wanglab/gogpt-training-data huggingface dataset:
Protein: GTPase, IMAP family member 4 (G5E9W9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAQYGSMSFNPSTPGASYGERAFSAPQTRLQGGPGRQEPRNSQLRIVLVGKTGAGKSATGNSILGRKVFHSGTAAKSITKKCEKRSSSWKETELVVVDTPGIFDTEVPNAETSKEIIRCILLTSPGPHALLLVVPLGRYTEEEHKATEKILKMFGERARSFMILIFTRKDDLGDTNLHDYLREAPEDIQDLMDIFGDRYCALNNKATGAEQEAQRAQLLGLIQRVVRENKEGCYTNRMYQRAEEEIQKQTQAMQELHRVELEREKARIREEYEEKIRKLEDKVEQEKRKKQMEKKLAEQEAHYAVRQQRARTEVESKDGILELIMTALQIASFILLRLFAED
Protein: Mitochondrial import inner membrane translocase subunit Tim29 (TIM29) (Q9BSF4)
Organism: Homo sapiens (Human)
Function: Component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. The TIM22 complex forms a twin-pore translocase that uses the membrane potential as the external driving force. Required for the stability of the TIM22 complex and functions in the assembly of the TIMM22 protein into the TIM22 complex. May facilitate cooperation between TIM22 and TOM complexes by interacting with TOMM40.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:27554484, ECO:0000269|PubMed:27718247}; Single-pass membrane protein {ECO:0000305}; Intermembrane side {ECO:0000269|PubMed:27718247}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit Tim10 B
- Acylglycerol kinase, mitochondrial
- Mitochondrial import inner membrane translocase subunit Tim22
- Mitochondrial import inner membrane translocase subunit Tim10
- Mitochondrial import inner membrane translocase subunit Tim9
Sequence:
MAAAALRRFWSRRRAEAGDAVVAKPGVWARLGSWARALLRDYAEACRDASAEARARPGRAAVYVGLLGGAAACFTLAPSEGAFEEALLEASGTLLLLAPATRNRESEAFVQRLLWLRGRGRLRYVNLGLCSLVYEAPFDAQASLYQARCRYLQPRWTDFPGRVLDVGFVGRWWVLGAWMRDCDINDDEFLHLPAHLRVVGPQQLHSETNERLFDEKYKPVVLTDDQVDQALWEEQVLQKEKKDRLALSQAHSLVQAEAPR
Protein: Large ribosomal subunit protein uL13 (23 kDa highly basic protein) (60S ribosomal protein L13a) (P40429)
Organism: Homo sapiens (Human)
Function: Associated with ribosomes but is not required for canonical ribosome function and has extra-ribosomal functions. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the ribosome and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation. In the GAIT complex interacts with m7G cap-bound eIF4G at or near the eIF3-binding site and blocks the recruitment of the 43S ribosomal complex. Involved in methylation of rRNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23636399, ECO:0000305|PubMed:14567916}.
