wanglab/gogpt-training-data huggingface dataset:
Protein: Histone H3.3 (P84243)
Organism: Homo sapiens (Human)
Function: Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome {ECO:0000269|PubMed:34876591}.
Interaction partners:
- Histone H4-like protein type G
- WD repeat-containing protein 5
- Transcriptional regulator ATRX
- Death domain-associated protein 6
- Histone H2A type 2-C
- DNA
- Histone H4
- Chromobox protein homolog 5
- DNA
- Histone H2B type 2-E
Sequence:
MARTKQTARKSTGGKAPRKQLATKAARKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
Protein: Hemoglobin subunit epsilon (Epsilon-globin) (Hemoglobin epsilon chain) (P02100)
Organism: Homo sapiens (Human)
Function: The epsilon chain is a beta-type chain of early mammalian embryonic hemoglobin.
Interaction partners:
- Hemoglobin subunit alpha
- Hemoglobin subunit zeta
- Hemoglobin subunit theta-1
- Alpha-hemoglobin-stabilizing protein
- Hemoglobin subunit gamma 1
- Krueppel-like factor 1
- Hemoglobin subunit mu
- Transcription factor NF-E2 45 kDa subunit
- Erythroid transcription factor
- Hemoglobin subunit gamma-2
Sequence:
MVHFTAEEKAAVTSLWSKMNVEEAGGEALGRLLVVYPWTQRFFDSFGNLSSPSAILGNPKVKAHGKKVLTSFGDAIKNMDNLKPAFAKLSELHCDKLHVDPENFKLLGNVMVIILATHFGKEFTPEVQAAWQKLVSAVAIALAHKYH
Protein: KIB1-4 beta-propeller domain-containing protein (Q1PE50)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Putative F-box protein At5g55150
- F-box protein At2g16300
- Probable F-box protein At4g22030
- Putative F-box protein At4g22180
- Putative F-box protein At2g16290
- F-box/kelch-repeat protein At1g57790
- Probable F-box protein At1g65740
- DUF724 domain-containing protein 2
- DUF724 domain-containing protein 1
Sequence:
MSQLINRLLKPSVCKNVIRSHSKQVRMFSSKPTYPYLLIDHLLKTTEHCSNDQVYYDDKYYEKNLVIKDQGLAEEVREVMTVGFSHKDDWRVHLEKSEDSSTSLMMVSNTSFVPVKHQLPPLSSNCRIQNVAISNSVDIKKEDLVVAVKFFGSDVSLCKPFSDSSSEWININTSGSVHPFSSLTYSKKNKKFLSVSPSGTYLWYLDLHFDEDDVEPYSSYLYFREDPLLRLYKMDLEDYIWRFRTDHLAELPSGEHFLVKWFFKDVMMNVGKITQKTDGFKVFRVDTICGHLTNTQDIGDLCIFLGHGEAYCVPASSSPGLRPNSIYYVGCNFGVHDIATDTTTNFYTHSNVPLRSTEFPYWPLPLS
Protein: mRNA cap guanine-N(7) methyltransferase (EC 2.1.1.56) (mRNA (guanine-N(7))-methyltransferase) (mRNA cap methyltransferase) (Q5ADX5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Responsible for methylating the 5'-cap structure of mRNAs.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- mRNA-capping enzyme subunit alpha
- Transcription elongation factor SPT5
- mRNA-capping enzyme subunit beta
- Hcm1p
- Nuclear cap-binding protein subunit 2
- Nuclear cap-binding protein complex subunit 1
- Nrd1 complex RNA-binding subunit
- General transcription and DNA repair factor IIH subunit TFB4
