wanglab/gogpt-training-data huggingface dataset:
Protein: GPI transamidase component GPI17 (Q04080)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the GPI transamidase complex. Involved in transfer of GPI to proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- GPI transamidase component GAA1
- GPI transamidase component GPI16
- GPI transamidase component GAB1
- GPI-anchor transamidase
- GPI ethanolamine phosphate transferase 3
- Glycosylphosphatidylinositol anchor biosynthesis protein 11
- GPI inositol-deacylase
- GPI mannosyltransferase 3
- Membrane protein PTM1
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI1
Sequence:
MSNANLRKWVGFCFVAIYLFLGVPLWYKLTTVYRASLPINYIESLQNNKFQDIHLVIPVYVKSDTYRFPDVHDAIQVQVNHLLNSQEQRVPWSLQVLPYNETIEQMESEGNQFHVVTLKLDEFIGYSSAYDTKETLVYYDDAAVLSNDLPFFVAQTLVEHTFQLEWTHLNKTCEGVSTNNDVAISYDPNIHLSVTLLSGDGNPVAWEIEPTLTDYFSPFRKFLSPLVNFTVDSSIVYHNDLNLHSLNGSCTSVTWFDLSHTIDLSELSSMAYYPEDSALNLAIVFPSASSSPDGLAFINGTRISDEITTLDWNSYLVPQWGVIIINKMPLKPNSVISEDYLEPMMYRFATDIFQLLGLTEGSQDLLSPYITIDSFKRLTILQNLDKATETLWSLVKLTQQFQGMSIPREVSDNVIEALDLRLQIIDLLNDPGKGGDIVWNNALHLSNELVKLCEKAFFNGEMVQQNFFPQEHMIAVYLPLLGPISAVMFFGFYNVMKEKNQKSKKNGTEREVAKEKLELKEAQKLHAIDGEDEL
Protein: Mei4-dependent protein 6 (O13730)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Protein ral2
- Guanine nucleotide-binding protein subunit beta
- GID complex subunit 1
Sequence:
MERKELSYTIQSWSSYSGAFHPINILIDNPHQANSRWSCNTSICKPNNSEEQYVILKLDKLALVTDITFGKFHTPHLCNLKDFIVYGGREQHLMFPLLRAGLTNDSNRETFPLCIKKYNKIENSIACKYIKIVPLQAHAHEFNMSIWYVALHGIDSASALSCTEKNRALHLEKKALNCLLSYFAFKGKLDICSVILQSYQLSIPHSPLMRMYDAFCRLGDTQKTILLFQQELQAEIIEKWPKHKLTKLRSHRIATFLKGISRRSGHQMVYNPKDNCIYLYGGWDGVKTFSDFWIYNVDKDLWIMENEYGIPGERVCHRMVIDTSQQKLYLLGNYFGSSRETEVPPDARTDFWEFDISKKVWTCLSYDTSKDGGPAAIFDHGMSVDEKRGIVYVSGGCKWDPDELVFEGLYAYDTKNRIWEQLAVRYEDRQKHCEFKIERMGHCMEYFPDENKLYIFGGQSYDQEFILDMCYIKLETREAVQHVRKNDTSQSPSPSFCQRSIMDSKNHRIFTMFGFEQRNIHKVLRPSLWIFYITTEEWVKISDINEEEGNEHPCSRFGHAVAADLNRNIIYLMGGNASTHPLRPMKLSDFWKLDILDRWGIKHCLSNVSLQLHLHRFHELVSENLAKAVEYLQKSMQPQFDKSPLFWNALILDAFSGTHKNKDIAQRRFETFQTIYDLLPVDENTVAPNESLLNMIEFFT
Protein: Selenocysteine lyase (hSCL) (EC 4.4.1.16) (Q96I15)
Organism: Homo sapiens (Human)
Function: Catalyzes the decomposition of L-selenocysteine to L-alanine and elemental selenium.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9JLI6}.
