSTRTSPPPKEGTVEIELESFEESGNRSYC
Protein: Uncharacterized ABC transporter ATP-binding protein Rv2326c (P9WQI7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein Rv2325c
- Conserved protein
- Possible conserved membrane protein
- O-acyltransferase WSD1 C-terminal domain-containing protein
- Oligopeptide transport system permease protein OppC
- Phosphate acetyltransferase
- Probable periplasmic dipeptide-binding lipoprotein DppA
Sequence:
MCCAVCGPEPGRIGEVTPLGPCPAQHRGGPLRPSELAQASVMAALCAVTAIISVVVPFAAGLALLGTVPTGLLAYRYRLRVLAAATVAAGMIAFLIAGLGGFMGVVHSAYIGGLTGIVKRRGRGTPTVVVSSLIGGFVFGAAMVGMLAAMVRLRHLIFKVMTANVDGIAATLARMHMQGAAADVKRYFAEGLQYWPWVLLGYFNIGIMIVSLIGWWALSRLLERMRGIPDVHKLDPPPGDDVDALIGPVPVRLDKVRFRYPRAGQDALREVSLDVRAGEHLAIIGANGSGKTTLMLILAGRAPTSGTVDRPGTVGLGKLGGTAVVLQHPESQVLGTRVADDVVWGLPLGTTADVGRLLSEVGLEALAERDTGSLSGGELQRLALAAALAREPAMLIADEVTTMVDQQGRDALLAVLSGLTQRHRTALVHITHYDNEADSADRTLSLSDSPDNTDMVHTAAMPAPVIGVDQPQHAPALELVGVGHEYASGTPWAKTALRDINFVVEQGDGVLIHGGNGSGKSTLAWIMAGLTIPTTGACLLDGRPTHEQVGAVALSFQAARLQLMRSRVDLEVASAAGFSASEQDRVAAALTVVGLDPALGARRIDQLSGGQMRRVVLAGLLARAPRALILDEPLAGLDAASQRGLLRLLEDLRRARGLTVVVVSHDFAGMEELCPRTLHLRDGVLESAAASEAGGMS
Protein: Histone H3.3 type 2 (Q9U281)
Organism: Caenorhabditis elegans
Function: Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus {ECO:0000269|PubMed:16846252}. Chromosome {ECO:0000269|PubMed:16846252}. Note=Depleted from the meiotically silenced X chromosome.
Interaction partners:
Sequence:
MARTKQTARKSTGGKAPRKQLATKAARKSAPTTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDMQLARRIRGERA
Protein: RE14391p (Secretory 63) (Q9VS57)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
- Translocation protein SEC62
- DSec61alpha
- Protein transport protein Sec61 subunit beta
- Protein transport protein Sec61 gamma-2 subunit
- Endoplasmic reticulum chaperone BiP
- Protein transport protein Sec61 subunit gamma
- Protein transport protein Sec61 gamma-1 subunit
- STE20-related kinase adapter protein stlk
- non-specific serine/threonine protein kinase
- Hypoxia up-regulated protein 1
Sequence:
MAGQKFQYDESGGTFYYFVLSFLALILIPTTIYYWPRKKKQDNSKLKEECQCADCQKKKTILANAEPYRALTSWTIKLTIVLGWALLLFLTYRVSQFDYEMASFDPFEILNVPPTSSQAEIKKAYYRLSKVLHPDKETGDEKSFMMLSKAYQALTDDVAKENYEKYGNPDGPGAMSFGIALPSWIVEKENSVWVLGLYGLVFMVAMPSAVGVWWYRSIRFSGDKVLLDTTQMYFYFIHKTPHMLLKRALMVLAASLEFDKRHNSQVQERQSDNDEVPALIRQLPNLNEKCKEHPLCRMYSIKARAILHAHLSRMPLNPETLERDRQFVVKKCPYLVQEMVSCVHQLVMMAYARRVPRLPSIETIENCMKMSPMIIQGLWEFKSPLLQLPHLTEDHLYFMNKKRHVKNLQQFAQLKPEESRQLLKNLSDFEYENTMKVLGKMPLIDFSIRCEVIDDENTNVVTAGAIVTVTVTLERKDMKTLFGDTKAPEKQGIKDETNEEAAGDEDEAAAAAPVKKASAWAKPRKGGKGKGGKKPAQNQKNQKKVPAKAATTATITASEDQAAAGNSDAESEAGNADGSDVESAAGSGSEDEEKGKNNSSLDDDDDEEWERLQAKLNKRERLEGKSRLSHTVHCPYFPEEKQEYWWTYICDRKSRTLLTAPYHVTNLVEKEEIQLKFTAPRWPGVYTFTVCLRSDSYLGMDQQQELKLDVQKAPAPPTDHPQWDLSESEPEHTDQQENLSDYTTDTSDEEDGE
Protein: Phospholipase A2-beta (EC 3.1.1.4) (Secretory phospholipase A2-beta) (AtsPLA2-beta) (Q8GZB4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Releases lysophospholipids (LPLs) and free fatty acids (FFAs) from membrane phospholipids in response to hormones and other external stimuli. Regulates the process of cell elongation and plays important roles in shoot gravitropism by mediating auxin-induced cell elongation. Involved in stomatal opening in response to light. Plays a role in pollen development and germination and tube growth.
