wanglab/gogpt-training-data huggingface dataset:
Protein: Caspase-6 (CASP-6) (EC 3.4.22.59) (Apoptotic protease Mch-2) [Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11] (O08738)
Organism: Mus musculus (Mouse)
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 (By similarity). 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. Involved in intrinsic apoptosis by mediating cleavage of RIPK1 (By similarity). 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.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P55212}. Nucleus {ECO:0000250|UniProtKB:P55212}.
Interaction partners:
- Caspase-8
- Caspase-9
- Prelamin-A/C
- Actin, cytoplasmic 1
- Lamin-B1
- Lamin-B2
- Caspase-1
- Caspase-3
- Actin, cytoplasmic 2
- Receptor-interacting serine/threonine-protein kinase 3
Sequence:
MTETDGFYKSREVFDPAEQYKMDHKRRGVALIFNHERFFWHLTLPERRGTNADRDNLTRRFSDLGFEVKCFNDLRAEELLLKIHEVSTSSHIDADCFICVFLSHGEGNHVYAYDAKIEIQTLTGLFKGDKCQSLVGKPKIFIIQACRGSQHDVPVVPLDMVDHQTDKLDNVTQVDAASVYTLPAGADFLMCYSVAEGYYSHRETVNGSWYIQDLCEMLARYGSSLEFTELLTLVNRKVSQRRVDFCKDPDAIGKKQVPCFASMLTKKLHFCPKPSK
Protein: Protein brunelleschi (NIK- and IKBKB-binding protein) (Q9VIL0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Cooperates with Rab11 and fwd/PI4K to mediate the flow of membrane through the Golgi, which is required to support cleavage furrow ingression, therefore promoting cytokinesis in male meiotic cells.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19934220}. Golgi apparatus {ECO:0000269|PubMed:19934220}. Note=Specific to spermatocytes.
Interaction partners:
- Trafficking protein particle complex subunit 10
- Trafficking protein particle complex subunit 5
- Probable trafficking protein particle complex subunit 2
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit 2-like protein
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit 6B
- RE19263p
- Trafficking protein particle complex subunit 11
Sequence:
MRAAVGLMLSHGAGGMEPALSRPDYEQSALHHSCLLVLLRGVGPSRARVLQRAFEKVRRVNHIRVNDSSGHPRSIWIRFVHDHPVEHNDWGDFQTHRRLLGLVTIGKFDSQIELNELCRQHESLKVRYGSTLYESRAIFFGPDEQPLETIGEVLGPPAAGGRRLQDEFTTPSNFKAQAFFYREQDSCADLESRIGDFASALFWVLESRRLERSREKADKVSLLLAPFEKRDFVGLDMESRNNRKRCVGRVMKNLADLSLQAGLVDDALSLYHNANETLRSVGDSLWVGATEEGLCAASAMLLYPQMRETETLHRNSSLQEAGTSPLKNTPEKWRASDATKKISASDATANNVDSNQPQQRVTSNSSSCSSVSSLVTTATNSSASDTPTTSSSSTSTISAAPIPGHQRNGDLPGNILKAEEISNYYRKAIINYSKYRHAATIETEAALKASRICIEQNRPLDVAMFLQNILYINLSMSEAERVKRFEVITDLYQQIGYQRKAAFFQRLAALKHVQQGSQAPDWNQSYRLMLGSFTGYRLCLDPLEVIENAAGWPALQIDLVQTLITAARRLGHSALATRHMTFLLQTQWDNMSPTEQSEMAVQLQNLSAQCEGSPVPLVLENGTVIPPANLTDLPYCIDLQVKDLPAHLRPQRIKVAKADSGPFLFTPIHFNSVDRRDKKKDKNKIAFQWVQNDLSEVTVRLRNPLPFELPVTDMRLLTNGVVFESLPQTLVLQPHVPTYVALHGTPIETGQLDLQGYSTHTLGVKSNCRLKHMRGRSFPPNYVVDVIPALPRISVKTSLPQTATFSNMNSADIVVTSASLTLYNGESSSCTITITNESATLPLEHLEFSINSNVEQELQQKIFRIDEEAIKAHLPVPPQGTIEIIVDVFAEADFVCPQPPASLHSAAAPGDYGASSLTHYSSVSTSGHASLPSRVGSPHHRRNEPQNSSFRSTISGGPPSLAALTLHPGGGGGVGPSSLGSQYNQHIEAQVRFKYSGGDALTAGYCRQCAVSFNLELLPSVQITSWDVLPAEVASQFYLVLDISNLTAQEMSLNYTDTKNILIEAKESCRVPIPVDRCSLEKVVAARAAEVAENLERELCFRTQLLSFNDALSKLCSIHIAERVKIKWLLTGTDIQGIASLRGIVLSQSMVDLTAVSPLEWAISFQDTLVQPHNEIVCTVGQRSLLSIQLANQSLQPLRNLVLSIKFYQDYLNGMENYNLETRVAISGPNRIAIPLLEKQEQKEHTCSVIFFTPGRFKASIECTSNPQKQSEQPSSLLTRSCPAEAESVGQSVMFSSSYDEQQAHVWKFIPPIEVTVVEQ
Protein: long-chain-fatty-acid--CoA ligase (EC 6.2.1.3) (Q20121)
Organism: Caenorhabditis elegans
Interaction partners:
- Fatty acid synthase
- carnitine O-palmitoyltransferase
- Choline/carnitine acyltransferase domain-containing protein
- Long-chain-fatty-acid--CoA ligase
- Palmitoyl-protein thioesterase 1
- Protein phosphatase
- Medium-chain acyl-CoA ligase ACSF2
- non-specific serine/threonine protein kinase
- AMP-dependent synthetase/ligase domain-containing protein
- long-chain-fatty-acid--CoA ligase
Sequence:
MKRKVSVYDSSKDKTLGQVVKGESPIWIRVAMAILRVWFFIYDCLNYLPYQLFNSPTEKLRKSERVKANWVDDRDGPIRNIQGHASETFPGKDTVDKVWRKCVELYDESPCLGTRQLIEVHEDKQPGGRVFEKWHLGEYVWQSYKEVETQVARLAAGIKDLAHEEQNPKVVIFAETRADWLITALACFRANVTIVTVYATLGEDAIAHAIGETEATILVTSSELLPKIVTLGKKCPTLKTLIYFAPVDQKAPAPELAPFRDQFKHVLSLSGLLTRNQEQVKESTAVKSDIALIMYTSGTTGQPKGVILLHQNVVAALLGQGDGVGIICNADTYIGYLPLAHILELDAELTCLTKGAKVGYSSPLTLHDRASKIQKGTHGDCHALRPTLMAAVPAIMDRIFKAVSEEVAASPRFMQELFKLNYERKRSRYLEGYCSPFLDRIVFKKIRRLLGGKLRGVLSGGAPLNAETQRFMNICMCCPVVQGYGLTETCGAACVADINDLSTGTVGPPVRCSDIALREWSEGGYSPFNDPPQGEILISGENISPGYYKQPEKTAEDFITYKGKVYFATGDIGQKRDDGSLLIIDRKKDLVKLQHGEYVSLAKVECALLNCPIVDNICVYGSGMEDSVVALVVPNQKHLEKIAEAEGVSTSEMKTMCEDKKVIAAYKKQLEEHAKKSKLSRSEIPAAIHLCPEIWTPDTGLLTEALKLKRKPIQMAYQKTLDDLYKQLKKN
Protein: Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit gamma (Protein phosphatase subunit G5PR) (Q9JK24)
Organism: Mus musculus (Mouse)
Function: May regulate MCM3AP phosphorylation through phosphatase recruitment. May act as a negative regulator of ABCB1 expression and function through the dephosphorylation of ABCB1 by TFPI2/PPP2R3C complex (By similarity). May play a role in the activation-induced cell death of B-cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:12167160}. Cytoplasm {ECO:0000269|PubMed:12167160}. Note=Excluded from the nucleoli. Localization is cell cycle-dependent. Localizes to the cytoplasm during cytokinesis.
