wanglab/gogpt-training-data huggingface dataset:
Protein: Polypyrimidine tract-binding protein 1 (PTB) (Heterogeneous nuclear ribonucleoprotein I) (hnRNP I) (P17225)
Organism: Mus musculus (Mouse)
Function: Plays a role in pre-mRNA splicing and in the regulation of alternative splicing events. Activates exon skipping of its own pre-mRNA during muscle cell differentiation. Binds to the polypyrimidine tract of introns. May promote RNA looping when bound to two separate polypyrimidine tracts in the same pre-mRNA. May promote the binding of U2 snRNP to pre-mRNA. Cooperates with RAVER1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA. Represses the splicing of MAPT/Tau exon 10. Binds to polypyrimidine-rich controlling element (PCE) of CFTR and promotes exon skipping of CFTR exon 9, thereby antagonizing TIA1 and its role in exon inclusion of CFTR exon 9. Plays a role in the splicing of pyruvate kinase PKM by binding repressively to a polypyrimidine tract flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform.
Subcellular location: Nucleus.
Interaction partners:
- Heterogeneous nuclear ribonucleoprotein K
- Heterogeneous nuclear ribonucleoprotein A1
- Heterogeneous nuclear ribonucleoprotein L
- Heterogeneous nuclear ribonucleoproteins C1/C2
- Heterogeneous nuclear ribonucleoproteins A2/B1
- Serine/arginine-rich splicing factor 1
- TAR DNA-binding protein 43
- Splicing factor U2AF 65 kDa subunit
- Heterogeneous nuclear ribonucleoprotein M
- Heterogeneous nuclear ribonucleoprotein H
Sequence:
MDGIVPDIAVGTKRGSDELFSTCVSNGPFIMSSSASAANGNDSKKFKGDNRSAGVPSRVIHVRKLPSDVTEGEVISLGLPFGKVTNLLMLKGKNQAFIEMNTEEAANTMVNYYTSVAPVLRGQPIYIQFSNHKELKTDSSPNQARAQAALQAVNSVQSGNLALAASAAAVDAGMAMAGQSPVLRIIVENLFYPVTLDVLHQIFSKFGTVLKIITFTKNNQFQALLQYADPVSAQHAKLSLDGQNIYNACCTLRIDFSKLTSLNVKYNNDKSRDYTRPDLPSGDSQPSLDQTMAAAFGAPGIMSASPYAGAGFPPTFAIPQAAGLSVPNVHGALAPLAIPSAAAAAAASRIAIPGLAGAGNSVLLVSNLNPERVTPQSLFILFGVYGDVQRVKILFNKKENALVQMADGSQAQLAMSHLNGHKLHGKSVRITLSKHQSVQLPREGQEDQGLTKDYGSSPLHRFKKPGSKNFQNIFPPSATLHLSNIPPSVSEDDLKSLFSSNGGVVKGFKFFQKDRKMALIQMGSVEEAVQALIELHNHDLGENHHLRVSFSKSTI
Protein: DNA repair endonuclease (Q9I7N6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGVTGLWKLIEPCGKPVPVETLEGKILAVDISIWLHQVVKGFQDNKGSALSNAHLLGLFHRLCKLLYYRVRPVFIFDGCVPQLKRDTIARRQQQRNKLSNEADRIQALLLQSLAKEKVVQQALGKNAELLLKSPVKRPPPAKKNDEDDLFKLPELPAASVQDNQDESEQDTSASASDSSFDESTARHSYNSSLQAIDVKSQHFRNLPADVRHEILTDIKETRKQSSWGRLHELPARSDDFCSFQMKRLLKRRAVQESLEQAEQEMGGHTLTYAELCDFFNEEGILTPTAIEQCTRQISSDEHTRFLLVRDLKKKAMESTKQEVKMEMIEEVPAEEEDEKPSTSTKKEAVKSVDLGTEFDEDLAKALSMSMEETKVYDEKDYEYDSDQELRLNRAQTKQLRHAAKGPARAYMIEYGGMNDEEVGNIMEATQFNDTQSLEKLLEITTVPTDMADNSIEEAKLISQAIEESKQLSQAIEESKNNLNEDKVEIVDTDTDSDLEEVMEVQELDKGKKNLEICVDITGQADSNDLFADIFEDGEANKIEKTISVEEDNDFIEVKGSEELKLDTEDENKPITNKSIKESNEVKPFIDEIIEVKDSQEAVPAEPNLKPDLDSILNDLKKQTAAVKDIQLNVNEEEKPKPKVEISSILDELKVKMADVKNITLDNVKLSNNAPIILSSDDESALKSSKIVPKQELIELCDSDDNKNNRLSPNKTPSKNKSIKDFFETSYVVKRTPDKSQASNETSPGTPKTPKPFFRKRTPKSGRKRASDANEDSDEEVSPTKRSSKASKSLFEPKEPEEEKTVDPEELIKDAAEALKSQKTSGELQEMATNLAQERKELEIERNRQDRMGMSISQRMSIDCQELLRLFGIPYIVAPMEAEAQCAFLNATDLTHGTITDDSDIWLFGGRTVYKNFFAQNKHVMEFRAEQIEQTFNCNRGKLIQLACLVGSDYTTGIHGIGAVTALEILASFSGQDANGPGICNQSVLQTLIKFRDWWQAHKCSNLPPGSSARLALRKKLKNIELHEGFPSGAVVEAYLAPTIDDNRDAFSWGTPDVESIREFTRKSFGWTTSKTDDILMPVMKKINEKKIQGSIRNYFTAKSALRVQQPHVSKRVQLAIDKMSGKIDETPEKPKKVTRTRRAKAAPPTDDDLAIADVATKAARPKRGKRKAAPESVVLDGELPSTSQSIPKPEKCPRIPSSVEVIPQREKDLEQMRLNKAKAAEILKNSAKANRK
