wanglab/gogpt-training-data huggingface dataset:
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q5B3E4)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- mRNA splicing factor
- 116 kDa U5 small nuclear ribonucleoprotein component
- mRNA splicing protein PRP8
- Pre-mRNA splicing factor, putative
- Pre-mRNA splicing factor
- DNA binding protein SART-1, putative
- PWI domain-containing protein
- SnRNP assembly factor, putative
- Splicing factor 3B subunit 1, putative
- FF domain protein
Sequence:
MSSRRSSTASEGEIIESGSETKATTSQSLLNDNSVDRPTRVSSSASVTRSPRRQRSRARTRSRSPSRSPYRDYRGYKRRRAGDYDHDDYWYGYDDDRHSGRTFPPPRRGCHRHDGYPQRQARSYYDYDREDNHLADLRYSDDYDRRREKRPRTRSRSPYREVRKRKQYSGDEWESQQSRREGSVASQSKRRSSTEQSVSERGNPPAVARDSRQDAETQKNQVQAASILPTSDGDSMNGQDVAERHEEPLDEAAQLEARRKRREAIKAKYRDQATPLRIQALHLGGDRGTTPTSEAATPNNETAESAATPDGGSFPDFSIGKDLDLVKDGAVDGADKDEPSAADYDPTIDMKAERERHGGQSNDVSAASYDETKTTKQDVLLPDAPSQQEPEAKDSFDIFAEDDDDMFAEDTEETSKPAHASAIAVPQARELDVSMMDNWDDPEGYYNLRIGELIDGRYHVQQNLGKGMFSSVVRAKDSKTGNVVAIKIIRQNDTMKKAGLKEIGILEKLREADPEDKKHMIKFERSFEHKGHLCMVFENLSMNLREVLKKFGRDVGLNLRAIRAYAQQIFLGLSLMRKCNILHADLKPDNMLVNEQRNILKVCDLGSASLASDNEITPYLVSRFYRAPEIILGIPYDYAIDMWSIGCTLFELYTGKILFTGRNNNQMLKSIMECRGKYPPKLLRRGSLAHLHFDEMANFHSTEEDKITGRLTTRIMDFKKPTRDLKTRLMGKGTRGMTDSEAKELALFVDLLDRCLSLNPEKRCTPAEALKHPFILRPKA
Protein: ATP-binding cassette sub-family C member 9 (Sulfonylurea receptor 2) (O60706)
Organism: Homo sapiens (Human)
Function: Subunit of ATP-sensitive potassium channels (KATP). Can form cardiac and smooth muscle-type KATP channels with KCNJ11. KCNJ11 forms the channel pore while ABCC9 is required for activation and regulation.
Subcellular location: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
Interaction partners:
- ATP-sensitive inward rectifier potassium channel 8
- ATP-sensitive inward rectifier potassium channel 11
- ATP-binding cassette sub-family C member 8
- RNA-binding protein 20
- Sodium channel protein type 5 subunit alpha
- Myosin-binding protein C, cardiac-type
- Cysteine and glycine-rich protein 3
- Lamina-associated polypeptide 2, isoform alpha
- Protein phosphatase EYA4
- Desmoglein-2
Sequence:
MSLSFCGNNISSYNINDGVLQNSCFVDALNLVPHVFLLFITFPILFIGWGSQSSKVQIHHNTWLHFPGHNLRWILTFALLFVHVCEIAEGIVSDSRRESRHLHLFMPAVMGFVATTTSIVYYHNIETSNFPKLLLALFLYWVMAFITKTIKLVKYCQSGLDISNLRFCITGMMVILNGLLMAVEINVIRVRRYVFFMNPQKVKPPEDLQDLGVRFLQPFVNLLSKATYWWMNTLIISAHKKPIDLKAIGKLPIAMRAVTNYVCLKDAYEEQKKKVADHPNRTPSIWLAMYRAFGRPILLSSTFRYLADLLGFAGPLCISGIVQRVNETQNGTNNTTGISETLSSKEFLENAYVLAVLLFLALILQRTFLQASYYVTIETGINLRGALLAMIYNKILRLSTSNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTSLSIFMNAAIPIAAVLATFVTHAYASGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKLNEFLLSDEIGDDSWRTGESSLPFESCKKHTGVQPKTINRKQPGRYHLDSYEQSTRRLRPAETEDIAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRNRYSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEHWKTLMNRQDQELEKDMEADQTTLERKTLRRAMYSREAKAQMEDEDEEEEEEEDEDDNMSTVMRLRTKMPWKTCWRYLTSGGFFLLILMIFSKLLKHSVIVAIDYWLATWTSEYSINNTGKADQTYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACIVLTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFLTMESENYEGTMDPSQVPEHWPQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSSIMDAGLVLVFSEGILVECDTVPNLLAHKNGLFSTLVMTNK
