wanglab/gogpt-training-data huggingface dataset:
Protein: Exosome complex component RRP45 (Autoantigen PM/Scl 1) (Exosome component 9) (P75 polymyositis-scleroderma overlap syndrome-associated autoantigen) (Polymyositis/scleroderma autoantigen 1) (Polymyositis/scleroderma autoantigen 75 kDa) (PM/Scl-75) (Q06265)
Organism: Homo sapiens (Human)
Function: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC9 binds to ARE-containing RNAs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11782436}. Nucleus {ECO:0000269|PubMed:24105744}. Nucleus, nucleolus {ECO:0000269|PubMed:24105744}. Nucleus, nucleoplasm {ECO:0000269|PubMed:24105744}. Note=Colocalizes with SETX in nuclear foci upon induction of transcription-related DNA damage at the S phase (PubMed:24105744). {ECO:0000269|PubMed:24105744}.; SUBCELLULAR LOCATION: [Isoform 1]: Nucleus, nucleolus.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus, nucleolus.; SUBCELLULAR LOCATION: [Isoform 3]: Nucleus. Note=Excluded from the nucleolus.
Interaction partners:
- Exosome complex component RRP4
- Exosome complex component RRP40
- Nuclear nucleic acid-binding protein C1D
- Exosome complex component CSL4
- Exosome complex component 10
- Exosome complex exonuclease RRP44
- Exosome complex component RRP46
- Exosome complex component MTR3
- Exosome RNA helicase MTR4
- Exosome complex component RRP43
Sequence:
MKETPLSNCERRFLLRAIEEKKRLDGRQTYDYRNIRISFGTDYGCCIVELGKTRVLGQVSCELVSPKLNRATEGILFFNLELSQMAAPAFEPGRQSDLLVKLNRLMERCLRNSKCIDTESLCVVAGEKVWQIRVDLHLLNHDGNIIDAASIAAIVALCHFRRPDVSVQGDEVTLYTPEERDPVPLSIHHMPICVSFAFFQQGTYLLVDPNEREERVMDGLLVIAMNKHREICTIQSSGGIMLLKDQVLRCSKIAGVKVAEITELILKALENDQKVRKEGGKFGFAESIANQRITAFKMEKAPIDTSDVEEKAEEIIAEAEPPSEVVSTPVLWTPGTAQIGEGVENSWGDLEDSEKEDDEGGGDQAIILDGIKMDTGVEVSDIGSQDAPIILSDSEEEEMIILEPDKNPKKIRTQTTSAKQEKAPSKKPVKRRKKKRAAN
Protein: FAST kinase domains 3 (D6RHY4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MALITLRKNLYRLSDFQMHRALAALKNKPLNHVHKVVKERLCPWLCSRQPEPFGVKFHHAHCKKFHSKNGNDLHPLGGPVFSQVSDCDRLEQNVKNEESQMFYRRLSNLTSSEEVLSFISTMETLPDTMAAGALQRICEVEKKDGDQGLPKEILENSIFQALCFQFEKEPSQLSNTSLVTALQALILLHVDPQSSLLLNLVAECQNRLRKGGMEVRNLCILGESLITLHSSGCVTLELIINQLQ
Protein: Dynein light chain roadblock-type 1 (Bithoraxoid-like protein) (BLP) (Dynein light chain 2A, cytoplasmic) (Dynein-associated protein Km23) (Roadblock domain-containing protein 1) (Q9NP97)
Organism: Homo sapiens (Human)
Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305|PubMed:36071160}.
Interaction partners:
- Cytoplasmic dynein 1 intermediate chain 2
- Cytoplasmic dynein 1 heavy chain 1
- Dynein light chain 1, cytoplasmic
- Cytoplasmic dynein 2 intermediate chain 1
- Cytoplasmic dynein 2 intermediate chain 2
- Cytoplasmic dynein 1 light intermediate chain 2
- Cytoplasmic dynein 2 light intermediate chain 1
- Cytoplasmic dynein 1 intermediate chain 1
- Dynein light chain Tctex-type 1
- Cytoplasmic dynein 1 light intermediate chain 1
Sequence:
MAEVEETLKRLQSQKGVQGIIVVNTEGIPIKSTMDNPTTTQYASLMHSFILKARSTVRDIDPQNDLTFLRIRSKKNEIMVAPDKDYFLIVIQNPTE
Protein: P2Y purinoceptor 1 (P2Y1) (ATP receptor) (Purinergic receptor) (P49651)
Organism: Rattus norvegicus (Rat)
Function: Receptor for extracellular adenine nucleotides such as ADP. In platelets, binding to ADP leads to mobilization of intracellular calcium ions via activation of phospholipase C, a change in platelet shape, and ultimately platelet aggregation (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:7779087}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P47900}.