Subcellular location: Secreted. Endoplasmic reticulum.
Interaction partners:
- RING-type E3 ubiquitin transferase
- Patatin-like protein 5
- Myosin-7
- At4g29070
- Phospholipase A I
- Patatin-like protein 7
- AT3g18860/MCB22_3
- Protein HOMOLOG OF MAMMALIAN LYST-INTERACTING PROTEIN 5
Sequence:
MMFRTSLMRFAAAFFAIVFVVLVGVARSEECTRTCIAQNCDTLSIRYGKYCGIGHSGCPGEEPCDDLDACCKIHDHCVELNGMTNISCHKKFQRCVNRLSKAIKQSKNKKVGFSTKCPYSVVIPTVNQGMDIGILFSQLGNDMKTEL
Protein: Rubredoxin (Rdxs) (P42453)
Organism: Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Function: Involved in the hydrocarbon hydroxylating system, which transfers electrons from NADH to rubredoxin reductase and then through rubredoxin to alkane 1 monooxygenase.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Rubredoxin-NAD
- Alkane 1-monooxygenase
- Putative flavohemoprotein
- EstB protein
- HTH-type transcriptional regulator EstR
- Siroheme synthase
Sequence:
MKKYQCIVCGWIYDEAEGWPQDGIAPGTKWEDIPDDWTCPDCGVSKVDFEMIEV
Protein: Actin, gamma (EC 3.6.4.-) (P20359)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Actin-related protein 4
- Nuclear actin-related protein
- Arp3 homolog
- Calmodulin
- Fimbrin
- Arp2 homolog
- Profilin
- Actin associated protein Wsp1
- Myosin II homolog
- Dynamitin homolog
Sequence:
MEEEVAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHHGIMIGMGQKDSYVGDEAQSKRGILTLRYPIEHGVVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPINPKSNREKMTQIVFETFNAPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYEGFALPHAISRVDMAGRDLTDYLMKILAERGYTFSTTAEREIVRDIKEKLCYVALDFEQEIQTASQSSSLEKSYELPDGQVITIGNERFRAPEALFQPSVLGLESGGIHVTTFNSIMKCDVDVRKDLYGNIVMSGGTTMYPGISDRMQKEITALAPSSMKVKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
Protein: Phosphoribosylaminoimidazole-succinocarboxamide synthase (EC 6.3.2.6) (SAICAR synthetase) (P27616)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the reaction of 4-carboxy-5-aminoimidazole ribotide (CAIR) and aspartic acid with the formation of N-succinyl-5-amino-imidazole-4-carboxamide ribotide (SAICAR) in the purine biosynthesis pathway.