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q9VEX2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MYSTRQSVSTTTGVLMVGPNFRVGKKIGCGNFGELRLGKNLYNNEHVAIKMEPMKSKAPQLHLEYRFYKLLGSHAEGVPEVYYFGPCGKYNALVMELLGPSLEDLFDICGRRFTLKSVLLIAIQLLHRIEYVHSRHLIYRDVKPENFLIGRTSTKREKIIHIIDFGLAKEYIDLDTNRHIPYREHKSLTGTARYMSINTHMGREQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCDGHPEEFATYLRYVRRLDFFETPDYDFLRRLFQDLFDRKGYTDEGEFDWTGKTMSTPVGSLQTGHEVIISPNKDRHNVTAKTNAKGGVAAWPDVPKPGATLGNLTPADRHGSVQVVSSTNGELNPDDPTAGHSNTPITQQPEVEVVDETKCCCFFKRKKKKSTRQK
Protein: Chloride channel protein 1 (ClC-1) (Chloride channel protein, skeletal muscle) (P35523)
Organism: Homo sapiens (Human)
Function: Voltage-gated chloride channel. Plays an important role in membrane repolarization in skeletal muscle cells after muscle contraction. The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons (Probable). The absence of conserved gating glutamate residues is typical for family members that function as channels (Probable).
Subcellular location: Cell membrane {ECO:0000269|PubMed:12456816, ECO:0000269|PubMed:26502825, ECO:0000269|PubMed:8112288, ECO:0000269|PubMed:9122265}; Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q64347}; Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:Q64347}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sodium channel protein type 4 subunit alpha
- Muscleblind-like protein 1
- CUGBP Elav-like family member 1
- Muscleblind-like protein 2
- Muscleblind-like protein 3
- Myotonin-protein kinase
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
- CCHC-type zinc finger nucleic acid binding protein
- Protein cereblon
- Troponin T, fast skeletal muscle
Sequence:
MEQSRSQQRGGEQSWWGSDPQYQYMPFEHCTSYGLPSENGGLQHRLRKDAGPRHNVHPTQIYGHHKEQFSDREQDIGMPKKTGSSSTVDSKDEDHYSKCQDCIHRLGQVVRRKLGEDGIFLVLLGLLMALVSWSMDYVSAKSLQAYKWSYAQMQPSLPLQFLVWVTFPLVLILFSALFCHLISPQAVGSGIPEMKTILRGVVLKEYLTMKAFVAKVVALTAGLGSGIPVGKEGPFVHIASICAAVLSKFMSVFCGVYEQPYYYSDILTVGCAVGVGCCFGTPLGGVLFSIEVTSTYFAVRNYWRGFFAATFSAFVFRVLAVWNKDAVTITALFRTNFRMDFPFDLKELPAFAAIGICCGLLGAVFVYLHRQVMLGVRKHKALSQFLAKHRLLYPGIVTFVIASFTFPPGMGQFMAGELMPREAISTLFDNNTWVKHAGDPESLGQSAVWIHPRVNVVIIIFLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLVGEIMAMLFPDGILFDDIIYKILPGGYAVIGAAALTGAVSHTVSTAVICFELTGQIAHILPMMVAVILANMVAQSLQPSLYDSIIQVKKLPYLPDLGWNQLSKYTIFVEDIMVRDVKFVSASYTYGELRTLLQTTTVKTLPLVDSKDSMILLGSVERSELQALLQRHLCPERRLRAAQEMARKLSELPYDGKARLAGEGLPGAPPGRPESFAFVDEDEDEDLSGKSELPPSLALHPSTTAPLSPEEPNGPLPGHKQQPEAPEPAGQRPSIFQSLLHCLLGRARPTKKKTTQDSTDLVDNMSPEEIEAWEQEQLSQPVCFDSCCIDQSPFQLVEQTTLHKTHTLFSLLGLHLAYVTSMGKLRGVLALEELQKAIEGHTKSGVQLRPPLASFRNTTSTRKSTGAPPSSAENWNLPEDRPGATGTGDVIAASPETPVPSPSPEPPLSLAPGKVEGELEELELVESPGLEEELADILQGPSLRSTDEEDEDELIL
Protein: C-terminal binding protein 1 isoform C (X5D8Y5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGSSHLLNKGLPLGVRPPIMNGPLHPRPLVALLDGRDCTVEMPILKDVATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGVERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLKNCVNKDHLTAATHWASMDPAVVHPELNGAAYRYPPGVVGVAPTGIPAAVEGIVPSAMSLSHGLPPVAHPPHAPSPGQTVKPEADRDHASDQL