Interaction partners:
- Guanine nucleotide-binding protein G
- RRP15-like protein
- Ribosome biogenesis protein BOP1
- Probable ATP-dependent RNA helicase DDX27
- Ribosome production factor 1
- Pescadillo homolog
- CCAAT/enhancer-binding protein zeta
- Probable ATP-dependent RNA helicase DDX56
- Ribosome production factor 2 homolog
- RNA binding motif protein 28
Sequence:
MTEVPWSAVPNGTDAAFLAGLGSLWGNSTIASTAAVSSSFRCALIKTGFQFYYLPAVYILVFIIGFLGNSVAIWMFVFHMKPWSGISVYMFNLALADFLYVLTLPALIFYYFNKTDWIFGDVMCKLQRFIFHVNLYGSILFLTCISAHRYSGVVYPLKSLGRLKKKNAIYVSVLVWLIVVVAISPILFYSGTGIRKNKTVTCYDSTSDEYLRSYFIYSMCTTVAMFCIPLVLILGCYGLIVRALIYKDLDNSPLRRKSIYLVIIVLTVFAVSYIPFHVMKTMNLRARLDFQTPEMCDFNDRVYATYQVTRGLASLNSCVDPILYFLAGDTFRRRLSRATRKASRRSEANLQSKSEEMTLNILSEFKQNGDTSL
Protein: T-complex protein 1 subunit epsilon (CCT-epsilon) (Q6NVI6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Tcp1 protein.
- Chaperonin-containing TCP1, subunit 6A
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit gamma.
- Chaperonin-containing TCP1, subunit 2
- Chaperonin-containing TCP1, subunit 2
- Protein FAM161A
- Bardet-Biedl syndrome 10.
Sequence:
MSALGTLAFDEYGRPFIIIKDQDKKSRLTGLEALKSHILAAKAVANTLRTSLGPNGLDKMMVDKDGEVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEQAEQLLDRGIHPIRIADGYDQAAKIAIEQLDKIGDSFPVDPNNTESLVQTAMTTLGSKVINRCHRQMAEIAVNAILTVADMERKDVDFELIKVEGKVGGKLEDTQLIKGVIVDKEFSHPQMPKVLKDTKIAILTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKDKFQEMIRQVKENGANLAICQWGFDDEANHLLLQNELPAIRWVGGPEIELIAIATGGRIVPRFCELTPEKLGTAGLVKEICFGTTKDRMLVIEECKNSRAVTIFIRGGNKMIIEEAKRALHDALCVIRNLVRDNRIVYGGGASEIACALAVNEAADKCPSLEQYAMRAFADALEVIPMALAENSGLNPIQTMTEVRARQVKENNSALGIDCLHLSTNDMKQQHVIETLIGKKQQISLATQVVKMILKIDDIRGPGEPED
Protein: SD16903p (Q8MRW8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKGFNDFKRIAVVCIPSEDELKRRIAEKEEKGNAFTVKESTINNLRANFTLPSLEFGWFDDINYTELTGDEAKSEVKKYNEKGKKAIDAERSRDKRSRGSRDNYRRDDRNRNRYNDDRRRDYGGQRHESRWSDSRRGGGGGGYSSNSGGGGSRGYDNRRNYNSGSGGQQNWVQNSRRSGYDDRGYGGGGSGSRGYDNRNRGYAGGSGGGGGGGGGGGGGGGQQNWMQNNRRSGYDDRGYGSSRDYRDRDRGNDRSRMGSNDRNRGSSQSSYRSGGGTHQQRDFRPGHRDTKEDSRGGYERSAGQSLPKYGNNTAVGGGYDQYKQQGGAPGGGKASLSGKWSTYSQHHQQQQAPQHQQTGIWQTQQQSQQYQQPQQAAAGQQQYWAYNQMQTGYGNQQAWQSADPQQQQQWMSWWQQQQQGSGGAAAGNASGGSGVNVGGGAGNNDGGAANHYWSQYSYSTQSNAGADKK
Protein: V-set and immunoglobulin domain-containing protein 4 (Protein Z39Ig) (Q9Y279)
Organism: Homo sapiens (Human)
Function: Phagocytic receptor, strong negative regulator of T-cell proliferation and IL2 production. Potent inhibitor of the alternative complement pathway convertases.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Complement C3
