wanglab/gogpt-training-data huggingface dataset:
Protein: Interleukin cytokine receptor-related protein 1 (Interleukin-17 receptor-like protein 1) (Q9NA64)
Organism: Caenorhabditis elegans
Function: Forms a receptor complex together with receptor ilcr-2, which upon activation acts as a modulator of neuronal activity. Binding of the ligand ilc-17.1 to the ilcr-1/2 receptor complex triggers a signaling cascade that activates the downstream signaling components actl-1, pik-1 and nfki-1, and results in increased neuronal activity in RMG interneurons in response to input from oxygen-sensing neurons. This leads to increased animal movement and promotes aggregation behavior.
Subcellular location: Cell membrane {ECO:0000269|PubMed:28099418}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Interleukin cytokine receptor-related protein 2
- ACT1-like protein
- Interleukin cytokine-related protein 17.1
- ANK repeat-containing protein nipk-1
- Interleukin-17
- Clip domain-containing protein
- Pelle-like serine/threonine-protein kinase pik-1
- FMRFamide-like neuropeptides 6
Sequence:
MFLHSPALLIWLFLFCLAGPQAVRTEPYNSTSSSSSPTANDVTSSDLLLLASEETPTRAPKPVTKQGKKNVVKVKKGGNGTVDDSPWVTDCSEPLNKDISCSVNIIGCSDNVFKYVDAGQEPPRAHDVRIAPTTKVMGANRIDKRKHRLHVDVSWQIPQLEASTHLKAFKLIVNGPDGKNTCFVFNVTQTHVDDEGISPRYRFSSNTLFDFGHNYTVTIVSLPMSRKRAPKVSATSLMPDDPDAAPVKIVKTNEQMCEGKSNPQASKWAASFRKIFLFSAIRLIQIEFLAAPPQYCFEEYEVRLLDSSGIVMLQSAIITKDELRTEIINGRPVQFGEFNFTDIELDTDLIPSVIPIESAHDGRCLCVTENGCSCLAADWKPVKLTRIEKPPATSNQTEESDGKAEKDKKEDTTWTWHTYAITGGAIIAILFILSVCAGLKCYKKFNNKKKASNIHLLNENPAFSHSGSIPLILKQSISVLIVYSHDSAQHEAAVLAFAELLRDVFNLNVHLDVWDEDDIEENRAEYINSSIVRANKVIIINSIGAYFRTVFRHQREPAIERITTGRNDVIFDMQCELALQHPCVISCHFSYTNPKYVFFPINRLLQYSIPNSLMTMTTALTEQPARPEQLAGFNQVFARLQAAISRKLNYIESDPQWFENTHHRVATRRVSELEAHNIVPLPPSLEVKVEDEDAFGQMETLPIDELKEKFAAKRDLEVEVLDSEDVKLLEDVKCAPGPIHVEPTEPEVLEPAEEPMEEAEEDEEDEDDVDSVEGQTARIEELQRLIVHKDMNHDSGNLDSAYVSGSDFSADIHNEILDKPRLNAEMDLRKANREDSAFHDEVIGIH
Protein: Precursor of CEP11 (PCEP11) [Cleaved into: C-terminally encoded peptide 11 (CEP11)] (P0DN98)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Extracellular signaling peptide that may regulate primary root growth rate and systemic nitrogen (N)-demand signaling (By similarity). Mediates up-regulation of genes involved in N uptake and assimilation pathways.
Subcellular location: [C-terminally encoded peptide 11]: Secreted, extracellular space, apoplast {ECO:0000250|UniProtKB:O80460}. Note=Accumulates in xylem sap. {ECO:0000250|UniProtKB:O80460}.
