wanglab/gogpt-training-data huggingface dataset:
Protein: tRNA-splicing endonuclease subunit SEN54 (Splicing endonuclease of 54 kDa) (tRNA-intron endonuclease SEN54) (Q02825)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Non-catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5' and 3' splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. May be required to embody the molecular ruler of the complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:12925762}. Endomembrane system {ECO:0000269|PubMed:12925762}; Peripheral membrane protein {ECO:0000269|PubMed:12925762}. Mitochondrion outer membrane {ECO:0000269|PubMed:12925762, ECO:0000269|PubMed:16823961}; Peripheral membrane protein {ECO:0000269|PubMed:12925762, ECO:0000269|PubMed:16823961}; Cytoplasmic side {ECO:0000269|PubMed:12925762, ECO:0000269|PubMed:16823961}. Note=The tRNA splicing endonuclease complex is predominantly associated with the outer membrane of mitochondria, suggesting that tRNA splicing mainly takes place on the mitochondrial surface.
Interaction partners:
- tRNA-splicing endonuclease subunit SEN15
- tRNA-splicing endonuclease subunit SEN2
- tRNA-splicing endonuclease subunit SEN34
- tRNA ligase
- tRNA 2'-phosphotransferase
- Ribonucleases P/MRP protein subunit POP3
- RNases MRP/P 32.9 kDa subunit
- Ribonuclease P/MRP protein subunit POP5
- Ribonuclease P/MRP protein subunit RPP1
- Ribonucleases P/MRP protein subunit POP7
Sequence:
MQFAGKKTDQVTTSNPGFEEEEEEEEELQQDWSQLASLVSKNAALSLPKRGEKDYEPDGTNLQDLLLYNASKAMFDTISDSIRGTTVKSEVRGYYVPHKHQAVLLKPKGSFMQTMGRADSTGELWLDFHEFVYLAERGTILPYYRLEAGSNKSSKHETEILLSMEDLYSLFSSQQEMDQYFVFAHLKRLGFILKPSNQEAAVKTSFFPLKKQRSNLQAITWRLLSLFKIQELSLFSGFFYSKWNFFFRKYTTSPQLYQGLNRLVRSVAVPKNKKELLDAQSDREFQKVKDIPLTFKVWKPHSNFKKRDPGLPDFQVFVYNKNDDLQHFPTYKELRSMFSSLDYKFEFLSEIEDDDDWETNSYVEDIPRKEYIHKRSAKSQTEKSESSMKASFQKKTAQSSTKKKRKAYPPHIQQNRRLKTGYRSFIIAIMDNGLISFVKMSEADFGSESVWYTPNTQKKVDQRWKKH
Protein: Shieldin complex subunit 1 (RINN1-REV7-interacting novel NHEJ regulator 3) (Shield complex subunit 1) (Q8IYI0)
Organism: Homo sapiens (Human)
Function: Component of the shieldin complex, which plays an important role in repair of DNA double-stranded breaks (DSBs). During G1 and S phase of the cell cycle, the complex functions downstream of TP53BP1 to promote non-homologous end joining (NHEJ) and suppress DNA end resection. Mediates various NHEJ-dependent processes including immunoglobulin class-switch recombination, and fusion of unprotected telomeres.
Subcellular location: Chromosome {ECO:0000269|PubMed:29656893}.
