wanglab/gogpt-training-data huggingface dataset:
Protein: BEN domain-containing protein 5 (Q7L4P6)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional repressor.
Interaction partners:
- Cytosolic carboxypeptidase 6
Sequence:
MYAFVRFLEDNVCYALPVSCVRDFSPRSRLDFDNQKVYAVYRGPEELGAGPESPPRAPRDWGALLLHKAQILALAEDKSDLENSVMQKKIKIPKLSLNHVEEDGEVKDYGEEDLQLRHIKRPEGRKPSEVAHKSIEAVVARLEKQNGLSLGHSTCPEEVFVEASPGTEDMDSLEDAVVPRALYEELLRNYQQQQEEMRHLQQELERTRRQLVQQAKKLKEYGALVSEMKELRDLNRRLQDVLLLRLGSGPAIDLEKVKSECLEPEPELRSTFSEEANTSSYYPAPAPVMDKYILDNGKVHLGSGIWVDEEKWHQLQVTQGDSKYTKNLAVMIWGTDVLKNRSVTGVATKKKKDAVPKPPLSPHKLSIVRECLYDRIAQETVDETEIAQRLSKVNKYICEKIMDINKSCKNEERREAKYNLQ
Protein: Coagulation factor II (thrombin) receptor-like 1, tandem duplicate 2 (I3IRY7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Low-density lipoprotein receptor-related protein 11
- Suppressor of tumorigenicity 14 protein homolog
- Solute carrier family 38 member 5a.
Sequence:
MAVSESYRILLFLACVIFASAQPGTGKGRSLVVIQNDAGHMFVDQIARETLQSSLTTVFMPIIYIIVFVVGLPTNAMAIYVLLFRSKKVHPAAIYMGNLALADLMFVIWTPLKIAYHLKGNNWTYGEEMCKVSVGFFYGNMYCSILFITCLSVQRYWVCAHPLTQQRRDNRLAIIISVCVWVFIGVSTTPLYLYNQTVQLQDLNITTCHDVNIITKKSFDNHNAFLDVQEPYYYFMVMAGLVFFVPMVVIIMAYVLLLRSLGNSSVKGSAGKSRKRAVILIVTVLITFLVCFIPSNVMLVVHYSLLRNNSFNASYGFYLTALCIASLNSCLDPFIYYYVSDDFREEVKNTLQCRSSRTVERMRVSFSSMKYSKRTNTYTSSSGNTETSTC
Protein: At1g48620 (High mobility group A5) (Q4V3D1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Non-structural maintenance of chromosomes element 1 homolog
- Structural maintenance of chromosomes protein 5
- E3 SUMO-protein ligase MMS21
- Transcription regulator NOT2/NOT3/NOT5 family protein
- Winged-helix DNA-binding transcription factor family protein
- Non-structural maintenance of chromosomes element 4 homolog A
- Non-structural maintenance of chromosomes element 4 homolog B
- Winged helix-turn-helix transcription repressor DNA-binding protein
- Structural maintenance of chromosomes protein 6B
- Structural maintenance of chromosomes protein 6A
Sequence:
MDPSLSATNDPHHPPPPQFTSFPPFTNTNPFASPNHPFFTGPTAVAPPNNIHLYQAAPPQQPQTSPVPPHPSISHPPYSDMICTAIAALNEPDGSSKQAISRYIERIYTGIPTAHGALLTHHLKTLKTSGILVMVKKSYKLASTPPPPPPTSVAPSLEPPRSDFIVNENQPLPDPVLASSTPQTIKRGRGRPPKAKPDVVQPQPLTNGKLTWEQSELPVSRPEEIQIQPPQLPLQPQQPVKRPPGRPRKDGTSPTVKPAASVSGGVETVKRRGRPPSGRAAGRERKPIVVSAPASVFPYVANGGVRRRGRPKRVDAGGASSVAPPPPPPTNVESGGEEVAVKKRGRGRPPKIGGVIRKPMKPMRSFARTGKPVGRPRKNAVSVGASGRQDGDYGELKKKFELFQARAKDIVIVLKSEIGGSGNQAVVQAIQDLEGIAETTNEPKHMEEVQLPDEEHLETEPEAEGQGQTEAEAMQEALF
Protein: Translin-1 (Meiotically up-regulated gene 90 protein) (Translin homolog) (Q9P7V3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: DNA-binding protein that specifically recognizes consensus sequences at the breakpoint junctions in chromosomal translocations. Selectively binds single-stranded d(GT)n and d(GTT)n microsatellite repeats. Has much higher affinities for the homologous RNA sequences (GU)n and (GUU)n. Does not bind double-stranded DNA. Has a role in meiosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Translin-associated protein X homolog
- Protein argonaute
- Pre-mRNA-splicing factor srp1
- UV-induced protein uvi31
Sequence:
MNKSIFIQLQDQIDKEHSIREKLTAEVDLLDEKLRVLQLLLANCEQNLENQEEILEALEIIKSKTRGLAELASNFPYYKYNGVWDRSIQKVVYLYLLASWTGRLDKSLRPTYSLLSLSEVGQILQVPVFPEESTFHLSIEQYLHAVLSLCSELARQSVNSVISGNYHIPFEALNTIQKVHSSFQVLSLKNDSLRRHFDGLKYDLKRSEDVVYDLRIHKLV
Protein: Dynein light chain (Q38BD2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|RuleBase:RU365010}.