Interaction partners:
- Precursor of CEP15
- Precursor of CEP8
- Precursor of CEP14
- Precursor of CEP4
- Precursor of CEP7
- Precursor of CEP6
- Precursor of CEP13
- Protein IDA-LIKE 5
- Precursor of CEP9
- Protein IDA-LIKE 4
Sequence:
MAKTRRVIYLFLTIVLLFCELIDEAQGSRFRCHHSEDYSCKKRSSHHHHHHHHHQQQQHHHKDTPPEELQGSIKTRRSKDIYGLNAFRSTEPGHSPGVGHLIKT
Protein: Exocyst complex component 5 (Exocyst complex component Sec10) (Q9XTM1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Interaction partners:
- Exocyst complex component 7
- Exocyst complex component 3
- Exocyst complex component 2
- Exocyst complex component 8
- Exocyst complex component 6
- Exocyst complex component 4
- Exocyst complex component 1
- ADP-ribosylation factor 6
- Rab11
- LD44762p
Sequence:
MLSQYMEEFEQEPFEVGEFIERLTWRTNNELQNSEDFHPVALHDTFIQTIKDLKILQEKQQSKCERLEESLRQEKESHAKKIAKLQERHQTAIDVFGQLDEKINSVAGKIMHLGEQLENVNTPRSRSVEAQKLLNFMSEFLAAGPVIVNDIFADAARLSEAADVIQKLYAISQDLPPGNFAESKRKIEKKYDEVERRLIEEFATAQKSEDIERMKTLAQILSQFKGYTQCVDAYIEQSQMQPYSGKDIFIGIVPLCKHHYEIIQKVFANPQQVMSKFILNIYQLKLHQYAMTKLEDKKDEEKYLRTLYELYSRTLKLSTDLQIYMSTIDDDLLQKLTQQIFIKHLAGYAEMETKCLTAKCSTELEKFYASKKHQKTATTKGFRRNMEVLIATRANINIAAIEDYGGETFLSEELAINMLQEAKASLKRCRLLSNETELPGNAIKLNDILLRFLMHEHVDYALELGLQAVPLAEGRVFPQLYFFDVVQKTNIIVHLLDKLCHTSVIPCVSNTPKYSDYVFKKRILMEQIETKLDQGLDRSISAVIGWVKVYLQYEQKKTDYKPETDVDTISSAACLQVVQNLQPVIVQIKKCVDGENLQNVLTEFGTRLHRVIYDHLQTMQFNTAGAMCAICDVNEYRKCIRELDSPLVTQLFDILHALCNLLLVKPQNLQEVCTGDTLNYLDKSVVRQFIQLRTDFRIIKNTNYLKGIIE
Protein: Lectin-related NK cell receptor LY49U (Q9JHV1)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MSEQEVTFPTMRFHKSSGLNSQVRLEGTQRSRKAGLRVCSVPWQLIVIALGILCSLRLVIVAVFVTKIFQYSQHKQEINETLNHHHNCSNMQRDFNLKEEMLTNKSIDCRPSYELLEYIKREQDRWDSETKTVLHSTQNTGRGVKYWFCYSTKCYYFIMNKTTWSGCKANCQHYSVPIVNIEDKDELKFLQRHVITEGYWIGLSYDKKKKEWAWIDNGQSKLDMKIRKMNFKSRGCVFLSKARIEDTDCNIPYYCICGKKLDKFPD
Protein: Geraniol synthase, chloroplastic (PfTps-PL) (EC 3.1.7.11) (Q308N0)
Organism: Perilla frutescens (Beefsteak mint) (Perilla ocymoides)
Function: Monoterpene synthase (mono-TPS) involved in the biosynthesis of monoterpenes natural products. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into geraniol.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MSSISQKVVIGLNKAAANNNLQNLDRRGFKTRCVSSSKAASCLRASCSLQLDVKPVQEGRRSGNYQPSIWDFNYVQSLNTPYKEERYLTRHAELIVQVKPLLEKKMEAAQQLELIDDLNNLGLSYFFQDRIKQILSFIYDENQCFHSNINDQAEKRDLYFTALGFRILRQHGFDVSQEVFDCFKNDSGSDFKASLSDNTKGLLQLYEASFLVREGEDTLEQARQFATKFLRRKLDEIDDNHLLSCIHHSLEIPLHWRIQRLEARWFLDAYATRHDMNPVILELAKLDFNIIQATHQEELKDVSRWWQNTRLAEKLPFVRDRLVESYFWAIALFEPHQYGYQRRVAAKIITLATSIDDVYDIYGTLDELQLFTDNFRRWDTESLGRLPYSMQLFYMVIHNFVSELAYEILKEKGFIVIPYLQRSWVDLAESFLKEANWYYSGYTPSLEEYIDNGSISIGAVAVLSQVYFTLANSIEKPKIESMYKYHHILRLSGLLVRLHDDLGTSLFEKKRGDVPKAVEICMKERNVTEEEAEEHVKYLIREAWKEMNTATTAAGCPFMDELNVAAANLGRAAQFVYLDGDGHGVQHSKIHQQMGGLMFEPYV
Protein: Inner kinetochore subunit MHF2 (CENP-X homolog) (Constitutive centromere-associated network protein MHF2) (MHF histone-fold complex subunit 2) (MPH1-associated histone-fold protein 2) (Q3E829)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DNA-binding component of a FANCM-MHF complex involved in DNA damage repair and genome maintenance. FANCM-MHF promotes gene conversion at blocked replication forks, probably by reversal of the stalled fork (By similarity). Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.