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerase subunit
Sequence:
MSTDSYTPSQEPGSKRLKTGESVFARRGVSPSTGGVASAYGNESEKKPSWLQTNKSDIDGKYDKYGERRNAHTTTRDSRLDRLKRVRQKSAEREDVGHEGDEGDEDEGILPYIHLQAANPAIIHNEKQENYRTFQSRISNRENRDINSIVRAHYNQRTQQAKQQGSRVNSPIYKMRNFNNAIKYILLGNWAKHNPEELDLFSFLDLCCGKGGDLNKCQFIGIDQYIGIDIADLSVKEAFERYTKQKARFRHSNQNSNRYTFEACFATGDCFTQFVPDILEPNFPGIIERAFPVDIVSAQFSLHYSFESEEKVRTLLTNVTRSLRSGGTFIGTIPSSDFIKAKIVDKHLQRDEKGKAKFGNSLYSVTFEKDPPEDGVFRPAFGNKYNYWLKDAVDNVPEYVVPFETLRSLCEEYDLVLKYKKSFTDIFNQEIPKYFSKLNKNLIDGMKRSDGKYGAEGDEKEAVAFYIGFVFEKV
Protein: Transcription factor tau subunit sfc4 (TFIIIC subunit sfc4) (Transcription factor C subunit 4) (O74458)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauA domain of TFIIIC that binds boxA DNA promoter sites of tRNA and similar genes. Sfc4 is the TFIIIB assembling subunit of TFIIIC.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Transcription factor tau subunit sfc1
- Transcription factor IIIB 60 kDa subunit
- Transcription factor tau subunit sfc3
- Transcription factor tau subunit sfc6
- Transcription factor TFIIIB component B''
- DNA-directed RNA polymerase III subunit rpc4
- Cleavage factor two protein 2
- Protein cft1
- TATA-box-binding protein
- Putative transcription factor tau subunit sfc9
Sequence:
MIQNGGNSYVDSNMNETQNDTTDNFDAEMQDLNGYISEIVDEARNVSEVDAKFLGDTSALQAEGLWSDEESDYEGSDDESNFSKTASRTEDDIANEEWEENLKAVAGFRKVRKGHKGRGRVSRADMLPSVEVQQMLSLANHLFAQEGNFDEAQKLAEEIVRIDNNVIAAWKMLGECHRQRGNGRVNIEKCLIAWMAAAHLKPKDHELWFTCAKLSESLEFWDQADYCYNRAVSAKPPNKSELKKYIWNRSVLNKEHGSLKKAAEGFKFLLQSSPYNASILKNLAEIYIKIHAPREILKQFEIAWKYFYQYPAPPIGNDIFDLPTLNLYAELLLLDHQWSNLIRLINRGVRWFRGRKSESFWDEFDDDREWDVDERRREFPNASEEHTNKEAYLLPHLFRTKLGIARLKTGELPEAELHFSVIKNLPPDYAWGMLYDIAKAYMDIERLDLALEYFVLICNHEPAQNIGLWYNMGVCYLELKEYEHAQQCMEAILIVDNSNTNALIKLAEINELQDNRDAALEIVTNIFEQRRNINELEREQSQNEDHEKNVGSQLFVGNQKVPQDKWEKRARISRSKEEARQFTIWKTEETQRRFHKLDILRQSLKKEENVSESLNEWLAIASELIDEFVSIKAFFPSEKKARARAGLLTRRTRYASLNDQLTSMINRLNDSLTRTKYGDLDLDTILRTGYFRNVSIDAWYQLFVEFSLRLTKVGSVQQAYDVLTTAMGAILFDQDTIKRQNLRWCMLACSMYARDPQGALTPLRWVFTTFQFRQDTYRLFSAVLSQGYECSRAFVDSANQKFLLRLIKLMDQLMSNSLVSGAATLVKNDDGLATVPTSYDPVLVLLYGHIMARNRSWIPAINYYSRAFAINPDCPITNLSLGLAYLHRAMQRLSDNRHYQILQGFTFLYRYYDLRVNEGLGEKQEALYNLGKAYHFIGLEHYAVKYYEAVLGLSPMSQGDKMTSSESTVSTTYDFGFEAAYNLRLIYICSGNIKLAFQISSKYLIF
Protein: Rho GTPase-activating protein 4 (Rho-type GTPase-activating protein 4) (Q9CAX8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a GTPase activator for the Rac-type GTPase by converting it to an inactive GDP-bound state. Acts as negative feedback regulator in tolerance to oxygen deprivation which requires ARAC4/ROP2.