Interaction partners:
- Troponin I, cardiac muscle
- Ryanodine receptor 2
- D
- Apoptosis regulator Bcl-2
- Protein phosphatase 1 regulatory subunit 1A
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Beta-arrestin-1
- Beta-arrestin-2
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoform
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform
Sequence:
MDWKDVLRRRLASPNTDPKRKKSEQELKDEEMDLFTKYYSEWKGGRKNTNEFYKTIPRFYYRLPAEDEVLLQKLREESRAVFLQRKSRELLDNEELQNLWFLLDKHQIPPMIGEEAMINYENFLKVGEKAGPKCKQFFTAKVFAKLLHTDSYGRISIMQFFNYVMRKVWLHQTRIGLSLYDVAGQGYLRESDLENYILELIPTLPQLDGLEKSFYSFYVCTAVRKFFFFLDPLRTGKIKIQDILACSFLDDLLELRDEELSKESQETNWFSAPSALRVYGQYLNLDKDHNGMLSKEELSRYGTATMTNVFLDRVFQECLTYDGEMDYKTYLDFVLALENRKEPAALQYIFKLLDIENKGYLNVFSLNYFFRAIQELMKIHGQDPVSFQDVKDEIFDMVKPKDPLKISLQDLINSNQGDTVTTILIDLNGFWTYENREALVANDNENSADLDDT
Protein: Protein YdaY (P76069)
Organism: Escherichia coli (strain K12)
Interaction partners:
Sequence:
MSRSSDNDQYRSRNALIRRHIEKMDASLHVGTKEFDISKVSEVDSVDDLLIDNAARYLLKDWKGVGELVNGVEVALEYTAERGIALLKQNPELYWQILAEAASIAQGKEQQKQDTIKKP
Protein: Acetyl-coenzyme A synthetase 2 (EC 6.2.1.1) (Acetate--CoA ligase 2) (Acyl-activating enzyme 2) (P52910)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the production of acetyl-CoA. Provides the acetyl-CoA source for histone acetylation in the nucleus. 'Anaerobic' isozyme of acetyl-coenzyme A synthetase, which is required for growth on fermentable carbon sources such as glucose. May be involved in the PDH (pyruvate dehydrogenase complex) bypass.
Subcellular location: Cytoplasm. Nucleus. Note=Predominantly nuclear.
Interaction partners:
- Magnesium-activated aldehyde dehydrogenase, cytosolic
- Acetyl-CoA acetyltransferase
- Citrate synthase, peroxisomal
- Aldehyde dehydrogenase [NAD
- Citrate synthase 3, mitochondrial
- Acetyl-CoA hydrolase
- Citrate synthase, mitochondrial
- Aldehyde dehydrogenase [NAD
- Malate synthase 1
- Potassium-activated aldehyde dehydrogenase, mitochondrial
Sequence:
MTIKEHKVVYEAHNVKALKAPQHFYNSQPGKGYVTDMQHYQEMYQQSINEPEKFFDKMAKEYLHWDAPYTKVQSGSLNNGDVAWFLNGKLNASYNCVDRHAFANPDKPALIYEADDESDNKIITFGELLRKVSQIAGVLKSWGVKKGDTVAIYLPMIPEAVIAMLAVARIGAIHSVVFAGFSAGSLKDRVVDANSKVVITCDEGKRGGKTINTKKIVDEGLNGVDLVSRILVFQRTGTEGIPMKAGRDYWWHEEAAKQRTYLPPVSCDAEDPLFLLYTSGSTGSPKGVVHTTGGYLLGAALTTRYVFDIHPEDVLFTAGDVGWITGHTYALYGPLTLGTASIIFESTPAYPDYGRYWRIIQRHKATHFYVAPTALRLIKRVGEAEIAKYDTSSLRVLGSVGEPISPDLWEWYHEKVGNKNCVICDTMWQTESGSHLIAPLAGAVPTKPGSATVPFFGINACIIDPVTGVELEGNDVEGVLAVKSPWPSMARSVWNHHDRYMDTYLKPYPGHYFTGDGAGRDHDGYYWIRGRVDDVVNVSGHRLSTSEIEASISNHENVSEAAVVGIPDELTGQTVVAYVSLKDGYLQNNATEGDAEHITPDNLRRELILQVRGEIGPFASPKTIILVRDLPRTRSGKIMRRVLRKVASNEAEQLGDLTTLANPEVVPAIISAVENQFFSQKKK