Interaction partners:
- Iron-sulfur cluster assembly enzyme ISCU
- Selenide, water dikinase 2
- Selenide, water dikinase 1
- Frataxin, mitochondrial
- Thioredoxin reductase 3
- Thioredoxin reductase 1, cytoplasmic
- NFU1 iron-sulfur cluster scaffold homolog, mitochondrial
- Thioredoxin reductase 2, mitochondrial
- Molybdenum cofactor sulfurase
- LYR motif-containing protein 4
Sequence:
MEAAVAPGRDAPAPAASQPSGCGKHNSPERKVYMDYNATTPLEPEVIQAMTKAMWEAWGNPSSPYSAGRKAKDIINAARESLAKMIGGKPQDIIFTSGGTESNNLVIHSVVKHFHANQTSKGHTGGHHSPVKGAKPHFITSSVEHDSIRLPLEHLVEEQVAAVTFVPVSKVSGQAEVDDILAAVRPTTRLVTIMLANNETGIVMPVPEISQRIKALNQERVAAGLPPILVHTDAAQALGKQRVDVEDLGVDFLTIVGHKFYGPRIGALYIRGLGEFTPLYPMLFGGGQERNFRPGTENTPMIAGLGKAAELVTQNCEAYEAHMRDVRDYLEERLEAEFGQKRIHLNSQFPGTQRLPNTCNFSIRGPRLQGHVVLAQCRVLMASVGAACHSDHGDQPSPVLLSYGVPFDVARNALRLSVGRSTTRAEVDLVVQDLKQAVAQLEDQA
Protein: 3-ketoacyl-CoA thiolase 5, peroxisomal (EC 2.3.1.16) (Acetyl-CoA acyltransferase 5) (Beta-ketothiolase 5) (Peroxisomal 3-oxoacyl-CoA thiolase 5) (Q570C8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably involved in long chain fatty-acid beta-oxidation prior to gluconeogenesis during germination and subsequent seedling growth. Involved in systemic jasmonic acid (JA) biosynthesis after wounding and may be during senescence.
Subcellular location: Peroxisome {ECO:0000305}.
Interaction partners:
- Hydroxymethylglutaryl-CoA synthase
- Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2
- Peroxisomal fatty acid beta-oxidation multifunctional protein AIM1
- Peroxisomal acyl-coenzyme A oxidase 1
- Putative peroxisomal acyl-coenzyme A oxidase 1.2
- Acyl-coenzyme A oxidase 3, peroxisomal
- Acyl-coenzyme A oxidase 2, peroxisomal
- Putative acyl-coenzyme A oxidase 3.2, peroxisomal
- Acyl-coenzyme A oxidase 4, peroxisomal
- Putative acyl-coenzyme A oxidase At3g06690
Sequence:
MERAMERQKILLRHLNPVSSSNSSLKHEPSLLSPVNCVSEVSPMAAFGDDIVIVAAYRTAICKARRGGFKDTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAMECRVAAYFAGFPDSVPVRTVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMSTDHIPGGGFHGSNPRAQDFPKARDCLLPMGITSENVAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVATKIVDPETKAEKAIVVSVDDGVRPNSNMADLAKLKTVFKQNGSTTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLAGLNVSDIDLFEINEAFASQYVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRGKDCRFGVISMCIGTGMGAAAVFERGDSVDNLSNARVANGDSH
Protein: Interleukin-10 receptor subunit alpha (IL-10 receptor subunit alpha) (IL-10R subunit alpha) (IL-10RA) (CDw210a) (Interleukin-10 receptor subunit 1) (IL-10R subunit 1) (IL-10R1) (CD antigen CD210) (Q13651)
Organism: Homo sapiens (Human)
Function: Cell surface receptor for the cytokine IL10 that participates in IL10-mediated anti-inflammatory functions, limiting excessive tissue disruption caused by inflammation. Upon binding to IL10, induces a conformational change in IL10RB, allowing IL10RB to bind IL10 as well. In turn, the heterotetrameric assembly complex, composed of two subunits of IL10RA and IL10RB, activates the kinases JAK1 and TYK2 that are constitutively associated with IL10RA and IL10RB respectively. These kinases then phosphorylate specific tyrosine residues in the intracellular domain in IL10RA leading to the recruitment and subsequent phosphorylation of STAT3. Once phosphorylated, STAT3 homodimerizes, translocates to the nucleus and activates the expression of anti-inflammatory genes. In addition, IL10RA-mediated activation of STAT3 inhibits starvation-induced autophagy.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22087322, ECO:0000269|PubMed:26962683}; Single-pass type I membrane protein. Cytoplasm {ECO:0000269|PubMed:26962683}.