Interaction partners:
- Rho GTPase-activating protein 6
Sequence:
MAKVLKSSQSCHFPSPSSSSSTSCGGGNDGSNRDPHSPFNISRREEEEEEEERSEKERERFELSSALEILVSAIRRSVIGGCVGEEDLCSMEIGVPTDVRHVAHVTFDRFHGFLGLPVEFEPEVPRRAPSASATVFGVSTESMQLSYDTRGNIVPTILLMMQSHLYSRGGLRVEGIFRINGENGQEEYIREELNKGIIPDNIDVHCLASLIKAWFRELPSGVLDSLSPEQVMESESEDECVELVRLLPSTEASLLDWAINLMADVVEMEQLNKMNARNIAMVFAPNMTQMLDPLTALMYAVQVMNFLKTLIVKTLKDRKESRDKLVPASNPSPRDHNGDQSSSRQLLHLMKANKEETLDNFEAEMKDKEESADEEEEECAESVELVDIKKSSLVNNSSGGFGQKHIGWEEQRTMSKASSIVGRVNYRVELFEAWR
Protein: Autophagy-related protein 17 (Q06410)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Autophagy-specific protein that functions with ATG13, ATG29, and CIS1/ATG31 in response to autophagy-inducing signals as a scaffold to recruit other ATG proteins to organize pre-autophagosomal structure (PAS) formation. Modulates the timing and magnitude of the autophagy response, such as the size of the sequestering vesicles, through interacting with and regulating ATG1 kinase activity. Plays particularly a role in pexophagy and nucleophagy. With ATG13, is required for ATG1 activation by autophosphorylation of 'Thr-226'. Recruits ATG9 to the pre-autophagosomal structure. Also plays a role in regulation of filamentous growth.
Subcellular location: Cytoplasm. Preautophagosomal structure membrane; Peripheral membrane protein.
Interaction partners:
- Autophagy-related protein 31
- Autophagy-related protein 11
- Autophagy-related protein 13
- Autophagy-related protein 29
- Autophagy-related protein 9
- Serine/threonine-protein kinase ATG1
- Putative lipase ATG15
- Golgi apparatus membrane protein TVP23
- Serine/threonine protein kinase KIN1
- Sorting nexin-4
Sequence:
MNEADVTKFVNNARKTLTDAQLLCSSANLRIVDIKKKLSSWQLSISKLNFLIVGLRQQGKFLYTILKEGIGTKLIQKQWNQAVLVVLVDEMKYWQYEITSKVQRLDGIVNELSISEKDDTDPSKLGDYISRDNVNLLNDKLKEVPVIERQIENIKLQYENMVRKVNKELIDTKLTDVTQKFQSKFGIDNLMETNVAEQFSRELTDLEKDLAEIMNSLTQHFDKTLLLQDKKIDNDEREELFKVVQGDDKELYNIFKTLHEVIDDVDKTILNLGQFLQAKIKEKTELHSEVSEIINDFNRNLEYLLIFKDISNLIDSFKNSCTQDIQTTKELCEFYDNFEESYGNLVLEAKRRKDVANRMKTILKDCEKQLQNLDAQDQEERQNFIAENGTYLPETIWPGKIDDFSSLYTLNYNVKNP
Protein: Pyruvate carboxylase, mitochondrial (EC 6.4.1.1) (Pyruvic carboxylase) (PCB) (P11498)
Organism: Homo sapiens (Human)
Function: Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. Catalyzes in a tissue specific manner, the initial reactions of glucose (liver, kidney) and lipid (adipose tissue, liver, brain) synthesis from pyruvate.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:9585002}.
