wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphoribosylformylglycinamidine synthase (FGAM synthase) (FGAMS) (EC 6.3.5.3) (Formylglycinamide ribonucleotide amidotransferase) (FGAR amidotransferase) (FGAR-AT) (Formylglycinamide ribotide amidotransferase) (Protein adenosine-2) (P35421)
Organism: Drosophila melanogaster (Fruit fly)
Function: Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. Because of its role in metabolisms, is involved in sleep regulation.
Interaction partners:
- Trifunctional purine biosynthetic protein adenosine-3
- Bifunctional purine biosynthesis protein ATIC
- Adenylosuccinate lyase
- Amidophosphoribosyltransferase
- Serine hydroxymethyltransferase
- Adenylosuccinate synthetase
- Amidophosphoribosyltransferase
- GMP synthase
- C-1-tetrahydrofolate synthase, cytoplasmic
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial
Sequence:
MVILRYYDVQAHSAAEEESVLRRLREEDGAVVSVRMERCYHLEYSAQAEHSLALDELLVWLVKQPLSKGQSLSRQPALQSTGSSQLLLEIGPRFNFSTPYSTNCVNIFQNLGYSEVRRMETSTRYLVTFGEGSKAPEAARFVPLLGDRMTQCLYTEENTPKASFDEQLPERQANWHFVPVLEEGRAALERINQELGLAFNDYDLDYYHDLFAKELGRNPTTVELFDCAQSNSEHSRHWFFRGRMVIDGVEQPKSLIRMIMDTQAHTNPNNTIKFSDNSSAMVGFDHQTIVPSSVVAPGAVRLQSVQSDLIFTAETHNMPTAVAPFSGATTGTGGRLRDVQGVGRGGVPIAGTAGYCVGALHIPGYKQPYEPLDFKYPATFAPPLQVLIEASNGASDYGNKFGEPVISGFALSYGLNSAADASQRDEYVKPIMFSGGLGTMPATMREKLPPARGQLLAKIGGPVYRIGVGGGAASSVEIQGSGDAELDFNAVQRGDAEMENKLNRVVRACLDLGEQNPILAIHDQGAGGNGNVLKELVEPGFAGAVIFSKEFQLGDPTITALELWGAEYQENNAILCNADQRELLEKICRRERCPISFVGVVTGDGRVTLLEKPAPKDLEQALNASNRSEVSPFDLELKYVLGDMPKRTYDLKREQTPLKELSLPKGLLLDEALERVLSLVAVGSKRFLTNKVDRCVGGLIAQQQCVGPLQAPLADYALTTVSHFSHSGIATSIGTQPLKGLLDPAAMARMCVAEALSNLVFVKISELADVKCSGNWMWAAKLPGEGARMFDACKELCQILEELHIAIDGGKDSLSMAAKVGGETIKSPGTLVISTYAPCPDVRLKVTPDLKGPGAGSKTSLLWINLENSARLGGSALAQAYAQQGKDTPNLTRSDVLGKAFAVTQSLLGDGLIQAGHDVSDGGLLVCVLEMAIGGLSGLRVDLSEPLAKLKNFDKSVEKLNRPELAVLFAEECGWVVEVLDTDLERVRSTYEKAGVPNYYLGVTEGFGLDSRVVLKNGKSELLDQPLRVLYKKWERTSYELEKLQANPECAEAEYNSLEYRQAPQYRGPQNVQAELTLKRSSAPVRVAVLREEGVNSEREMMACLLRANFEVHDVTMSDLLQGTASVSQYRGLIFPGGFSYADTLGSAKGWAANILHNPRLLPQFEAFKRRQDVFSLGICNGCQLMTLIGFVGSAKSEVGADPDVALLHNKSQRFECRWATVKIPSNRSIMLGSMKDLVLGCWVAHGEGRFAFRDEKLISHLQSEQLVTLQYVDDVGKPTELYPLNPNGSPQGIAGLCSSDGRHLALMPHPERCSSMYQWPYVPSSFEVSPTQSESPWQIMFNNAYNWCVKSNQ
Protein: Protein-ADP-ribose hydrolase (SpyMacroD) (EC 3.2.1.-) (P67343)
Organism: Staphylococcus aureus (strain Mu50 / ATCC 700699)
Function: ADP-ribose glycohydrolase that hydrolyzes ADP-ribosyl-cysteine bonds (By similarity). Specifically reverses the SirTM-mediated mono-ADP-ribosylation of GcvH-L (SAV0324), by releasing ADP-ribose from the target protein. May be involved in the modulation of the response to host-derived oxidative stress.