Interaction partners:
- Interleukin-10
- Interleukin-10 receptor subunit beta
- Tyrosine-protein kinase JAK1
- Non-receptor tyrosine-protein kinase TYK2
- Signal transducer and activator of transcription 3
- Interleukin-22 receptor subunit alpha-1
- Interleukin-6
- Cathepsin S
- Interleukin-22
- Interferon lambda-3
Sequence:
MLPCLVVLLAALLSLRLGSDAHGTELPSPPSVWFEAEFFHHILHWTPIPNQSESTCYEVALLRYGIESWNSISNCSQTLSYDLTAVTLDLYHSNGYRARVRAVDGSRHSNWTVTNTRFSVDEVTLTVGSVNLEIHNGFILGKIQLPRPKMAPANDTYESIFSHFREYEIAIRKVPGNFTFTHKKVKHENFSLLTSGEVGEFCVQVKPSVASRSNKGMWSKEECISLTRQYFTVTNVIIFFAFVLLLSGALAYCLALQLYVRRRKKLPSVLLFKKPSPFIFISQRPSPETQDTIHPLDEEAFLKVSPELKNLDLHGSTDSGFGSTKPSLQTEEPQFLLPDPHPQADRTLGNREPPVLGDSCSSGSSNSTDSGICLQEPSLSPSTGPTWEQQVGSNSRGQDDSGIDLVQNSEGRAGDTQGGSALGHHSPPEPEVPGEEDPAAVAFQGYLRQTRCAEEKATKTGCLEEESPLTDGLGPKFGRCLVDEAGLHPPALAKGYLKQDPLEMTLASSGAPTGQWNQPTEEWSLLALSSCSDLGISDWSFAHDLAPLGCVAAPGGLLGSFNSDLVTLPLISSLQSSE
Protein: Fascin (F7FMC7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR005682}.
Interaction partners:
Sequence:
MAEVDWIHRHPKAEALRVGLISWAGTYLTFEAYKSTVTATAKSLGRRQTWELLVSNEHETQAVVRLKSLQGLYLLCEADGTVCYGKPRTSHHGCFLLRFHRNGKWTLQCIISGRYLESDGQDVFCNSRVLSAYHMWTPRPALHVHVILYSPTYHSYARADHTVGRVWVDAAVPCLEECGFLLHFQDGCYHLETSTHHFLSRVDRLVPKRSTQTAFHMQVRPRGLVALCDGEGGSLYPQGSHLLLGLGSTPMKGEEWFVLQHFPAWVSLKSKSRRFLSVIYDAEVCAASERLTQMSLFQYECDSESPILQLRSANGFYLAQRRHRAIIADGHPMESDTFFRVHWNCGKITLQSPNGRFLSIASNGLLMSNVTIPGPNEELGIRFANRPFLVLRGRYGYVGSSSDHDLLKCNMDQPDCIQLLPCHQGIYHFQGWILLVNNILWHLPPLGKICPQLLYRTSGEQLAYGAGTQWLLPPS
Protein: Regulatory protein cro (P03040)
Organism: Escherichia phage lambda (Bacteriophage lambda)
Function: Plays an essential role in the switch from lysogenic to lytic state and in fine-tuning the lytic phase activation. Mediates the de-repression of the lytic promoters from repression by cI at an early stage of prophage induction. Turns down the expression of the transcriptional activator cII, a factor that initiates the expression of repressor cI, the major component promoting latency. Additionally, cro is able to directly bind to the promoter region of cI thereby preventing the transcription of cI repressor. These two mechanisms ultimately lead to a strong decrease in the amount of cI that will become unable to maintain the latent phase, allowing the transition to lytic growth. Low level of Cro also stimulates the lytic promoters while cI repressor is still present. Cro-mediated up-regulation of pR and pL ultimately leads to its own increased expression and to a successful switch to lytic growth. The second function assigned to Cro is the fine-tuning of the lytic phase activation. Indeed, cro initially diminishes the strength of activation by turning down the expression of lytic genes as well as its own expression.