Interaction partners:
- Small ribosomal subunit protein eS24
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL30
- Small ribosomal subunit protein eS21
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein eL18
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein uL15
- Small ribosomal subunit protein eS10
- Large ribosomal subunit protein eL8
Sequence:
MAEVQVLVLDGRGHLLGRLAAIVAKQVLLGRKVVVVRCEGINISGNFYRNKLKYLAFLRKRMNTNPSRGPYHFRAPSRIFWRTVRGMLPHKTKRGQAALDRLKVFDGIPPPYDKKKRMVVPAALKVVRLKPTRKFAYLGRLAHEVGWKYQAVTATLEEKRKEKAKIHYRKKKQLMRLRKQAEKNVEKKIDKYTEVLKTHGLLV
Protein: Gibberellin receptor GID1A (EC 3.-.-.-) (AtCXE10) (Carboxylesterase 10) (GID1-like protein 1) (Protein GA INSENSITIVE DWARF 1A) (AtGID1A) (Q9MAA7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as soluble gibberellin (GA) receptor. GA is an essential hormone that regulates growth and development in plants. Binds with high affinity the biologically active gibberellin GA4, but has no affinity for the biologically inactive GAs. In response to GA, interacts with specific DELLA proteins, known as repressors of GA-induced growth, and targets them for degradation via proteasome. Seems to be required for GA signaling that controls root growth, seed germination, stem elongation and flower development. Partially redundant with GID1B and GID1C.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DELLA protein GAI
- DELLA protein RGL1
- DELLA protein RGA
- DELLA protein RGL2
- DELLA protein RGL3
- Gibberellin receptor GID1C
- Gibberellin receptor GID1B
- F-box protein GID2
- Gibberellin 3-beta-dioxygenase 1
- Gibberellin 20 oxidase 1
Sequence:
MAASDEVNLIESRTVVPLNTWVLISNFKVAYNILRRPDGTFNRHLAEYLDRKVTANANPVDGVFSFDVLIDRRINLLSRVYRPAYADQEQPPSILDLEKPVDGDIVPVILFFHGGSFAHSSANSAIYDTLCRRLVGLCKCVVVSVNYRRAPENPYPCAYDDGWIALNWVNSRSWLKSKKDSKVHIFLAGDSSGGNIAHNVALRAGESGIDVLGNILLNPMFGGNERTESEKSLDGKYFVTVRDRDWYWKAFLPEGEDREHPACNPFSPRGKSLEGVSFPKSLVVVAGLDLIRDWQLAYAEGLKKAGQEVKLMHLEKATVGFYLLPNNNHFHNVMDEISAFVNAEC
Protein: Interleukin 8X (Interleukin-8) (Q7SX73)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MSIRMSASLVVVLLALLTITEGMSLRGMGADLRCRCIETESRRIGKLIKKVEMFPPSSHCRDTEIIATLSKSGQEICLDVSAPWVKKVIEKMLANNK
Protein: Glutamate--cysteine ligase (EC 6.3.2.2) (Gamma-ECS) (Gamma-glutamylcysteine synthetase) (Q389A6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Glutathione synthetase
- Branched-chain amino acid aminotransferase, putative
- Branched-chain amino acid aminotransferase, putative
- Cytosolic leucyl aminopeptidase, putative
- Kynurenine aminotransferase, putative
- Multifunctional fusion protein
- aspartate transaminase
- NAD-specific glutamate dehydrogenase
- Aspartate aminotransferase
- glutamine synthetase
Sequence:
MGLLTTGGQPLQWGTEENNRAKEYVSAHGIQQFLWVYNKQKELPDFPFLWGDEIEHQLVRLESRKVKLSLNAADVIKRLSQSSGESTAEWRPEYGSFMVESLPGKPYSSNVDSLCSVEVNMRRRYHMLDAAAGDNTFAVTLVTFPLMGVGGFTTSTETESPCSQSLFVPDACINDSHPRFKALTNNIRLRRGRKVCIQVPMFIDRYTMERTVDPRVNIDLHPRNVEIVCTFSGEKTSSKGKKFSCDTITPKRVPLENEAVTNMTHLYTPVTHYYYAQYFQNLQAERVKQRYQACPCPVPSVNHPCIYMDCMAFGMGCNCLQLTMQLPNEAQARHIYDQLGILCPLFLALSSATPFQKGILCESDVRWLTITASVDDRKYEEVPHIIKSRYDSISVFVSSLTPNLEEFNDEVLRINDSYYNLLTREGVDSRLATHIAHLFIRDPLVIYDQMIDIDDHTHVDHFENIQSTNWQTVRLKLPVLDSTLGWRVEFRVMDVMPTPFENAAYSVFVVLLTRAIMRFGAVFYTKLSIVDENMGRAHNINPCQQHYIMRRDIFASKVTTDPSENCELTVGEVINGKPGEYYGLIPLVRRYLEEENIQSDVVEGYLNFISKRACGEIPTAAQYLRNFVKKHPDYREDSRLTEQIAHDVVNHVHQLACGGNASESMIGAYTLGSKRQREG
Protein: Queuine tRNA-ribosyltransferase, putative (EC 2.4.2.29) (Q8I507)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Queuine tRNA-ribosyltransferase-like protein
Sequence:
MIKLKLQIFFVYIILNILIVLVISKNVVYNEKKLKNKNCMLPNRRHKNDLLKRQVKNRKVILFNDHNIELINLKRKYNKRTKYKNLDAFITNLKVTHVVNHNKSIITYVKKKKLLFSNKIYNHFNYPGFDFSVLKENNNEQDKSRIGIIKTPRGDIETPNFLFCATKGCMKSTPIDFIKKCNTQVILSNTFHLLIQPKPHIIFQLGGLHKFMNWNSPILTDSGGYQIFSMSFGSVSNEIKRKCAGTPQITKMSIKNKKKDNLNNEEDQVNNNFINNNCENNMYNKKGKCLSNNNNSNNNNNNNNNNSEKSVTDTNNLNKQIILKLNEKGAEYKSYYDGSIDLLSPESSIQSQYLLGSDFILVLDECTPYHVDKIYTEKSMHRSHRWYVRCLAEFYKSQNMKNYHEYLNDIYNKKYKTNDKWIKRDKNNQAIYGIIQGGIYPDLRLKSCDFVYNLPFFGLCIGGCLGKDKDMMYAVIKQTMDIIHDIKKKKEKNTYKEKPIHLLGIGQIKDIIYGVKQGIDTFDCVIPSRLARHGYFLSKIKTIETIEKKLKRKLQNEYIKIKLSIFQSDNQPLEEDCACYTCQHYSRAYLHHLYKINDNLLGTLLTIHNVYYMNHLMQDIRNSIKEGNINQIEQKYIKK
Protein: Heat shock protein homolog C338.06c (O74984)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Heat shock protein 16
Sequence:
MLFDAFTNGFMNDIFEFGDRSKFNRSAWLSCWGPALELRETEDTIEVDVEVPGIDKQNLKVDLHGSKLTISGERKKPEEEKAGPLIRWSERCVGAFSRTITLPQPVDEKLIHASLNNGILSIVMKKKNPEFTTRIVEIQ
Protein: Proteinase-activated receptor 1 (Thrombin receptor) (A2BIP6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Beta-arrestin-1
- Arrestin, beta 2a.
- Guanine nucleotide-binding protein subunit alpha
- G-protein alpha 12 alpha 12) alpha 12a)
- Peptidase S1 domain-containing protein
- Peptidase S1 domain-containing protein
- trypsin
- Zgc:171509
- Serine protease 59, tandem duplicate 2
- Zgc:92590
Sequence:
MLRVLLVTGLLALNGSASALPNNETFIRSFSGFFLTVTDEPFDYLDVQEGGSGFSSGQEPTLRKEHLHPPAKKTYHISQEASSFLTGRVATAVIPTIYIIVFIISAPLNLLALVMFARKVRPKKPAAIYMMNLACADLLFVLLLPFRIAYNYNGNNWIYGAGMCRVVTAAFYCNMYCSVLLIMCISVDRFLAVVYPMDSLTWRSPQTATVTCAAMWLLSVGGVTPLLISNQTIHLPDLGITTCHDVLDIQLLREYYLYFFPIFCSLFFFIPLIFSTVCYLRIIQALCAANVENRAKKTRAVIMAVTVFAVFVICFTPTNIILLSHYVRFAYKHNDASYAAYLVSMCMGSISCCLDPLIYYFGSSQCQKQVLAFLRCQGVPGIERSAQFTSSTRSSNLETLKSSVNSQYIKLMA
Protein: Polypeptide N-acetylgalactosaminyltransferase 6 (EC 2.4.1.41) (Polypeptide GalNAc transferase 6) (GalNAc-T6) (pp-GaNTase 6) (Protein-UDP acetylgalactosaminyltransferase 6) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6) (Q8C7U7)
Organism: Mus musculus (Mouse)
Function: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. May participate in synthesis of oncofetal fibronectin. Has activity toward Muc1a, Muc2, EA2 and fibronectin peptides (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q14435}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q14435}.