Interaction partners:
- NADP-dependent malic enzyme
- Biotin--protein ligase
- Glutamate dehydrogenase 1, mitochondrial
- Propionyl-CoA carboxylase beta chain, mitochondrial
- Citrate synthase, mitochondrial
- Phosphoenolpyruvate carboxykinase, mitochondrial
- Malate dehydrogenase, mitochondrial
- NADP-dependent malic enzyme, mitochondrial
- NAD-dependent malic enzyme, mitochondrial
- Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
Sequence:
MLKFRTVHGGLRLLGIRRTSTAPAASPNVRRLEYKPIKKVMVANRGEIAIRVFRACTELGIRTVAIYSEQDTGQMHRQKADEAYLIGRGLAPVQAYLHIPDIIKVAKENNVDAVHPGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDAPITSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVEIAPAAHLDPQLRTRLTSDSVKLAKQVGYENAGTVEFLVDRHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVAEGRSLPDLGLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISPHYDSLLVKVIAHGKDHPTAATKMSRALAEFRVRGVKTNIAFLQNVLNNQQFLAGTVDTQFIDENPELFQLRPAQNRAQKLLHYLGHVMVNGPTTPIPVKASPSPTDPVVPAVPIGPPPAGFRDILLREGPEGFARAVRNHPGLLLMDTTFRDAHQSLLATRVRTHDLKKIAPYVAHNFSKLFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSLQYYMGLAEELVRAGTHILCIKDMAGLLKPTACTMLVSSLRDRFPDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAADSMSGMTSQPSMGALVACTRGTPLDTEVPMERVFDYSEYWEGARGLYAAFDCTATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGVPHGGFPEPFRSKVLKDLPRVEGRPGASLPPLDLQALEKELVDRHGEEVTPEDVLSAAMYPDVFAHFKDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDLNRAGQRQVFFELNGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDIKVVAGAKVAKGQPLCVLSAMKMETVVTSPMEGTVRKVHVTKDMTLEGDDLILEIE
Protein: FIP (Fungus-Induced Protein) Related (Q9XXF1)
Organism: Caenorhabditis elegans
Interaction partners:
- Late embryogenesis abundant protein D-29-like
- FIP
- Uncharacterized protein
- Neuropeptide
- TransThyretin-Related family domain
- MSP domain-containing protein
- Transthyretin-like family protein
- Uncharacterized protein
- Neuropeptide-Like Protein
- Transthyretin-like protein 3
Sequence:
MRVILISILIIVAFCIHTADAQYGYYSPYYGGGYGNYGGYGNYYPSYSSYSYYPSYGYNNYGYGNYGGYGGYNNYGYNSFGFCGIRCRRFQRRLMWAQMMNYGMYGKK
Protein: Dihydromethanophenazine:CoB--CoM heterodisulfide reductase subunit E (EC 1.8.98.1) (CoB--CoM heterodisulfide reductase subunit E) (Coenzyme B:coenzyme M:methanophenazine oxidoreductase subunit E) (P96796)
Organism: Methanosarcina barkeri (strain Fusaro / DSM 804)
Function: Part of a complex that catalyzes the reversible reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB (coenzyme B). HdrE may be responsible for anchoring the complex to the membrane.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Dihydromethanophenazine:CoB--CoM heterodisulfide reductase subunit D
- CoB--CoM heterodisulfide reductase iron-sulfur subunit A
- Methylcoenzyme M reductase system, component A2
- Methyl-coenzyme M reductase subunit gamma
- CoB--CoM heterodisulfide reductase subunit B
- CoB--CoM heterodisulfide reductase subunit C
- Methyl-coenzyme M reductase operon protein D
- Methyl-coenzyme M reductase operon protein C
- CoB--CoM heterodisulfide reductase iron-sulfur subunit A
- Heterodisulfide reductase subunit HdrC
Sequence:
MSEEMLYFSGLSDVLRMTFVQIMIFSTIAIVIFLYGLISNFQKWGTGVTGYALEPQEGKKGSAITFLKTWWSQVTAESHHRGESILEILILDILFQRRILKRSPFRWVMHLFIFGGWMTLFALSGMMFAVEMTEKIGIALPFTPAEFRDFLSIPNYIFGYILLIGVLVALVRRLFVSEVREASIMYDWVLIGIVFLVTISGFIADGIRTGFIWSFGLDPSVAPPAALFHSIFSLLFCIAFIPYSKYIHIIAIPLALLANKGGE
Protein: Alpha-protein kinase 2 (EC 2.7.11.1) (Heart alpha-protein kinase) (F1QU13)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Protein kinase that recognizes phosphorylation sites in which the surrounding peptides have an alpha-helical conformation (By similarity). Regulates cardiac development and cardiomyocyte differentiation by negatively regulating Wnt/beta-catenin signaling.
Subcellular location: Basolateral cell membrane {ECO:0000250|UniProtKB:Q86TB3}.