Protein: Syntaxin-binding protein 2 (Protein unc-18 homolog 2) (Unc18-2) (Protein unc-18 homolog B) (Unc-18B) (Q28288)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Involved in the protein trafficking from the Golgi apparatus to the plasma membrane.
Interaction partners:
- Syntaxin 11
- Syntaxin 19
- Amyloid beta precursor protein binding family A member 1.
- Unc-13 homolog D.
- Syntaxin 3
- Syntaxin 4
- Syntaxin 2
- Amyloid beta precursor protein binding family A member 2.
- Syntaxin 5
- V-SNARE coiled-coil homology domain-containing protein.
Sequence:
MAPSGLKEVVGEKILNGVIRSVKKDGEWKVLIMDHPSMRILSSCCKMSDILAEGITIVEDINKRREPIPSLEAIYLLSPTEKSVQALIADFRGTPTFTYKAAHIFFTDTCPEPLFTELSRSRLAKVVKTLKEIHLAFLPYEAQVFSLDAPHSTYNLYCPFRVGERARQIEALAQQIATLCATLQEYPAIRYRKGPEVTAQLANAVLAKLNAFKADNPSLGEGPEKTRSQLLIVDRGADPVSPLLHELTFQAMAYDLLNIEQDTYRYETTGLSEAREKAVLLDEDDDLWVELRHMHIADVSKKVTELLKTFCESKRLTTDKANIKDLSHILKKMPQYQKELNKYSTHLHLADDCMKHFKGSVEKLCGVEQDLAMGSDTEGEKIKDAMKLIVPVLLDAAVPAYDKIRVLLLYILLRNGVSEENLAKLIQHANVQAHSSLIRNLEQLGGTVTNPGGPGTSSRLERRERLEPTYQLSRWTPVIKDVMEDAVEDRLDRKLWPFVSDPAPTSSSQAAVSARFGHWHKNKAGVEMRAGPRLIIYVMGGVAMSEMRAAYEVTRATDGKWEVLIGSSHILTPTRFLDDLKTLDQKLEDIALP
Protein: Stomatin-like protein 2, mitochondrial (SLP-2) (mslp2) (Q99JB2)
Organism: Mus musculus (Mouse)
Function: Mitochondrial protein that probably regulates the biogenesis and the activity of mitochondria. Stimulates cardiolipin biosynthesis, binds cardiolipin-enriched membranes where it recruits and stabilizes some proteins including prohibitin and may therefore act in the organization of functional microdomains in mitochondrial membranes. Through regulation of the mitochondrial function may play a role into several biological processes including cell migration, cell proliferation, T-cell activation, calcium homeostasis and cellular response to stress. May play a role in calcium homeostasis through negative regulation of calcium efflux from mitochondria. Required for mitochondrial hyperfusion a pro-survival cellular response to stress which results in increased ATP production by mitochondria. May also regulate the organization of functional domains at the plasma membrane and play a role in T-cell activation through association with the T-cell receptor signaling complex and its regulation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22623988}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UJZ1}. Mitochondrion {ECO:0000269|PubMed:22623988}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9UJZ1}; Lipid-anchor {ECO:0000250|UniProtKB:Q9UJZ1}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:Q9UJZ1}. Membrane raft {ECO:0000250|UniProtKB:Q9UJZ1}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9UJZ1}. Note=Behaves as an integral membrane protein of the mitochondrion despite the absence of a detectable transmembrane domain. Also associates with the actin cytoskeleton and membrane rafts in activated T-cells. A minor pool is associated with the plasma membrane and is enriched at the immunological synapse in activated T-cells. {ECO:0000250|UniProtKB:Q9UJZ1}.
Interaction partners:
- Prohibitin 1
- Presenilin-associated rhomboid-like protein, mitochondrial
- COP9 signalosome complex subunit 5
- COP9 signalosome complex subunit 6
- Prohibitin-2
- ATP synthase F
- COP9 signalosome complex subunit 1
- Small ribosomal subunit protein uS7m
- COP9 signalosome complex subunit 3
- Heat shock protein HSP 90-beta
Sequence:
MLARAARGTGALLLRGSVQASGRVPRRASSGLPRNTVILFVPQQEAWVVERMGRFHRILEPGLNVLIPVLDRIRYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNANIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGEASAVLAKAKAKAEAIRILAGALTQHNGDAAASLTVAEQYVSAFSKLAKDSNTVLLPSNPSDVTSMVAQAMGVYGALTKAPVPGAQNSSQSRRDVQATDTSIEELGRVKLS
Protein: Pantothenate kinase 2 (A0A2R8YF29)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XSGPTSVSRQRVESLRKKRPQLLLAFISFSLLFPLQLPMSKSFFPWFGLDIGGTLVKLVYFEPKDITAEEEEEEVESLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLCGRKGNLHFIRFPTHDMPAFIQMGRDKNFSSLHTVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSVGFNGRSQCYYFENPADSEKCQKLPFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRDIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAMRLLAYALDYWSKGQLKALFSEHEGYFGAVGALLELLKIP
Protein: DNA-directed RNA polymerase subunit beta' (RNAP subunit beta') (EC 2.7.7.6) (RNA polymerase subunit beta') (Transcriptase subunit beta') (Q727C6)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Interaction partners:
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit omega
- Small ribosomal subunit protein uS7
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein bL12
- Large ribosomal subunit protein uL6
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein uL11
Sequence:
MTLDDLFTVRGSAANIANIRNLKAIQITIASPENIREWSYGEVKKPETINYRTFKPERDGLFCAKIFGPVKDYECNCGKYKRMKHRGIVCEKCGVEVIASKVRRERMGHIELAAPVAHIWFLKTLPSKIGTLLDMTMADLEKVLYFDSYIVLDPGSTNLTKMQVISEDQYLQVIDHYGEDALTVGMGAEAVRSLLEELNLEELRVQLREESQATKSQTKKKKLTKRLKIVEAFLESNNKPEWMVMEVIPVIPPELRPLVPLDGGRFATSDLNDLYRRVINRNNRLKRLMELGAPDIIIRNEKRMLQEAVDALFDNGRRGRAITGTNGRPLKSLSDMIKGKQGRFRQNLLGKRVDYSGRSVIVVGPKLKLHQCGLPKKMALELFKPFIYSELEKRGLASTIKSAKKMVEREELVVWDILEEVVREYPIMLNRAPTLHRLGIQSFEPLLVEGKAIQLHPLVCSAYNADFDGDQMAVHVPLSVEAQIECRVLMMSTNNILSPANGSPVIVPSQDIVLGLYYMTVDRSFEKGENMSFCAPWEVVAAYDAGVVALHARINVRMEDGKVVRTTVGRILVWELLPHCVPFSMVNTTLTKKNIARLVSTAYRDAGTKATVILCDRLKDVGYEYATRAGVTIAVKDLTIPSTKKGLIETAQNEVDDIERQYRDGIITRTEKYNKVVDVWTKATQDVSNEMIREISSDIVEDPRTGAKEANSSFNSIYMMSTSGARGNQDQMRQLAGMRGLMAKPSGEIIETPITSSFREGLSVLQYFTSTHGARKGLADTALKTANSGYLTRRLVDVVQDVIVSEHDCGTVDGIELTHIKEGGEIKIPLADRALGRVLLYPVYDPETRDLLFPENTLVDENVAKVLVEREVSSVMIRSALTCQSDRGICTLCYGRDLARGHIVNIGETVGIIAAQSIGEPGTQLTMRTFHIGGTASREIERSSFEAQHPGRVILSRVKAVRNRDGQYMVMGKSGQLAIVDDQGREREKYTLPNGSRLLVTEGEEIRKGQILAEWDPFNEPFVSEVDGVIRFSDIVEGKTFQEKMDEATRMTTQTIIEYRTTNFRPSISICDEHGEVKMRGNNIPATYSLPVGAIIMVKNGQDLQAGDIIARKPRETSKTKDIVGGLPRVAELFEVRKPKDMAVVSEIAGIVTYAGETKGKRKLVVTPEIGEAKEYLVPKGKHITVTDGDFVEAGDLLTEGHPELHDILRTRGEKYLARYLTDEIQEVYRFQGVAIDDKHIEVIVRQMLKKVTVLDPGGTTFLVGEQVDKGEFRVENTRAMGEGRTPATAEPLVLGITQASLTTSSFISAASFQETTKVLTEASLRGKMDYLRGLKENVIVGRLIPAGTGYREYVNTDILVPEQRERPDKFLEDLEENPLLVDIY
Protein: Tubulin beta-1 chain (Beta-1-tubulin) (P12411)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Tubulin alpha-2 chain
- Tubulin alpha-6 chain
- Tubulin alpha-5 chain
- Tubulin alpha-1 chain
- Kinesin-like protein KIN-8A
- Protein Abitram
- Mitotic spindle checkpoint protein MAD2
- Microtubule-associated protein RP/EB family member 1C
- Tubulin alpha-4 chain
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
Sequence:
MREILHVQGGQCGNQIGSKFWEVICDEHGVDPTGRYNGDSADLQLERINVYYNEASGGRYVPRAVLMDLEPGTMDSIRSGPYGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDAVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLSTPSFGDLNHLISATMSGVTCSLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYISLTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGKMSTKEVDEQILNVQNKNSSYFVEWIPNNVKSSVCDIPPTGIKMASTFVGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEEDEYDEEEEQVYES
Protein: GPI ethanolamine phosphate transferase 1 (EC 2.-.-.-) (MCD4 homolog) (Phosphatidylinositol-glycan biosynthesis class N protein) (PIG-N) (O95427)
Organism: Homo sapiens (Human)
Function: Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor (By similarity). May act as suppressor of replication stress and chromosome missegregation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- GPI alpha-1,6-mannosyltransferase 2
- GPI alpha-1,2-mannosyltransferase 3
- Inner nuclear membrane protein Man1
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
- GPI-anchor transamidase
- Glucosaminyl-phosphatidylinositol-acyltransferase PIGW
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- GPI alpha-1,4-mannosyltransferase I, catalytic subunit
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit H
- GPI-anchor transamidase component PIGT
Sequence:
MLLFFTLGLLIHFVFFASIFDIYFTSPLVHGMTPQFTPLPPPARRLVLFVADGLRADALYELDENGNSRAPFIRNIIMHEGSWGISHTRVPTESRPGHVALIAGFYEDVSAVAKGWKENPVEFDSLFNESKYTWSWGSPDILPMFAKGASGDHVYTYSYDAKREDFGAQDATKLDTWVFDNVKDFFHHARNNQSLFSKINEEKIVFFLHLLGIDTNGHAHRPSSRDYKHNIKKVDDGVKEIVSMFNHFYGNDGKTTFIFTSDHGMTDWGSHGAGHPSETLTPLVTWGAGIKYPQRVSAQQFDDAFLKEWRLENWKRLDVNQADIAPLMTSLIGVPFPLNSVGILPVDYLNNTDLFKAESMFTNAVQILEQFKVKMTQKKEVTLPFLFTPFKLLSDSKQFNILRKARSYIKHRKFDEVVSLCKELIHLALKGLSYYHTYDRFFLGVNVVIGFVGWISYASLLIIKSHSNLIKGVSKEVKKPSHLLPCSFVAIGILVAFFLLIQACPWTYYVYGLLPLPIWYAVLREFQVIQDLVVSVLTYPLSHFVGYLLAFTLGIEVLVLSFFYRYMLTAGLTAFAAWPFLTRLWTRAKMTSLSWTFFSLLLAVFPLMPVVGRKPDISLVMGAGLLVLLLSLCVVTSLMKRKDSFIKEELLVHLLQVLSTVLSMYVVYSTQSSLLRKQGLPLMNQIISWATLASSLVVPLLSSPVLFQRLFSILLSLMSTYLLLSTGYEALFPLVLSCLMFVWINIEQETLQQSGVCCKQKLTSIQFSYNTDITQFRQLYLDDIRRAFFLVFFLVTAFFGTGNIASINSFDLASVYCFLTVFSPFMMGALMMWKILIPFVLVMCAFEAVQLTTQLSSKSLFLIVLVISDIMALHFFFLVKDYGSWLDIGTSISHYVIVMSMTIFLVFLNGLAQLLTTKKLRLCGKPKSHFM
Protein: E3 ubiquitin protein ligase RIN2 (EC 2.3.2.27) (AMF receptor-like protein 1A) (RING-type E3 ubiquitin transferase RIN2) (RPM1-interacting protein 2) (Q8VYC8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin protein ligase that acts as positive regulator of RPM1- and RPS2-dependent hypersensitive response (HR), in association with RIN3. Probably not required for RPM1 degradation during HR.
Subcellular location: Membrane {ECO:0000269|PubMed:16212605}; Multi-pass membrane protein {ECO:0000269|PubMed:16212605}.
Interaction partners:
- E3 ubiquitin protein ligase RIN3
- Protein OS-9 homolog
- Disease resistance protein RPM1
- RING-H2 finger protein ATL14
Sequence:
MGIKYLPVSVASTALSFVGLQVWTELSLDRLRADGLIAKNISLGDSEHALELLLGSYFTIALLTNFVLNVYILLVLSLKTLFFGDLYDVETKKLVERLANYIIYKGTFLPLVIPPTIFQGVLWTVWLTVLCTLKMFQALARDRLERLNASPSSTPWTYFRVYSVLFLVLSVDMFWIKLSLMTYNTIGSAVYLLLLFEPCSIAFETLQALLIHGFQLLDMWINHLAVKNSDCQRSKFIDSMTAGSLLEWKGLLNRNLGFFLDMATLVMALGHYLHIWWLHGIAFHLVDAVLFLNIRALLSAILKRIKGYIKLRIALGALHAALPDATSEELRAYDDECAICREPMAKAKRLHCNHLFHLGCLRSWLDQGLNEVYSCPTCRKPLFVGRTENEVNPRTVEVSSDEQLARQLERQNNPVHALATGLFPAEVPDSVENDTSRNLGLDPSWLQTWSSQGSDVAGPSTTSRTVGLGRVQMMMRHLASVGESYAQTALDDAAWSLWPMNPSQASTSSTTVPPGNGGRTGGLHLRTVSNTTNESLTNILAMAETVREVMPHVPDEIIFQDLQRTNSVAVTVNNLLQM
Protein: Heterogeneous nuclear ribonucleoprotein L (M0QXS5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XCCTGRLVGGHPLQGRGQDLLWCSEGSSCQENYDDPHKTPASPVVHIRGLIDGVVEADLVEALQEFGPISYVVVMPKKRQALVEFEDVLGACNAVNYAADNQIYIAGHPAFVNYSTSQKISRPGDSDDSRSVNSVLLFTILNPIYSITTDVLYTICNPCGPVQRIVIFRKNGVQAMVEFDSVQSAQRAKASLNGADIYSGCCTLKIEYAKPTRLNVFKNDQDTWDYTNPNLSGQGDPGSNPNKRQRQPPLLGDHPAEYGGPHGGYHSHYHDEGYGPPPPHYEGRRMGPPVGGHRRGPSRYGPQYGHPPPPPPPPEYGPHADSPVLMVYGLDQSKMNCDRVFNVFCLYGNVEKVKFMKSKPGAAMVEMADGYAVDRAITHLNNNFMFGQKLNVCVSKQPAIMPGQSYGLEDGSCSYKDFSESRNNRFSTPEQAAKNRIQHPSNVLHFFNAPLEVTEENFFEICDELGVKRPSSVKVFSGKSERSSSGLLEWESKSDALETLGFLNHYQMKNPNGPYPYTLKLCFSTAQHAS