Interaction partners:
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1
- Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- C1GALT1-specific chaperone 1
Sequence:
MRLLRRRHMSLRLAMLGSVFMLFLFIRQKDVSNQEQAMEKPWLKSLAGQKDQVLDFMLGAVNNIRDVMPKLQIRAPEPPQTLVSTNHSCLPGFYTPAELKPFWDRPPQDPNSPGADGKAFQKKEWTNLETKEKEEGYKKHCFNAFASDRISLQRSLGPDTRPPECVDQKFRRCPPLPTTSVIIVFHNEAWSTLLRTVYSVLHTSPAILLKEIILVDDASTDEHLKERLEQYVQQLQIVRVVRQRERKGLITARLLGASVAQAEVLTFLDAHCECFHGWLEPLLARIAEDKTAVVSPDIVTIDLNTFQFSRPVQRGKAHSRGNFDWSLTFGWEMLPEHEKQRRKDETYPIKSPTFAGGLFSISKAYFEHIGTYDNQMEIWGGENVEMSFRVWQCGGQLEIIPCSVVGHVFRTKSPHTFPKGTSVIARNQVRLAEVWMDDYKKIFYRRNLQAAKMVQENNFGDISERLRLREQLRCHNFSWYLHNVYPEMFVPDLNPTFYGAIKNLGTNQCLDVGENNRGGKPLIMYVCHNLGGNQYFEYTSQRDLRHNIGKQLCLHASGSTLGLRSCQFVGKNSRVPKDEEWELTQDQLIRNSGSGTCLTSQDKKPAMAPCNPRDPYQLWLFV
Protein: sn-1-specific diacylglycerol lipase ABHD11 (EC 3.1.1.116) (Alpha/beta hydrolase domain-containing protein 11) (Q9W3R8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Beta-lactamase-like protein 2 homolog
- GH24548p
- FI03239p
- alkaline phosphatase
- UPF0488 protein CG14286
- AlkB, isoform A)
- Obg-like ATPase 1
Sequence:
MQRLTKSLRSLPFPAGKILRTQLVVRREYSSEIPDPVELSFDSYTGENPETSPPLLTYHGLFGSKQNWRGISKALVRKVSRKVYAIDVRNHGESPHSSVHNSKAMSEDLRLFMEQRSHPNAACMGHSMGGRSMMYFARKYPELVERLIVVDISPISVPRSTGEMTEIFDAMVSLDLSPSMSMSEGRKIAREKLLKATEDETVDFIMLNLRKNPDTGAFSWACNAHVLREFLTRFDKYQSNLEELPPYTGPTTFICGTRSPYMRREQWPQIQKMFPNSEIHWLDAGHLVHFEKPQEFLTIVSEFLNRTE
Protein: Tachykinin-4 (Preprotachykinin-C) (PPT-C) [Cleaved into: Hemokinin (HK1) (Hemokinin-1) (Hemokinin-I) (HK-I)] (Q99N14)
Organism: Mus musculus (Mouse)
Function: Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles. Hemokinin induces plasma extravasation, mast cell degranulation, muscle contraction, salivary secretion and scratching behavior. Increases sperm motility. Induces potent analgesic effects and may play a role in pain modulation. Promotes survival of bone marrow B lineage cells and of cultured LPS-stimulated pre-B cells and may act as an autocrine factor required for B-cell survival and proliferation. Lowers systemic arterial pressure following intravenous injection. Induces interferon-gamma production and may play a role in the inflammatory response. Shows potent affinity and specificity for the NK-1 receptor.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Substance-P receptor
- Protachykinin-1
- Substance-K receptor
- Tachykinin-3
- Neuromedin-K receptor
Sequence:
MLPLLALLLLIGPSVCTTAGDREELAFGAEAESWVTVNLKGIPVPSIELKLQELKRSRTRQFYGLMGKRVGGYQLGRIVQDLLGTRGLSIEGTCRQAASQQRARPGAVTRESLQSREEDEAPLTTSNV
Protein: Heat shock factor protein 4 (HSF 4) (hHSF4) (Heat shock transcription factor 4) (HSTF 4) (Q9ULV5)
Organism: Homo sapiens (Human)
Function: Heat-shock transcription factor that specifically binds heat shock promoter elements (HSE). Required for denucleation and organelle rupture and degradation that occur during eye lens terminal differentiation, when fiber cells that compose the lens degrade all membrane-bound organelles in order to provide lens with transparency to allow the passage of light (By similarity). In this process, may regulate denucleation of lens fiber cells in part by activating DNASE2B transcription (By similarity). May be involved in DNA repair through the transcriptional regulation of RAD51. May up-regulate p53/TP53 protein in eye lens fiber cells, possibly through protein stabilization. In the eye lens, controls the expression of alpha-crystallin B chain/CRYAB and consequently may be involved in the regulation of lysosomal acidification (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:10488131}.