Interaction partners:
- Inner kinetochore subunit MHF1
- ATP-dependent DNA helicase MPH1
- Uncharacterized protein YGR042W
Sequence:
MLSKEALIKILSQNEGGNDMKIADEVVPMIQKYLDIFIDEAVLRSLQSHKDINGERGDKSPLELSHQDLERIVGLLLMDM
Protein: Vacuolar iron transporter homolog 2.1 (Protein NODULIN-LIKE 21) (Vacuolar iron transporter-like 5) (AtVTL5) (Q9LSF6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable vacuolar iron transporter involved in the transfer of iron ions from the cytosol to the vacuole for intracellular iron storage. Involved in regulation of cellular iron homeostasis. Vacuolar iron storage is required for seed embryo and seedling development.
Subcellular location: Vacuole membrane {ECO:0000250|UniProtKB:Q9LPU9}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cation-chloride cotransporter 1
- Solute carrier family 40 member 2
- U-box domain-containing protein 6
- At2g17660 family protein)
- WAT1-related protein At4g08300
- WAT1-related protein At4g01450
- At2g28120/F24D13.9
- Monothiol glutaredoxin-S1
- Zinc transporter 3
- WAT1-related protein At4g08290
Sequence:
MTSNVQLSETNSPRNQKTRPRAEKEEVDYMQRAQWLRAALLGANDGLVTVASLMMGVGSIKEDVKAMLLVGFAGLVAGACSMAIGEFVSVCTQRDIETAQMKRAIEHKTSLSAIDEQEEEEKKERLPNPGQAAIASALAFSVGAAMPLLGAVFIENHKVRMVVVAVVATIALVVFGVTGAVLGKTSVVKSSVRVVIGGWMAMALTFGLTKFIGSAAMQI
Protein: 309 kDa centrosomal protein (Q6UBD8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}.
Interaction partners:
Sequence:
MTIEMADQRTTTTTTTTATTATTPSSANVLATTATTTTTTSSSIEEEIEEAIEISEVEEQLNTPLESLSEAAAYARPKDEQSSAKSLSSNPAEDEDADEFRIDDAQLSGGQLAQHFLVDEDESEEGSDLPAASKVEVSLSSNDDDFDISLPLEQKKPVHSLHEDDESVDQSLSNQSTTDDVSELVEEPVHERDDKTDGSAAISASAPQEPQVDESQITDEQDHSMEEIVATNESIEVTYEAEETVNTSQKQDLITDLDEESEDQVHVDNRPTSTLQALKLPVLQQPQIVERKAATALTTLRLQADVLEPLELTILEMDDDENEEDDDDEESSLQLMKLRLMAMNQQMIVDNAPKLSPTEAEQTQVTSSSNNLEIKQMERVPLTEFSKDVLEDITEESERLLSMSTTMEEEQDPPSLSLDESKTLLQPGAHKTGGSSSSLVSLNMLKQLEAKVQELHTQLETKDNCLASLNLQLETARRESSAGPASARDSSSLMTNSTEYRTLQEELGGPTLDIYVEMSRRDELIAKLTDSLQQSLNVRDKLQVDADRLGGEVQNLRRQLQETLDAVKRSSAVWPDQECNPGQRISEISMDLISESDDDLDRHFLTDNEERGSRSSKERQLTQLQTNEELGLQASNPEWTPTFSKQIEQFHTYLLPTEQRIFQMVQRKFDDYLNQQITLCRDLGAQELKIARDQWESEKLTSEQNQQAAHAKQMEDLRKYFEHKCADLEKQFSDDVFSHKSQHQTGDSSSECSEVDQLPEEGAAAVSSKEPSPRKRKRAELLLSPSHRQMTPCGLDSLGENTGKTEKDNTADIADIKIFYQTHIKELKRAHEDQVRKLSDRIKFYERQQGDDDYKPATESPERTCPDQESAGGVANTSLIIIDEDELNFNNESQVIQRIIEEYEKRLQEQLALARQDIATELEQQIQSLLSENTVDDQHWPKELILLREKFTAKSQLEITQLNIKHAEEMSRLKLEFEKQLNRKNKRHLTFDAARDLEQVICERDGLRELSKSFRSVLCRLAKCVAHCEEDLNATLSEEVQRLLFHSRSQDGGDDLEATISSSLNNTKHMLRVPDVHSLLEVVEDPSLVQFIDSKSNEEPSEDFDLNDCLERLKSEASYLLHLSEDLHKQRTHDESSEHLDEPEKQEHELCCEAEDGLKTTGAVNQQVLSKFLRTNSLNDQQMGVANQRKNSNPEAGKTHSSLPPDLQEHAGNASELSFQLVQLKNRLIKSEADRQNLQQQLSHTIDRNAELGQELQALRDQLSQLNSLNHTDYNEGYGLGTMKSLQEQGLDQSSASFLALQERARHLLSSSPVKEQPSRDHGNSTVILLQMIEDFCREGDKVVEFSKKDREDLQSQIDTADKQLKDTRRFLEDQAAEREQERDEFQREIERLKAQLRDKEKEHSSYANASEEYAQLESQFREVNQQLCESNAKRDKFEVELKASIDKIFVLREIISELETQVQTKALNEEVLAEKAQQLEEYVSLQMRDNDILQQEVHSLKTDIGEGYQSRIRVLEEKLKQSRPTAEQGVVLSQVAEKLRDIETTLDQKTKALESLHNSNATSNSASLSVTEDVSIHGSKEPTAVGSPSHPSLTVEGVQRVTEKLDRHTRVEEAAIKRIRDLEMQVHQMRAGCVELQHERDTLQGRMEEQTQRISTLQNRLEEQRQRAEQLHRTGTSDLNTRVHELQGEVQNLYEQLAARDKQMANMRQQLQRSKEEITRLETEVEVRTQPDRSLVNKLQAEVQQKGAEIVKLKDKIRTEMINRLAIPDLMETMLADKNDEIDHLRDQLEAKEKELQASQQEASQISSPSGAAGKQEGSGGKLSARTLSDIGSITEFPEPDVERRAAMRSLTALQMSEGAGGFLHQTMETSKEAVANLTHKRTDDLSGFIVPCPVNTFEHPHYFQALGVTAQSTDGLTPGLVPRQINFSNLTEDSKLKTTSLLMHTPELPRPTTPPEIHQLRVKLSDLQTEKQRQQSELEKKLQDLQKELEQEKEKLSRQAQTLQSYEESEAKYRLRIENLESKVLETAAQGASDRENLRKELNCVSAAHEQCENAAAARKRELEKLNSEVKVKADQLHAALRRCADLELQVLTLERDLERLKNSDNSSKQYSVDEIAQQVEKELNYSAQLDSNILKAIESEEENNLDKKLQKGVQTEEETLPGTGNGTDDENFTGERELLNQLEALRAQLAVEREQCEAMSKELLGEKQHSQDIQEQDVIIIEAMRKRLETALDAEDELHKQLDQERERCERLQTQLTSLQRAESRRNSSLLLKSPGDSPRKSPRADFESELGDRLRSEIKLLVAQNERERERSADAQRSSERERQRYEKELQERVAYCERLKQEMEKLSRDKESAETELEHFNERLTLQASEIESLEARLVTLQEAETRRANTRTRQHQENVKLQAEIHELKSKLLAAEAARDCLDQKVTQLRFDVSRSGQREAKLAEALAQANDRLAHSTDDNVPAQFMQKMKEINALLAENTQENRQMAETVQFLVGERIALQKKCEELGGAGNTNVTELEERCRQLIGRYLRVESHRKALVYQKRYLKLTLEGYQASEQLALQNLRGGAAQPPQRNIKKKFKTVALAIIAIQRIKYIGRIWHTGKRIVSKSVFTITQQRSPGLNLNVAPPQSPLPGPNSNPPTNNNNLMGRLSYAPLSPPMVNFSTVQPIMLPSDFTLQAPTTSLQTTIANNNSENTLPSLARLDWPTMQKPKRAHARHH
Protein: Putative heat shock 70 kDa protein 7 (Heat shock 70 kDa protein B) (Heat shock protein family A member 7) (P48741)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQAPRELAVGIDLGTTYSCVGVFQQGRVEILANDQGNRTTPSYVAFTDTERLVGDAAKSQAALNPHNTVFDAKRLIGRKFADTTVQSDMKHWPFQVVSEGGKPKVRVCYRGEDKTFYPEEISSMVLSKMKETAEAYLGQPVKHAVITVPTYFSNSQRQATKDAGAIAGLKVLPIINEATAAAIAYGLDRRGAGKRNVLIFDLGGGTFDVSVLSIDAGVFEVKATAGDTHLGGEDFDNRLVNHFMEEFRRKHGKDLSGNKRALRRLRTACERAKRTPSSSTQATLEIDSLFEGVDFYKSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDFVLGGGLHSHPQGAEVAAGLLQRQGAEQEHQP
Protein: MYH11 protein (Myosin heavy chain 11) (A6QLN6)
Organism: Bos taurus (Bovine)
Interaction partners:
- Actin, aortic smooth muscle
- Myosin light chain 9
- Myosin regulatory light polypeptide 9
- Myosin light polypeptide 6
- Actin, gamma-enteric smooth muscle
- Myosin light chain 6B