Interaction partners:
- Shieldin complex subunit 2
- Mitotic spindle assembly checkpoint protein MAD2B
- Shieldin complex subunit 3
- TP53-binding protein 1
- CST complex subunit CTC1
Sequence:
MAARDATSGSLSEESSALDLPSACDIRDYVLQGPSQEANSEAFSSLEFHSFPYSSDVDPDTSNLNIEQNNSWTAENFWLDPAVKGQSEKEEDDGLRKSLDRFYEMFGHPQPGSANSLSASVCKCLSQKITQLRGQESQKYALRSFQMARVIFNRDGCSVLQRHSRDTHFYPLEEGSTSLDDEKPNPGLSKDITHFLLQQNVMKDL
Protein: Uncharacterized protein (Q57UQ0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MWFTSLARSRCGGPTWRLFSATPIVSGCVGEFHSIALYAPVRNEFKTSPDCAASGFKAHSSSAGSSSSSSSSSRFTSAAEEEKMSTPSSGAKVRALQLHNLPRSWMYEEIVEFLHQVAEHAGIEQPSYHSTASCNSDGNEESDSAVPHVTSPFVARLHIPFGRRTGIVYGTPIILITSDSLADYLLRDLTFDPDDYRSRIYFTETKADRWYNGVGGLSAVSEEAAVVAEQQQALSTLELDRYLLAPDLLYDMAKMRQRRLVTRRSKLLLHTFADDESDMKDTHDVEGCDASAGGNAVFGERTEEQNEEEEEDRTRKGGGKAPTLKCAGEYKDLGRGSMHSVPLPAPYVRGRRGA
Protein: Ferredoxin-1, chloroplastic (Ferredoxin I) (Fd I) (P27787)
Organism: Zea mays (Maize)
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. Occupies a key position both for transferring the photoreducing power to Fd-NADP(+) oxidoreductase (FNR), hence the formation of NADPH, and for mediating the cyclic electron flow around photosystem I (PSI).
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:9952443}.
Interaction partners:
- Ferredoxin--NADP reductase, chloroplastic
- Sulfite reductase [ferredoxin], chloroplastic
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic
- Photosystem I reaction center subunit III
- Photosystem I reaction center subunit III
- Photosystem I reaction center subunit IV A
Sequence:
MATVLGSPRAPAFFFSSSSLRAAPAPTAVALPAAKVGIMGRSASSRRRLRAQATYNVKLITPEGEVELQVPDDVYILDQAEEDGIDLPYSCRAGSCSSCAGKVVSGSVDQSDQSYLDDGQIADGWVLTCHAYPTSDVVIETHKEEELTGA
Protein: Mitochondrial import inner membrane translocase subunit TIM22 (A0A1D8PI78)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Essential core component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. In the TIM22 complex, it constitutes the voltage-activated and signal-gated channel. Forms a twin-pore translocase that uses the membrane potential as external driving force in 2 voltage-dependent steps (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q12328}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit TIM9
- Mitochondrial import inner membrane translocase subunit TIM54
- Mitochondrial import inner membrane translocase subunit
- Mitochondrial import inner membrane translocase subunit
- Uncharacterized protein
- Mitochondrial import inner membrane translocase subunit TIM23
- NADH-ubiquinone oxidoreductase
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- Mitochondrial import inner membrane translocase subunit TIM17
- NADH-ubiquinone oxidoreductase chain 1
Sequence:
MSLWGVYTGPQPPKKPLQEMTQEEQAEEGARQMIGFMNSCPGKTVMAGVSGFALGGFFGLFMASMAYDTPIGTDAVKHISELPFKQQMKLQFTDMAKRSYSSAKNFGYIGMVYSGVECTIESLRAKHDIYNGVSAGCITGAGLAIRAGPQAALVGCAGFAAFSLAIDMYLNSDAAPPPKNDYDI
Protein: sn-glycerol-3-phosphate transport system permease protein UgpA (P10905)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex UgpBAEC involved in sn-glycerol-3-phosphate (G3P) import. Probably responsible for the translocation of the substrate across the membrane (Probable). Can also transport glycerophosphoryl diesters, which are hydrolyzed to G3P and alcohol during transport. The G3P moiety can be detected in the cytoplasm whereas the corresponding alcohol is usually found in the culture medium. It was proposed by Yang et al that the complex could also transport glycerol-2-phosphate (G2P) in vivo, but it was shown later by Wuttge et al that UgpB does not bind G2P, questioning this transport activity. G2P might be converted in the periplasm to G3P before its transport.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- sn-glycerol-3-phosphate-binding periplasmic protein UgpB
- sn-glycerol-3-phosphate import ATP-binding protein UgpC
- sn-glycerol-3-phosphate transport system permease protein UgpE
- Maltose/maltodextrin import ATP-binding protein MalK
- Maltose/maltodextrin transport system permease protein MalG
- Inner membrane ABC transporter permease protein YcjP