Interaction partners:
Sequence:
MTAKRVDMAAPDNLLFLDSDAVNSSPASVPIEQNEPTHVLDNQTDDSLRSMPDPHTNTALESTGLMPVPCQDETLETHSQHNEGENESSLVSTQHMDHTRLTEMTINDEKSNNWDFDISGVKENDNSTNLNPDLIHHAGTDSVMERNLNDKQTDLNHKDETFGSLMSSEVLLLKENRQQEMSQDTNLHQCSSSESTGIEYSQTANDAISDAMNSEQSPDQPFSIASNDTDKTTSECSVQTCWDTVESAATSKTQPELHDDVKDVMCESFTTSQTLNIDYLSTDISVCLADLPETDSLNILTPASTLLGILGKNNNVLKTADVPINDSEMVQSINKDLASPNADISKTVFTQMDQNLLHVTDHNVKVLESNRADTVVDQYVFSENIGQEVSQASSHDEDLNSSVQSHDQQLSTANSEIEETSSEFHTQTCQDIHEGVIIAEEAMNGHNTLPEMHDIADVTTSQTPIMKDPMIDEPSYLPDLHKADTPNVITTASTLSDTLETDDSIFETADVSVSDCELIQTVTLKTVTTYETLLMMHDVGEDLTCCDFTTSAIEEPETSHPLSLDDLHESNTPNIPPHASALLDSLGMNKNFLETADVPVSDCEVIQTVTFETVTTYETFPVMHDIAEDLTCCDFTTSETPKIEEPETSHSLSLDDLNEANTPNILPHASALLESLGMNNNFLEAADMPVSDREIIHPVNKDLDSSSVEICTVVLTQTDPKEVQDSDLDEKETESNRIDDSIDGMIDTKFSLDVSKLQPVCSNDLSGTVIHSESLFSQSIPDTPQIGEKYKNDLLQVISPPTPVTNEDLGNCSEEIDDACLKFTGTERDVEGDSELWLEPSQFLAGEEDEGAIFDKWGRSCSSSPPTTHPDNTKASDYTWRENISIDHNAEDWELTFPPVERWSSSDSWASALSDWFQAVNTYPEDSFKSASTGSKLGMAIQDNILEQRTSSDNANNDEQTCLSLNLMQPDEPGQALERGLVKSDNTNGTVFKQGDKERLASCLDMDKDTTTMESQMSLLETSTPESHKADNNAVMETFNASLTHEFNAKLHGSLDISGKLLSAKREGNVLVEVTGGKVSQLGLVFEEERQSIFTSPSSSAYTRDKNLTGCVSNEERCHSSDVHLCICPSQSDSHVSSKAGHAEGNGSFLHSNIGNCTVKPYVEENIPQFIMPFAPICTGNTFLHRSFLKEDRSQADLDLPDKKIINKINLKSNKKSSSSDDSSEDNFHTCPDQSLSSSSGDSDDPSITDSGRKPAYSDTCDIGKELSKLLLLTGEHFMVSEDKRIAYVTLDLDESQHFGRFSLPNCEKQSKPDNMPHKTSKTSSDGKMRSKHKEKPDDKQQHGIQASKKQDPQPQSQVKNEGAGCEDCPVAVIETIVITEKIIPKTQGKKKKKHVQHGTPKPENDAPTDVRSESRQKNVNGKAENLELKVASNSLNKPVAQPSGKTDITKKDSAQKVMSVRPKVEPSMAKMDPAGVNATQKSSPIKLKADTFNTAKMENKTCTTDSLSTCLPSMLNDDIKRRRIADDLSRAVPIRTRPQLPAIFRQARKDGEDVTRRAYSEVVKQKNSTPKEVVVPRVVSEIQADPVPADPQNISLWCQFSPIPPEATIKWTKEAAVLSEINKVEKEDGRFTLTIIKACSKDLGFYKCSLIVANISVSTSEYHLTSEVLMELVIPSHDQPAEPRVMEGDEENIQCSPLLFKEDFLSDQYFGKNQPASILTEKVHFGEGMHRKAFRTTLTEGNLPRFRPGHPCVLKVHNSISYGTKNNEELVQKNYSLAVEECHVQNTAREYIKAYNSVAKSAESFGDLPEIIPIYLVHRPSNDIPYATLEEELLGDFVKYSVKDGKEINLMRRDSEAGQKCCAFQHWVYTQTEGNLLVTDMQGVGMKLTDVGIATCKKGYKGFRGNCATSFIDQFKALHQCNRYCELLGLVSLQPKPKRTVAPPKPKTQPVPKKKTFGPVLNAKS
Protein: Calmodulin (P24044)
Organism: Plasmodium falciparum
Function: Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+) (By similarity). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:3313391}. Note=In trophozoites and schizonts, localizes throughout the cytoplasm (PubMed:3313391). In merozoites, localizes to the apical complex (PubMed:3313391). {ECO:0000269|PubMed:3313391}.