- Myosin regulatory light chain 12B
- Actin, cytoplasmic 1
- Actin, cytoplasmic 2
- Leiomodin-1
Sequence:
MAQKDQLSEDEKFLFVDKNFINNPVAQADWAAKKLVWVPSEKQGFEAASIKEEKGDEVIVELVENGKKVTVGKDDIQKMNPPKFSKVEDMAELTCLNEASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIIEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAMVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSNGFVPIPAAQDDEMFNETVEAMAIMGFTEEEQLSILRVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPTNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFMADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFRTGVLAHLEEERDLKITDVIMAFQAMCRGYLARKAFAKRQQQLTAMKVIQRNCAAYLKLRNWQWWRLFTKVKPLLQVTRQEEEMQAKEDELQKTKERQQKAESELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRSQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLDGEASDLHEQIAELQAQIAELKMQLAKKEEELQAALGRLDDEMAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTMLKKALDEETRSHESQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKNKQALEKENAELAGELRVLSQAKQEVEHKKKKLEVQLQELQSKYSDGEKVRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVELLEEGKKKFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKVQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAVAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKDELAEELASSVSGRNALQDEKRRLEARIAQLEEELEEEQGNTEAMSERVRKATQQAEQLSNELATERSAAQKNENARQQLERQNKELRSKLQEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQATAKALKQKDKKLKEALLQVEDERKMAEQYKEQAEKGNLRVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVTALKSKLRRGNETSFVPTRRSGGRRVIENADGSEEEMDARDADFNGTKASE
Protein: Uncharacterized protein (Q381P4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRPTDVACVFYRHETLGQSEPIKVCEKISDVFHTVEHHVGKGAAAVPTSNADDDNMSVLHRHLSALAHQESLSMMASYAGYTVQTRSHIAEDLSEKSAELLWKHAAHRAAASIFGTDRCTPRRRALVMGVYITRTSANYFTVGIVTQGDTRDPRIRKAITTLSGTHKLTRLDSELQICAAHRSMSIRLWWEPRSDRVTPRSVMPPIRVILEREQQELSKTCVTYMTGYGAVNIFLCRPVASKLLGTTRKLLNTGECHPTEDAAAWFDGRRFPSCAKETQQRRRLTVVLYFNDLHPVEVGEHLVGVEVEPLPPFRPFVPSQYAHLPPFLVVGRSGA
Protein: Protein SLENDER RICE1-LIKE 1 (Protein SLR1-LIKE 1) (B7F9I5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable transcriptional regulator that acts as a repressor of the gibberellin (GA) signaling pathway. Its repressive activity is weaker than that of SLR1. Its overexpression prevents the GA signaling pathway and induces a dwarf phenotype.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q7G7J6}.
Interaction partners:
- Gibberellin receptor GID1
- DELLA protein SLR1
- F-box protein GID2
- Os04g0618600 protein.