- Glycerophosphodiester phosphodiesterase, cytoplasmic
- Spermidine/putrescine import ATP-binding protein PotA
- Putrescine transport system permease protein PotH
- Maltose/maltodextrin transport system permease protein MalF
Sequence:
MSSSRPVFRSRWLPYLLVAPQLIITVIFFIWPAGEALWYSLQSVDPFGFSSQFVGLDNFVTLFHDSYYLDSFWTTIKFSTFVTVSGLLVSLFFAALVEYIVRGSRFYQTLMLLPYAVAPAVAAVLWIFLFNPGRGLITHFLAEFGYDWNHAQNSGQAMFLVVFASVWKQISYNFLFFYAALQSIPRSLIEAAAIDGAGPIRRFFKIALPLIAPVSFFLLVVNLVYAFFDTFPVIDAATSGGPVQATTTLIYKIYREGFTGLDLASSAAQSVVLMFLVIVLTVVQFRYVESKVRYQ
Protein: Mixed lineage kinase domain-like protein (hMLKL) (Q8NB16)
Organism: Homo sapiens (Human)
Function: Pseudokinase that plays a key role in TNF-induced necroptosis, a programmed cell death process. Does not have protein kinase activity. Activated following phosphorylation by RIPK3, leading to homotrimerization, localization to the plasma membrane and execution of programmed necrosis characterized by calcium influx and plasma membrane damage. In addition to TNF-induced necroptosis, necroptosis can also take place in the nucleus in response to orthomyxoviruses infection: following activation by ZBP1, MLKL is phosphorylated by RIPK3 in the nucleus, triggering disruption of the nuclear envelope and leakage of cellular DNA into the cytosol.following ZBP1 activation, which senses double-stranded Z-RNA structures, nuclear RIPK3 catalyzes phosphorylation and activation of MLKL, promoting disruption of the nuclear envelope and leakage of cellular DNA into the cytosol (By similarity). Binds to highly phosphorylated inositol phosphates such as inositolhexakisphosphate (InsP6) which is essential for its necroptotic function.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24316671}. Cell membrane {ECO:0000269|PubMed:24316671, ECO:0000269|PubMed:29883610}. Nucleus {ECO:0000250|UniProtKB:Q9D2Y4}. Note=Localizes to the cytoplasm and translocates to the plasma membrane on necroptosis induction (PubMed:24316671). Localizes to the nucleus in response to orthomyxoviruses infection (By similarity). {ECO:0000250|UniProtKB:Q9D2Y4, ECO:0000269|PubMed:24316671}.
Interaction partners:
- Receptor-interacting serine/threonine-protein kinase 3
- Tumor necrosis factor
- Receptor-interacting serine/threonine-protein kinase 1
- Serine/threonine-protein phosphatase PGAM5, mitochondrial
- Caspase-8
- FAS-associated death domain protein
- NACHT, LRR and PYD domains-containing protein 3
- Charged multivesicular body protein 1a
- Charged multivesicular body protein 3
- RNF103-CHMP3 readthrough
Sequence:
MENLKHIITLGQVIHKRCEEMKYCKKQCRRLGHRVLGLIKPLEMLQDQGKRSVPSEKLTTAMNRFKAALEEANGEIEKFSNRSNICRFLTASQDKILFKDVNRKLSDVWKELSLLLQVEQRMPVSPISQGASWAQEDQQDADEDRRAFQMLRRDNEKIEASLRRLEINMKEIKETLRQYLPPKCMQEIPQEQIKEIKKEQLSGSPWILLRENEVSTLYKGEYHRAPVAIKVFKKLQAGSIAIVRQTFNKEIKTMKKFESPNILRIFGICIDETVTPPQFSIVMEYCELGTLRELLDREKDLTLGKRMVLVLGAARGLYRLHHSEAPELHGKIRSSNFLVTQGYQVKLAGFELRKTQTSMSLGTTREKTDRVKSTAYLSPQELEDVFYQYDVKSEIYSFGIVLWEIATGDIPFQGCNSEKIRKLVAVKRQQEPLGEDCPSELREIIDECRAHDPSVRPSVDEILKKLSTFSK
Protein: Endo-1,4-beta-xylanase xynf11a (Xylanase xynf11a) (EC 3.2.1.8) (1,4-beta-D-xylan xylanohydrolase xynf11a) (Q4WG11)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Endo-1,4-beta-xylanase C
- Probable exo-1,4-beta-xylosidase xlnD
- Xylanolytic transcriptional activator xlnR
- Probable DNA-binding protein creA
- Probable alpha-L-arabinofuranosidase B
- Probable D-xylulose reductase A
- Probable catabolite repression protein creC
Sequence:
MVSFSYLLLACSAIGALAAPVEPETTSFNETALHEFAERAGTPSSTGWNNGYYYSFWTDGGGDVTYTNGAGGSYSVNWRNVGNFVGGKGWNPGSARTINYGGSFNPSGNGYLAVYGWTTNPLIEYYVVESYGTYNPGSGGTFRGTVNTDGGTYNIYTAVRYNAPSIEGTKTFTQYWSVRTSKRTGGTVTMANHFNAWSRLGMNLGTHNYQIVATEGYQSSGSASITVY
Protein: Bifunctional protein PutA [Includes: Proline dehydrogenase (EC 1.5.5.2) (Proline oxidase); Delta-1-pyrroline-5-carboxylate dehydrogenase (P5C dehydrogenase) (EC 1.2.1.88) (L-glutamate gamma-semialdehyde dehydrogenase)] (P10503)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Oxidizes proline to glutamate for use as a carbon and nitrogen source and also function as a transcriptional repressor of the put operon.