Interaction partners:
Sequence:
MEQRITLKDYAMRFGQTKTAKDLGVYQSAINKAIHAGRKIFLTINADGSVYAEEVKPFPSNKKTTA
Protein: Beta-secretase 2 (EC 3.4.23.45) (Aspartic-like protease 56 kDa) (Aspartyl protease 1) (ASP1) (Asp 1) (Beta-site amyloid precursor protein cleaving enzyme 2) (Beta-site APP cleaving enzyme 2) (Down region aspartic protease) (DRAP) (Memapsin-1) (Membrane-associated aspartic protease 1) (Theta-secretase) (Q9Y5Z0)
Organism: Homo sapiens (Human)
Function: Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves APP, between residues 690 and 691, leading to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase. It has also been shown that it can cleave APP between residues 671 and 672. Involved in the proteolytic shedding of PMEL at early stages of melanosome biogenesis. Cleaves PMEL within the M-beta fragment to release the amyloidogenic PMEL luminal fragment containing M-alpha and a small portion of M-beta N-terminus. This is a prerequisite step for subsequent processing and assembly of PMEL fibrils into amyloid sheets. Responsible also for the proteolytic processing of CLTRN in pancreatic beta cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21907142}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus {ECO:0000269|PubMed:11423558}. Endoplasmic reticulum. Endosome. Melanosome {ECO:0000269|PubMed:23754390}. Note=Colocalizes with PMEL in stage I and II melanosomes. {ECO:0000269|PubMed:23754390}.
Interaction partners:
- Reticulon-3
- Reticulon-4
- Tyrosine-protein kinase Fyn
- Beta-secretase 1
- Probable non-functional immunoglobulin heavy variable 3-16
- Amyloid-beta precursor protein
- Presenilin-1
Sequence:
MGALARALLLPLLAQWLLRAAPELAPAPFTLPLRVAAATNRVVAPTPGPGTPAERHADGLALALEPALASPAGAANFLAMVDNLQGDSGRGYYLEMLIGTPPQKLQILVDTGSSNFAVAGTPHSYIDTYFDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLVTIPKGFNTSFLVNIATIFESENFFLPGIKWNGILGLAYATLAKPSSSLETFFDSLVTQANIPNVFSMQMCGAGLPVAGSGTNGGSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEILKLEIGGQSLNLDCREYNADKAIVDSGTTLLRLPQKVFDAVVEAVARASLIPEFSDGFWTGSQLACWTNSETPWSYFPKISIYLRDENSSRSFRITILPQLYIQPMMGAGLNYECYRFGISPSTNALVIGATVMEGFYVIFDRAQKRVGFAASPCAEIAGAAVSEISGPFSTEDVASNCVPAQSLSEPILWIVSYALMSVCGAILLVLIVLLLLPFRCQRRPRDPEVVNDESSLVRHRWK
Protein: Transcription factor BOA (Protein BROTHER OF LUX ARRHYTHMO) (Protein PHYTOCLOCK 1-like) (Protein PCL1-like) (Q9LTH4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that is a critical component of the regulatory circuit of the circadian clock. Binds to specific sites on CCA1 promoter leading to CCA1 activation. Is required for the rhythmic expression of other clock genes such as LHY, GI and APRR1/TOC1.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:21447790}.
Interaction partners:
- CCT motif family protein
- 2-oxoglutarate
- Gibberellin-regulated protein 8
- Scarecrow-like protein 30
- Transcription factor bHLH110
- DCL protein
- Protein EARLY FLOWERING 5
Sequence:
MGKEVMVSDYGDDDGEDAGGGDEYRIPEWEIGLPNGDDLTPLSQYLVPSILALAFSMIPERSRTIHDVNRASQITLSSLRSSTNASSVMEEVVDRVESSVPGSDPKKQKKSDGGEAAAVEDSTAEEGDSGPEDASGKTSKRPRLVWTPQLHKRFVDVVAHLGIKNAVPKTIMQLMNVEGLTRENVASHLQKYRLYLKRIQGLTTEEDPYSSSDQLFSSTPVPPQSFQDGGGSNGKLGVPVPVPSMVPIPGYGNQMGMQGYYQQYSNHGNESNQYMMQQNKFGTMVTYPSVGGGDVNDK
Protein: Tetraspanin (F8VWK8)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cell surface {ECO:0000256|ARBA:ARBA00004241}. Endosome, multivesicular body {ECO:0000256|ARBA:ARBA00004559}. Late endosome membrane {ECO:0000256|ARBA:ARBA00004107}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004107}. Lysosome membrane {ECO:0000256|ARBA:ARBA00004155}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004155}. Melanosome {ECO:0000256|ARBA:ARBA00004223}. Membrane {ECO:0000256|RuleBase:RU361218}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361218}. Secreted, extracellular exosome {ECO:0000256|ARBA:ARBA00004550}.