- Os07g0143200 protein
- Transcription factor PHYTOCHROME INTERACTING FACTOR-LIKE 13
- Transcription factor PHYTOCHROME INTERACTING FACTOR-LIKE 15
- Transcription factor APG
- Helix-loop-helix DNA-binding domain containing protein, expressed
- Os01g0885250 protein
Sequence:
MAMDTFPFQWPMDPAASSGLDAGFLPPPAAVAPDDGVGYYDPPAGADVDAAALPEFAAAFPPCAPDAAAAVLAMRREEEEVAGIRLVHLLMSCAGAIEAGDHALASAQLADSHAALAAVSAASGIGRVAVHFTTALSRRLFPSPVAPPTTDAEHAFLYHHFYEACPYLKFAHFTANQAILEAFHGCDHVHVIDFSLMQGLQWPALIQALALRPGGPPFLRITGIGPPSPTGRDELRDVGLRLADLARSVRVRFSFRGVAANSLDEVRPWMLQIAPGEAVAFNSVLQLHRLLGDPADQAPIDAVLDCVASVRPKIFTVIEQEADHNKTGFLDRFTEALFYYSAVFDSLDAASASGGAGNAMAEAYLQREICDIVCGEGAARRERHEPLSRWRDRLTRAGLSAVPLGSNALRQARMLVGLFSGEGHSVEEADGCLTLGWHGRPLFSASAWEAAGDGGGDNNNNSNSNVSGSSGSDSNNSGSSNGKSSGARDGSSVCL
Protein: 7beta-hydroxysteroid dehydrogenase (7beta-HSDH) (EC 1.1.1.201) (NADP-dependent 7beta-hydroxysteroid dehydrogenase) (A7B4V1)
Organism: Mediterraneibacter gnavus (strain ATCC 29149 / DSM 114966 / JCM 6515 / VPI C7-9) (Ruminococcus gnavus)
Function: 7beta-hydroxysteroid dehydrogenase that catalyzes the reduction of the 7-oxo group of 7-oxo-lithocholate (7-oxo-LCA), to yield ursodeoxycholate (UDCA). As R.gnavus is a common core bacterium of the human gut microbiota, this enzyme contributes to the formation of UDCA in the human colon. UDCA is regarded as a chemopreventive beneficial secondary bile acid due to its low hydrophobicity; it protects hepatocytes and bile duct epithelial cells against necrosis and apoptosis induced by more hydrophobic secondary bile acids like deoxycholate (DCA). This enzyme is also able to catalyze the reverse reaction in vitro, i.e. the oxidation of the 7beta-hydroxy group of UDCA to 7-oxo-LCA, but much less efficiently than the reduction reaction.
Interaction partners:
Sequence:
MTLREKYGEWGIILGATEGVGKAFCERLAKEGMNVVMVGRREEKLKELGEELKNTYEIDYKVVKADFSLPDATDKIFAATENLDMGFMAYVACLHSFGKIQDTPWEKHEAMINVNVVTFMKCFYHYMKIFAAQDRGAVINVSSMTGISSSPWNGQYGAGKAFILKMTEAVACETEKTNVDVEVITLGTTLTPSLLSNLPGGPQGEAVMKTAQTPEEVVDEAFEKLGKELSVISGERNKASVHDWKANHTEDDYIRYMGSFYQE
Protein: RAB11 family interacting protein 2 (A0A8I6ASH5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}. Recycling endosome {ECO:0000256|ARBA:ARBA00004172}.
Interaction partners:
Sequence:
MMLSEQAQKWFPTHVQVTVLQAKDLKPKGKSGTNDTYTIIQLGKEKYSTSVAEKTLEPVWKEEASFELPGLLMQGNPEKYILFLIVMHRSLVGLDKFLGQVAINLNDIFEDKQRRKTEWFRLESKQGKRIKNRGEIKVNIQFMRNNMTASMFDLSMKDKTRSPFAKLKDKMKGRKSDGVFSDTSSAIVPSTHMPDANPEFSSGEMQMKSKPKKPFLLGPQRLSSAHSMSDLTGSHLSSEKLKSSTVGPTHLLSHQINSFGVVPESGSLKSPHRRTLSFDTSKLNQPGSIVDEGEHCFGRQSDPFTNVTASLPQKFATLPRKKNPFEESSEPWDSSTNLFSKPIEVRKESKREKREKVSLFERVTGKRDSRRSDKLNNGGSDSPCDLKSPSAFNENRQDYFEYESTNPFTAKFRASTIMPSSSFHMNPTSSDDLRKIPDSNPFDATAGYRSLTYEEVLQELVKHKELLRRKDTHIRELEDYIDNLLVRVMEETPSILRVPYEPSRKAV
Protein: DNA polymerase processivity factor (DNA-binding gene 18 protein) (Polymerase accessory protein) (PAP) (P28958)
Organism: Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus)
Function: Plays an essential role in viral DNA replication by acting as the polymerase accessory subunit. Associates with the viral polymerase to increase its processivity and forms high-affinity direct interactions with DNA. Facilitates the origin-binding protein loading onto DNA thus increasing its ability to assemble into a functional complex capable of unwinding duplex DNA (By similarity).