Interaction partners:
- Sodium/proline symporter
- Pyrroline-5-carboxylate reductase
- Glutamate 5-kinase
- NADP-specific glutamate dehydrogenase
- Glutamate dehydrogenase
- Gamma-glutamyl phosphate reductase
- Glutamine synthetase
- Sodium/glucose cotransporter
- Glutamate synthase large chain
- Glutamate synthase small chain
Sequence:
MGTTTMGVKLDDATRERIKMAASRIDRTPHWLIKQAIFSYLDKLENSDTLPELPALFVGAANESEEPVAPQDEPHQPFLEFAEQILPQSVSRAAITAAWRRPETDAVSMLMEQARLSPPVAEQAHKLAYQLAEKLRNQKSASGRAGMVQGLLQEFSLSSQEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGRLVSTHNEANLSRSLNRIIGKSGEPLIRKGVDMAMRLMGEQFVTGETIAQALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASNGRGIYEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGLNIDAEEADRLEISLDLLEKLCFEPELAGWNGIGFVIQAYQKRCPLVIDYLVDLASRSRRRLMIRLVKGAYWDSEIKRAQMEGLEGYPVYTRKVYTDVSYLACAKKLLAVPNLIYPQFATHNAHTLAAIYHLAGQNYYPGQYEFQCLHGMGEPLYEQVTGKVADGKLNRPCRIYAPVGTHETLLAYLVRRLLENGANTSFVNRIADATLPLDELVADPVEAVEKLAQQEGQAGIPHPKIPLPRDLYGEGRINSAGLDLANEHRLASLSSALLSNAMQKWQAKPVLEQPVADGEMTPVINPAEPKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADARVRGVMFTGSTEVATLLQRNIATRLDAQGRPIPLIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHIQTMRAKGRPVFQAARENSDDAQEWQTGTFVMPTLIELENFAELEKEVFGPVLHVVRYNRNQLAELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLAHRPPNALNTTLTRQDARYPVDAQLKTTLLAPLTALTQWAADRPALQTLCRQFADLAQAGTQRLLPGPTGERNTWTLLPRERVLCLADDEQDALTQLAAVLAVGSQALWSDDAFHRDLAKRLPAAVAARVQFAKAETLMAQPFDAVIFHGDSDKLRTVCEAVAAREGAIVSVQGFARGESNILLERLYIERSLSVNTAAAGGNASLMTIG
Protein: FrnE protein-like (Putative frnE protein) (Thioredoxin superfamily protein) (Q9FMB1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAESASNTASKKLIQIDVSSDSVCPWCFVGKKNLDKAIEASKDQYNFEIRWRPFFLDPSAPKEGVSKKEFYLQKYGNRYQGMFARMSEVFKGLGLEFDTAGLTGNSLDSHRLIHYTGKQAPEKQHTLVEELFIGYFTQGKFIGDREFLVETANKVGIEGAEEFLSDPNNGVTEVKEELAKYSKNITGVPNYTINGKVKLSGAQPPETFQSAFKAASA
Protein: Basic leucine zipper transcriptional factor ATF-like 3 (B-ATF-3) (Q9D275)
Organism: Mus musculus (Mouse)
Function: AP-1 family transcription factor that controls the differentiation of CD8(+) thymic conventional dendritic cells in the immune system. Acts via the formation of a heterodimer with JUN family proteins that recognizes and binds DNA sequence 5'-TGA[CG]TCA-3' and regulates expression of target genes. Required for development of CD8-alpha(+) classical dendritic cells (cDCs) and related CD103(+) dendritic cells that cross-present antigens to CD8 T-cells and produce interleukin-12 (IL12) in response to pathogens.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