Interaction partners:
- Bifunctional purine biosynthetic protein ADE5,7
- Adenylosuccinate lyase
- Phosphoribosylaminoimidazole carboxylase
- Bifunctional purine biosynthesis protein ADE17
- Phosphoribosylformylglycinamidine synthase
- Amidophosphoribosyltransferase
- Phosphoribosylglycinamide formyltransferase
- C-1-tetrahydrofolate synthase, cytoplasmic
- Eukaryotic peptide chain release factor GTP-binding subunit
- Orotidine 5'-phosphate decarboxylase
Sequence:
MSITKTELDGILPLVARGKVRDIYEVDAGTLLFVATDRISAYDVIMENSIPEKGILLTKLSEFWFKFLSNDVRNHLVDIAPGKTIFDYLPAKLSEPKYKTQLEDRSLLVHKHKLIPLEVIVRGYITGSAWKEYVKTGTVHGLKQPQGLKESQEFPEPIFTPSTKAEQGEHDENISPAQAAELVGEDLSRRVAELAVKLYSKCKDYAKEKGIIIADTKFEFGIDEKTNEIILVDEVLTPDSSRFWNGASYKVGESQDSYDKQFLRDWLTANKLNGVNGVKMPQDIVDRTRAKYIEAYETLTGSKWSH
Protein: Uncharacterized TPR repeat-containing protein At2g32450 (Q8S8L9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MTTRGSRSEKVKRIFQQFDGNLDGGLSREEMSALVVAVNPRVKFSDEQISAILDEVFRTYAEFIDGDKGLTFDGLLRTYDDGAGDVDRDFDALGIEFNEETKGASEASSSSITDERAVEAQKQQRTAAWAVSPNHGIVFDETWKLVDDLEILVKRLKSKQEKDGKLKVDNNNVDAFSEAGWSRELGPSSDISDKRIYWEESSHDYGVFVKELGVLRSKADGARSREEAFDGHMAIGKVLYEHQLFKEALVSFKRACELQPTDVRPHFKAGNCLYVLGKYKESKDEFLLALEAAESGGNQWAYLLPQIYVNLGISLEGEGMVLSACEYYREAAILCPTHYRALKLLGSALFGVGEYRAAVKALEEAIYLKPDYADAHCDLASSLHAMGEDERAIEVFQRAIDLKPGHVDALYNLGGLYMDLGRFQRASEMYTRVLAVWPNHWRAQLNKAVSLLGAGETEEAKRALKEALKMTNRVELHDAVSHLKQLQKKKKVKKGNSANEEGPFIVVESSKFKTVGEKTTLRPDLAIALQVRAFQRVTRLWKCDVEALRREMRDNNVPVSYSGNGIPTKSIRRPNLEEILRRLLNVLKPETFQGAIKAINEKILSVLDDSGSGRVDLGMFYAVIAPLCGGHPDKRKRVAFDALLWKPVNEGSSQITKMEAVKYIKLLRAIYIPSQGMSEMLEVHGESDDTSTVTFNQFLEMYDDSEWGFGIMSTVFKLETRDRNRHGNQVCSVCRYPIIGSRFKEVKTGFSLCNQCYSEGKIPPTFKQQEEYKFREYASEVEAMKAKCVCFSMQSHKKTIAT
Protein: Mitochondrial ribonuclease P catalytic subunit (EC 3.1.26.5) (Mitochondrial ribonuclease P protein 3) (Mitochondrial RNase P protein 3) (Protein only RNase P catalytic subunit) (O15091)
Organism: Homo sapiens (Human)
Function: Catalytic ribonuclease component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3, which cleaves tRNA molecules in their 5'-ends. The presence of TRMT10C/MRPP1, HSD17B10/MRPP2 is required to catalyze tRNA molecules in their 5'-ends.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:18984158}.
Interaction partners:
- 3-hydroxyacyl-CoA dehydrogenase type-2
- tRNA methyltransferase 10 homolog C
- Ribonuclease P/MRP protein subunit POP5
- Ribonuclease P protein subunit p29
- Ribonuclease P protein subunit p20
- Ribonucleases P/MRP protein subunit POP1
- Ribonuclease P protein subunit p30
- Ribonuclease P protein subunit p38
- Ribonuclease P protein subunit p21
- Ribonuclease P protein subunit p25
Sequence:
MTFYLFGIRSFPKLWKSPYLGLGPGHSYVSLFLADRCGIRNQQRLFSLKTMSPQNTKATNLIAKARYLRKDEGSNKQVYSVPHFFLAGAAKERSQMNSQTEDHALAPVRNTIQLPTQPLNSEEWDKLKEDLKENTGKTSFESWIISQMAGCHSSIDVAKSLLAWVAAKNNGIVSYDLLVKYLYLCVFHMQTSEVIDVFEIMKARYKTLEPRGYSLLIRGLIHSDRWREALLLLEDIKKVITPSKKNYNDCIQGALLHQDVNTAWNLYQELLGHDIVPMLETLKAFFDFGKDIKDDNYSNKLLDILSYLRNNQLYPGESFAHSIKTWFESVPGKQWKGQFTTVRKSGQCSGCGKTIESIQLSPEEYECLKGKIMRDVIDGGDQYRKTTPQELKRFENFIKSRPPFDVVIDGLNVAKMFPKVRESQLLLNVVSQLAKRNLRLLVLGRKHMLRRSSQWSRDEMEEVQKQASCFFADDISEDDPFLLYATLHSGNHCRFITRDLMRDHKACLPDAKTQRLFFKWQQGHQLAIVNRFPGSKLTFQRILSYDTVVQTTGDSWHIPYDEDLVERCSCEVPTKWLCLHQKT
Protein: Expansin (Q283Q7)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Secreted, cell wall {ECO:0000256|RuleBase:RU365023}. Membrane {ECO:0000256|RuleBase:RU365023}; Peripheral membrane protein {ECO:0000256|RuleBase:RU365023}.