Interaction partners:
Sequence:
MAVEGGMKCVKFLLYVLLLAFCACAVGLIAVGVGAQLVLSQTIIQGATPGSLLPVVIIAVGVFLFLVAFVGCCGACKENYCLMITFAIFLSLIMLVEVAAAIAGYVFRDKVMSEFNNNFRQQMENYPKNNHTASILDRMQADFKCCGAANYTDWEKIPSMSKNRVPDSCCINVTVGCGINFNEKAIHKEGCVEKIGGWLRKNVLVVAAAALGIAFVE
Protein: Protocadherin 18 (Protocadherin-18a precursor) (A9QUV5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
METSKGTVLCATLLKLALLVTLAGYTTAATLKYQVYEEQKVGTVIARLREDVADVLSKLPSSIPLRFRAMQRGSASLLSVRDQDGEISIRTKIDREKLCEKNLNCTIEFDVLTLPTEHLQLFHIEVEILDINDNAPQFARPVIPIEISETAAVGTRIPLDSATDPDVGENSLNTYSLTPSGFFKIDILTRTDGAKYAELVVLKELDREVRASYELQLTASDRGVPPKFGTTLLKISIADSNDNNPVFEKPSYVINLLENSPLGSLLIDLNATDPDEGTNGKIIYSFSSHVSPKILETFKINSDNGHLTLMRKVDFESTNSYDIDVQAQDMGPNSMPAHCKVIIKVVDVNDNKPDISVNLMSTGNEEIAYISETAPVDTFVALVSVNDLDSGLNGEVECRLYGQGHFRLQKSYEKNYMILTNVTLDREKRSEFSLTVIAEDKGSPSLSTIKNFIVEVQDENDNAPSFAKSRYEISKAENNSPGAYLSSVKASDPDLGPNGQVSYSILESMVHGSSISTYVTIDPSNGDIYALRTFDREDVSQISFLVQARDSGNPPLRSNVTVVLTVLDENDNRPVIMMPQLWNHTADVPVSKYAEIGDVVTVVRAMDHDAGANGDLSCSVVGGNEAGYFNMDPKTCEIRTNVSIQEVPQDHVELTILVQDHGTPTLSARALLRLSLYENIENLMNPHLTGGRNGDGPLDVSMIIIISLGAICAVLLLIMVAFALRCSREKKDTRSYNCRVAESTYQQHPKKPSRQIHKGDITLMPTVNGTLPIRAHHRSPTSSPGAERAHMGSRQSQHSRQSLNSLVTISSNHIPENFALELTHATPPVEGQYQPRPSFRGNKYSRSYRYALQDMDKFSLKDSGRGDSDAGDSDCEMGRDSPIDRLLGDGFGDLFHSDGHHRLHPVMRLCTEECRVLGHSDQCWMPSQASSDYRANMFIPGEESRPQVLEEDQQSVDSAKKSFSTFGKDNEEECGGSLLSEMNNVLQRLLPTSYADVRELDECTSQPASSIGMEIGKGFLPGKASSTGSAYPQGVAVWAANTHFQNPGGAVTSGHAATNHAASQAHLKWLPAMEEIPENYEEDDLESVLSQRQGKRNDTRHEVVDASELVAEINKLLQDVRQS
Protein: Coiled-coil domain-containing protein 60 (Q8IWA6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTKVPATKKLQSSPNSGAVRPFYASENLRQVPDKPMKSIKYMDKEIINLKKDLIRSRFLIQSVKIGRGYFAILREETAKKKKQQQLQKLKEEERNKFQPAEKISEIHYGDTLLSTYDDEKLKTLGARVTRRPFTPIHSCIISPSLTEAHVEPLFRQLCALHWLLEALTIDHTHHTMKPVITCWNPKDPGGSKSTIKKINKDKSMGQKWEHFITAPKTKKFKIPTMRVTNRKPSRRGSTLSLSRASGGSSPQSSMISVNPGSDEPPSVNTQVTSSKDIEDNESSSTKPDEEPLYMNLQKLLEMVREDARRTVTIENGMQRKAPSILSVLKQNKSNSAYKEMQTTLKSSERSSSTSAESHIQPVQKKSKNRTNCDINIHYKSGVCNTMRAKFYSVAQEAGFCLQDKMEILMKRQEERGIQKFRAFVLVSNFQKDIAKMRHHISVVKGDAEEIADHWYFDLLSKLPEDLKNFRPAKKILVKLQKFGENLDLRIRPHVLLKVLQDLRIWELCSPDIAVAIEFVREHIIHMPQEDYISWLQSRINIPIGPYSALR
Protein: Sorting nexin-20 (Q9D2Y5)
Organism: Mus musculus (Mouse)
Function: May play a role in cellular vesicle trafficking. Has been proposed to function as a sorting protein that targets SELPLG into endosomes, but has no effect on SELPLG internalization from the cell surface, nor on SELPLG-mediated cell-cell adhesion.