- Basic leucine zipper transcriptional factor ATF-like
- Basic leucine zipper transcriptional factor ATF-like 2
- Transcription factor Jun
- Interferon regulatory factor 8
- Integrin alpha-E
- Chemokine XC receptor 1
- Interferon regulatory factor 4
- C-type lectin domain family 9 member A
- Integrin alpha-X
- Zinc finger and BTB domain-containing protein 46
Sequence:
MSQGPPAVSVLQRSVDAPGNQPQSPKDDDRKVRRREKNRVAAQRSRKKQTQKADKLHEEHESLEQENSVLRREISKLKEELRHLSEVLKEHEKMCPLLLCPMNFVQLRSDPVASCLPR
Protein: Regulator of mucoid phenotype (Q8GM81)
Organism: Klebsiella pneumoniae
Interaction partners:
Sequence:
MEKYIYFICNKDVNIVLTDDYFFYYGLKQLTGLPLLHITYEGVINKSIAIKHKRNIRVLVDSRIFYSGKWGGYKMLRGSINMISQWMWLDVSGGGRFYPKGCDYDIYVNMQGNVKNNIEKLYFAFLKKNVSQVVNHYPRLTQKEQAVLQCLLKNGGINEIKSQLKIEEKTLSCYRSKITRKFGCKRYIRLMYLYSLNKEMGDERWLMPSI
Protein: MHC class I antigen (Major histocompatibility complex class I b) (O19440)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MAQRTLFLLLAAALTMIETRAGPHSMRYFETAVFRPGLGEPRFISVGYVDNTQFVSFDSDAENPRSEPRAPWMEQEGPEYWERETQIAKDNEQSFGWSLRNLIHYYNQSKGGFHTFQRLSGCDMGLDGRLLRGYLQFAYDGRDYITLNEDLKTWMAADLVALITRRKWEQAGAAELYKFYLEGECVEWLRRYLELGNETLLRTDPPKAHVTHHPRPAGDVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWAAVVVPLGKEQNYTCHVYHEGLPEPLTLRWEPPPSTGSNMVNIAVLVVLGAVIIIEAMVAFVLKSSRKIAILPGPAGTKGSSAS
Protein: Presenilin spe-4 (Q01608)
Organism: Caenorhabditis elegans
Function: Potential catalytic subunit of the gamma-secretase complex during spermatogenesis, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors (lin-12 or glp-1) (Probable). Involved in spermatid formation during meiosis II. May be required for proper localization of macromolecules that are subject to asymmetric partitioning during spermatogenesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9819355}; Multi-pass membrane protein {ECO:0000269|PubMed:9819355}. Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:9819355}; Multi-pass membrane protein {ECO:0000269|PubMed:9819355}. Note=Predominantly located in the endoplasmic reticulum and in the cis-Golgi.