Interaction partners:
Sequence:
MADKLTEEQISEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEIDTDGNGTIDFPEFLTLMARKLKDTDTEEELIEAFRVFDRDGDGYISADELRHVMTNLGEKLTNEEVDEMIREADIDGDGQINYEEFVKMMIAK
Protein: Interferon-inducible protein AIM2 (Absent in melanoma 2) (O14862)
Organism: Homo sapiens (Human)
Function: Involved in innate immune response by recognizing cytosolic double-stranded DNA and inducing caspase-1-activating inflammasome formation in macrophages. Upon binding to DNA is thought to undergo oligomerization and to associate with PYCARD initiating the recruitment of caspase-1 precursor and processing of interleukin-1 beta and interleukin-18. Detects cytosolic dsDNA of viral and bacterial origin in a non-sequence-specific manner. Also acts as a mediator of pyroptosis, necroptosis and apoptosis (PANoptosis), an integral part of host defense against pathogens, in response to bacterial infection (By similarity). Can also trigger PYCARD-dependent, caspase-1-independent cell death that involves caspase-8 (By similarity). Tumor suppressor which may act by repressing NF-kappa-B transcriptional activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19158675, ECO:0000269|PubMed:19158676, ECO:0000269|PubMed:19158679, ECO:0000269|PubMed:24531343, ECO:0000269|PubMed:8454910}. Inflammasome {ECO:0000269|PubMed:19158676, ECO:0000269|PubMed:19158679}. Nucleus {ECO:0000269|PubMed:15582594}. Note=Activated inflammasomes can aggregate in the cytosol as speck-like particles (PubMed:19158675, PubMed:19158676, PubMed:19158679). Activated inflammasomes can also aggregate in the nucleus in response to DNA damage: AIM2 is recruited to double-strand DNA breaks and mediates activation of the AIM2 inflammasome (By similarity). {ECO:0000250|UniProtKB:Q91VJ1, ECO:0000269|PubMed:19158675, ECO:0000269|PubMed:19158676, ECO:0000269|PubMed:19158679}.
Interaction partners:
- Apoptosis-associated speck-like protein containing a CARD
- Pyrin
- NLR family CARD domain-containing protein 4
- NACHT, LRR and PYD domains-containing protein 3
- Caspase-1
- NACHT, LRR and PYD domains-containing protein 1
- NACHT, LRR and PYD domains-containing protein 6
- Baculoviral IAP repeat-containing protein 1
- Caspase-5
- Caspase recruitment domain-containing protein 8
Sequence:
MESKYKEILLLTGLDNITDEELDRFKFFLSDEFNIATGKLHTANRIQVATLMIQNAGAVSAVMKTIRIFQKLNYMLLAKRLQEEKEKVDKQYKSVTKPKPLSQAEMSPAASAAIRNDVAKQRAAPKVSPHVKPEQKQMVAQQESIREGFQKRCLPVMVLKAKKPFTFETQEGKQEMFHATVATEKEFFFVKVFNTLLKDKFIPKRIIIIARYYRHSGFLEVNSASRVLDAESDQKVNVPLNIIRKAGETPKINTLQTQPLGTIVNGLFVVQKVTEKKKNILFDLSDNTGKMEVLGVRNEDTMKCKEGDKVRLTFFTLSKNGEKLQLTSGVHSTIKVIKAKKKT