Interaction partners:
Sequence:
MATKTMMLQIFPLFFFLFSVCNSIFLGANGDDNGGWQTAHATFYGGADATGTMGGACGYGNLYSQGYGTSTAALSTALFNNGLSCGACYELRCNNDPQWCISRTITVTATNFCPPNYALSSDNGGWCNPPREHFDLAEPAFLRIAEYRAGIVPVMFRRVSCVKKGGIRYTMNGHSYFNMVLITNVGGAGDITSVSIKGSRTGWLPMSRNWGQNWQSNAYLNGQSLSFKVTASDGRTITAYNVVPAGWQFGQTFEGGQF
Protein: Activin receptor type-1 (EC 2.7.11.30) (Activin receptor type I) (ACTR-I) (Serine/threonine-protein kinase receptor R1) (SKR1) (TGF-B superfamily receptor type I) (TSR-I) (P80201)
Organism: Rattus norvegicus (Rat)
Function: Bone morphogenetic protein (BMP) type I receptor that is involved in a wide variety of biological processes, including bone, heart, cartilage, nervous, and reproductive system development and regulation. As a type I receptor, forms heterotetrameric receptor complexes with the type II receptors AMHR2, ACVR2A ors ACVR2B. Upon binding of ligands such as BMP7 or GDF2/BMP9 to the heteromeric complexes, type II receptors transphosphorylate ACVR1 intracellular domain. In turn, ACVR1 kinase domain is activated and subsequently phosphorylates SMAD1/5/8 proteins that transduce the signal. In addition to its role in mediating BMP pathway-specific signaling, suppresses TGFbeta/activin pathway signaling by interfering with the binding of activin to its type II receptor (By similarity). Besides canonical SMAD signaling, can activate non-canonical pathways such as p38 mitogen-activated protein kinases/MAPKs (By similarity).
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Bone morphogenetic protein receptor type-2
- Bone morphogenetic protein 7
- Bone morphogenetic protein 4
- Bone morphogenetic protein 6
- Activin receptor type-2A
- Bone morphogenetic protein receptor type-1A
- Serine/threonine-protein kinase receptor
- Mothers against decapentaplegic homolog 5
- Mothers against decapentaplegic homolog 1
- Activin receptor type-2B
Sequence:
MVDGAMILSVLMMMALPSPSMEDEEPKVNPKLYMCVCEGLSCGNEDHCEGQQCFSSLSVNDGFRVYQKGCFQVYEQGKMTCKTPPSPGQAVECCQGDWCNRNVTARLPTKGKSFPGSQNFHLEVGLIILSVVFAVCLFACILGVALRKFKRRNQERLNPRDVEYGTIEGLITTNVGDSTLAELLDHSCTSGSGSGLPFLVQRTVARQITLLECVGKGRYGEVWRGSWQGENVAVKIFSSRDEKSWFRETELYNTVMLRHENILGFIASDMTSRHSSTQLWLITHYHEMGSLYDYLQLTTLDTVSCLRIVLSIASGLAHLHIEIFGTQGKSAIAHRDLKSKNILVKKNGQCCIADLGLAVMHSQSTNQLDVGNNPRVGTKRYMAPEVLDETIQVDCFDSYKRVDIWAFGLVLWEVARRMVSNGIVEDYKPPFYDVVPNDPSFEDMRKVVCVDQQRPNIPNRWFSDPTLTSLAKLMKECWYQNPSARLTALRIKKTLTKIDNSLDKLKTDC
Protein: Somatostatin receptor type 1 (SS-1-R) (SS1-R) (SS1R) (SRIF-2) (P30873)
Organism: Mus musculus (Mouse)