Protein: Lysophospholipid acyltransferase 5 (LPLAT 5) (EC 2.3.1.-) (Probable 1-acylglycerophosphocholine O-acyltransferase) (EC 2.3.1.23) (Probable 1-acylglycerophosphoethanolamine O-acyltransferase) (EC 2.3.1.n7) (Probable 1-acylglycerophosphoserine O-acyltransferase) (EC 2.3.1.n6) (Probable lysophosphatidylcholine acyltransferase) (LPCAT) (Lyso-PC acyltransferase) (Probable lysophosphatidylethanolamine acyltransferase) (LPEAT) (Lyso-PE acyltransferase) (Probable lysophosphatidylserine acyltransferase) (LPSAT) (Lyso-PS acyltransferase) (O01925)
Organism: Caenorhabditis elegans
Function: Probable acyltransferase which may mediate the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (LPCAT activity). May also catalyze the conversion of lysophosphatidylethanolamine (1-acyl-2-hydroxy-sn-glycero-3-phosphoethanolamine or LPE) into phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine or PE) (LPEAT activity), as well as the conversion of lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero-3-phospho-L-serine or LPS) into phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine or PS) (LPSAT activity). Required for incorporation of arachidonic acid into PC, PE, and PS.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Lysophospholipid acyltransferase
- EthanolaminePhosphoTransferase 1 homolog
- Membrane Bound O-Acyl transferase, MBOAT
- PLD phosphodiesterase domain-containing protein
- PhosphoLipase A2 Group
- Phospholipase
- Probable phospholipase D F09G2.8
- Phosphatidylserine synthase
- Phosphatidylserine synthase
- Phosphatidylserine decarboxylase proenzyme, mitochondrial
Sequence:
MGVVGALSEVTSASEDALRLLISVLAGYPLAVVHRTFFYNKPAQHQHLFFVIVGLSLWMFNCGSSVIHPILSIFGAFFITNFMAGTDASIYAAHIVFLGHLLIGYWFHETDTYDITWTTPFCIMTLRFIGLVMDVYDGAQKPEHLKPDQKLTAISDKPGLLEIAAFGLFFQGTLVGPQFTLSKFRSFVNGDWLDSDGQPPKSAFLPSIGRFLAGCTYMVLHQWGQFWIPDQYFNSDAYNNLSFFWRWSWVTLWFRLTMYKYCAMWLITEGASILSGLGHNGKDAEGNDRWDGVRDLHIIKWETGHDYNSVVESFNCGTNTFAKNHIHRRLRWVNNKLASHVITLSYLAIWHGYHLGYFLLFGVELGCVQAQNQLYALIKRTPGWSEAISKPISRPFIWIFGKLTISYSMGFAFLMFGLIKTKYWIGPVKSLYFIGFIIYFIVWPILHMVLLRVLPRHPKKAAAEKPEEVKKEL
Protein: PDE4DIP protein (Q8TBR0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MFLCQGFRKYLPEHLNDLKKENFSLKLRIYFLEERMQQKYEASREDIYRRNTELKVEVESLKRELQDKKQHLDKTWADVENLNSQNEAELRRQFEERQQETEHVYELLENKMQLLQEESRLAKNEAARMAALVEAEKECNLELSEKLKGVTKNWEDVPGDQVKPDQYTEALAQRDKI