Protein: Solute carrier family 35, member C1, isoform CRA_b (cDNA FLJ33926 fis, clone CTONG2017409, highly similar to GDP-fucose transporter 1) (cDNA FLJ90448 fis, clone NT2RP3001271, highly similar to GDP-fucose transporter 1) (B3KQH0)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MNRAPLKRSRILHMALTGASDPSAEAEANGEKPFLLRALQIALVVSLYWVTSISMVFLNKYLLDSPSLRLDTPIFVTFYQCLVTTLLCKGLSALAACCPGAVDFPSLRLDLRVARSVLPLSVVFIGMITFNNLCLKYVGVAFYNVGRSLTTVFNVLLSYLLLKQTTSFYALLTCGIIIGGFWLGVDQEGAEGTLSWLGTVFGVLASLCVSLNAIYTTKVLPAVDGSIWRLTFYNNVNACILFLPLLLLLGELQALRDFAQLGSAHFWGMMTLGGLFGFAIGYVTGLQIKFTSPLTHNVSGTAKACAQTVLAVLYYEETKSFLWWTSNMMVLGGSSAYTWVRGWEMKKTPEEPSPKDSEKSAMGV
Protein: Receptor tyrosine-protein kinase erbB-4 (EC 2.7.10.1) (A0A061IIH6)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MVCNHLCSSDGCWGPGPDQCLSCRRFSRGKICIESCNLYDGEFREFENGSICVECDSQCEKMEDGLLTCHGPIIGASSSLVPRRTNAASFTNWDLTTAQSVLILRMVQTVWRNVQMAYREQTVSFSSMRIRIGNATHAIQTAPKVGSRTPARACCDPQLRKIKILFPQLILSGNTLTLIKVYLINTRSASPSRTPLIAAGVIGGLFIVVIMALTFAVYVRRKSIKKKRALRRFLETELVEPLTPSGTAPNQAQLRILKETELKRVKVLGSGAFGTVYKGIWVPEGETVKIPVAIKILNETTGPKANVEFMDHNVSNNTNDFDFKEDHIE
Protein: Oncostatin-M (OSM) (P13725)
Organism: Homo sapiens (Human)
Function: Growth regulator. Inhibits the proliferation of a number of tumor cell lines. Stimulates proliferation of AIDS-KS cells. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells. Uses both type I OSM receptor (heterodimers composed of LIFR and IL6ST) and type II OSM receptor (heterodimers composed of OSMR and IL6ST). Involved in the maturation of fetal hepatocytes, thereby promoting liver development and regeneration (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Oncostatin-M-specific receptor subunit beta
- Leukemia inhibitory factor receptor
- Interleukin-6 receptor subunit beta
- Leukemia inhibitory factor
- Interleukin-6
- Interleukin-11
- Cardiotrophin-1
- Interleukin-31 receptor subunit alpha
- Tyrosine-protein kinase JAK2
- Signal transducer and activator of transcription 3
Sequence:
MGVLLTQRTLLSLVLALLFPSMASMAAIGSCSKEYRVLLGQLQKQTDLMQDTSRLLDPYIRIQGLDVPKLREHCRERPGAFPSEETLRGLGRRGFLQTLNATLGCVLHRLADLEQRLPKAQDLERSGLNIEDLEKLQMARPNILGLRNNIYCMAQLLDNSDTAEPTKAGRGASQPPTPTPASDAFQRKLEGCRFLHGYHRFMHSVGRVFSKWGESPNRSRRHSPHQALRKGVRRTRPSRKGKRLMTRGQLPR
Protein: Probable glucan endo-1,3-beta-glucosidase BG5 (EC 3.2.1.39) (Beta-1,3-glucanase 5) (O49353)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in plant defense against pathogens.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P33157}.