Subcellular location: Early endosome membrane {ECO:0000269|PubMed:25882846}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q7Z614}; Cytoplasmic side {ECO:0000250|UniProtKB:Q7Z614}. Cell membrane {ECO:0000250|UniProtKB:Q7Z614}. Cytoplasm {ECO:0000250|UniProtKB:Q7Z614}. Nucleus {ECO:0000250|UniProtKB:Q7Z614}.
Interaction partners:
Sequence:
MASPEHPGSPGWRGPINQCRTRTRQEVLPPGPDLPCPGPEEAQDGPSSNSSMTTRELQEHWQKEKSRWKHVRLLFEIASARIEERKVSKFVMYQVVVIQTGSFDSDKAVVERRYSDFERLQKALLKRFGPELEDVTFPRKRLTGNLSAETICERRRELREYLRLLYAVRAVRRSREFLDFLTRPELREAFGCLRAGQYARALELLGRALPLQEKLTAHCPSAAVPALCAALVCLRDLERPAEAFAVGERALRCLRTRENHRYYAPLLDAMVRLAYALGKDFAALQSRLDENQLRRPTHRDATLKELTVREYLS
Protein: Ornithine decarboxylase antizyme 2 (AZ2) (ODC-Az 2) (O95190)
Organism: Homo sapiens (Human)
Function: Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis and uptake in response to increased intracellular polyamine levels. Binds to ODC monomers, inhibiting the assembly of the functional ODC homodimers. Does not target the ODC monomers for degradation, which allows a protein synthesis-independent restoration of ODC activity. Involved in the translocation of AZIN2 from ER-Golgi intermediate compartment (ERGIC) to the cytosol (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Antizyme inhibitor 1
- Ornithine decarboxylase
- Antizyme inhibitor 2
Sequence:
MINTQDSSILPLSNCPQLQCCRHIVPGPLWCSDAPHPLSKIPGGRGGGRDPSLSALIYKDEKLTVTQDLPVNDGKPHIVHFQYEVTEVKVSSWDAVLSSQSLFVEIPDGLLADGSKEGLLALLEFAEEKMKVNYVFICFRKGREDRAPLLKTFSFLGFEIVRPGHPCVPSRPDVMFMVYPLDQNLSDED
Protein: Glyoxalase I (Glx I) (EC 4.4.1.5) (Aldoketomutase) (Ketone-aldehyde mutase) (Methylglyoxalase) (S-D-lactoylglutathione methylglyoxal lyase) (actoylglutathione lyase) (P50107)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Can use gamma-glutamylcysteine as a substrate.
Interaction partners:
- Hydroxyacylglutathione hydrolase, mitochondrial
- Hydroxyacylglutathione hydrolase, cytoplasmic isozyme
- Glutathione-independent glyoxalase HSP31
- Probable glutathione-independent glyoxalase HSP32
- NADPH-dependent methylglyoxal reductase GRE2
- NADPH-dependent aldose reductase GRE3
- Urea amidolyase
- Probable glutathione-independent glyoxalase HSP33
- Probable glutathione-independent glyoxalase SNO4
- Threonine dehydratase, mitochondrial
Sequence:
MSTDSTRYPIQIEKASNDPTLLLNHTCLRVKDPARTVKFYTEHFGMKLLSRKDFEEAKFSLYFLSFPKDDIPKNKNGEPDVFSAHGVLELTHNWGTEKNPDYKINNGNEEPHRGFGHICFSVSDINKTCEELESQGVKFKKRLSEGRQKDIAFALGPDGYWIELITYSREGQEYPKGSVGNKFNHTMIRIKNPTRSLEFYQNVLGMKLLRTSEHESAKFTLYFLGYGVPKTDSVFSCESVLELTHNWGTENDPNFHYHNGNSEPQGYGHICISCDDAGALCKEIEVKYGDKIQWSPKFNQGRMKNIAFLKDPDGYSIEVVPHGLIA
Protein: Spindle assembly abnormal protein 4 (P34402)
Organism: Caenorhabditis elegans
Function: Required for centrosome duplication. Plays a central role in determining centrosome size.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:12600319, ECO:0000269|PubMed:12636923}. Note=Localizes to the centrosome throughout the cell cycle. Localizes to a tiny dot in the center of centrosome. Recruited to the centrosome once per cell cycle, at the time of organelle duplication and remains stably associated after.