Subcellular location: Host nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MALPRAMRPGGSHPNNFLFNTLPVIDNPVERQRAMAVFERESLRDAFEMLTPIAPSLKNAFLIFNEDGLLIHTSVGGEQVYIPIQTNNMESYSWKKAPPAVFLANVDGRRGLLDAFKAKTQTNVSKVVFEIENYSPSRILTQTVFSARDQTEEDTEMGSDAEGATQTVSSRLVKHEFNNYALMLPTRQPDVSMSLSKAQLNKILGVCKQAGDPITFQCLFDDTLQVRSGDRQVVFSVDYQHADNCGVESSSSLLEKMPMKTKKSAPEPIRGISGRRLFTLVLDEDTNFKQLIQKLKLKNAGAVLNFFLDPDSIPMIGLSTKQPFSVMMFFMCSYPTQPCQVGFSPAAFSSTPMGAGVKRRASEEEESDQPPKKLFPDGKLFKSNFVLLMDKTGAKIPCPEQPMHF
Protein: Caspase-6 (CASP-6) (CSP-6) (EC 3.4.22.59) (Apoptotic protease Mch-2) [Cleaved into: Caspase-6 subunit p18 (Caspase-6 subunit p20); Caspase-6 subunit p11 (Caspase-6 subunit p10)] (P55212)
Organism: Homo sapiens (Human)
Function: Cysteine protease that plays essential roles in programmed cell death, axonal degeneration, development and innate immunity. Acts as a non-canonical executioner caspase during apoptosis: localizes in the nucleus and cleaves the nuclear structural protein NUMA1 and lamin A/LMNA thereby inducing nuclear shrinkage and fragmentation. Lamin-A/LMNA cleavage is required for chromatin condensation and nuclear disassembly during apoptotic execution. Acts as a regulator of liver damage by promoting hepatocyte apoptosis: in absence of phosphorylation by AMP-activated protein kinase (AMPK), catalyzes cleavage of BID, leading to cytochrome c release, thereby participating in nonalcoholic steatohepatitis. Cleaves PARK7/DJ-1 in cells undergoing apoptosis (By similarity). Involved in intrinsic apoptosis by mediating cleavage of RIPK1. Furthermore, cleaves many transcription factors such as NF-kappa-B and cAMP response element-binding protein/CREBBP. Cleaves phospholipid scramblase proteins XKR4 and XKR9 (By similarity). In addition to apoptosis, involved in different forms of programmed cell death. Plays an essential role in defense against viruses by acting as a central mediator of the ZBP1-mediated pyroptosis, apoptosis, and necroptosis (PANoptosis), independently of its cysteine protease activity. PANoptosis is a unique inflammatory programmed cell death, which provides a molecular scaffold that allows the interactions and activation of machinery required for inflammasome/pyroptosis, apoptosis and necroptosis. Mechanistically, interacts with RIPK3 and enhances the interaction between RIPK3 and ZBP1, leading to ZBP1-mediated inflammasome activation and cell death. Plays an essential role in axon degeneration during axon pruning which is the remodeling of axons during neurogenesis but not apoptosis (By similarity). Regulates B-cell programs both during early development and after antigen stimulation (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:27911442}. Nucleus {ECO:0000269|PubMed:27911442}.