Protein: B double prime 1, subunit of RNA polymerase III transcription initiation factor IIIB (A0A0A0MRX7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFRRARLSVKPNVRPGVGARGSTASNPQRGRESPRPPDPATDSASKPAEPTDVPTVDFGGAEPQEKAPRSSTEKTGGDNDVEESSRSSSTVSQRRKRISSTSSLVKSSVSVPSESHPLSTINQEAPQPTATSTKEKQPCSDRYRIYKAQKLREMLKEELRKEKKQWKNKYAINESQRPPDRSKMTMRDFIYYLPDNNPMTSSLEQEKKTEKPSTPVQTREQEGKSTPNAEDNEMEEETDDGPLLVPRVKVAEDGSIILDEESLTVEVLRTKGPCVVEENDPIFERGSTTTYSSFRKNYYSKPWSNKETDMFFLAISMVGTDFSMIGQLFPHRARIEIKNKFKREEKTNGWRIDKAFQEKRPFDFDFFAHLLQKVLAEEEKRKQKSVKNHSLKEKKSTKPRKNVKVKKVACEGVNNDPDESMSSRISDTERSQKDAQTVEEESLTLSREDAEQVALEVDLNQKKRRRKKQDGANELGVNNLLENATVQAGPSKGEKHKNKCQAIRPELKEGECSKEQMLSCTQNIDGIVGFASTEKVEKRTDPILSLSNQQDATSVATESSESSTSDLPSFEVGIRALCEVNNAEGSCIEERNVDLKNNSLEIDQTENVKPMLRGRFQRPKPNLSRAGKKSVLSQGKTESESKNSHSKTSVEKNHVEKDKMNTLDILRMETTERENPEAETVSVLGEKNCLQEGSQLKALRPVQVRGRLQKPKPNAGKAAERKEILISQEEIGANVEKNENESCADRDTPQHMEDQSRKDFEEEDVILQPEKNDSFQNVQPDEPKVLNECLSVQENNKANKLNQVPILRTRFQKPKPNIGRGTGRREISSKEEVLEKILSLGKWRQH
Protein: 1-cys peroxiredoxin DPx-6005 (Q9GPQ2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSGKALNIGDQFPNFTAETSEGRIDFYDWMQDSWAILFSHPADFTPVCTTELSRVAALIPEFQKRGVKPIALSCDPVESHKGWIEDIKSFGKLSSFDYPIIADDKRELALKFNMLDKDEINAEGIPLTCRAVFVVDDKKKLRLSILYPATTGRNFDEILRVIDSLQLTQTKSVATPADWKQGGKCMVLPTVKAEDVPKLFPDGIETIELPSGKSYLRITPQP
Protein: Histone H2B type 1-A (Histone H2B, testis) (TSH2B.1) (hTSH2B) (Testis-specific histone H2B) (Q96A08)
Organism: Homo sapiens (Human)
Function: Variant histone specifically required to direct the transformation of dissociating nucleosomes to protamine in male germ cells (By similarity). Entirely replaces classical histone H2B prior nucleosome to protamine transition and probably acts as a nucleosome dissociating factor that creates a more dynamic chromatin, facilitating the large-scale exchange of histones (By similarity). Core component of nucleosome (By similarity). Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template (By similarity). Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability (By similarity). DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (By similarity). Also found in fat cells, its function and the presence of post-translational modifications specific to such cells are still unclear.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P70696}. Chromosome {ECO:0000250|UniProtKB:P70696}.
Interaction partners:
- Histone H2A type 2-C
- Histone H2A type 1-A
- Histone H4
- Histone H3.1
- Histone H2A type 1-B/E
- Histone H2A type 1-D
- Histone H2A.Z
- Histone H3.1t
- E3 ubiquitin-protein ligase BRE1A
- Histone H3.3
Sequence:
MPEVSSKGATISKKGFKKAVVKTQKKEGKKRKRTRKESYSIYIYKVLKQVHPDTGISSKAMSIMNSFVTDIFERIASEASRLAHYSKRSTISSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK
Protein: Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1) (E5L8C9)
Organism: Gallus gallus (Chicken)
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR002527}.