Protein: 5-hydroxytryptamine receptor 1D (5-HT-1D) (5-HT1D) (Serotonin receptor 1D) (P28565)
Organism: Rattus norvegicus (Rat)
Function: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Regulates the release of 5-hydroxytryptamine in the brain, and thereby affects neural activity. May also play a role in regulating the release of other neurotransmitters. May play a role in vasoconstriction.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19912901, ECO:0000269|PubMed:8978753}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P28221}.
Interaction partners:
- Basigin
- 5-hydroxytryptamine receptor 1B
- Sodium-dependent serotonin transporter
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- 5-hydroxytryptamine receptor 3A
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MSLPNQSLEGLPQEASNRSLNATGAWDPEVLQALRISLVVVLSIITLATVLSNAFVLTTILLTKKLHTPANYLIGSLATTDLLVSILVMPISIAYTTTRTWNFGQILCDIWVSSDITCCTASILHLCVIALDRYWAITDALEYSKRRTAGHAAAMIAAVWAISICISIPPLFWRQATAHEEMSDCLVNTSQISYTIYSTCGAFYIPSILLIILYGRIYVAARSRILNPPSLYGKRFTTAQLITGSAGSSLCSLNPSLHESHTHTVGSPLFFNQVKIKLADSILERKRISAARERKATKTLGIILGAFIICWLPFFVVSLVLPICRDSCWIHPALFDFFTWLGYLNSLINPVIYTVFNEDFRQAFQRVVHFRKAS
Protein: Odorant receptor 67a (Q9VT08)
Organism: Drosophila melanogaster (Fruit fly)
Function: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. Forms a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability. Involved in the behavioral responses to benzaldehyde and acetophenone.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Odorant receptor 98a
- Odorant receptor 65a
- Odorant receptor 85a
- Odorant receptor 42b
- Odorant receptor 67d
- Putative odorant receptor 65c
- Odorant receptor 67b
- Odorant receptor 23a
- Odorant receptor 10a
Sequence:
MDNVAEMPEEKYVEVDDFLRLAVKFYNTLGIDPYETGRKRTIWFQIYFALNMFNMVFSFYAEVATLVDRLRDNENFLESCILLSYVSFVVMGLSKIGAVMKKKPKMTALVRQLETCFPSPSAKVQEEYAVKSWLKRCHIYTKGFGGLFMIMYFAHALIPLFIYFIQRVLLHYPDAKQIMPFYQLEPWEFRDSWLFYPSYFHQSSAGYTATCGSIAGDLMIFAVVLQVIMHYERLAKVLREFKIQAHNAPNGAKEDIRKLQSLVANHIDILRLTDLMNEVFGIPLLLNFIASALLVCLVGVQLTIALSPEYFCKQMLFLISVLLEVYLLCSFSQRLIDASENVGHAAYDMDWLGSDKRFKKILIFISMRSQKPVCLKATVVLDLSMPTMSIFLGMSYKFFCAVRTMYQ
Protein: Ferredoxin-thioredoxin reductase subunit A1, chloroplastic (FTR-A1) (Ferredoxin-thioredoxin reductase, variable chain FTRA1) (FTR-V 1) (Q9FHL4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Variable subunit of the ferredoxin-thioredoxin reductase (FTR), which catalyzes the two-electron reduction of thioredoxins by the electrons provided by reduced ferredoxin.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic
- Ferredoxin C 1, chloroplastic
- Probable ferredoxin-4, chloroplastic
- Ferredoxin C 2, chloroplastic
- Malate dehydrogenase, chloroplastic
- Protein PROTON GRADIENT REGULATION 5
Sequence:
MSSQIALSPAIAAAIRRPSSHDCLSASATTATATPMALKSCIVAPLSLFTSQSQIKHSSSRKTSRTTIRCDVAIKSADSINADANPSSSPSSEEEIEAEAKAKIGSRVRVTAPLKVYHVNRVPEVDLEGMEGKLKDYVAVWKGKRISANLPYKIEFFKEIEGRGLVKFVSHLKEDEFEFIDQ
Protein: Mediator of RNA polymerase II transcription subunit 22 (Mediator complex subunit 22) (Surfeit locus protein 5) (Surf-5) (Q15528)
Organism: Homo sapiens (Human)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 29
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 28
- Mediator of RNA polymerase II transcription subunit 26
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 16
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 27
- Mediator of RNA polymerase II transcription subunit 20
Sequence:
MAQQRALPQSKETLLQSYNKRLKDDIKSIMDNFTEIIKTAKIEDETQVSRATQGEQDNYEMHVRAANIVRAGESLMKLVSDLKQFLILNDFPSVNEAIDQRNQQLRTLQEECDRKLITLRDEISIDLYELEEEYYSSSSSLCEANDLPLCEAYGRLDLDTDSADGLSAPLLASPEPSAGPLQVAAPAHSHAGGPGPTEHA
Protein: Macrophage migration inhibitory factor (EC 5.3.2.1) (EC 5.3.3.12) (L-dopachrome isomerase) (L-dopachrome tautomerase) (Phenylpyruvate tautomerase) (I4AY87)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MPMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLMAFGGSSEPCALCSLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVYINYYDMNAANVGWNNSTFA
Protein: Putative transferase At4g12130, mitochondrial (EC 2.1.-.-) (Iron-sulfur cluster assembly factor homolog COG0354) (Q8L733)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Folate-dependent protein involved in Fe/S cluster biogenesis. Functionally complements an E.coli mutant defective in ygfZ.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:21984653}.
Interaction partners:
- Putative transferase At1g60990, chloroplastic
- glutamate formimidoyltransferase
- Threonylcarbamoyl-AMP synthase
- Threonylcarbamoyl-AMP synthase
- Methyltransferase-like protein 5
- Bifunctional dihydrofolate reductase-thymidylate synthase 1
- Bifunctional dihydrofolate reductase-thymidylate synthase 2
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Aminomethyltransferase, mitochondrial
- Uncharacterized protein At5g03900
Sequence:
MFRFNFRREISKYTGIYHRKIHSGLEDAGPMASRLKSRSVVRFSGPDTVKFLQGLLTNDVRRFGESSGEKNSAVPTPNMASVTNPPMYAALLTPQGRFLYDFFLYSPSRPDEKLDRTGSGPGSDSGRDGSVELFADVDVDVLDELLETLKKYRLRSKVDIENVAEEFSCWQRYGRNLTGSSSVGWGGGVDRAGESTASGNKYGWQWYKDPRLECLGYRSIFPSDATPPLVEADKETDESNYLLWRLEHGVAEGSAEIPKGEAIPLEYNFVGLNAISFDKGCYVGQELIARTHHRGVIRKRLIPLRFIDSNGKELNQKIAAGAEVVESGTGKKMGTVSTALGSRGMGVMRVEEAFKPSAELAVKDSEEVKVEAIKPTWWPAEWFQQNQSGVAAA
Protein: GH02075p (Translocator protein) (Q9VPR1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- RIM-binding protein, isoform F
- ADP,ATP carrier protein
- Voltage-dependent anion-selective channel
Sequence:
MADRPCAGNILRIAGAVILPNLGGIYNGRLTRQHLQSWYANLKFPSFKPPNSVFAPMWISLYAGMGYGSYLVWRDGGGFAGEAAKLPLIAYGTQLALNWAWTPIFFGQHNIKGGLIDIVALTAAASACGVLFYRVNKTAGLLFVPYVAWLGFATALNYAIWKLNPEKEQAPKDEEKPSSSHAKSS
Protein: Kinesin-like protein NACK2 (NPK1-activating kinesin 2) (Q8S949)
Organism: Nicotiana tabacum (Common tobacco)
Function: Probable plus end-directed motor protein that may function in the NACK-PQR (NPK1-NQK1/MEK1-NRK1) MAP kinase signaling pathway, which is essential for somatic cell cytokinesis, especially for the cell-plate formation and its expansion. May regulate the activity and the localization of NPK1, probably by association through the non-catalytic region of the kinase.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8S950}. Nucleus {ECO:0000250|UniProtKB:Q8S950}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000250|UniProtKB:Q8S950}.
Interaction partners:
- mitogen-activated protein kinase kinase
- Protein MKS1-like
- Protein MKS1-like
- Protein MKS1-like
- Protein MKS1-like
- Protein MKS1-like
- Protein MKS1
- Mitogen-activated protein kinase kinase kinase NPK1.
- Mitogen-activated protein kinase
- Mitogen-activated protein kinase kinase kinase NPK1
Sequence:
MVIGTPVTTPLSKIVRTPSRVPGSRRTTPSKIREEKILVTIRVRPLSPKEQAAYDLIAWDFPDEQTIVSKNLNHERHTGPYSFDYVFDPTCSTSKVYEQGARDVALSALNGINATIFAYGQTSSGKTFTMRGITESAVNDIYGRIKLTTERDFVLKFSALEIYNETVVDLLNRESVSLRLLDDPEKGVIVEKQVEEIVKDEEHLKTLIGTVEAHRQVGETALNDKSSRSHQIIRLTIESSIRENSGCVKSFLATLNLVDLAGSERASQTSADGTRLKEGSHINRSLLTVTNVIRKLSCSGGKRSGHIPYRDSKLTRILQASLGGNSRTAIICTLSPALSHLEQSRNTLCFATSAKEVTTTAQVNMVVAEKQLLKHLQKEVSRLEAELRSPDPAASPCLRSLLIEKERKIQKMEEEMNELKRQRDLAQSQLELERRSKKELKGSDHHGPSRQVVKCLSFTPEDEEVSGASLSTNLGRKSLLERQAAIRRSTNSTNPSMLVHEIRKLEMRQRQLGDEANHALQLLHKEFASHRIGSQGATETIAKLFSEIKELQKISCIPEQIEIKDKASLKEEIARLRSQESNIASLEQKLENVQRSIDELVMHLPSCHESADSRTAPSKKKRVLPFNLSNTSNIPNIIRSPCSPMSPSSCNIVEGEIENRAPPECNNVGSAGDSFCSQLSTPVKSKDDNCTPGSRQSNSVNMKKMQTMFKKAAEDNIRSIKAYVTELKERVAKLQYQKQLLVCQVLELEANEAASDEADISDQSPLSWHLVFEDQRQQIIMLWHLCHVSLVHRTQFYMLFKGDPSDQIYLEVELRRLTWLDEHLAGLGNASPALLGDDAAGYVSSSIKALKQEREYLAKRVSSKLNAEEREMLYVKWDIPPDGKQRRRLQLVNKLWSDPLNMQNVRDSAEVVAKLVGFCETGEHVSKEMFQLNFVSPSDKKTWIGWNLISNLLHL