Interaction partners:
Sequence:
METLKSNKARLEYLINDMRRERNDNDVLVMPSSFEDLWELYRGLANVRPALPVSDEYLAVQDAMLSDLNHQHVTDLKDLKPIKGDNIFVWQGDITTLKIDAIVNAANSRFLGCMQANHDCIDNIIHTKAGVQVRLDCAEIIRQQGRNEGVGKAKKTRGYNLPAKYIIHTVGPQIRRLPVSKMNQDLLAKCYLSCLKLADQHSLNHVAFCCISTGVFAFPQDEAAEIAVRTVESYLKETNSTLKVVFNVFTDKDLQLYKEALNRDAE
Protein: Lipopolysaccharide core heptose(II) kinase WaaY (EC 2.7.1.-) (P27240)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the phosphorylation of heptose(II) of the outer membrane lipopolysaccharide core.
Interaction partners:
- Lipopolysaccharide 1,2-glucosyltransferase
- Probable 3-deoxy-manno-octulosonic acid transferase
- Lipopolysaccharide 1,6-galactosyltransferase
- Lipopolysaccharide glucosyltransferase WaaO
- Lipopolysaccharide core biosynthesis protein WaaS
- Lipopolysaccharide glucosyltransferase WaaG
- Putative lipopolysaccharide heptosyltransferase 4
- Lipopolysaccharide core heptose
- Lipopolysaccharide heptosyltransferase 3
- O-antigen ligase
Sequence:
MIQKSKIKDLVVFTDENNSKYLNVLNDFLSYNINIIKVFRSIDDTKVMLIDTDYGKLILKVFSPKVKRNERFFKSLLKGDYYERLFEQTQKVRNEGLNTLNDFYLLAERKTLRFVHTYIMIIEYIDGIELCDMPDIDDALKNKIQQSINALHQHGMVSGDPHRGNFIIKNGEVRIIDLSGKRASAQRKAKDRIDLERHYGIKNEIRDLGYYLLVYRKKMRNFMRRLKGKPAR
Protein: WRKY transcription factor WRKY76 (OsWRKY76) (Q6EPZ2)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcription repressor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element. Regulates, probably indirectly, the activation of defense-related genes during defense response (By similarity). Modulates plant innate immunity against X.oryzae pv. oryzae (Xoo).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q6QHD1, ECO:0000255|PROSITE-ProRule:PRU00223}.
Interaction partners:
- Os09g0101800 protein
Sequence:
MDAAWRGGVGCSPVCLDLCVGLSPVREPSAARHELLDRPAGCRGGGDSKSMTNDEAKIVEAKVTQMSEENRRLTEVIARLYGGQIPRLGLDGSASPPRPVSPLSGKKRSRESMETANSCDANSNRHQGGDADHAESFAADDGTCRRIKVSRVCRRIDPSDTSLVVKDGYQWRKYGQKVTRDNPSPRAYFRCAFAPSCPVKKKVQRSAEDSSLLVATYEGEHNHPHPSPRAGELPAAAGGAGGSLPCSISINSSGPTITLDLTKNGGAVQVVEAAHPPPPPDLKEVCREVASPEFRTALVEQMASALTSDPKFTGALAAAILQKLPEF
Protein: Dapper homolog 1 (Dapper antagonist of catenin 1) (Frodo homolog) (MDpr1) (Thymus-expressed novel gene 3 protein) (Q8R4A3)
Organism: Mus musculus (Mouse)
Function: Involved in regulation of intracellular signaling pathways during development. Specifically thought to play a role in canonical and/or non-canonical Wnt signaling pathways through interaction with DSH (Dishevelled) family proteins. The activation/inhibition of Wnt signaling may depend on the phosphorylation status. Proposed to regulate the degradation of CTNNB1/beta-catenin, thereby modulating the transcriptional activation of target genes of the Wnt signaling pathway. Its function in stabilizing CTNNB1 may involve inhibition of GSK3B activity. Promotes the membrane localization of CTNNB1. The cytoplasmic form can induce DVL2 degradation via a lysosome-dependent mechanism; the function is inhibited by PKA-induced binding to 14-3-3 proteins, such as YWHAB (By similarity). Seems to be involved in morphogenesis at the primitive streak by regulating VANGL2 and DVL2; the function seems to be independent of canonical Wnt signaling and rather involves the non-canonical Wnt/planar cell polarity (PCP) pathway. The nuclear form may prevent the formation of LEF1:CTNNB1 complex and recruit HDAC1 to LEF1 at target gene promoters to repress transcription thus antagonizing Wnt signaling (By similarity). May be involved in positive regulation of fat cell differentiation. During neuronal differentiation may be involved in excitatory synapse organization, and dendrite formation and establishment of spines.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Synapse {ECO:0000269|PubMed:20335472}. Note=Shuttles between the nucleus and the cytoplasm. Seems to be nuclear in the absence of Wnt signaling and to translocate to the cytoplasm in its presence (By similarity). {ECO:0000250}.