Interaction partners:
- Neurotrimin
- Phakinin
- Cell surface A33 antigen
- Heat shock factor protein 2
- V-set and immunoglobulin domain-containing protein 2
- Beta-crystallin B1
- Gap junction alpha-8 protein
- Lens fiber membrane intrinsic protein
- Gamma-crystallin D
- Beta-crystallin B3
Sequence:
MQEAPAALPTEPGPSPVPAFLGKLWALVGDPGTDHLIRWSPSGTSFLVSDQSRFAKEVLPQYFKHSNMASFVRQLNMYGFRKVVSIEQGGLLRPERDHVEFQHPSFVRGREQLLERVRRKVPALRGDDGRWRPEDLGRLLGEVQALRGVQESTEARLRELRQQNEILWREVVTLRQSHGQQHRVIGKLIQCLFGPLQAGPSNAGGKRKLSLMLDEGSSCPTPAKFNTCPLPGALLQDPYFIQSPLPETNLGLSPHRARGPIISDIPEDSPSPEGTRLSPSSDGRREKGLALLKEEPASPGGDGEAGLALAPNECDFCVTAPPPLPVAVVQAILEGKGSFSPEGPRNAQQPEPGDPREIPDRGPLGLESGDRSPESLLPPMLLQPPQESVEPAGPLDVLGPSLQGREWTLMDLDMELSLMQPLVPERGEPELAVKGLNSPSPGKDPTLGAPLLLDVQAALGGPALGLPGALTIYSTPESRTASYLGPEASPSP
Protein: RNA helicase (EC 3.6.4.13) (Q9N5K1)
Organism: Caenorhabditis elegans
Interaction partners:
- peptidylprolyl isomerase
- RING-type domain-containing protein
- NF-kappa-B-activating protein C-terminal domain-containing protein
- Peptidyl-prolyl cis-trans isomerase
- Probable pre-mRNA-splicing factor ATP-dependent RNA helicase mog-5
- Splicing factor Cactin
- RNA helicase
- Pre-mRNA-splicing factor CWC22 homolog
- Pre-mRNA-splicing factor syf-2
- Serrate RNA effector molecule homolog
Sequence:
MSTDVEAARRKYEDRRRKIQEEEMKERRDGMNLSSGDDDQDVDDMFLTALQRKREKVHRRALLKQVLAPTMNQKEEIERKRKKKEEDKQSEEARKTLLEKHAEIMETQGVIDESERQLMEEEELLDKVTRGGGLLAVAELTKGEKYEEPIVTAWRPPGHIRRQSQEDYEIQRKRLGISCEGDHIPPPIGSFLEMKFPKSLLEFMQKQKGIVTPTAIQIQGIPVALSGRDMIGIASTGSGKTMTFVLPLVMFCLEQEMKLPFMRSEGPFGLIIVPSRELARQIFDLIIEMFDALGKAGLPEMRAGLCIGGVPIGEQAKDVRDGIHIVVATPGRLSDMLTKKIINLEVCRYLVLDEADRMLDMGFEDEIKSIFYFFKAQRQTLLFSATMPRKIQFFAKSALVKPIVVNVGRAGAASLNVLQELEFVRSENKLVRVLECLQKTSPKVLIFAEKKVDVDNIYEYLLVKGVEVASIHGGKDQSDRHAGIEAFRKNEKDVLVATDVASKGLDFQGIEHVINFDMPEDIENYVHRIGRTGRSGRKGLATTFINKKSEMSVLSDLKQLLAEAGQELPEFLKMLAGDEEGTAPAGTNAEKGCAYCSGLGHRITDCPKLAGIGNKTTQALARGGGDDGGF
Protein: Pre-piRNA 3'-exonuclease trimmer (EC 3.1.13.-) (PARN-like domain-containing protein 1 homolog) (BmPNLDC1) (H9JAQ7)
Organism: Bombyx mori (Silk moth)
Function: 3'-5' exonuclease that specifically cleaves precursor piRNAs (pre-piRNAs) at their 3' ends. Trims pre-piRNAs to their mature size, a process required for piRNAs maturation and stabilization, and subsequent pre-piRNAs 2'-O-methylation. The piRNA metabolic process mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons.