Protein: Glutamine-dependent asparagine synthetase (C9JM09)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MCGIWALFGSDDCLSVQCLSAMKIAHRGPDAFRFENVNGYTNCCFGFHRLAVVDPLFGMQPIRVKKYPYLWLCYNGEIYNHKKMQQHFEFEYQTKVDGEIILHLYDKGGIEQTICMLD
Protein: LD29902p (Well-rounded, isoform A) (Q9VEC6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVFGAMLLTGNGLKGPKQQQQQHQQEPQQQQQQSQQQQQEQKKPAPIKSSSKEQETQPIAAGYYALGIRIPKSPSFHSGLDQLADDELDDQVQDQQQEQQQTGSRFRFSSVEELKAKFEGRKTPLSPPEAAAGGAAGSGAPTTSSSPSSSSTSSNSSASALSSLSQAASSSLASAAANSSASSSAATYGGGANSAAAALIASSPFGSQSSTSSLSLSSNAGMSKNAAGAGSGSGSGTTSTGAASGSNSLVSTLAQHFSAATSAAASAAAAAASSASAASSSSASSSSTATNNAASSSIAASKSPVSAAAAIKNILNATKSVGTSAAAAAAAAATSSSSSPSSAAAVPSSAATAVAAVPTTSDVPAEEMRPTVAQNLVGGISISLGIGQRNGGAAPASSAVMVTPNATMVVTTSSLSIRQNGDILPGHPAGLQPSPQTLQQLTGSPGRARDRNLFYTPPTASVAMALPALRETAASEREELFIQKIQQCCTLFDFSEPLSDLKFKEVKRAALHEMVDFLTNQNGVITEVIYPEAINMFAVNLFRTLPPSSNPNGAEFDPEEDEPTLESSWPHLQLVYELFLRFLESPDFQPSMAKRFIDHQFVLQLLDLFDSEDPRERDFLKTVLHRIYGKFLGLRAFIRKQINNVFYRFIYETEHHNGIAELLEILGSIINGFALPLKEEHKQFLLKVLLPLHKAKSLSVYHPQLTYCVVQFLEKDPSLSEAVIKSLLKFWPKTHSPKEVMFLNELEELLDVIEPAEFQKVMVPLFRQIAKCVSSPHFQVAERALYYWNNEYIMSLITDNSAVILPIMFPALNRNSKTHWNKTIHGLIYNALKLFMEIDQRLFDECSKNYKQEKQMEREKLSQREELWQQVESLAKTNPEWTKARRFNDCLPVSDSRALCDQYSENSDSAYDQSEQRARQPPPPLPPQKQAHQEPREVRQALATLTTLNNY
Protein: Albumin (H0YA55)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
XFSKFRYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL
Protein: Protein LURP-one-related 15 (Q9LZX1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Might be related to the phospholipid scramblase and tubby-like superfamily of membrane tethered transcription factors.
Interaction partners:
- Phospholipid scramblase
- UPF0725 protein At2g20625
- F22D16.19 protein
- Translation initiation factor eIF2B subunit alpha
- Metallo-beta-lactamase family protein
- Splicing factor YJU2
- Outer envelope pore protein 16-1, chloroplastic
Sequence:
MEQPYVYAYPQGSGPSGAPTPQAGGVVVDPKYCAPYPIDMAIVRKMMSLTDGNFVITDVNGNLLFKVKEPVFGLHDKRVLLDGSGTPVVTLREKMVSMHDRWQVFRGGSTDQRDLLYTVKRSSMLQLKTKLDVFLGHNKDEKRCDFRVKGSWLERSCVVYAGESDAIVAQMHRKHTVQSVFLGKDNFSVTVYPNVDYAFIASLVVILDDVNREDRAA
Protein: Protein AUXIN-REGULATED GENE INVOLVED IN ORGAN SIZE (OsARGOS) (Q7X6L2)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Promotes both cell expansion and proliferation-dependent organ growth.