Interaction partners:
- Spindle assembly abnormal protein 5
- Probable serine/threonine-protein kinase zyg-1
- Spindle assembly abnormal protein 6
- Spindle-defective protein 2
- Spindle assembly abnormal protein 7
- Spindle-defective protein 5
- Centriolar and ciliogenesis-associated protein hyls-1
- Serine/threonine-protein kinase plk-1
- Tubulin gamma chain
- Suppressor of zyg-1 protein 20
Sequence:
MASDENIGADGEQKPSRPFLRKGQGTARFRMPRNNKTSAGAPPTSELSSASSPSINVPRFSLSNALPNSARTVDSGISNEDETRPPTTASLPMDQPSLSSSPENRLNPAPSVAEEHGHSGQHAEEEEDNDTDEVSAMPSFVPDEPSTLVNSDHELSDDALKYKNAAAEFKAFERRMDSMRSASTITTSLATPSSCAPSNSSEPPTRSTPIMNDLGVGPNNHNWPSSMQELSGISLETPQARPLGSNRINQLVRSEAQTGISLLQHHERPTVTAPLRRNDMMNSSRQNPQNGNVQDENRPEHVYDQPIHVPGSSLDRQKLEIEIRRHRNLNIQLRDTIAHLDYAEESVHTTKRQLEEKISEVNNFKKELIEEFKKCKKGVEEEFEKKFEKIKEDYDELYEKLKRDQRDLERDQKILKKGTGERNKEFTETIATLRDKLRASETKNAQYRQDIRVRDEKLKKKDEEIEKLQKDGNRLKSTLQTLEKRVKQLRTEKERDDKEKEMFAKVAMNRKTSNPVPPVLNQSVPISITSNGPSRHPSSSSLTTFRKPSTSNRERGVSWADEPNEQSLEAVPQEFLMMPVKEMPGKFGKCTIYRDSLGETSKVTDTIANGLLFEYSNGDLRWVNRQNAVNIYISAVDKTVRIDLPTYNISIIHTFQRQVEVLRPGNNITLISIKRREVRTDLIYQNGMYKTEIFNRDGRYVTKDFSNQEVSRKYNPGTHTYRDNQCRYVLVTDYNDFELVEPEFRLRWYQGDPTGLNNQYILKIIGRPECSEKTLRLEVNLSTCEGTLETAEMIGDKRRKTTLFQWKK
Protein: Eukaryotic translation initiation factor 4B (F8VX11)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAASAKKKNKKGKTISLTDFLAEDGGTGGGSTYVSKPVSWADETDDLEGDVSTTWHSNDDDVYRAPPIDRSILPTAPRAAREPNIDRSRLPKSPPYTAFLGNLPYDVTEESIKEFFRGLNISAVRLPREPSNPERLKGFGYAEFEDLDSLLSALSLNEESLGNRRIRVDVADQAQDKEYRDRYDSDRYRDGYRDGYRDGPRRDMDRYGGRDRYDDRGSRDYDRGYDSRIGSGRRAFGSGYRRDDDYRGGGDRYEDRYDRRDDRSWSSRDDYSRDDYRRDDRGPPQRPKLNLKPRSTPKEDDSSASTSQSTRAASIFGGAKPVDTAAREREVEERLQKEQEKLQRQLDEPKLERRPRERHP
Protein: Casein kinase 1-like protein HD16 (EC 2.7.11.1) (Os03g0793500 protein) (Protein EARLY FLOWERING 1) (Protein HEADING DATE 16) (Q852L0)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins (Probable). Can phosphorylate casein on threonine residues in vitro. Involved in the regulation of flowering time through gibberellin (GA) signaling, and independently of photoperiod. Phosphorylates the DELLA protein SLR1, stabilizing SLR1 protein and sustaining SLR1 activity as repressor of GA signaling. Required for normal development of male floral organs and grains, through modulation of GA signaling. Targeted and repressed by the homeobox protein HAZ1 during GA signaling. Can phosphorylate phosvitin and SLR1 in vitro. Is not required for clock function in either the presence or the absence of light signals. Involved in a genetic control pathway for photoperiodic flowering under long day (LD) conditions that includes HD1, GHD7, HD5 and HD2. Phosphorylates and activates GHD7, a major floral repressor under LD conditions. Phosphorylation of GHD7 enhances its function in the repression of EHD1, HD3A and HD3B/RFT1, and obviously delaying flowering.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P48730}. Nucleus {ECO:0000269|PubMed:20400938}.