Interaction partners:
- Caspase-8
- Caspase-3
- Caspase-9
- Actin, cytoplasmic 1
- Lamin-B1
- Lamin-B2
- Prelamin-A/C
- Caspase-1
- Actin, cytoplasmic 2
- Amyloid-beta precursor protein
Sequence:
MSSASGLRRGHPAGGEENMTETDAFYKREMFDPAEKYKMDHRRRGIALIFNHERFFWHLTLPERRGTCADRDNLTRRFSDLGFEVKCFNDLKAEELLLKIHEVSTVSHADADCFVCVFLSHGEGNHIYAYDAKIEIQTLTGLFKGDKCHSLVGKPKIFIIQACRGNQHDVPVIPLDVVDNQTEKLDTNITEVDAASVYTLPAGADFLMCYSVAEGYYSHRETVNGSWYIQDLCEMLGKYGSSLEFTELLTLVNRKVSQRRVDFCKDPSAIGKKQVPCFASMLTKKLHFFPKSN
Protein: Variant surface glycoprotein (VSG), putative (Q583L7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MNMLIIRFLALCILLRNANAAKNQHAVEFGALCNLFTLKDAADPPATEETSATFSELRTPIYNLNVSVADDDFLKDANGKYKDLMQGNDAAKLKAWQQHITEIINSKHGDENKQIYAKLTNKAQKASAQAIITQLIKQTDAIQEKYDAAQKTATESHAKAIEDILTAIYGDKDSKYTEGDFGGSRNSCGPTSNGNSAAGKNLLDDMICLCTNKAAATTTECGSATAPQVDGAGNTGQQAITHVISLCKSPAKPPALTGELIEARLAIFHSMLGRNPNGETGDEIRYVLGKYSASQCDGASEQNCVNYVAQLKTPGTGITWENKMRDAIEKLKAGQTASAALRHYRQQLKNLALTARNAYEAAKLATEGTTLPLPQTTPGVVEITETDTTCEKKGTGDECKPPCKVEGTGKDAKCKLNKEEAKKLEEKTEQKDGGDSKTTNTTGSNSFLIKTSLLTLAFLLF
Protein: Geranylgeranyl transferase type-1 subunit beta (GGTase-I-beta) (EC 2.5.1.59) (Cell division cycle protein 43) (Geranylgeranyl transferase type I subunit beta) (RAS proteins geranylgeranyltransferase subunit beta) (Type I protein geranyl-geranyltransferase subunit beta) (PGGTase I beta) (P18898)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl diphosphate to proteins having the C-terminal sequence Cys-Ile-Ile-Leu or Cys-Val-Leu-Leu. Acts, among other substrates, on Rho1 and Rho2 and CDC42 proteins. Participates in a RAS-like C-terminal modification of proteins involved in nuclear division and bud growth. It is involved in bud positioning and cell polarity. The beta subunit is responsible for isoprenoid and peptide-binding.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Cell division control protein 42
- GTP-binding protein RHO1
Sequence:
MCQATNGPSRVVTKKHRKFFERHLQLLPSSHQGHDVNRMAIIFYSISGLSIFDVNVSAKYGDHLGWMRKHYIKTVLDDTENTVISGFVGSLVMNIPHATTINLPNTLFALLSMIMLRDYEYFETILDKRSLARFVSKCQRPDRGSFVSCLDYKTNCGSSVDSDDLRFCYIAVAILYICGCRSKEDFDEYIDTEKLLGYIMSQQCYNGAFGAHNEPHSGYTSCALSTLALLSSLEKLSDKFKEDTITWLLHRQVSSHGCMKFESELNASYDQSDDGGFQGRENKFADTCYAFWCLNSLHLLTKDWKMLCQTELVTNYLLDRTQKTLTGGFSKNDEEDADLYHSCLGSAALALIEGKFNGELCIPQEIFNDFSKRCCF
Protein: Jiangshi, isoform A (Jiangshi, isoform B) (RE15157p) (Q9VEW1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLAQTQIIPTPWRLLTLALFCSALFLASEAQNAIPKTNPASLLIQKTSFSCAGRPAGYYADVETGCQVYHMCDGLGRQFSYTCPNTTLFQQRMLICDHWYMVNCSKAESNYAANLLIGQRDKPFVNDEENSLRTPRPDLLDRPYAPDYSGESFRSQYKQFTSNQNQIRDESVKGAGAGKSDPQISQTRWRIPPPSRTILPPAYEPQIELPSAQSAKPRIPIITSTTTTTRATTTTRPTTTTRATTTTTTTRRPPVTARPKEALHNRRPNFQEHDMDDLGTSHSTRYNTSADFNSAESPLRETKQSSTKLTKFIKPPSKIYEPPFVYPIYNLEESQTQNAAVATTLRTSTAAPFSPVPSRKEVSTTTPRPLSRPTTLAGVPFSSATHPTTVTTVGVPPRSDNRTPAPAQSFRLATPTSTAAPPSRPAQLPFNDLLPPFVDFVPHDIATTQGPPIYYEWKVPSNGLEPPKLDPPIGVDGREYPETTGDYGVTSKQDVFNTRLNDIGSHQKKPVQITSPLQQSSTSHRLAISRSIKPKEEQESAQRRSDVVASSTDISHLRKQFLIPEYAFPLETIGRTGYGPGAGAAAGGSGSSNGDLYNSFQLKIPEQRAKWFGENPKCPECHPSFVLPGTCEPCLRR