Interaction partners:
Sequence:
MTSNVKEPDGPCNIDTIRQYVTPLNYPLEKMSDMAEEMRAECKEIVVNAIEKHEDSYELAARHIKEQMDKKYGPSWHCVMGEGFGFEISYEMKHLMYMFHKGYVAIVVFKGL
Protein: Reticulon-like protein B5 (AtRTNLB5) (O82352)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Reticulon-like protein B18
- non-specific serine/threonine protein kinase
- BAG family molecular chaperone regulator 8, chloroplastic
- Uncharacterized protein
- O-fucosyltransferase 15
- Ras-related protein RABE1a
Sequence:
MAEEIEKSVPTEESLMEKISEKIHHHDSSSSSESEYEKPDSPSAVKAKIYRMFGREKPVHKVLGGGKPADVFLWRDKKLSGAVLGVATAIWVLFELVEYHLLSLLCHISILALGGLFLWSNAHTLINKTSPQIPEIHVPEEAFLVVASSLRNELNQAFVILRSIALGRDLKKFLMVVVGLWIISVVGNWFNFLTLVYICFVILHTVPMLYEKHEDKVDPLAEKAMKELQKQYVVFDEKVLSKIPIASLKAKAKLG
Protein: Glutamate decarboxylase (Q8I4D9)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MLCSRILLRKSCEDVLRLGVRTGHPRFFNQISCGLDLVSMAGEWLTATANTNMFTYEIAPVFILMEKSVMARMWEAVGWDPEKADGIFAPGGAIANLYAMNAARHQLWPRSKHLGMKDIPTLCCFTSEDSHYSIKSASAVLGIGADYCFNIPTDKNGKMIPEALEAKIIECKKEGLTPFFACCTAGSTVYGAFDPLERVANICERHKLWFHVDAAWGGGMLLSPEHRYKLAGIERANSVTWNPHKLMGALLQCSACLFRQDGLLFQCNQMSADYLFQQDKPYDVSFDTGDKAIQCGRHNDVFKLWLMWKSKGMEGYRQQINKLMDLANYFTRRIKETEGFELIIENPEFLNICFWYVPSKIRNLEPAEMRARLEKIAPKIKAGMMQRGTTMVGYQPDKQRPNFFRMIISNQAITREDLDFLIKEIVDIGESLE
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (F1LNJ1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Alpha-synuclein
- Parkinson disease protein 7 homolog
- Serine/threonine-protein kinase PINK1, mitochondrial
- Tyrosine-protein kinase
- E3 ubiquitin-protein ligase parkin
- Ras-related protein Rab-7L1
- Segment polarity protein dishevelled homolog DVL-1
- Catenin beta-1
- Moesin
- Stratifin
Sequence:
MASGACQGCDEEEEEEALKKLIVRLNNVQEGKQIETLLQLLEDILVFTYSDRASKLFEGKNVHVPLLIVLDSYMRVASVQQVGWSLLCKLIEVCPGTLQSLIGPQDIGNDWEVLGIHRLILKMLTVHHANVNLSIVGLKALDLLLDSGKITLLILDEECDVFLLIFDAMHRYSANEEVQKLACKALHVLFERVSEEQLTEFVENKDYMTLLSTFRSFKRDEEIVHHVLCCLHSLAVTCSNVEVLMSGNVRCYNIVVEAMKTFPTSENIQEVSCSLLHKLTLGNFFNILVLNEVHVFVVKAVQRYPENVALQISALSCLALLTETIFLNQDLEERSETQENSDEDSEKPFWLEPCYKALMRHRKNKHVQEAACWALNNLLMYQSSLHEKIGDEDGQFPAHREVMLSMLMHSSSKDVFQAAAHALSTLLEQNVNFRKILLAKGVYLNVLELMQRHAQVPEVAESGCKMLSHLFEGSNPSLDTVAAVIPKILTVMRTHGTSLSVQLEALRALLHFVVPGVSEDSRDDSRCQPNVLRTQCFRTDIHKLVLAALNRFIGNPGIQKCGLKVISSFAHLPDALEMLSLHGAVDSVLHTLQMYPDDQEIQCLGLHLMGCLMTKKNFCIGTGHLLAKILASTLQRFKDVAEVQTTGLQTVLSMLDLSVSFSKLLVHYSFDVVMFHQMSSGVLEQKDEQFLNLCCKCFAKVAVDDELKSKMLERACDQNNSIMVECLLLLGADANQAKGATSLIYQVCEKESSPKLVELLLNSGCREQDVRKALTVSIQKGDNQVISLLLRRLALDLANNSICLGGFCIGKLDPSWLGPLFPDKSSNLRKQTNAGSVLARKVLRYQMRNTLQEGVASGSEGNFSEDALAKFGEWTFIPDSSMDSVFGQSDDLDSEGSESSFLVKKKSNSVSVGEVYRDLALQRCSPNAQRHSSSLGPVFDHEDLLRRKRKILSSDESLRSSRLQSHTRQSDSSSSLASEREHITSLDLSANELKDIDALGQKCCLSSHLEHLTKLELHQNSLTSFPQQLCETLKCLTHLDLHSNKFATFPSFMLKMPSVIHLDASRNDIGPTVVLDPVVKCPSLKQFNLSYNQLSSIPENLDQVVEKLEQLLLEGNKISGICSPLSLKELKILNLSKNHIPSLPEDFLEACPKVESFSARMNFLAAMPALPSSITSLKLSQNSFTCIPEAIFSLPHLRSLDMSHNNIEHLPGPAHWKSLNLRELIFSKNQISTLDLSENPHIWSRVEKLHLSHNKLKEIPPEIGRLENLTSLDVSYNLELRSFPNEMGKLSKIWDLPLDGLHLNFDFKHIGCKAKDIIRFLQQRLKKAVPYNRMKLMIVGNTGSGKTTLLQQLMKMKKSELGMQGATVGIDVRDWPIQIRGKRKKDLVLNVWDFAGREEFYSTHPHFMTQRALYLAVYDLSKGQAEVDAMKPWLFNIKARASSSPVILVGTHLDVSDEKQRKACIGKITKELLNKRGFPTIRDYHFVNATEESDALAKLRKTIINESLNFKIRDQPVVGQLIPDCYVELEKIILSERKAVPTEFPVINRKHLLQLVKEHQLQLDENELPHAVHFLNESGVLLHFQDPALQLSDLYFVEPKWLCKVMAQILTVKVDGCLKHPKGIISRRDVEKFLSKKKRFPKNYMAQYFKLLEKFQIALPIGEEYLLVPSSLSDHRPVIELPHCENSEIIIRLYEMPYFPMGFWSRLINRLLEISPFMLSGRERALRPNRMYWRQGIYLNWSPEAYCLVGSEVLDSRPESFLKITVPSCRKGCILLGRVVDHIDSLMEEWFPGLLEIDICGEGETLLKKWALYSFNDGEEHQKILLDELMKKAEEGDLLINPDQPRLTIPISQIAPDLILADLPRNIMLNNDELEFEEAPEFLLGDGSFGSVYRAAYEGEEVAVKIFNKHTSLRLLRQELVVLCHLHHPSLISLLAAGIRPRMLVMELASKGSLDRLLQQDKASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNAAIIAKIADYGIAQYCCRMGIKTSEGTPGFRAPEVARGNVIYNQQADVYSFGLLLHDIWTTGNRIMEGLRFPNEFDELAIQGKLPDPVKEYGCAPWPMVEKLITKCLKENPQERPTSAQVFDILNSAELICLMRHIFIPKDITVECIAATNLNSKRATLWLGCGNTEKGQLSLLDLNTERYSYEEVTDSRILCLALVHLAAEKESWVVCGTQSGALLVINAEDETRRHTLDKMTDSVTCLYCNSFAKQSKQSHFLLVGTADGNLMIFEDKTIKCKGAAPLKTLHIGDVSTPLMCLSESMNSSERHITWGGCGTKIFSFSNDFTIQKLIETRTNQLFSYSAFSDSNIIAVAVDTALYIAKKNSPVVEVWDKKTEKLCELIDCVHFLKEVMVKINKDSKHKLSYSGRVKALCLQKNTALWIGTGGGHILLLDLSTRRVIRTIHNFCDSVRAMATAQLGSLKNVMLVLGYKRKSTEGTQEQKEIQSCLSIWDLNLPHEVQNLEKHIEVRTELADKMRKTSVE
Protein: Splicing factor 3A subunit 2 (Q6AXT8)
Organism: Rattus norvegicus (Rat)
Function: Involved in pre-mRNA splicing as a component of the splicing factor SF3A complex that contributes to the assembly of the 17S U2 snRNP, and the subsequent assembly of the pre-spliceosome 'E' complex and the pre-catalytic spliceosome 'A' complex. Involved in pre-mRNA splicing as a component of pre-catalytic spliceosome 'B' complexes, including the Bact complex. Interacts directly with the duplex formed by U2 snRNA and the intron.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00130}.