Subcellular location: Mitochondrion outer membrane {ECO:0000305|PubMed:26919431}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- RNA_bind domain-containing protein.
- Tudor and KH domain-containing protein homolog
- Piwi-like protein Siwi
Sequence:
MDITKENYYEELDNIAKNIKDSCFISFDAEFSAILTKESFKYSLFDTNEERYNKYKTQISTMKMMQVGLTMFQYDRELDAYLATGYTFHLCPQLIGTINQSLIFQASTLKFLCKHNFDFNKFIYEGLPYLSKSDEALLNRYRIENNLFDYVSESLEFDEEKQINQCSSEVSKWLSSSIEDTMYLDIDNAICRYLLHLELRQRYPGILTTDSLGNSKKILIYRDKNVEGAKNAPIAILEDNLIAYLLGFLHVIKLLETHKKPIVGHNMFLDMLFLHNQFIGPLPDSYTMFKKNINSVFPTIFDTKYISHAMSKKLTFSESWKSNALQDLYEFFAERKCKKLEYGINIVRLTTPFDIKQSYHEAGWDAYCSGYCFIRLGHWAACENRGKSHVIGPREKLAALAPYCNKVNVIRGGVSYMNFSENDPPRNRPVLLHVKCLKDTVIDVEKVASLLGSFGSIDIKPCGKRAALVATGAQFMVDKILKTYENNRDYRISKYSVYKHSVAGRFAIWSGSIVTGGLALYLIHKKFKSILL
Protein: Dioscorin DB3S (EC 1.6.5.4) (EC 4.2.1.1) (Tuber storage protein DB3S) (allergen Dio p TSP) (Q75N34)
Organism: Dioscorea polystachya (Chinese yam)
Function: Storage protein of tuber. Involved in protection against oxidative stress (Probable). Has carbonate dehydratase and weak trypsin inhibitor activity detected by measuring the dehydration of sodium bicarbonate and the inhibition of trypsin-catalyzed hydrolysis of N-benzoyl-L-arginine-4-nitro anilide, respectively. Contrarily, no carbonate dehydratase or trypsin inhibitor activity detected by measuring the hydrolysis of 4-nitrophenyl acetate or the inhibition of bovine trypsin-catalyzed hydrolysis of N-benzoyl-L-arginine ethyl ester, respectively. Has dehydroascorbate (DHA) reductase and monodehydroascorbate (MDA) reductase activities (Ref.5). Catalyzes the reactions of carbonate dehydratase and DHA reductase independently of zinc and glutathione (GSH). The coupled reaction is capable of recycling a plant antioxidant ascorbate using ubiquitous compounds H(2)O and CO(2) (By similarity). Exhibits antioxidant activity. Able to scavenge 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical and hydroxyl radicals. Exhibits immunomodulatory activity. Activates Toll-like receptor 4 signaling pathways by up-regulating the gene expression of pro-inflammatory cytokines, such as tumor necrosis factor alpha, interleukin-1 beta and interleukin-6, and chemokines RANTES and MCP-1, in mouse RAW 264.7 macrophages. Stimulates the phagocytosis of E.coli by the LPS-treated mouse macrophages (By similarity).