Interaction partners:
- Segment polarity protein dishevelled homolog DVL-2
- Segment polarity protein dishevelled homolog DVL-1
- Glycogen synthase kinase-3 beta
- Catenin beta-1
- Vang-like protein 2
- Axin-1
- Vang-like protein 1
- E3 ubiquitin-protein ligase SIAH1B
- Beta-catenin-interacting protein 1
- Adenomatous polyposis coli protein
Sequence:
MKPDAAREPEPLSPGRGAEAEGRWRERGEADTERQRTRERQEATLAGLAELGYLRQRQELLVRGALRCSGTVGTVAPRSGELRGDAAQRSRLEEKFLEENILLLRRQLNCLRRRDAGLLNQLQELDKQISDLRLDVEKTSEEHLETDSRPSSGFYELSDGASGSLSNSSNSVFSECLSSCHSSTCFCSPLEAALTISDGCPKSADVNPKYQCDLVSKNGNDVYRYPSPLHAVAVQSPMFLLCLTGNTLREEEGLGSHASDICIGSELNATKTDNSLPSPSSLWSASHPASSKKMDGYILSLVQKKTHPVRTNKPRTSVNADPTKGLLRNGSVCVRAPSGVPPGSSVNFKNTKQMCLPAGGITSLENGPFSPPKQRSKDSKTDQLESKRLALPESCSAGAAMEPQSKHVPKAAKAASQELTRCQAGLGESMKESNQASAVSPKTSPGRGPVAPAESKALQLPKKMSQKNSLQAVPALDRPALDFKSEGSSQSLEEGHLVKAQFIPGQQAAARPHRAHRNPGVARSATLKARGQAAMEHGLPTVREKPRAAGKKCRFPDDSDTNKKFRKTSAKGRRSGGLQDAGLPGRALGTGGHRAGSRAHAHGREPVVAKPKHKRTDYRRWKSSAEVSYEEALRRARRARREHGAAYRVAVALPYASPYAYVPSDSEYSAECESLFHSTVVDTSEDEQSNYTTNCFGDSESSVSEGDFVGESTTTSDSEESGGLIWSQFVQTLPIQTVTAPDLHTRPTKTFVKIKASHNLKKKILRFRSGSLKLMTTV
Protein: Phospholipase D (Q9HYC2)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Tle cognate immunity protein 4 C-terminal domain-containing protein
- Type VI secretion system spike protein VgrG4b
- Type VI secretion system spike protein VgrG2b
- Peptidoglycan muramidase Tse3
- Type VI secretion system spike protein VgrG5
- Type VI secretion system spike protein VgrG1a
- Type VI secretion system spike protein VgrG2a
- PLD phosphodiesterase domain-containing protein
- Peptidoglycan amidase Tse1
- Transmembrane protein
Sequence:
MLQKKPYNGLHEKELNQINQQDGSPCVAISAPGCFIKGSNLFSEKRAGNRVRFFTTGRDYFSDLASALDSASSSIFITGWQVNYDVLLDGRRSLWQCLRQALERSPALKVYVMPWLSPSGSLGTYDFETMLAVFQLNAGLEGGARAFCTPAIQQSDMQGLGVAFSHHQKSVVIDNRIGYVGGIDLAYGRRDDNDFSLDASGRRGNDAYNPGLPHLGWMAEDEHVSSMGLMMATLFDLSRPLASLTLHAPTLRLSPFPHIAASDEPLLSIPLAPSRARALNGAAYLSDLFRSPMLPSLQWLGRAYNSSKEGLDEGFERLDALRRQMVASSIRAIANLIADNLDALPIEPELERRLRAWLEELRTAALNLPEALRIKSLLLINQWMSETELGQVLTLISGKGFEDIPQNLSGKAGELAGSLFWTLHRLMQARAGGHQQPYRYLDEAPQPLASPDNARLAADQPRMPWQDVHCRIEGPSVYDLARNFIDRWNGQQAYLAKTPALQDTALVRSALEAVMKWLNSLAAAAGLENYLDEKRNLRLELDPPTPCWINAPEQLPQEPEVRRGGMTVQVLRSAAARMLEQEQAGRLGAGVNLPLQVGVSTEGVQSNCKDAMLLAISGAQQFIYIENQFFQSEFGKEGEVFKDLPLSGPMASLRDVGSLRRDFVVRIRLEEALEQRDLWLLDWAEVEKIAQEPGTEARQFLKSMLAMWGVNAQGWLTHKLGEAQHGLLNEIGEALARRIERAIQREHPFHVYLVLPVHPEGALNVPNIMHQVHLTQQSLVFGEQSLVKRIQRQMALKALEGKSDPAQAREIIERKDARGRPVYEQQDWSRYLTLLNLRTWAVLGGRVVTEQIYVHSKLLIADDRVAILGSANINDRSLQGERDSELAVMVRDSEPLTVRLDGKNDAIVGKAIHQLRVNLWKKHFGLSQGPGGFVKPASELSAYLSIPAAQEAWEAIQTLAKENTRAYERTFNFIPQNISQTQLQLTPEPPKGFEDGFPASIWPTWAYRKPGELRAGGQLMEPMPYQEIFWRSSNLTSVKTFPPPNGVSGFITALPTSWTRGERNDSGLNLSILAHQDSRSLPTQVAMNGDSSAQGKHRT
Protein: Nuclear factor 1 (A0A590UK09)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU000690}.
Interaction partners:
Sequence:
MYSPLCLTQDEFHPFIEALLPHVRAFAYTWFNLQARKRKYFKKHEKRMSKEEERAVKDELLSEKPEVKQKWASRLLAKLRKDIRPEYREDFVLTVTGKKPPCCVLSNPDQKGKMRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLVKSPQCSNPGLCVQPHHIGVSVKELDLYLAYFVHAADSSQSESPSQPSDADIKDQPENGHLGFQDSFVTSGVFSVTELVRVSQTPIAAGTGPNFSLSDLESSSYYSMSPGAMRRSLPSTSSTSSTKRLKSVEDEMDSPGEEPFYTGQGRSPGSGSQSSGWHEVEPGMPSPTTLKKSEKSGFSSPSPSQTSSLGTAFTQHHRPVITGPRASPHATPSTLHFPTSPIIQQPGPYFSHPAIRYHPQETLKEFVQLVCPDAGQQAGQVGFLNPNGSSQGKVHNPFLPTPMLPPPPPPPMARPVPLPVPDTKPPTTSTEGGAASPTSPTYSTPSTSPANRFVSVGPRDPSFVNIPQQTQGCSC
Protein: 5'-nucleotidase, cytosolic IB (A0A8I6AG86)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSQTSLKTKKKGSQEIPVPNTDSRGYVVRNQWSRTSRSPSTRAPSVDENRSRNTVVKQAPNSSANSRTSSASASQHETSTSPPPQVSEKSPVQQPSPQTRTITPLDSQPPTPPETEPDSRRTSKMYTATDPWAHRDNREPRDLQLREYAHSCDSREGIPKTREYPRTPPTEWKSYVQRRLQYGSSVDMDPDCLPDGQHHRQKQQIEEDEVDEAYWSSVSMLYEKIPSCTRPRPPKPKHAITIAVSSRALFNMVDDRKIYEEEGLEKYMEYQLTNENVILTPGPAFRFVKALQHVNSRLRDLYPDEQDLFDIVLMTNNHAQVGVRLINSVNHYGLLIDRFCLTGGKSPIGYLKAYLTNLYLSADSEKVQEAIKEGIASATMFAGAKDMAYCDTQLRVAFDGDAVLFSDESEHIAKDHGLDKFFQHETLFENKPLAQGPLKGFLEDLGKLQKKFYAKDERLLCPIRTYLVTARSAASSGARVLKTLRRWGLEIDEALFLAGAPKGPILVKIRPHIFFDDQMFHIEAAQKFGTITAHVPYGIAQKRN
Protein: Cilia- and flagella- associated protein 210 (E1BJL9)
Organism: Bos taurus (Bovine)
Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:34715025}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:37327785}.