Interaction partners:
- Splicing factor 3A subunit 1
- Splicing factor 3a, subunit 3
- Splicing factor 3B subunit 3
- Splicing factor 3B subunit 5
- Splicing factor 3B subunit 4
- Splicing factor 3b, subunit 2
- Pre-mRNA-processing factor 6
- Small nuclear ribonucleoprotein polypeptide A'
- PHD finger-like domain-containing protein 5A
- Splicing factor 3B subunit 1
Sequence:
MDFQHRPGGKTGSGGVASSSESNRDRRERLRQLALETIDINKDPYFMKNHLGSYECKLCLTLHNNEGSYLAHTQGKKHQTNLARRAAKEAKEAPAQPAPEKVKVEVKKFVKIGRPGYKVTKQRDTEMGQQSLLFQIDYPEIAEGVMPRHRFMSAYEQRIEPPDRRWQYLLMAAEPYETIAFKVPSREIDKAEGKFWTHWNRETKQFFLQFHFKMEKPPAPPSLPAGPPGVKRPPPPLMNGLPPRPPLPDALPPPPPGGLPLPPMPPTGPAPSGPPGPPQMPPPAPGVHPPAPVVHPPTSGVHPPAPGVHPPAPVVHPPTSGVHPPAPGVHPPAPGVHPPAPGVHPPAPGVHPPAPGVHPPAPGVHPPAPGVHPPAPGVHPPPSAGVHPQAPGVHPPAPAVHPQAPGVHPPAPGIHPQAPGVHPQPPPGVHPAAPGVHPQPPGVHPTPMPPMLRPPLPSDGPGNMPPPPPGN
Protein: 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha (EC 2.3.1.51) (1-acylglycerol-3-phosphate O-acyltransferase 1) (1-AGP acyltransferase 1) (1-AGPAT 1) (Lysophosphatidic acid acyltransferase alpha) (LPAAT-alpha) (Protein G15) (Q99943)
Organism: Homo sapiens (Human)
Function: Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21873652, ECO:0000269|PubMed:9461603}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
- 1-acyl-sn-glycerol-3-phosphate acyltransferase delta
- Membrane-bound glycerophospholipid O-acyltransferase 2
- Phosphatidate cytidylyltransferase 2
- Phosphatidate cytidylyltransferase 1
- 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon
- Phospholipid phosphatase 2
- Phospholipid phosphatase 3
- Lysocardiolipin acyltransferase 1
- Phospholipid phosphatase 5
Sequence:
MDLWPGAWMLLLLLFLLLLFLLPTLWFCSPSAKYFFKMAFYNGWILFLAVLAIPVCAVRGRNVENMKILRLMLLHIKYLYGIRVEVRGAHHFPPSQPYVVVSNHQSSLDLLGMMEVLPGRCVPIAKRELLWAGSAGLACWLAGVIFIDRKRTGDAISVMSEVAQTLLTQDVRVWVFPEGTRNHNGSMLPFKRGAFHLAVQAQVPIVPIVMSSYQDFYCKKERRFTSGQCQVRVLPPVPTEGLTPDDVPALADRVRHSMLTVFREISTDGRGGGDYLKKPGGGG
Protein: Kappa-type opioid receptor isoform 1 (Opioid receptor, kappa 1) (B3DGN0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Pro-opiomelanocortin protein
- Prodynorphin.
- Proenkephalin a
- Prepronociceptin a.