Interaction partners:
Sequence:
MTMTLHTKASGVTLLHQIQGTELETLSRPQLKIPLERSLSDMYVESNKTGVFNYPEGATYDFGTTAPVYGSTTLSYAPTSESFGSSSLAGFHSLNNVPPSPVVFLQTAPQLSPFIHHHSQQVPYYLENEQGSFGMREAAPPAFYRPSSDNRRHSIRERMSSTNEKGSLSMESTKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGRMMKQKRQREEQDSRNGEASSTELRAPTLWTSPLVVKHNKKNSPALSLTAEQMVSALLEAEPPIVYSEYDPNRPFNEASMMTLLTNLADRELVHMINWAKRVPGFVDLTLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATAARFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEERDYIHRVLDKITDTLIHLMAKSGLSLQQQHRRLAQLLLILSHIRHMSNKGMEHLYNMKCKNVVPLYDLLLEMLDAHRLHAPAARSAAPMEEENRNQLTTAPASSHSLQSFYINSKEEESMQNTI
Protein: Non-selective voltage-gated ion channel VDAC2 (VDAC-2) (hVDAC2) (Outer mitochondrial membrane protein porin 2) (P45880)
Organism: Homo sapiens (Human)
Function: Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules (By similarity). The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV (By similarity). The open state has a weak anion selectivity whereas the closed state is cation-selective (By similarity). Binds various lipids, including the sphingolipid ceramide, the phospholipid phosphatidylcholine, and the sterol cholesterol. Binding of ceramide promotes the mitochondrial outer membrane permeabilization (MOMP) apoptotic pathway.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:31015432, ECO:0000269|PubMed:7539795}. Membrane {ECO:0000269|PubMed:27641616}. Note=May localize to non-mitochondrial membranes. {ECO:0000269|PubMed:27641616}.
Interaction partners:
- Non-selective voltage-gated ion channel VDAC1
- Non-selective voltage-gated ion channel VDAC3
- Cytochrome c
- ADP/ATP translocase 3
- ADP/ATP translocase 2
- ADP/ATP translocase 1
- ADP/ATP translocase 4
- Steroidogenic acute regulatory protein, mitochondrial
- Peptidyl-prolyl cis-trans isomerase F, mitochondrial
- Translocator protein
Sequence:
MATHGQTCARPMCIPPSYADLGKAARDIFNKGFGFGLVKLDVKTKSCSGVEFSTSGSSNTDTGKVTGTLETKYKWCEYGLTFTEKWNTDNTLGTEIAIEDQICQGLKLTFDTTFSPNTGKKSGKIKSSYKRECINLGCDVDFDFAGPAIHGSAVFGYEGWLAGYQMTFDSAKSKLTRNNFAVGYRTGDFQLHTNVNDGTEFGGSIYQKVCEDLDTSVNLAWTSGTNCTRFGIAAKYQLDPTASISAKVNNSSLIGVGYTQTLRPGVKLTLSALVDGKSINAGGHKVGLALELEA
Protein: Keratin, type I cytoskeletal 15 (Cytokeratin-15) (CK-15) (Keratin-15) (K15) (Type I keratin Ka15) (Q6IFV3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Keratin, type I cytoskeletal 14
- Leucine-rich repeats and immunoglobulin-like domains 1
- Keratin, type II cytoskeletal 5
Sequence:
MATTFLQTSSTFGSGSTRGGSLRVGGGSFGGGSLYGGGGSRSISASSARFVSSGAGVGFGGGMSCGFGGGFGGGFGGGFGDFGGGDGGLLSGNEKVTMQNLNDRLASYLDKVRALEEANTELEVKIRDWYQKQSPASPDRDYSHYFKTMEEIRDKILAATIDNSRVILEIDNARLAADDFRLKYENELALRQGVEADINGLRRVLDELTLARTDLEMQIEQLNEELAYLKKNHEEEMKEFSSQLAGQVNVEMDAAPGVDLTRMLAEMREQYEAIAEKNRRDVEAWFFSKTEELNKEVASNTEMIQTSKTEITDLRRTLQGLEIELQSQLSMKAGLENSLAEVECRYATQLQQIQGLITGLETQLSELRCEMEAQNQEYNMLLDIKTRLEQEISTYRNLLEGQDAKMAAIGVREASLRGGSSGGGSNFHISVEESVDGKVVSSRKRES