Interaction partners:
Sequence:
MSSSTLLHLLLLSSLLFSCLANVEDEFSYIEGNPNGPENWGNLKPEWETCGKGMEQSPIQLRDNRVIFDQTLGRLRRNYRAVDARLRNSGHDVLVEFKGNAGSLSINRVAYQLKRIHFHSPSEHEMNGERFDLEAQLVHESQDQKRAVVSILFIFGRADPFLSDLEDFIKQFSSSQKNEINAGVVDPNQLQIDDSAYYRYMGSFTAPPCTEGISWTVMRKVATVSPRQVLLLKQAVNENAINNARPLQPTNFRSVFYFEQLKSKVCAI
Protein: Sister chromatid cohesion protein PDS5 homolog A (Cell proliferation-inducing gene 54 protein) (Sister chromatid cohesion protein 112) (SCC-112) (Q29RF7)
Organism: Homo sapiens (Human)
Function: Probable regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair.
Subcellular location: Nucleus {ECO:0000269|PubMed:11076961, ECO:0000269|PubMed:15019998}. Note=Associated with chromatin through most of the cell cycle. Dissociates from chromatin in late prophase, reassociates during late telophase. {ECO:0000269|PubMed:11076961, ECO:0000269|PubMed:15019998}.
Interaction partners:
- Wings apart-like protein homolog
- Cohesin subunit SA-1
- Cohesin subunit SA-2
- Double-strand-break repair protein rad21 homolog
- Sororin
- Structural maintenance of chromosomes protein 3
- Structural maintenance of chromosomes protein 1A
- Nipped-B-like protein
- N-acetyltransferase ESCO1
- MAU2 chromatid cohesion factor homolog
Sequence:
MDFTAQPKPATALCGVVSADGKIAYPPGVKEITDKITTDEMIKRLKMVVKTFMDMDQDSEDEKQQYLPLALHLASEFFLRNPNKDVRLLVACCLADIFRIYAPEAPYTSHDKLKDIFLFITRQLKGLEDTKSPQFNRYFYLLENLAWVKSYNICFELEDCNEIFIQLFRTLFSVINNSHNKKVQMHMLDLMSSIIMEGDGVTQELLDSILINLIPAHKNLNKQSFDLAKVLLKRTVQTIEACIANFFNQVLVLGRSSVSDLSEHVFDLIQELFAIDPHLLLSVMPQLEFKLKSNDGEERLAVVRLLAKLFGSKDSDLATQNRPLWQCFLGRFNDIHVPVRLESVKFASHCLMNHPDLAKDLTEYLKVRSHDPEEAIRHDVIVTIITAAKRDLALVNDQLLGFVRERTLDKRWRVRKEAMMGLAQLYKKYCLHGEAGKEAAEKVSWIKDKLLHIYYQNSIDDKLLVEKIFAQYLVPHNLETEERMKCLYYLYASLDPNAVKALNEMWKCQNMLRSHVRELLDLHKQPTSEANCSAMFGKLMTIAKNLPDPGKAQDFVKKFNQVLGDDEKLRSQLELLISPTCSCKQADICVREIARKLANPKQPTNPFLEMVKFLLERIAPVHIDSEAISALVKLMNKSIEGTADDEEEGVSPDTAIRSGLELLKVLSFTHPTSFHSAETYESLLQCLRMEDDKVAEAAIQIFRNTGHKIETDLPQIRSTLIPILHQKAKRGTPHQAKQAVHCIHAIFTNKEVQLAQIFEPLSRSLNADVPEQLITPLVSLGHISMLAPDQFASPMKSVVANFIVKDLLMNDRSTGEKNGKLWSPDEEVSPEVLAKVQAIKLLVRWLLGMKNNQSKSANSTLRLLSAMLVSEGDLTEQKRISKSDMSRLRLAAGSAIMKLAQEPCYHEIITPEQFQLCALVINDECYQVRQIFAQKLHKALVKLLLPLEYMAIFALCAKDPVKERRAHARQCLLKNISIRREYIKQNPMATEKLLSLLPEYVVPYMIHLLAHDPDFTRSQDVDQLRDIKECLWFMLEVLMTKNENNSHAFMKKMAENIKLTRDAQSPDESKTNEKLYTVCDVALCVINSKSALCNADSPKDPVLPMKFFTQPEKDFCNDKSYISEETRVLLLTGKPKPAGVLGAVNKPLSATGRKPYVRSTGTETGSNINVNSELNPSTGNRSREQSSEAAETGVSENEENPVRIISVTPVKNIDPVKNKEINSDQATQGNISSDRGKKRTVTAAGAENIQQKTDEKVDESGPPAPSKPRRGRRPKSESQGNATKNDDLNKPINKGRKRAAVGQESPGGLEAGNAKAPKLQDLAKKAAPAERQIDLQR
Protein: BH3-interacting domain death agonist (p22 BID) (BID) [Cleaved into: BH3-interacting domain death agonist p15 (p15 BID); BH3-interacting domain death agonist p13 (p13 BID); BH3-interacting domain death agonist p11 (p11 BID)] (P55957)