Sequence:
MDSNVVQIFKEDKCPSSHPEKCLPNFTWQSAVSDIYNSSLNESWTTEQEAMSPLIPIITAVYSVVFVVGLVGNCLVMYVIIRYTKMKTATNIYIFNLAVADALVTTTMPFQSTDYLLNSWPFGEVVCKVFISIDYYNMFTSIFTLTMMSVDRYVAVCHPVKALDFRTPMKAKIINILIWVLSSAAGIPAMVLGSTQTNNGTTECALQFPDPYVYWDTLMKICVFIFGFVAPLLIITVCYTLMVLRLKSVRLLSGSREKDRNLRRITRLVLVVVAVFVVCWTPIHIFILVKALSHGVPETTSVMAAYFFCVALGYTNSSLNPILYAFLDENFKRCFRDFCCPGRTAGDGRGVSRVRSTLREHTCPAEAKNDGGQGRPV
Protein: 3'(2'),5'-bisphosphate nucleotidase (EC 3.1.3.7) (3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase) (DPNPase) (Halotolerance protein tol1) (Inositol-polyphosphate 1-phosphatase) (EC 3.1.3.57) (Target of lithium protein 1) (O94505)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Regulates the flux of sulfur in the sulfur-activation pathway by converting PAPS to APS.
Interaction partners:
- Adenylyl-sulfate kinase
- Sulfate adenylyltransferase
- Probable phosphoadenosine phosphosulfate reductase
- 5'-3' exoribonuclease 2
- tRNA
Sequence:
MSFDAEKQLAIAAVRRASYLTEKVFNQLIKEKSAAGALTKDDKSPVTIGDFGAQAIVISMLKDAFPNDPIVGEEDSDFLRENTQTCSRVWELVQETIQHATEYKELGQIKSAEEMMSIIDQGSYHGGRNGRMWTLDPIDGTKGFLRGAQYAICLALIENGKPVVSAIGCPNLPYDFNQPETSPKGIIMSAVRNHGCFQYSLHNEKLEPVQVHMQDVQNTKDSKFCEGVEAGHSMQGTQEEIAKYLGITRGPTKMDSQAKYASLARGDGDIYLRLPTKMTFEEKIWDHAGGSLLVEEAGGVVSDMFGKPLDFGVGRTLKNNNGVIAAYKGIFEKVIEATAAVTSKDPHFQKVAQ
Protein: Epididymis secretory sperm binding protein (IQ motif and Sec7 domain ArfGEF 1) (A0A0C4DGT3)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MLERKYGGRLVTRHAARTIQTAFRQYQMNKNFERLRSSMSENRMSRRIVLSNMRMQFSFEGPEKVHSSYFEGKQVSVTNDGSQLGALVSPECGDLSEPTTLKSPAPSSDFADAITELEDAFSRQVKSLAESIDDALNCRSLHTEEAPALDAARARDTEPQTALHGMDHRKLDEMTASYSDVTLYIDEEELSPPLPLSQAGDRPSSTESDLRLRAGGAAPDYWALAHKEDKADTDTSCRSTPSLERQEQRLRVEHLPLLTIEPPSDSSVDLSDRSERGSLKRQSAYERSLGGQQGSPKHGPHSGAPKSLPREEPELRPRPPRPLDSHLAINGSANRQSKSESDYSDGDNDSINSTSNSNDTINCSSESSSRDSLREQTLSKQTYHKEARNSWDSPAFSNDVIRKRHYRIGLNLFNKKPEKGVQYLIERGFVPDTPVGVAHFLLQRKGLSRQMIGEFLGNRQKQFNRDVLDCVVDEMDFSTMELDEALRKFQAHIRVQGEAQKVERLIEAFSQRYCICNPGVVRQFRNPDTIFILAFAIILLNTDMYSPNVKPERKMKLEDFIKNLRGVDDGEDIPREMLMGIYERIRKRELKTNEDHVSQVQKVEKLIVGKKPIGSLHPGLGCVLSLPHRRLVCYCRLFEVPDPNKPQKLGLHQREIFLFNDLLVVTKIFQKKKNSVTYSFRQSFSLYGMQVLLFENQYYPNGIRLTSSVPGADIKVLINFNAPNPQDRKKFTDDLRESIAEVQEMEKHRIESELEKQKGVVRPSMSQCSSLKKESGNGTLSRACLDDSYASGEGLKRSALSSSLRDLSEAGVHH
Protein: GTP-binding protein ERG (O82653)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Has a crucial role in plant growth and development, possibly by influencing mitochondrial division.