Protein: cGMP-dependent protein kinase (EC 2.7.11.12) (W7JX98)
Organism: Plasmodium falciparum (isolate NF54)
Function: Serine/threonine protein kinase which acts as a downstream effector of the second messenger cGMP. Controls the release of Ca(2+) from intracellular stores by regulating phosphoinositide biosynthesis. Ca(2+) signals are essential for merozoite and sporozoite invasion and egress from host hepatocytes and erythrocytes, and, in the mosquito vector, for gametocyte activation, and ookinete and sporozoite motility (By similarity). During the host liver stage, regulates the initial invasion of host hepatocytes by sporozoites by regulating sporozoite motility and microneme exocytosis. Following parasite development in the hepatocytes, required for the release of merosomes, a vesicle containing the mature merozoites (By similarity). During the asexual blood stage, required for the progression from schizont to the ring stage following merozoite invasion of host erythrocytes and for merozoite egress. Regulates merozoite egress by promoting the release of exonemes and micronemes which contain proteins essential for egress. Phosphorylates CDPK1 predominantly at the late schizont stage; phosphorylation at 'Ser-64' regulates CDPK1 protein-protein interaction and phosphorylation at 'Thr-231' may regulate CDPK1 kinase activity. In the mosquito vector, required for the initiation of gametogenesis induced by xanthurenic acid, specifically the gametocyte differentiation from the crescent-shaped form to the spherical form (By similarity). Required for the gliding motility of ookinetes to reach and penetrate the midgut epithelium by promoting Ca(2+)-mediated activation of CDPK1 and CDPK4. Also required for microneme secretion in ookinete by promoting Ca(2+)-mediated activation of CDPK3 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8I719}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8I719}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8I719}; Cytoplasmic side {ECO:0000250|UniProtKB:Q8I719}. Note=Predominantly localizes to the cytoplasm during schizogony. {ECO:0000250|UniProtKB:Q8I719}.
Interaction partners:
Sequence:
MEEDDNLKKGNERNKKKAIFSNDDFTGEDSLMEDHLELREKLSEDIDMIKTSLKNNLVCSTLNDNEILTLSNYMQFFVFKSGNLVIKQGEKGSYFFIINSGKFDVYVNDKKVKTMGKGSSFGEAALIHNTQRSATIIAETDGTLWGVQRSTFRATLKQLSNRNFNENRTFIDSVSVFDMLTEAQKNMITNACVIQNFKSGETIVKQGDYGDVLYILKEGKATVYINDEEIRVLEKGSYFGERALLYDEPRSATIIAKEPTACASICRKLLNIVLGNLQVVLFRNIMTEALQQSEIFKQFSGDQLNDLADTAIVRDYPANYNILHKDKVKSVKYIIVLEGKVELFLDDTSIGILSRGMSFGDQYVLNQKQPFKHTIKSLEVCKIALITETCLADCLGNNNIDASIDYNNKKSIIKKMYIFRYLTDKQCNLLIEAFRTTRYEEGDYIIQEGEVGSRFYIIKNGEVEIVKNKKRLRTLGKNDYFGERALLYDEPRTASVISKVNNVECWFVDKSVFLQIIQGPMLAHLEERIKMQDTKVEMDELETERIIGRGTFGTVKLVHHKPTKIRYALKCVSKRSIINLNQQNNIKLEREITAENDHPFIIRLVRTFKDSKYFYFLTELVTGGELYDAIRKLGLLSKSQAQFYLGSIILAIEYLHERNIVYRDLKPENILLDKQGYVKLIDFGCAKKVQGRAYTLVGTPHYMAPEVILGKGYGCTVDIWALGICLYEFICGPLPFGNDEEDQLEIFRDILTGQLTFPDYVTDTDSINLMKRLLCRLPQGRIGCSINGFKDIKDHPFFSNFNWDKLAGRLLDPPLVSKSETYAEDIDIKQIEEEDAEDDEEPLNDEDNWDIDF