Interaction partners:
- Gamma-secretase subunit pen-2
- Gamma-secretase subunit aph-1
- Nicastrin
- Protein lin-12
- cAMP-dependent protein kinase catalytic subunit
- Presenilin sel-12
- Presenilin hop-1
- Beta-catenin/armadillo-related protein 1
- Armadillo repeat-containing protein wrm-1
- Beta-catenin-like protein hmp-2
Sequence:
MDTLRSISSELVRSSQLRWTLFSVIANMSLTLSIWIGVYNMEVNSELSKTYFLDPSFEQTTGNLLLDGFINGVGTILVLGCVSFIMLAFVLFDFRRIVKAWLTLSCLLILFGVSAQTLHDMFSQVFDQDDNNQYYMTIVLIVVPTVVYGFGGIYAFFSNSSLILHQIFVVTNCSLISVFYLRVFPSKTTWFVLWIVLFWDLFAVLAPMGPLKKVQEKASDYSKCVLNLIMFSANEKRLTAGSNQEETNEGEESTIRRTVKQTIEYYTKREAQDDEFYQKIRQRRAAINPDSVPTEHSPLVEAEPSPIELKEKNSTEELSDDESDTSETSSGSSNLSSSDSSTTVSTSDISTAEECDQKEWDDLVSNSLPNNDKRPATAADALNDGEVLRLGFGDFVFYSLLIGQAAASGCPFAVISAALGILFGLVVTLTVFSTEESTTPALPLPVICGTFCYFSSMFFWEQLYG
Protein: Agouti-signaling protein (ASP) (Agouti coat color protein) (Agouti switch protein) (Q03288)
Organism: Mus musculus (Mouse)
Function: Involved in the regulation of melanogenesis. The binding of ASP to MC1R precludes alpha-MSH initiated signaling and thus blocks production of cAMP, leading to a down-regulation of eumelanogenesis (brown/black pigment) and thus increasing synthesis of pheomelanin (yellow/red pigment). Causes hair follicle melanocytes to synthesize phaeomelanin instead of black or brown pigment eumelanin and produces hairs with a subapical yellow band on an otherwise black or brown background when expressed during the mid-portion of hair growth.
Subcellular location: Secreted {ECO:0000269|PubMed:8449404}.
Interaction partners:
- Melanocyte-stimulating hormone receptor
- Attractin
- Pro-opiomelanocortin
- Melanocortin receptor 4
- 5,6-dihydroxyindole-2-carboxylic acid oxidase
- Tyrosinase
- Agouti-related protein
Sequence:
MDVTRLLLATLVGFLCFFTVHSHLALEETLGDDRSLRSNSSMNSLDFSSVSIVALNKKSKKISRKEAEKRKRSSKKKASMKKVARPPPPSPCVATRDSCKPPAPACCDPCASCQCRFFGSACTCRVLNPNC
Protein: Probable ATP-dependent RNA helicase DHX35 (EC 3.6.4.13) (DEAH box protein 35) (Q9H5Z1)
Organism: Homo sapiens (Human)
Function: May be involved in pre-mRNA splicing.
Interaction partners:
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor SYF2
- Splicing factor YJU2
- 116 kDa U5 small nuclear ribonucleoprotein component
- Pre-mRNA-processing factor 17
- Pleiotropic regulator 1
- E2F-associated phosphoprotein
- U5 small nuclear ribonucleoprotein TSSC4
- Pre-mRNA-splicing factor SLU7
- Cell division cycle 5-like protein
Sequence:
MAAPVGPVKFWRPGTEGPGVSISEERQSLAENSGTTVVYNPYAALSIEQQRQKLPVFKLRNHILYLIENYQTVVIVGETGCGKSTQIPQYLAEAGWTAEGRVVGVTQPRRVAAVTVAGRVAEERGAVLGHEVGYCIRFDDCTDQLATRIKFLTDGMLVREMMVDPLLTKYSVIMLDEAHERTLYTDIAIGLLKKIQKKRGDLRLIVASATLDADKFRDFFNQNETSDPARDTCVILTVEGRTFPVDIFYLQSPVPDYIKSTVETVVKIHQTEGDGDVLAFLTGQEEVETVVSMLIEQARALARTGMKRHLRVLPMYAGLPSFEQMKVFERVSRSVRKVIVATNVAETSITISGIVYVIDCGFVKLRAYNPRTAIECLVVVPVSQASANQRAGRGGRSRSGKCYRLYTEEAFDKLPQSTVPEMQRSNLAPVILQLKALGIDNVLRFHFMSPPPAQSMVQALELLYALGGLDKDCRLTEPLGMRIAEFPLNPMFAKMLLESGNFGCSQEILSIAAMMQIQNIFVVPPNQKSHAIRVHRKFAVEEGDHLTMLNIYEAFIKHNKDSKWCQEHFLNYKGLVRAATVREQLKKLLVKFQVPRKSSEGDPDLVLRCIVSGFFANAARFHSTGAYRTIRDDHELHIHPASVLYAEKPPRWVIYNEVIQTSKYYMRDVTAIESAWLLELAPHFYQQGTHLSLKAKRAKVQDP
Protein: Serine/threonine-protein phosphatase PP1-gamma catalytic subunit A (PP-1G-A) (xPP1-gamma1) (EC 3.1.3.16) (P36874)
Organism: Xenopus laevis (African clawed frog)
Function: Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis (By similarity). Promotes nuclear envelope reassembly by targeting nuclear membrane vesicles to chromatin at the end of mitosis. Acts by dephosphorylating membrane proteins such as lamin B receptor (lbr) to regulate the binding of membrane proteins to chromatin.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17448463}. Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cleavage furrow {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Nucleus speckle {ECO:0000250}. Midbody {ECO:0000250}. Mitochondrion {ECO:0000250}. Membrane {ECO:0000269|PubMed:17448463}.