Interaction partners:
- Protein Flattop
- Tektin-1
- Tektin-4
- Cilia- and flagella-associated protein 276
- Tubulin alpha-1D chain
- Tektin-3
- Cilia- and flagella-associated protein 52
- Outer dynein arm-docking complex subunit 1
- Tubulin beta-4B chain
- Cilia and flagella associated protein 45.
Sequence:
MLVRFGRRSGQAKESAEMKNCEEDPVLYPPLLPTKVDLRQVTIIPHNEWERIRDSLDSLTREAACLRAERKAKKEMHLRSQEVVKHWTNTYAGMKEQKLEAKKKRDEEIEAERQILDIEEAIYKQGERKKAIELAKQYQFYQTERVKNFHSGLLLSRVMKERDAQIEFQKSKIKSDKKWEEQVKLNVEKAFKEEREKAEKQRRERVALAKDHLKQIKEHEEEEERRRKEEEKDAEEIKRQNSLYEIEMKKKQGKKKEEINESRRLFFEHLNDKHIIKAVEQQQQEEEDEKIRKFIKAKKRLTQMGKEKEAETHRLMEERRKRINNFLSKLMKEKFDNEDLIIARDIAEAEAEWEKREREKYEKNKAELKAIAEHRALVMKNKEEEERQRKIEATEQMLAILKADQIFWEHEKEKKQKADKERREVQDAHIQQMAKHKFNALQAKQAESEYCRLTEALVAEKEKEFQDYAREVIESESESTKKYIYPLVKAVQEGPGGGRGPVLVDRGGLRPSYQANDTTGVQLPFYNSPGSKYNNFQKSKGRLGFTW
Protein: Global transcriptional regulator CodY (Branched-chain amino acid-responsive transcriptional regulator) (GTP-sensing transcriptional pleiotropic repressor CodY) (Vegetative protein 286B) (VEG286B) (P39779)
Organism: Bacillus subtilis (strain 168)
Function: DNA-binding global transcriptional regulator which is involved in the adaptive response to starvation and acts by directly or indirectly controlling the expression of numerous genes in response to nutrient availability. During rapid exponential growth, CodY is highly active and represses genes whose products allow adaptation to nutrient depletion.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00621, ECO:0000305}.