Protein: TPR domain protein (O51213)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Interaction partners:
- Tetratricopeptide repeat domain protein
- Uncharacterized protein
- Tetratricopeptide repeat domain protein
- Hydrolase, TatD family
Sequence:
MLNEKILDALGDLSSISDDQLLDVTEKSKRGYQLIKEERLSEAESLFSDILEKDNENNYALVGLGDIERKKNNYDKAIVYYQKCLVKHPSNNYALFGLGDCYRNLDNYKKATDIWEEYLKYDPENITVLTRVAASYRKLKNFQKSKQTYLKVMELIPDNDYALVGIGHLYYDFKEYKEALKYWLKMYELNQSKVDVRVLTSIGNCYRKLREFTRGIYFFKKALEISPSNFYAVFGLADCYRGNKEYKEALKYWLDIIEKDPKNNLVLTRVGDAYRYLNDYENSQIYYKKALDVDFDMFAILGLALIQKEQGKYEEALIAIKSLIKNNPKNSALYVNAAECYEALGQIGNAVDILSSFLQLGMKNIVVIDYLAVLRKKME
Protein: Troponin C, skeletal muscle (Q9I8U8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Fast muscle troponin I, tandem duplicate 4)
- Fast skeletal muscle troponin T
- Troponin I type 2b
- Slow troponin T
- Tnnt3b protein)
- Troponin T type 1
- Troponin I, fast skeletal muscle
- Troponin I4b, tandem duplicate 2.
- Troponin I type 1a
- Troponin T type 2a
Sequence:
MTDAQQEARSYLSEEMLAEFKAAFDMFDTDGGGDISTKELGTVMRMLGQNPTREELEEIIEEVDEDGSGSIDFEEFLVMMVRLLKEDQAGKSEEELAECFRVLDKNGDGYIDRDEFAEIIRSTGESISEEEIDELLKDGDKNNDGMLDFDEFLKMMENVQ
Protein: ER membrane protein complex subunit 10 (O80798)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004115}.
Interaction partners:
- ER membrane protein complex subunit 1
- ER membrane protein complex subunit 3
- Membrane magnesium transporter
- ER membrane protein complex subunit 4
- ER membrane protein complex subunit 6
- ER membrane protein complex subunit 7 homolog
- ER membrane protein complex subunit 2
- ER membrane protein complex subunit-like protein
- ER membrane protein complex subunit 2
- ER membrane protein complex subunit 8/9 homolog
Sequence:
MAKLTLLFFLSFLIFSSSIAFQSDELLVDDDEFGLEGAKPRSTDLYTSSSSSPQQQQQTPTIRRRYSDPTDLDSKVQFTLEHAFGDSDFSPAGTFSARLKTWSHGGKTLTKLRFSRNDFSAEEKDAFKNLLKGDDFYRIRLPSNVVSPPGREFVIASVRARCLPRDGLDEHFIIHMEGANILAVSYGSPGACQYPRQLKLPAKWSFNSHTILKSSEQAPRTPIFTEEILGSENVEGEVEPPPERSFWAKYWMYLIPLGLVVMNAVTQASNMAEEPAGGQAGGAQVQPAARRR
Protein: Zinc finger protein 675 (TRAF6-binding zinc finger protein) (TRAF6-inhibitory zinc finger protein) (Q8TD23)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation. May play a role during osteoclast differentiation by modulating TRAF6 signaling activity.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MGLLTFRDVAIEFSLEEWQCLDTAQRNLYKNVILENYRNLVFLGIAVSKQDLITCLEQEKEPLTVKRHEMVNEPPVMCSHFAQEFWPEQNIKDSFEKVTLRRYEKCGNDNFQLKGCKSVDECKLHKGGYNGLNQCLPTMQSKMFQCDKYVKVFNKFSHSDRHKIKHMENKPFKCKECGRSFCMLSHLTRHERNYTKVNFCKCEECEKAVNQSSKLTKHKRIYTCEKLYKCQECDRTFNQFSNLTEYKKDYAREKPYKCEECGKAFNQSSHLTTHKIIHTGEKPYKCEECGKAFNQFSNLTTHKKIHTGEQPYICEECGKAFTQSSTLTTHKRIHTGEKPYKCEECGKAFNRSSKLTEHKNIHTGEQPYKCEECGKAFNRSSNLTEHRKIHTEEKPYKCKECGKAFKHSSALTTHKRIHTGEKPYKCEECGKAFNRSSKLTEHKKLHTGKKPYKCEECGKAFIQSSKLTEHKKIHSGEIPYKCEECGKAFKHSSSLTTHKRIHTGEKPYKCEECGKAFSRSSKLTEHKIIHTGEKPYKCERCDKAFNQSANLTKHKKIHTGEKLQNWNV