Protein: DNA polymerase delta catalytic subunit (EC 2.7.7.7) (3'-5' exodeoxyribonuclease) (EC 3.1.11.-) (DNA polymerase III) (P30316)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalytic component of DNA polymerase delta (DNA polymerase III) which participates in chromosomal DNA replication. Required during synthesis of the lagging DNA strands at the replication fork, binds at/or near replication origins and moves along DNA with the replication fork. Participates in leading strand synthesis during replication initiation and termination. Has 3'-5' proofreading exonuclease activity that corrects errors arising during DNA replication (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- DNA polymerase subunit delta-2
- DNA polymerase delta subunit 3
- DNA polymerase delta subunit 4
- DNA polymerase epsilon catalytic subunit A
- Proliferating cell nuclear antigen
- DNA replication licensing factor mcm2
- Cell division cycle protein cdt1
- Flap endonuclease 1
- DNA polymerase epsilon subunit B
- Replication factor A protein 1
Sequence:
MTDRSSNEGVVLNKENYPFPRRNGSIHGEITDVKRRRLSERNGYGDKKGSSSKEKTSSFEDELAEYASQLDQDEIKSSKDQQWQRPALPAINPEKDDIYFQQIDSEEFTEGSVPSIRLFGVTDNGNSILVHVVGFLPYFYVKAPVGFRPEMLERFTQDLDATCNGGVIDHCIIEMKENLYGFQGNEKSPFIKIFTTNPRILSRARNVFERGEFNFEELFPVGVGVTTFESNTQYLLRFMIDCDVVGMNWIHLPASKYQFRYQNRVSNCQIEAWINYKDLISLPAEGQWSKMAPLRIMSFDIECAGRKGVFPDPSIDPVIQIASIVTQYGDSTPFVRNVFCVDTCSQIVGTQVYEFQNQAEMLSSWSKFVRDVDPDVLIGYNICNFDIPYLLDRAKSLRIHNFPLLGRIHNFFSVAKETTFSSKAYGTRESKTTSIPGRLQLDMLQVMQRDFKLRSYSLNAVCSQFLGEQKEDVHYSIITDLQNGTADSRRRLAIYCLKDAYLPQRLMDKLMCFVNYTEMARVTGVPFNFLLARGQQIKVISQLFRKALQHDLVVPNIRVNGTDEQYEGATVIEPIKGYYDTPIATLDFSSLYPSIMQAHNLCYTTLLDSNTAELLKLKQDVDYSVTPNGDYFVKPHVRKGLLPIILADLLNARKKAKADLKKETDPFKKAVLDGRQLALKVSANSVYGFTGATNGRLPCLAISSSVTSYGRQMIEKTKDVVEKRYRIENGYSHDAVVIYGDTDSVMVKFGVKTLPEAMKLGEEAANYVSDQFPNPIKLEFEKVYFPYLLISKKRYAGLFWTRTDTYDKMDSKGIETVRRDNCPLVSYVIDTALRKMLIDQDVEGAQLFTKKVISDLLQNKIDMSQLVITKALSKTDYAAKMAHVELAERMRKRDAGSAPAIGDRVAYVIIKGAQGDQFYMRSEDPIYVLENNIPIDAKYYLENQLSKPLLRIFEPILGEKASSLLHGDHTRTISMAAPSVGGIMKFAVKVETCLGCKAPIKKGKTALCENCLNRSAELYQRQVAQVNDLEVRFARLWTQCQRCQGSMHQDVICTSRDCPIFYMRIAEHKKLQQSVDLLKRFDEMSW
Protein: [histone H3]-lysine(27) N-trimethyltransferase (EC 2.1.1.356) (F1LZH3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- SUZ12 polycomb repressive complex 2 subunit
- Polycomb protein EED
- Histone-binding protein RBBP7
- RB-binding protein 4, chromatin-remodeling factor.