Interaction partners:
- Catabolite control protein A
- ATP-dependent protease ATPase subunit ClpY
- Transition state regulatory protein AbrB
- Stage 0 sporulation protein A
- HTH-type transcriptional regulator TnrA
- RNA polymerase sigma-H factor
- RNA polymerase sigma-D factor
- HTH-type transcriptional regulator SinR
- DNA-binding transcriptional repressor ScoC
- ATP-dependent protease subunit ClpQ
Sequence:
MALLQKTRIINSMLQAAAGKPVNFKEMAETLRDVIDSNIFVVSRRGKLLGYSINQQIENDRMKKMLEDRQFPEEYTKNLFNVPETSSNLDINSEYTAFPVENRDLFQAGLTTIVPIIGGGERLGTLILSRLQDQFNDDDLILAEYGATVVGMEILREKAEEIEEEARSKAVVQMAISSLSYSELEAIEHIFEELDGNEGLLVASKIADRVGITRSVIVNALRKLESAGVIESRSLGMKGTYIKVLNNKFLIELENLKSH
Protein: Novel immune-type receptor 14b (Novel immune-type receptor protein) (cDNA, clone cssl:d0274) (A4JYR2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
Sequence:
MILWAFVTVLCVARTAHSRIEQPEKVMIVELGNSVTLRCISCNNNIFWYKQVAGQQPRVISAFQKLSEPIFYNKYKNERFWGKRLSCSTNLTISDIIQSDEAVYYCASREFYTEFGNGTHLKIKGHQAAAYKNSNLDHLNSSIKCRQKFNENSTTEMCNYL
Protein: 50S ribosomal protein L2, putative (Q57Z57)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Large ribosomal subunit protein mL46
- Small ribosomal subunit protein mS29
- Large ribosomal subunit protein bL21m
- Ribosomal protein L11, putative
- 30S Ribosomal protein S17, putative
- Large ribosomal subunit protein uL3m
- 40S ribosomal protein S5, putative
- 50S ribosomal protein L13, putative
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL43
Sequence:
MATWRRPITLIYGNVLHRSVAARTAAVSDLSTLLPVVLCGSKRGVKLSNPIGKQGSQHYGTEPKLEAGKDVQIKHTEMYDGYTDDFGVFKEGPPMTLRLEYVRSPDHGFSQQLLQKDIWSPFQVNANMMIYTPLYYDWQGFSSRDYWGHRSGTNPGSKVVMGHYRRVEERSWGYRIMVNHKPQKRVPKWLACIVHLPRKKKFVGFFLYANGAYVAELLTYKQLPRICYNKRSSSGLPTIGQTVSLSEVTYGKELHSVEMYPGHGGVICRASGAAAVVLRGAEPNLVPLLLPSKEVRLFDNECHAVFGRRAGVMYRYQRNFGKRNVEEYMPHRPKVHSKTKRVSSHPAGGGNGGSSNLLVPLDWRIHPRNCVKTKYWLSGYILRGRQYNKGQTVADIKSKTYSWANRDPVYR
Protein: Caspase-6 (CASP-6) (EC 3.4.22.59) (Apoptotic protease Mch-2) [Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11] (O35397)
Organism: Rattus norvegicus (Rat)
Function: Cysteine protease that plays essential roles in programmed cell death, axonal degeneration, development and innate immunity (By similarity). 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 (By similarity). 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 (By similarity). Cleaves phospholipid scramblase proteins XKR4 and XKR9. 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. Regulates B-cell programs both during early development and after antigen stimulation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P55212}. Nucleus {ECO:0000250|UniProtKB:P55212}.
Interaction partners:
- Caspase-8
- Caspase-9
- Actin, cytoplasmic 1
- Prelamin-A/C
- Lamin-B1
- Lamin B2
- Actin, cytoplasmic 2
- Caspase-3
- Caspase-1
- Apoptotic protease-activating factor 1
Sequence:
MTETDGFYRSREVLDPAEQYKMDHKRRGTALIFNHERFFWHLALPERRGTNADRDNPTRRFSELGFEVKCFNDLRAEELLLKIHEVSTSSHVDADCFLCVFLSHGEGNHIYAYDAKIEIQTLTGLFKGDKCQSLVGKPKIFIIQACRGSQHDVPLVPLDVVDHQTDKLDDNVTQVDAASVYTLPAGADFLMCYSVAEGYYSHRETVNGSWYIQDLSEMLARHGSSLEFTELLTLVNRKVSQRRVDFCKDPGAIGKKQVPCFASMLTKKLHFCPKPSK
Protein: Cyclic nucleotide gated channel beta 1 (A0A1D5RLJ2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MLGWVQRVLPQPPGTPQKTVETAGPQPETESKPEANPQPEPEPQQEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPVPEEAPPEVQALPPEEPMEGEGEAEAGPSLQETQVADPAQPTSQAQVAVAKVNRPSSWMLSWFWRGMQKVVPQPVCSNGGQNLAAGERDPDQQGGAQIPEPCGTGDPGSAEASGTQDTEPSLWLLRWLEQNLEKVLPQPPPPSLVSDELGVGS
Protein: Chihuahua (Collagen, type I, alpha 1a precursor) (Q6U1J5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MFSFVDILLALLLNATVLLARGQGEDDRTGGSCTLDGQVYNDRDVWKPEPCQICVCDSGTVMCDEVICEDTSDCPNPVIAHDECCPVCPDDDFQEPSVEGPRGSPGDKGERGPANPPGNDGIHEQSVLPVPTSHSGPAALGGNLSPQMSGGFDEKSSPMAVPGPMGPMGPRGAPGPPGPSGPQGFTGPPGEPGEAGAPGPMGPRGAAGPPGKNGEDGESGKPGRPGERGPPGPQGARGFPGTPGLPGIKGHRGFSGLDGAKGDAGPAGPKGEPGAPGENGTPGAMGPRGLPGERGRAGPPGAAGARGNDGAAGAAGPPGPTGPAGPPGFPGGPGSKGEVGPQGSRGAEGPQGARGEAGNPGPAGPAGPAGNNGADGAPGAKGAPGAPGIAGAPGFPGPRGPPGAAGAAGAPGPKGNTGEAGAPGAKGEAGAKGEAGAQGVQGPPGPPGEEGKRGPRGEPGAGGARGPTGERGAPGARGFPGADGAAGPRGAPGERGGPGVVGPKGATGEPGRNGEPGMPGSKGMTGSPGSPGPDGKTGPGGAPGQDGRPGPPGPVGARGQPGVMGFPGPKGAAGEAGKPGERGVMGAIGATGAPGKDGDVGAPGAPGPAGPAGERGEQGAAGPPGFQGLPGPQGATGEPGKSGEQGAPGEAGAPGPSGSRGDRGFPGERGAPGPAGPVGARGSPGSAGNDGAKGESGAAGAPGAQGPPGLQGMPGERGAAGLPGLKGDRGDQGAKGADGAAGKDGIRGMTGPIGPPGPAGAPGDKGESGAQGLVGPTGARGPPGERGETGAPGPAGFAGPPGADGLPGAKGEPGDNGAKGDAGAPGPAGATGAPGPQGPVGATGPKGARGAAGPPGATGFPGAAGRVGPPGPSGNSGPPGPPGPAGKEGQKGNRGETGPAGRTGEVGAAGPPGAPGEKGNPGAEGATGPAGIPGPQGIGGQRGIVGLPGQRGERGFPGLPGPSGEIGKQGPSGPSGERGPPGPMGPPGLAGPPGEPGREGTPGNEGSAGRDGAAGPKGDRGETGPSGTPGAPGPPGAAGPIGPAGKTGDRGETGPAGVPGPAGPSGPRGPSGPAGARGDKGETGEAGERGMKGHRGFTGMPGPPGPPGPSGESGPAGASGPAGPRGPAGSAGSAGKDGMSGLPGPIGPPGPRGRNGEIGPAGPPGPPGPPGAPGPSGGGFDIGFIAQPQEKAPDPFRHFRADDANVMRDRDLEVDTTLKSLSQQIESIISPDGTKKNPARTCRDLKMCHPDWKSGEYWIDPDQGCNQDAIKVYCNMETGETCVNPTESAIPKKNWYTSKNIKEKKHVWFGEAMTDGFQFEYGSEGSKPEDVNIQLTFLRLMSTEASQNITYHCKNSIAYMDQASGNLKKALLLQGSNEIEIRAEGNSRFTYSVTEDGCTSHTGAWGKTVIDYKTTKTSRLPIIDIAPMDVGAPNQEFGIEVGPVCFL
Protein: Calbindin (Calbindin D28) (D-28K) (Vitamin D-dependent calcium-binding protein, avian-type) (P05937)
Organism: Homo sapiens (Human)
Function: Buffers cytosolic calcium. May stimulate a membrane Ca(2+)-ATPase and a 3',5'-cyclic nucleotide phosphodiesterase.