Interaction partners:
- Small ribosomal subunit protein mS29
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- At1g64880
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein uS9c
- EMBRYO DEFECTIVE 3147
- Small ribosomal subunit protein bS16cz
- Small ribosomal subunit protein bS16cy
- Small ribosomal subunit protein bS16m/bS16c
- Short integuments 2, mitochondrial
Sequence:
MKAFRSLRILISISRTTTKTTPRNPHQAQNFLRRFYSAQPNLDEPTSINEDGSSSDSVFDSSQYPIDDSNVDSVKKPKEATWDKGYRERVNKAFFGNLTEKGKVKVAEEESSEDDEDSVDRSRILAKALLEAALESPDEELGEGEVREEDQKSLNVGIIGPPNAGKSSLTNFMVGTKVAAASRKTNTTTHEVLGVLTKGDTQVCFFDTPGLMLKKSGYGYKDIKARVQNAWTSVDLFDVLIVMFDVHRHLMSPDSRVVRLIKYMGEEENPKQKRVLCMNKVDLVEKKKDLLKVAEEFQDLPAYERYFMISGLKGSGVKDLSQYLMDQAVKKPWEEDAFTMSEEVLKNISLEVVRERLLDHVHQEIPYGLEHRLVDWKELRDGSLRIEQHLITPKLSQRKILVGKGGCKIGRIGIEANEELRRIMNRKVHLILQVKLK
Protein: Hepatocyte growth factor-like protein (Macrophage stimulatory protein) (Macrophage-stimulating protein) (MSP) [Cleaved into: Hepatocyte growth factor-like protein alpha chain; Hepatocyte growth factor-like protein beta chain] (P26927)
Organism: Homo sapiens (Human)
Subcellular location: Secreted.
Interaction partners:
- Macrophage-stimulating protein receptor
- Kunitz-type protease inhibitor 1
- Acylamino-acid-releasing enzyme
- Serine protease hepsin
- Kunitz-type protease inhibitor 2
- Protein salvador homolog 1
- Hepatocyte growth factor receptor
Sequence:
MGWLPLLLLLTQCLGVPGQRSPLNDFQVLRGTELQHLLHAVVPGPWQEDVADAEECAGRCGPLMDCRAFHYNVSSHGCQLLPWTQHSPHTRLRRSGRCDLFQKKDYVRTCIMNNGVGYRGTMATTVGGLPCQAWSHKFPNDHKYTPTLRNGLEENFCRNPDGDPGGPWCYTTDPAVRFQSCGIKSCREAACVWCNGEEYRGAVDRTESGRECQRWDLQHPHQHPFEPGKFLDQGLDDNYCRNPDGSERPWCYTTDPQIEREFCDLPRCGSEAQPRQEATTVSCFRGKGEGYRGTANTTTAGVPCQRWDAQIPHQHRFTPEKYACKDLRENFCRNPDGSEAPWCFTLRPGMRAAFCYQIRRCTDDVRPQDCYHGAGEQYRGTVSKTRKGVQCQRWSAETPHKPQFTFTSEPHAQLEENFCRNPDGDSHGPWCYTMDPRTPFDYCALRRCADDQPPSILDPPDQVQFEKCGKRVDRLDQRRSKLRVVGGHPGNSPWTVSLRNRQGQHFCGGSLVKEQWILTARQCFSSCHMPLTGYEVWLGTLFQNPQHGEPSLQRVPVAKMVCGPSGSQLVLLKLERSVTLNQRVALICLPPEWYVVPPGTKCEIAGWGETKGTGNDTVLNVALLNVISNQECNIKHRGRVRESEMCTEGLLAPVGACEGDYGGPLACFTHNCWVLEGIIIPNRVCARSRWPAVFTRVSVFVDWIHKVMRLG
Protein: Rumba zinc finger protein (Zinc finger protein 574) (D2KMS9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MESSSVYMCFPCYREFPTLEEVLAHQMTCTAENPQLLPNETPVEAAAAAAGLPQVAMQAVTVPQIQTQTAVDLSSLLQQKKTIQADAPRVLYQCADCEVLFDALSLWQQHRKMGCCLETEPAGEQTGETYEAVAQPQPSQKENENAVQEQNTPEQTQVKEVVEIRFESVSQGSVEVAGKVAAPATSEEEESSNSVSKEASATHEASSVETSAEASSPATRRRGQKKAKPPSSLLCVECGQSFSLVPELVTHRRTQHGLKDAIHRCAVCGEGFLNTTLFLYHRRQHRSEVEEEPKQASSGIPQISTAMLEAPGEGLLLLATAGEGQSLMEVTTLEQTITETPVAQVEVELEGNEMRGTEQEPMVEGAEILVEKTEEMLEEHEAPDQEVKMELVIEKVEGNVQMEKIGADEEIQDAVESNASENTSTAFLCHQCGSVFSNDQELAKHRKAEHGLEAALHTCGDCGAKFMSTTQFLYHRRQHKNTTAGHLVTAEVKSRLYTTAASATGAAAAADGGLEAPAKLSREWSRTALPHECPHCGQGFTRRSRLREHVFQHTGEKLFNCKICKKSFPSPANLLRHSLIHGGSRIYSCPICDKRFFQPTSLKRHMMTHQEGVQERRTRGRGKGRGPSSDGRLHICPECPASFKLEAQLKSHRLLHTSHPFPCSVCGEAFIRRKELDLHSLIHQDKEPKMCPNCGSQFLNQTVLDTHLQRCTGEQTGQRKYKGQGRGKVGGQLECDMCGHRCVTQDGLDLHRLSHTGQTPLRCPLAPCRRRFASSAALGEHLVAHCCGALGKRNAPRRFTCEFCGKEFAYASTFTVHMRTHTNERPFECAQCGKRFRQLPHLQDHERIHSGERPFTCWVCGKSFSVAARLTEHARVHSGERPYVCPRCPTAFRSRPNLDKHMRIHANDPVDPTAQNVMDDDAAVQTILLVQESASSSPSSSSSVMPVVQEGMFVTEEGGSSVVFLHPNMSMPTITVPAISVPSMNMPNISVVAGQDVPHTIEVILEETV
Protein: Lysophosphatidylserine lipase ABHD12 (EC 3.1.-.-) (2-arachidonoylglycerol hydrolase ABHD12) (Abhydrolase domain-containing protein 12) (Monoacylglycerol lipase ABHD12) (EC 3.1.1.23) (Oxidized phosphatidylserine lipase ABHD12) (EC 3.1.-.-) (Q08C93)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Lysophosphatidylserine (LPS) lipase that mediates the hydrolysis of lysophosphatidylserine, a class of signaling lipids that regulates immunological and neurological processes (By similarity). Represents a major lysophosphatidylserine lipase in the brain, thereby playing a key role in the central nervous system (By similarity). Also able to hydrolyze oxidized phosphatidylserine; oxidized phosphatidylserine is produced in response to severe inflammatory stress and constitutes a proapoptotic 'eat me' signal. Also has monoacylglycerol (MAG) lipase activity: hydrolyzes 2-arachidonoylglycerol (2-AG), thereby acting as a regulator of endocannabinoid signaling pathways. Has a strong preference for very-long-chain lipid substrates; substrate specificity is likely due to improved catalysis and not improved substrate binding (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8N2K0}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- acylglycerol lipase
- N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
- Abhydrolase domain-containing 16A.
- Abhydrolase domain-containing 4.
- Abhydrolase domain-containing 6b.
- Fatty acid amide hydrolase.
- Fatty-acid amide hydrolase 2-A
- Glycerophosphodiester phosphodiesterase 1.
Sequence:
MRKRKGSADHDSSFTATLTDGSSDLKQCHKGTDADTDPGGSGKEMGRRCRRGGLMWRLRRILIWLLGIYIAIPVIIKVCPSIQAKLVFLNFVRVPYFIDLKRPQDQGMNHTHNFYLQPEEGINIGVWHTVPAGMWREAQAKDAEWYEKSFQSSHPVILYLHGNAGTRGGDHRVQLYKVLSSLGYHVVTFDYRGWGDSEGSPSERGMTSDALFLYQWIKQRIGPKPLYIWGHSLGTGVATNLVRRLCDRGTPPDALILESPFTNIREEAKSHPFSMVYRYLPGFDWFFLDAISANDIRFASDENVNHISCPVLILHAEDDTVVPFQLGKKLYDLAAQSKSLNGHKVQFIPFSSSLGYRHKFIYKSPQLPNILSDFLRAPHPHG
Protein: UDP-glucuronosyltransferase 3A2 (UDPGT 3A2) (EC 2.4.1.17) (Q3SY77)
Organism: Homo sapiens (Human)
Function: UDP-glucuronosyltransferases catalyze phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase water solubility and enhance excretion. They are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds (By similarity).