Protein: Protein SCP160 (Protein HX) (P06105)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the control of mitotic chromosome transmission. Required during cell division for faithful partitioning of the ER-nuclear envelope membranes which, in S.cerevisiae, enclose the duplicated chromosomes.
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Note=Attached to the cytoplasmic surface of the ER-nuclear envelope membranes.
Interaction partners:
- Nuclear segregation protein BFR1
- Protein EAP1
- Small ribosomal subunit protein RACK1
- Elongation factor 1-alpha
- Heterogeneous nuclear rnp K-like protein 2
- Protein SMY2
- ATP-dependent RNA helicase DHH1
- SWIRM domain-containing protein YOR338W
- Haze protective factor 1
- SWI5-dependent HO expression protein 2
Sequence:
MSEEQTAIDSPPSTVEGSVETVTTIDSPSTTASTIAATAEEHPQLEKKPTPLPSLKDLPSLGSNAAFANVKVSWGPNMKPAVSNSPSPSPSAPSLTTGLGAKRMRSKNIQEAFTLDLQSQLSITKPELSRIVQSVKKNHDVSVESTLSKNARTFLVSGVAANVHEAKRELVKKLTKPINAVIEVPSKCKASIIGSGGRTIREISDAYEVKINVSKEVNENSYDEDMDDTTSNVSLFGDFESVNLAKAKILAIVKEETKNATIKLVVEDEKYLPYIDVSEFASDEGDEEVKVQFYKKSGDIVILGPREKAKATKTSIQDYLKKLASNLDEEKVKIPSKFQFLIDAEELKEKYNVIVTFPSTPDDELVSFVGLRDKVGEAITYARSSSKSYVVESLDISKAHSKNLTHAKNLIMYFTKYSVLKGLEESHPNVKISLPSIQSLPTAETVTIHISAKSDEANDIKAVRKELISFVNNIPPSETLVITDLDYELFGGSIKHCLLASESSVAFVQFGDYYPNDNSILLVALTEDEDFKPSIEEIQASLNKANESLNSLRTKQNNMETKTYEFSEEVQDSLFKPSSATWKLIMEDISEQEGHLQIKLHTPEENQLTVRGDEKAAKAANKIFESILNSPSSKSKMTVNIPANSVARLIGNKGSNLQQIREKFACQIDIPNEENNNASKDKTVEVTLTGLEYNLTHAKKYLAAEAKKWADIITKELIVPVKFHGSLIGPHGTYRNRLQEKYNVFINFPRDNEIVTIRGPSRGVNKAHEELKALLDFEMENGHKMVINVPAEHVPRIIGKNGDNINDIRAEYGVEMDFLQKSTDPKAQETGEVELEITGSRQNIKDAAKRVESIVAEASDFVTEVLKIDHKYHKSIVGSGGHILREIISKAGGEEIRNKSVDIPNADSENKDITVQGPQKFVKKVVEEINKIVKDAENSVTKTIDIPAERKGALIGPGGIVRRQLESEFNINLFVPNKDDPSGKITITGAPENVEKAEKKILNEIIRENFDREVDVPASIYEYVSERGAFIQKLRMDLSVNVRFGNTSKKANKLARAPIEIPLEKVCGSTEGENAEKTKFTIEEVGAPTSSEEGDITMRLTYEPIDLSSILSDGEEKEVTKDTSNDSAKKEEALDTAVKLIKERIAKAPSATYAGYVWGADTRRFNMIVGPGGSNIKKIREAADVIINVPRKSDKVNDVVYIRGTKAGVEKAGEMVLKSLRR
Protein: Endolysin (EC 3.5.1.28) (N-acetylmuramoyl-L-alanine amidase) (T7 endolysin) (P00806)
Organism: Escherichia phage T7 (Bacteriophage T7)
Function: Plays an important role in the switch between viral transcription and genome replication. Once produced in sufficient amount, interacts with and inhibits the viral RNA polymerase that becomes unable to produce additional late transcripts. This lysozyme-polymerase complex in turn plays an active role in viral genome replication and packaging.