Organism: Homo sapiens (Human)
Function: Induces caspases and apoptosis. Counters the protective effect of BCL2 (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14583606}. Mitochondrion membrane {ECO:0000269|PubMed:14583606}. Mitochondrion outer membrane {ECO:0000269|PubMed:29531808}. Note=When uncleaved, it is predominantly cytoplasmic. {ECO:0000269|PubMed:14583606}.; SUBCELLULAR LOCATION: [BH3-interacting domain death agonist p15]: Mitochondrion membrane {ECO:0000250|UniProtKB:P70444}. Note=Translocates to mitochondria as an integral membrane protein. {ECO:0000250|UniProtKB:P70444}.; SUBCELLULAR LOCATION: [BH3-interacting domain death agonist p13]: Mitochondrion membrane {ECO:0000250|UniProtKB:P70444}. Note=Associated with the mitochondrial membrane. {ECO:0000250|UniProtKB:P70444}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:14583606}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:14583606}.; SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion membrane {ECO:0000269|PubMed:14583606}. Note=A significant proportion of isoform 2 localizes to mitochondria, it may be cleaved constitutively. {ECO:0000269|PubMed:14583606}.
Interaction partners:
- Bcl-2 homologous antagonist/killer
- Bcl-2-like protein 1
- Apoptosis regulator BAX
- Apoptosis regulator Bcl-2
- Induced myeloid leukemia cell differentiation protein Mcl-1
- Caspase-8
- Bcl-2-like protein 11
- Bcl-2-related protein A1
- Caspase-10
- Caspase-2
Sequence:
MDCEVNNGSSLRDECITNLLVFGFLQSCSDNSFRRELDALGHELPVLAPQWEGYDELQTDGNRSSHSRLGRIEADSESQEDIIRNIARHLAQVGDSMDRSIPPGLVNGLALQLRNTSRSEEDRNRDLATALEQLLQAYPRDMEKEKTMLVLALLLAKKVASHTPSLLRDVFHTTVNFINQNLRTYVRSLARNGMD
Protein: GTP-binding nuclear protein GSP1/CNR1 (Chromosome stability protein 17) (GTPase Ran homolog) (Genetic suppressor of PRP20-1) (P32835)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Essential for cell viability. By analogy with Ras, Ran may be activated when GTP is exchanged for bound GDP by RCC1 and inactivated when GTP is hydrolyzed by Ran upon activation by RanGAP1.
Subcellular location: Nucleus.
Interaction partners:
- Exportin-1
- Ran-specific GTPase-activating protein 1
- Ran GTPase-activating protein 1
- Exportin-T
- Importin subunit beta-1
- Guanine nucleotide exchange factor SRM1
- Nucleoporin NUP2
- Importin subunit beta-4
- U3 small nucleolar RNA-associated protein 8
- Importin subunit beta-3
Sequence:
MSAPAANGEVPTFKLVLVGDGGTGKTTFVKRHLTGEFEKKYIATIGVEVHPLSFYTNFGEIKFDVWDTAGQEKFGGLRDGYYINAQCAIIMFDVTSRITYKNVPNWHRDLVRVCENIPIVLCGNKVDVKERKVKAKTITFHRKKNLQYYDISAKSNYNFEKPFLWLARKLAGNPQLEFVASPALAPPEVQVDEQLMQQYQQEMEQATALPLPDEDDADL