Interaction partners:
- Os07g0634300 protein
- Low temperature viability protein, expressed
- Bystin
- Serine/threonine-protein kinase RIO2
- LOC495115 protein, putative, expressed
- Os02g0114700 protein
- protein-serine/threonine phosphatase
- Os01g0185400 protein
- Os01g0788950 protein.
- Os03g0115200 protein
Sequence:
MPELRGGVWRARLRSKKVYDVQDADPAASPVSPAPRGRTGRRGGAAAGRGNKTVAEGGGRKALKPRGKGCRAVDLCKDQPCKDLPEVIARKAVTGKAQEDLGLNKVADRAANLMMDGESGDKFAAAEDESTTTPVPERVQVGNSPEYITDRKLGKGGFGQVYVGRRVSGGGSRTGPDAQEVALKFEHRSSKGCNYGPPYEWQVYHTLNGCYGIPSVHYKGRLGDYYILVMDMLGPSLWDVWNSVGQAMSAHMVACIAVEAISILEKLHSKGFVHGDVKPENFLLGHPGSVDEKKLFLIDLGLASRWKEASSGQHVDYDQRPDVFRGTIRYASVHAHLGRTGSRRDDLESLAYTLIFLIRGRLPWQGYQGDNKSFLVCKKKMATSPELLCCFCPAPFKHFLEMVTNMKFDEEPNYPKLISLFDGLIEGPASRPIRIDGALKVGQKRGRMVVNLDDDEQPKKKVRLGSPATQWISVYNARRPMKQRYHYNVADSRLHQHIEKGNEDGLYISCVSSSANFWALIMDAGTGFCSQVYELSQVFLHKDWIMEQWEKNYYITAIAGATNGSSLVVMSKGTPYTQQSYKVSESFPYKWINKKWKEGFHVTSMATAGNRWGVVMSRNAGYSHQVVELDFLYPSEGIHRRWETGYRITSTAATPDQAAFILSIPKRKPMDETQETLRTSSFPSNHVKEKWSKNLYIASICYGRTVC
Protein: 4-hydroxyproline 2-epimerase (4Hyp 2-epimerase) (4HypE) (EC 5.1.1.8) (D2AV87)
Organism: Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / KCTC 9067 / NCIMB 10171 / NRRL 2505 / NI 9100)
Function: Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). Is likely involved in a degradation pathway that converts t4LHyp to alpha-ketoglutarate. Displays no proline racemase activity.
Interaction partners:
- Proline racemase
- Pyrroline-5-carboxylate reductase
- Proline dehydrogenase
- proline dehydrogenase
- Proline racemase
- prolyl aminopeptidase
- Dihydrodipicolinate reductase
- Dihydrodipicolinate reductase
- Proline iminopeptidase
- SoxB2
Sequence:
MRTKRVFHAVDSHTEGMPTRVITGGVGVIPGSTMAERREHFLAEMDHVRTLLMYEPRGHSAMSGAILQPPTRPDADYGVLYIEVSGCLPMCGHGTIGVATVLVETGMVEVVEPVTTIRLDTPAGLVVAEVRVEDGAATAVTITNVPSFSAGLDRTVKVPGIGEVTYDLAYGGNFYAILPIESVGLPFDRAHKQQILDAGLAIMDAINEQDEPVHPLDAGIRGCHHVQFTAPGSDARHSRHAMAIHPGWFDRSPCGTGTSARMAQLHARGELPLDTDFVNESFIGTRFVGRLVEETEVTDLPAVVPTITGRAWVTGTAQYFLDPRDPFPEGFLL