Interaction partners:
Sequence:
MADVDKLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAEKKKPNASRPVTPPRGMITKQAKK
Protein: Ring finger protein 32 (G5E940)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLKNKGHSSKKDNLAVNAVALQDHILHDLQLRNLSVADHSKTQVQKKENKSLKRDTKAIIDTGLKKTTQCPKLEDSEKEYVLDPKPPPLTLAQKLGLIGPPPPPLSSDEWEKVKQRSLLQGDSVQPCPICKEEFELRPQVLLSCSHVFHKACLQAFEKFTNKKTCPLCRKNQYQTRVIHDGARLFRIKCVTRIQAYWRGCVVRKWYRNLRKTVPPTDAKLRKKFFEKKFTEISHRILCSYNTNIEELFAEIDQCLAINRSVLQQLEEKCGHEITEEEWEKIQVQNETSACFEDPCLGAHGSHFSLSNFLL
Protein: Bifunctional NADP phosphatase/NAD kinase [Includes: NAD kinase (EC 2.7.1.23) (ATP-dependent NAD kinase) (Poly(P)-dependent NAD kinase) (PPNK); NADP phosphatase (NADPase) (pNPPase) (EC 3.1.3.-)] (Q58327)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Involved in the regulation of the intracellular balance between NAD(H) and NADP(H), and is a key enzyme in the biosynthesis of NADP. Catalyzes the phosphorylation and dephosphorylation of NAD and NADP, respectively. Although it shows conflicting dual activities and is able to supply NADP, it seems that its physiological role is to prevent excess accumulation of NADP. Kinase can use ATP and other nucleoside triphosphates (UTP, TTP, CTP, GTP) as well as inorganic polyphosphate (poly(P)) as phosphoryl donors, however poly(P) is not considered to be the physiological phosphoryl donor. NAD is the preferred substrate for the kinase, but NADH can also be used as phosphoryl acceptor. Phosphatase can use NADP or NADPH as phosphoryl donor, but NADP is the preferred substrate. Phosphatase also has an activity toward the terminal phosphate group at C-2 of adenosine in 2'-AMP and toward the phosphate group at C-1 of fructose 1,6-bisphosphate, but not toward inositol 1-phosphate.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00361}.
Interaction partners:
- NH
- Nicotinamide-nucleotide adenylyltransferase
- Uncharacterized protein MJ0636
Sequence:
MVIMEGFKIAMKVIDEIDKKIKPLIGWEKADEVVKIGADGTPTKRIDVIAENMAINILEKFSGGILISEEIGLKVVGDELEYIFILDPIDGTYNALKSIPIYSTSIAVAKIKGEDKKLIRENINNIDWIKSFIANKYTINDLYVGIVKNLATGDLYYAIKGEGSFLEKDGEKIKIETKNIKDLKEASVGLFVYGLSNDLLEFLKERKVRRVRLFGSMALEMCYVVSGALDAYINVNENSRLCDIAGAYVICREGNAIVTNKNGKPLNMKLHLMERTSLIVSNKYLHKKLIALFGNRWIIKPVKFGIVVREDKEEAINLAIEICKYLKDKNIPFCVEDFLRERVGGDKFDISAISHIIAIGGDGTILRASRLVNGETIPIIAVNMGKVGFLAEFCKDEVFEIIDKVIYGEYEIEKRSKLSCKIIKDNRVIKTPSALNEMVVITKNPAKILEFDVYVNDTLVENVRADGIIVSTPTGSTAYSLSAGGPIVEPNVDCFIISPICPFKLSSRPLVISASNRIKLKLKLEKPALLVIDGSVEYEINKDDELIFEKSDSYAYFVKGQSFYNKLSRCLGIK