Interaction partners:
- AT1G67850 protein
- 26S proteasome regulatory subunit 4 homolog B
- Cysteine/Histidine-rich C1 domain family protein
- Actin-related protein 4
- ARM repeat superfamily protein
Sequence:
MLYLPKKLFLFFFSCIVVIVNYNNSDFVNAANSIGFVNAANSIGLNYGLLGDNLPSPSKVITLYKSIDITKIRIFDPNTEVLNALRGHRDIAVTVGVRDQDLAALSASEEAVKGWFATNIEPYLSDINIAFITVGNEVIPGPIGPQVLPVMQSLTNLVKSRNLPISISTVVAMWNLEQSYPPSAGMFTSQAREQLVPVLKLLSQTNSPILVKIYPYFSYASDPSSIRLDYATFNTEAIVVQDGSLGYSNMFDAIFDAFVWAMEKEGVKDLPMVVSETGWPSAGNGNITTPDIAGTYNRNFVKHIASGKGTPKRPNKGIDGFLFATFNENQKPVGTEQNFGLYNPNDMKPIYNLF
Protein: Ras-related protein RabS (Q54SD0)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Rab escort protein 1
- Geranylgeranyl transferase type-2 subunit alpha
- Coatomer subunit gamma
- Anaphase-promoting complex subunit 6
- Putative mitotic check point protein BUB2
Sequence:
MAKMDHDYRLNIVLVGDNQCGKSFLLSRYCDGMFVENGIQLWHGIEIKNKIIELKNQSTNEIVKVKLMIFDGNGGCKFKELFYENYLKHQHGFIIMYDVTNLESFNNLSNWISKIKNSYQTSNLYPSPEPILFIVGNKCDLIDDSKITTIVDLKKPQEFCDSLSIPSIHNVSVKENINVDLIFQKLSQLIMDTYPPPKISEIKKIKNVDSGGDSINNCIIN
Protein: Serine/threonine-protein kinase-like protein CR4 (EC 2.7.11.1) (Protein CRINKLY 4) (OsCR4) (Q75J39)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Receptor protein kinase. Could play a role in a differentiation signal (By similarity). Controls formative cell division in meristems (By similarity). Regulates epidermal cell differentiation in many organs. During floral organogenesis, required to maintain the interlocking of the palea and lemma, and fertility. Triggers culm elongation.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9LX29}; Single-pass type I membrane protein {ECO:0000255}. Endosome, multivesicular body membrane {ECO:0000250|UniProtKB:Q9LX29}; Single-pass type I membrane protein {ECO:0000255}. Note=Also localized into protein export bodies. {ECO:0000250|UniProtKB:Q9LX29}.
Interaction partners:
- Calpain-type cysteine protease ADL1
Sequence:
MDIVPVVALCCCLVLLPSWAYGLGSMASIAVSYGEDGPVFCGLNSDGSHLVTCFGADASVVYGAPSRIPFVGVTAGDGFACGLLLDTNQPYCWGSNSYVKIGVPQPMVEGAMYSELSAGDNHLCALRTSVKGFHSVNGDTSVIDCWGYNMTATHTVTGAVSAISAGSVFNCGLFARNRTVFCWGDESVSGVIGLAPRNVRFQSIGAGGYHVCGVLENAQVFCWGRSLEMQQMSTPSSTDDGDVNIVPMDAMVSVVGGRFHACGIRSLDHQVACWGFTLQNSTLAPKGLRVYAIVAGDYFTCGVPAETSLKPMCWGHSGPLALPMAVSPGICVSDSCSHGYYEYANHGEVGSGSKTCKPANSRLCLPCSVGCPDDSYESSPCNATADRVCQFDCSKCASDECVSFCLSQKRTKNRKFMAFQLRIFVAEIAFAVILVFSVTAIACLYVRYKLRHCQCSKNELRLAKNTTYSFRKDNMKIQPDVEDLKIRRAQEFSYEELEQATGGFSEDSQVGKGSFSCVFKGILRDGTVVAVKRAIKASDVKKSSKEFHTELDLLSRLNHAHLLNLLGYCEDGSERLLVYEFMAHGSLYQHLHGKDPNLKKRLNWARRVTIAVQAARGIEYLHGYACPPVIHRDIKSSNILIDEDHNARVADFGLSILGPADSGTPLSELPAGTLGYLDPEYYRLHYLTTKSDVYSFGVVLLEILSGRKAIDMQFEEGNIVEWAVPLIKAGDISALLDPVLSPPSDLEALKKIAAVACKCVRMRAKDRPSMDKVTTALERALALLMGSPCIEQPILPTEVVLGSSRMHKKVSQRSSNHSCSENDLVDGDDQRIEYRAPSWITFPSVTSSQRRKSSASEADMDGRTTTDGRNVGSSIGDGLRSLEEEISPASPQENLYLQHNF