Function: Receptor for somatostatin with higher affinity for somatostatin-14 than -28. This receptor is coupled via pertussis toxin sensitive G proteins to inhibition of adenylyl cyclase. In addition it stimulates phosphotyrosine phosphatase and Na(+)/H(+) exchanger via pertussis toxin insensitive G proteins.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Somatostatin
- Cortistatin
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Pro-neuropeptide Y
- Appetite-regulating hormone
- Neuropeptide Y receptor type 5
- Oxytocin-neurophysin 1
- Pro-opiomelanocortin
Sequence:
MFPNGTASSPSSSPSPSPGSCGEGACSRGPGSGAADGMEEPGRNASQNGTLSEGQGSAILISFIYSVVCLVGLCGNSMVIYVILRYAKMKTATNIYILNLAIADELLMLSVPFLVTSTLLRHWPFGALLCRLVLSVDAVNMFTSIYCLTVLSVDRYVAVVHPIKAARYRRPTVAKVVNLGVWVLSLLVILPIVVFSRTAANSDGTVACNMLMPEPAQRWLVGFVLYTFLMGFLLPVGAICLCYVLIIAKMRMVALKAGWQQRKRSERKITLMVMMVVMVFVICWMPFYVVQLVNVFAEQDDATVSQLSVILGYANSCANPILYGFLSDNFKRSFQRILCLSWMDNAAEEPVDYYATALKSRAYSVEDFQPENLESGGVFRNGTCASRISTL
Protein: CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial (EC 2.7.8.5) (Phosphatidylglycerophosphate synthase 1) (PGP synthase 1) (Silencer-associated factor) (Q8BHF7)
Organism: Mus musculus (Mouse)
Function: Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Cardiolipin synthase
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Phosphatidate cytidylyltransferase 1
- Phosphatidate cytidylyltransferase 2
- Phosphatidate cytidylyltransferase, mitochondrial
- Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1
Sequence:
MAAPAAGPVFWRRLLGLLPGRPGLAALLGRLSDRLGRSRERRRRRSPWLLLAPLLSPTVPQVTSPPCCLCPEGVHRFQWIRNLVPEFGVSSSHVRVLSSPAEFFELMKGQIKIAKRRVVMASLYLGTGPLEQELVDCLESSLEKSLQAKFPSDLKVSILLDFTRGSRGRKNSRTMLLPLLQRFPERVRVSLFHTPNLRGLLRLLIPERFNETIGLQHIKVYLFDNNVILSGANLSDSYFTNRQDRYVFLQDCAEIADFFTELVDAVGDVSLQLQGDDTVEVVDGMVHPYKGDRAAYCRAANKRVMDVIHSARARQQMLHAQTFHSDSLLSQEEAAAAGDRRPAPDTWIYPLIQMKPFEIQIDEIVTETLLTEAERGAKVFLTTGYFNLTQAYMDLVLGTRAEYQILLASPEVNGFFGAKGVAGAIPAAYVHIERQFYSEVCSLGQQDRVQLQEYWRRGWTFHAKGLWLYLAGSSLPCLTLIGSPNFGYRSVHRDLEAQIAIVTESRSLQQQLHQEQEQLYLRSGVVTSATFEQPGRQVKLWVKMVTPLIKNFF
Protein: Alpha-mannosidase (EC 3.2.1.-) (Q8MSX9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSFKLFRRGSARCIGLLSAFVTILLCLYYISIGQPNPTPISETGAPSAALRGSPLSGLTGFSVDGGSSSIIHQQKQQLVIASNQKKSSETKSAQTSVSPEEQSEEQYTNSNWGDKCYELIQSNTNITASEEHSKFDFQPEWMRSKEYWDRGFEERFDAQKKDKQRPPLKIIVVPHSHNDPGWLKTFTNYFQSDSRQILNLLVTKMQEYTDMTFIWSEISFLQLWWDQAHPTKQRALKRLIDAGRIEITTGGWVMTDEANVHIYPMLDQLIEGHQWLKNNLNVTPKVGWSIDPFGHGSTVPYLLSGANFEGTIIQRIHYAWKQWFARQQSGDFIWKPYWRSRKDKDSEAGSLLTHNMPFDIYSIKGSCGPHPFICLNFDFRKIPGEYTEYSVKAQFITDDNLESKAQLLLEQYARTASLFPHNVALIPVGDDFRYNKDREVDQQYQNYKKLIDHIMANRRLYNADIRFGTPSDYFEAIKERMKDHTPGFPTFKGDFFVYSDIFSEGRPAYWSGYFTTRPFYKLLSSELEHQLRSAEIVFTLAYNTARQAKRENAIKIYEKNYELIINARRNLGLFQHHDAITGTSKAAVMRDYAMRLFESTQNMVKMQESCLELLLQKGQPRHHGFLLSEFERDNFNKLPRKMPIQMANGDESTPTVPAGEGGAGGSSSSGSVGSFVLYNSLAQKRLEVVTLRVQHPNVKIVNDKGVELNHIQINPVWNITDTYEQGLGTSVSGTVGRIRTSTRQFEVMFVAELEPLSLSTYRVQVDEVNFKRNIATIYCDDCTESQPASVSPPEEIESSPTSVFEARGKPAGDIQLENPHMRLLFDEKSGFLKTITRKNQKKELLKPLQCNIKFAAYRSAQFHSGAYLFKTDPEQSEAEKEVLEGYTDMRIIITSGPIASDVTVIYGPFLAHTVRIFNTRTHLDAAIYVENDIDF