Interaction partners:
- Protein S100-G
- Parvalbumin alpha
- 45 kDa calcium-binding protein
- Somatostatin
- Glutamate decarboxylase 1
- Oxidative stress-induced growth inhibitor 2
- 2,4-dienoyl-CoA reductase [
- Caspase-3
- RNA binding protein fox-1 homolog 3
- Transient receptor potential cation channel subfamily V member 5
Sequence:
MAESHLQSSLITASQFFEIWLHFDADGSGYLEGKELQNLIQELQQARKKAGLELSPEMKTFVDQYGQRDDGKIGIVELAHVLPTEENFLLLFRCQQLKSCEEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKTVDDTKLAEYTDLMLKLFDSNNDGKLELTEMARLLPVQENFLLKFQGIKMCGKEFNKAFELYDQDGNGYIDENELDALLKDLCEKNKQDLDINNITTYKKNIMALSDGGKLYRTDLALILCAGDN
Protein: Cysteine-rich secretory protein 2 (CRISP-2) (Cancer/testis antigen 36) (CT36) (Testis-specific protein TPX-1) (P16562)
Organism: Homo sapiens (Human)
Function: May regulate some ion channels' activity and therebye regulate calcium fluxes during sperm capacitation.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Trifunctional purine biosynthetic protein adenosine-3
- Phosphoglycerate kinase 2
- Cation channel sperm-associated protein 1
Sequence:
MALLPVLFLVTVLLPSLPAEGKDPAFTALLTTQLQVQREIVNKHNELRKAVSPPASNMLKMEWSREVTTNAQRWANKCTLQHSDPEDRKTSTRCGENLYMSSDPTSWSSAIQSWYDEILDFVYGVGPKSPNAVVGHYTQLVWYSTYQVGCGIAYCPNQDSLKYYYVCQYCPAGNNMNRKNTPYQQGTPCAGCPDDCDKGLCTNSCQYQDLLSNCDSLKNTAGCEHELLKEKCKATCLCENKIY
Protein: Mitotic arrest deficient 2 like 2 (B1AK43)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTTLTRQDLNFGQGREAGPAGPGAGASGPAGFLERATGLCPPAVVADVLCEFLEVAVHLILYVREVYPVGIFQKRKKYNVPVQMSCHPELNQYIQDTLHCVKPLLEKNDVEKVVVVILDKEHRPVEKFVFEITQPPLLSISSDSLLSHVEQLLRAFILKISVCDAVLDHNPPGCTFTVLVHTREAATRNMEKIQVIK
Protein: Protein INAPERTURATE POLLEN 1 homolog (OsINP1) (Q6H6M5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Required for pollen aperture formation, male fertility and LECRKS7/DAF1 function. Seems to be involved in operculum protrusion. Participates in the modification of plasma membrane at future aperture sites, possibly by creating close contact between the plasma membrane and callose wall to prevent primexine formation and sporopollenin deposition.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:32284546}. Note=Localizes uniformly in the cytoplasm of microspore mother cells (MMCs) during meiosis, in dyads and in the early tetrad stage. In the late tetrad stage, starts to move to distal poles of the tetrad, concentrating into prominent spots. Finally, localizes specifically at the site that marks the future aperture. {ECO:0000269|PubMed:32284546}.
Interaction partners:
Sequence:
MPRPPPPPPPGRGAPGARRPMREFFAAWLSTLRSPLLPLLRRALSSSSSSSSGGWDDPLSSAAAAVEAHFQAHWSALDAAARQDPAQAVSAGDWRSPLELPFLWVGDLHPSLVTSLLRSLSPSPRLLAATDRVDRRIRAAVPSISDRLRRVQEAFISAEVSGAADVEAFLEELKDVALDANRLRRGVLSELVAAAGGYQAALFLEALSRFVLSMHDPEVLRRFDQCRASPGS
Protein: Copine 1 (Q5JX52)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAHCVTLVQLSISCDHLIDKDIGSKSDPLCVLLQDVGGGSWAELGRTERVRNCSSPEFSKTLQLEYRFETVQKLRFGIYDIDNKTPELRDDDFLGGAECSLGQIVSSQVLTLPLMLKPGKPAGRGTITDFLGKSDPFLEFFRQGDGKWHLVYRSEVIKNNLNPTWKRFSVPVQHFCGGNPSTPIQVQCSDYDSDGSHDLIGTFHTSLAQLQAVPAEFECIHPEKQQKKKSYKNSGTIRVKICRVETEYSFLDYVMGGCQINFTVGVDFTGSNGDPSSPDSLHYLSPTGVNEYLMALWSVGSVVQD