Subcellular location: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04111}. Note=The endolysin is cytoplasmic, but can reach the periplasmic space with the help of the holins which disrupt the host cell membrane. {ECO:0000255|HAMAP-Rule:MF_04111}.
Interaction partners:
Sequence:
MARVQFKQRESTDAIFVHCSATKPSQNVGVREIRQWHKEQGWLDVGYHFIIKRDGTVEAGRDEMAVGSHAKGYNHNSIGVCLVGGIDDKGKFDANFTPAQMQSLRSLLVTLLAKYEGAVLRAHHEVAPKACPSFDLKRWWEKNELVTSDRG
Protein: Peroxisomal biogenesis factor 11 beta (A0A8I5Y5E1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Peroxisome membrane {ECO:0000256|ARBA:ARBA00046271}.
Interaction partners:
Sequence:
LPHQPTEDIVGREVREACPLLCLLSSRAAQYACSLLGHALQRHGASPELQKQIRQLEGHLSLGRKLLRLGNSADALESAKRAVHLSDVVLRFCITVSHLNRALYFACDNVLWAGKSGLAPRVDQEKWAQRSFRYYLFSLIMNLSRDAYEIRLLMEQETSAHSRRMKISGVGVSGLETGGPGGPGTPGGCLPQLALKFRLRILLLARVLRDHPPLLLDVLRNACDLFIPLDKLGLWRCGPGIVGLCGLISSVLSILTLICPWLRLKP
Protein: Angiomotin (E7ERM3)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
Interaction partners:
Sequence:
MEHRGPPPEYPFKGMPPQSVVCKPQEPGHFYSEHRLNQPGRTEGQLMRYQHPPEYGAARPAQDISLPLSARNSQPHSPTSSLTSGGSLPLLQSPPSTRLSPARHPLVPNQGDHSAHLPRPQQHFLPNQAHQGDHYRLSQPGLSQQQQQQQQQHHHHHHHQQQQQQQPQQQPGEAYSAMPRAQPSSASYQPVPADPFAIVSRAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRERLETANKQLAEKEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNCQPTNVSEYNAAALMELLREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSCMRPAKSLMSISNAGSGLLSHSSTLTGSPIMEEKRDDKSWKGSLGILLGGDYRAEYVPSTPSPVPPSTPLLSAHSKTGSRDCSTQTERGTESNKTAAVAPISVPAPVAAAATAAAITATAATITTTMVAAAPVAVAAAAAPAAAAAPSPATAAATAAAVSPAAAGQIPAAASVASAAAVAPSAAAAAAVQVAPAAPAPVPAPALVPVPAPAAAQASAPAQTQAPTSAPAVAPTPAPTPTPAVAQAEVPASPATGPGPHRLSIPSLTCNPDKTDGPVFHSNTLERKTPIQILGQEPDAEMVEYLI