Protein: Valosin-containing protein homolog (O44008)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MSAKAQQVKQQKLNRLIADDLAEDDNSVVVLNAKRMDELSIFRGDTVKLKGKKNRSTICIAMSDENCPEGSIMVNKVTRRNIRILLGDLITVSSHSNVPYGNHVHVLPIDDTVKNLTGDLFETFLKPYFLEAYRPVKTGDLFICRGAMRSVEFKVVEVDPGDCCIVAPETVVHCEGDPIRREDEERLDDVGYDDIGGCRRQLVQIREMVELPIRHPELFKSIGIKPPRGILMYGPPGSGKTLIARAVANETGAFFFLINGPEIMSKMAGESEGNLRNAFVESEKNAPAIIFIDEIDSIAPKREKAQGEVEKRIVSQLLTLMDGLKGRSQVIVMAATNRPNAIDPALRRFGRFDREIDIGVPDEIGRLEILRIHTKNMKLDPNVDVEKIAKDSHGYVGADLAQLCTEAAMQCVREKMAVVDWDDETIDAEVLDSMSVTNNHFLDALSKMNPSALRETQVETPNVTWSDVGGLLDVKRELQELVQYPVEFPWKFEKYGISAPKGVLFYGPPGCGKTLLAKAIATECQANFISIKGPELLTMWFGESEANVRDVFDKARAAAPCVLFFDELDSVARSRGHSGDGGASDRVINQILTEMDGMNSKKNVFIIGATNRPDVLDPAVMRPGRLDQLIYIPLPDKASRVAILKASFRKSPLAPDVDLDQLAAATHGFSGADLAGICQRACKLAIRESIAKEIQLEEARANGVLNEDQDIDPVPQITRLHVEEAMRGARRSVSDADIRKYELFATSLQQSRAFGNVSLDPGNQGGAGGDAGAGDDDLYS
Protein: Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, peroxisomal (AtDCI1) (EC 5.3.3.21) (Q9FHR8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Converts 3,5-dienoyl-CoAs to the corresponding 2,4-dienoyl-CoAs. Involved in degradation of unsaturated fatty acids.
Subcellular location: Peroxisome {ECO:0000269|PubMed:16040662}.
Interaction partners:
- Peroxisome biogenesis protein 5
- Peroxisome biogenesis factor 10
- Peroxisome biogenesis protein 12
- Alpha/beta-Hydrolases superfamily protein
- Peroxisomal membrane protein PEX14
- Glycerol-3-phosphate dehydrogenase [NAD
- Enoyl-CoA hydratase 2, peroxisomal
- Sterol carrier protein 2
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component 4 of pyruvate dehydrogenase complex, chloroplastic
Sequence:
MTMESYKTLEIIRKNTDSSVFHLIINRPSHLNALSLDFFIEFPKALSSLDQNPDVSVIILSGAGKHFCSGIDLNSLSSISTQSSSGNDRGRSSEQLRRKIKSMQAAITAIEQCRKPVIAAIHGACIGGGVDLITACDIRYCSEDAFFSIKEVDLAIVADLGTLQRLPSIVGYANAMELALTARRFSGSEAKDLGLVSKVFGSKSELDNGVTTIAEGIGGKSPLAVTGTKAVLLRSREVSVEQGLDYVATWNSAMLISDDLNEAVSAQMMKRKPRFAKL
Protein: Sorting nexin-24 (Q9CRB0)
Organism: Mus musculus (Mouse)
Function: May be involved in several stages of intracellular trafficking.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
Sequence:
MEVYIPSFRHEDSDLERGYTVFKIEVLMNGRKHFVEKRYSEFHALHKKLKKCIKTPEIPSKHVRNWVPKVLEQRRQGLETYLQAVILENEELPKLFLDFLNVRHLPSLPKAESCGSFDETESEESSKLSHQPVLLFLGDPYVLPAASDFPNVVIEGVLHGIFFSHLQPR