Subcellular location: Membrane {ECO:0000269|PubMed:19161943}; Multi-pass membrane protein {ECO:0000269|PubMed:19161943}. Nucleus {ECO:0000269|PubMed:19161943}. Cytoplasm {ECO:0000269|PubMed:19161943}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q6NMD6}.
Interaction partners:
- Probable methionine--tRNA ligase
- methionine--tRNA ligase
- Elongation factor 1-delta 2
- Elongation factor 1-delta 1
- Elongation factor 1-beta
- Homogentisate 1,2-dioxygenase
Sequence:
MYLLSPRNGDEEDEQEEIQELISDDEPPNLKLASCATAASSSSSSGSDMEKGRGKACGGGSTAPPPPPPSSSGKSGGGGGSNIREAAASGGGGGVWGKYFSVESLLLLVCVTASLVILPLVLPPLPPPPSMLMLVPVAMLVLLLALAFMPTTTSSSSSAGGGGGGGRNGATTGHAPYL
Protein: Chemosensory protein B 38c (Q9VIJ1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFATLLILILGSTDILATDYILLVEDPDIYTPCTDGPPGSVGLNEAFDVSEMQVEMDEEGIHVSGNITTRWSLPPTYRISARMSVLHFNRGNWEPTVFNTLTPDFCDAMFNPNLFWYKYWFKNFENREEIQEKCLATQGTVLVYNPFVVVPRLNNVLGPTLKGRYKVVFLFEAFNEQDERQPSSVCFEITGDAEKIKN
Protein: Subtilisin-like protease SBT3.5 (EC 3.4.21.-) (Subtilase subfamily 3 member 5) (AtSBT3.5) (Q9MAP7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine protease that cleaves the pectin methylesterase 17 (PME17) protein to release the PME17 mature form in the apoplasm.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:24665109}. Note=Identified in cell-wall-enriched root protein extracts. {ECO:0000269|PubMed:24665109}.
Interaction partners:
- Probable pectinesterase/pectinesterase inhibitor 17
- Pectinesterase inhibitor 4
- Endochitinase CHI
- Copper ion binding protein
Sequence:
MRNCRVLLVLVLSLVIVLNVVRASDESKVHIVYLGEKQHDDPEFVSESHHQMLSSLLGSKVDAHESMVYSYRHGFSGFAAKLTESQAKKLADSPEVVHVMADSFYELATTRTWDYLGLSVANPNNLLNDTNMGDQVIIGFIDTGVWPESESFNDNGVGPIPSHWKGGCESGEKFISTNCNRKLIGAKYFINGFLAENEGFNTTESRDYISARDFIGHGTHTASIAGGSFVPNISYKGLAGGNLRGGAPRARIAIYKACWYVDQLGAVACSSSDILKAMDESMHDGVDVLSLSLGAQIPLYPETDLRDRIATGAFHAVAKGIIVVCAGGNSGPAAQTVLNTAPWIITVAATTLDRSFPTPITLGNRKVILGQALYTGQELGFTSLVYPENAGFTNETFSGVCERLNLNPNRTMAGKVVLCFTTNTLFTAVSRAASYVKAAGGLGVIIARNPGYNLTPCRDDFPCVAIDYELGTDVLLYIRSTRSPVVKIQPSRTLVGQPVGTKVATFSSRGPNSISPAILKPDIGAPGVSILAATSPDSNSSVGGFDILAGTSMAAPVVAGVVALLKALHPNWSPAAFRSAIVTTAWRTDPFGEQIFAEGSSRKVADPFDYGGGIVNPEKAADPGLIYDMGPRDYILYLCSAGYNDSSITQLVGNVTVCSTPKTSVLDVNLPSITIPDLKDEVTLTRTVTNVGTVDSVYKVVVEPPLGIQVVVAPETLVFNSKTKNVSFTVRVSTTHKINTGFYFGNLIWTDSMHNVTIPVSVRTQILQNYYDEN