- Protein Jumonji
- Zinc finger protein AEBP2
- PHD finger protein 19
- Metal-response element-binding transcription factor 2
- RB binding protein 4, chromatin remodeling factor like 1
- E3 ubiquitin-protein ligase RING1
Sequence:
VRKMDIASPPTSKCITYWKRKVKSEYMRLRQLKRLQANMGAKALYVANFAKVQEKTQLLNEEWKKLRVQPVQPMKPVSGHPFLKKCTIESIFPGFDSQDMLMRSLNTVALVPIMYSWSPLQQNFMVEDETVLCNIPYMGDEVKEEDETFIEELINNYDGKVHGEEEMIPGSVLISDAVFLELVDALNQYSDEEEEGHNDTSDGKQDDSKEDLPVTRKRKRHAIEGNKKSSKKQFPNDMIFSAIASMFPENGVPDDMKERYRELTEMSDPNALPPQCTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNVYKRKNREIKIEPEPCGADCFLWLEGAKEYAMLHNPRSKCSGRRRRRHPVVSASCSNTSASAMAETKEGDSDRDTGNDWASSSSEANSRCQTPTKQKASPAPPQLCVVEAPSEPVEWTGAEESLFRVFHGTYFNNFCSIARLLGTKTCKQVFQFAVKESLILKLPTDELMNPSQKKKRKHRLWAAHCRKIQLKKDNNSTQVYNYQPCDHPDRPCDSTCPCIMTQNFCEKFCQCSPDCQNRFPGCRCKTQCNTKQCPCYLAVRECDPDLCLTCGASEHWDCKVVSCKNCSIQRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYDKYMSSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVVMVNGDHRIGIFAKRAIQAGEELFFDYRYSQADALKYVGIERETDVF
Protein: Branched-chain amino acid ABC transporter, ATP-binding protein (Q5LNC2)
Organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Interaction partners:
- Branched-chain amino acid ABC transporter, permease protein
- Phenylacetate-CoA ligase, putative
- Branched-chain amino acid ABC transporter, permease protein
- Branched-chain amino acid ABC transporter, ATP-binding protein
- Branched-chain amino acid ABC transporter, periplasmic branched-chain amino acid binding protein, putative
- Branched-chain amino acid ABC transporter, permease protein
- Branched-chain amino acid ABC transporter, permease protein
- Branched-chain amino acid ABC transporter, permease/ATP-binding protein
- Branched-chain amino acid ABC transporter, permease protein
- Branched-chain amino acid ABC transporter, permease protein
Sequence:
MLDAAKTTDTQVETLLEVNNIEVIYNHVILVLKGVSLTVPKGGITALLGGNGAGKTTTLKAVSNLLHSERGEVTKGSVKYRGETIHELDPAALVTKGVIQVMEGRHCFEHLTVEENLLTGAYTRKDGSANIQRDLELVYNYFPRLKERRRSQAGYTSGGEQQMVAMGRALMSRPETILLDEPSMGLAPQLVEEIFEIVRDLNEKEGVSFLLAEQNTNVALRYAHYGYILESGRVVMDGPAKELRENPDVKEFYLGMSDDGRKSFRDVRSYRRRKRWLS
Protein: 5'-AMP-activated protein kinase beta-2 subunit protein (Q2V357)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGNANGKDEDAAAGSGGADVTSSSARSNGGDPSARSRHRRPSSDSMSSSPPGSPARSPSPFLFAPQPTLLFHVTSYNICSPMRHLFHCLGLTCVPNGCISCRMVPVAPLQRANAPPPNNIQWNQSQRVFDNPPEQGIPTIITWNQGGNDVAVEGSWDNWRSRKKLQKSGKDHSILFVLPSGIYHYKVIVDGESKYIPDLPFVADEVGNVCNILDVHNFVPENPESIVEFEAPPSPDHSYGQTLPAAEDYAKEPLAVPPQLHLTLLGTTEETAIATKPQHVVLNHVFIEQGWTPQSIVALGLTHRFESKYITVVLYKPLTR