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- UDP-galactose translocator
Sequence:
MAGQRVLLLVGFLLPGVLLSEAAKILTISTVGGSHYLLMDRVSQILQDHGHNVTMLNHKRGPFMPDFKKEEKSYQVISWLAPEDHQREFKKSFDFFLEETLGGRGKFENLLNVLEYLALQCSHFLNRKDIMDSLKNENFDMVIVETFDYCPFLIAEKLGKPFVAILSTSFGSLEFGLPIPLSYVPVFRSLLTDHMDFWGRVKNFLMFFSFCRRQQHMQSTFDNTIKEHFTEGSRPVLSHLLLKAELWFINSDFAFDFARPLLPNTVYVGGLMEKPIKPVPQDLENFIAKFGDSGFVLVTLGSMVNTCQNPEIFKEMNNAFAHLPQGVIWKCQCSHWPKDVHLAANVKIVDWLPQSDLLAHPSIRLFVTHGGQNSIMEAIQHGVPMVGIPLFGDQPENMVRVEAKKFGVSIQLKKLKAETLALKMKQIMEDKRYKSAAVAASVILRSHPLSPTQRLVGWIDHVLQTGGATHLKPYVFQQPWHEQYLLDVFVFLLGLTLGTLWLCGKLLGMAVWWLRGARKVKET
Protein: Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (SMAD family member 7) (SMAD 7) (Smad7) (O88406)
Organism: Rattus norvegicus (Rat)
Function: Antagonist of signaling by TGF-beta (transforming growth factor) type 1 receptor superfamily members; has been shown to inhibit TGF-beta (Transforming growth factor) and activin signaling by associating with their receptors thus preventing SMAD2 access. Functions as an adapter to recruit SMURF2 to the TGF-beta receptor complex. Also acts by recruiting the PPP1R15A-PP1 complex to TGFBR1, which promotes its dephosphorylation. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O15105}. Cytoplasm {ECO:0000250|UniProtKB:O15105}. Note=Interaction with NEDD4L or RNF111 induces translocation from the nucleus to the cytoplasm. TGF-beta stimulates its translocation from the nucleus to the cytoplasm. PDPK1 inhibits its translocation from the nucleus to the cytoplasm in response to TGF-beta. {ECO:0000250|UniProtKB:O15105}.
Interaction partners:
- E3 ubiquitin-protein ligase
- E3 ubiquitin-protein ligase
- TGF-beta receptor type-1
- RING-type E3 ubiquitin transferase
- TGF-beta receptor type-2
- Transforming growth factor beta-1 proprotein
- Transcriptional coactivator YAP1
- Mothers against decapentaplegic homolog
- Mothers against decapentaplegic homolog 2
- Receptor protein serine/threonine kinase
Sequence:
MFRTKRSALVRRLWRSRAPGGEDEEEGVGGGGGGGGLRGEGATDGRAYGAGGGGAGRAGCCLGKAVRGAKGHHHPHPPSSGAGAAGGAEADLKALTHSVLKKLKERQLELLLQAVESRGGTRTACLLLPGRLDCRLGPGAPASAQPAQPPSSYSLPLLLCKVFRWPDLRHSSEVKRLCCCESYGKINPELVCCNPHHLSRLCELESPPPPYSRYPMDFLKPTADCPDAVPSSDETGGTNYLAPGGLSDSQLLLEPGDRSHWCVVAYWEEKTRVGRLYCVQEPSLDIFYDLPQGNGFCLGQLNSDNKSQLVQKVRSKIGCGIQLTREVDGVWVYNRSSYPIFIKSATLDNPDSRTLLVHKVFPGFSIKAFDYEKAYSLQRPNDHEFMQQPWTGFTVQISFVKGWGQCYTRQFISSCPCWLEVIFNSR
Protein: AT4g39150/T22F8_50 (DNAJ heat shock N-terminal domain-containing protein) (DnaJ-like protein) (Q9T024)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Very-long-chain aldehyde decarbonylase CER3
- Fatty acyl-CoA reductase 3
- Very-long-chain
Sequence:
MVKESEYYDILGVKIDASGAEIKKAYYVQARQVHPDKNPGDPQAAKNFQILGEAYQVLGDPEKRTAYDKYGKEGVQQDAMVDPAAVFGMLFGSELFEDYVGQLALASAASIDAELESYEPEIRKQMLQEKIKAIQKDRVDKLVTTLKIKLEPFVEGQTDEFVNWATAEAKRLSTAGFGEAMLHTVGYIYTRKAAKELGKDKRFMKVPFLAEWVRDKGHQVKSQVMAASGAVNLLLLQDEVSKLNQGENKEENIQKAIEAKKDAMLQSLWQINVVDIESTLSRVCQAVLKDPSVSKDVLRARARGLRKLGNVFQGSKKAYSRENSLRHEEETGVKVHTGDSSKPAT