- Complement C1q subcomponent subunit A
- Complement C1q subcomponent subunit B
- Membrane-spanning 4-domains subfamily A member 4A
- Complement C1q subcomponent subunit C
- Scavenger receptor cysteine-rich type 1 protein M130
- Macrophage colony-stimulating factor 1 receptor
- Folate receptor beta
- C3a anaphylatoxin chemotactic receptor
- Transmembrane domain-containing protein TMIGD3
Sequence:
MGILLGLLLLGHLTVDTYGRPILEVPESVTGPWKGDVNLPCTYDPLQGYTQVLVKWLVQRGSDPVTIFLRDSSGDHIQQAKYQGRLHVSHKVPGDVSLQLSTLEMDDRSHYTCEVTWQTPDGNQVVRDKITELRVQKLSVSKPTVTTGSGYGFTVPQGMRISLQCQARGSPPISYIWYKQQTNNQEPIKVATLSTLLFKPAVIADSGSYFCTAKGQVGSEQHSDIVKFVVKDSSKLLKTKTEAPTTMTYPLKATSTVKQSWDWTTDMDGYLGETSAGPGKSLPVFAIILIISLCCMVVFTMAYIMLCRKTSQQEHVYEAARAHAREANDSGETMRVAIFASGCSSDEPTSQNLGNNYSDEPCIGQEYQIIAQINGNYARLLDTVPLDYEFLATEGKSVC
Protein: Plasma membrane proteolipid 3 (Q9C1W4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Plays a role in the regulation of membrane potential. Could mediate a proton leak. Regulated by the spc1-atf1 pathway and so expression is stress-induced.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MALTGSDIFKVIFAIILPPLGVFLERGCGADVIINILLCCLGYVPGIIHALYIILKY
Protein: Inner membrane protein YphA (P0AD47)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Disulfide-bond oxidoreductase YfcG
- Uncharacterized protein YbdD
Sequence:
MNTLRYFDFGAARPVLLLIARIAVVLIFIIFGFPKMMGFDGTVQYMASLGAPMPMLAAIIAVVMEVPAAILIVLGFFTRPLAVLFIFYTLGTAVIGHHYWDMTGDAVGPNMINFWKNVSIAGAFLLLAITGPGAISLDRR
Protein: Avirulence protein (Q52432)
Organism: Pseudomonas syringae
Interaction partners:
Sequence:
MTRISTSSVNSSFSYSAPAEEAQNRVSSAPTNSSPPGTTTAVAQASEGQKKPGAVLSMHAQRLRQLCESSSHQYRQNALLAKSFDAQRLDINTQAGPSNSPHLNALNKLQQRDFKPAAGGLEIPFTPKSLLGGGKRVYQIGSSSRDVQVCPRGAGAALRQEIEDKQLMVNNLTDELQDAIDEANPAEIANTSQQLRHARADLADLQRRFAVLRNEDRRIN
Protein: Rasputin (Q9NH72)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, Stress granule {ECO:0000256|ARBA:ARBA00004210}.
Interaction partners:
Sequence:
MVMDATQSQQPSPQSVGREFVRQYYTLLNKAPNHLHRFYNHNSSYIHGESKLVVGQREIHNRIQQLNFNDCHAKISQVDAQATLGNGVVVQVTGELSNDGQPMRRFTQTFVLAAQSPKKYYVHNDIFRYQDLYIEDEQDGESRSENDEEHDVQVVGGTVDQAVQVAGDVVAQQPQQQQAPPQPQAQVVVPQQVAPVAAGGAAPQQIFYPLPAGAAAGRPVAVLPPAPQAAAVPLPAQFTVPPPQPIQNGVVSHEELQQQQVLVPPSVSPLVQQQQPTGTPVLPIVPVPSAGFQQSPLVAPQLIQQQQQQQPAQLPPQQQQQQQPIQQQQPLQQQQQPLAEPEEVEVAPRQQKPPTPVEDFKTIHEQQQQEKYEAAKQQQNEPKTYANLFKSTSSSPSGFVNAALQQQQQLQQQQQQQQSISSNTYNSSSATSGGGNGSQVSYSTTASSYNNSNGNSRLDNGGPLPQRNNSIRNNKGDFEQRRSSNTQQFGDNQQLFLGNIPHHASEDDLREIFSRFGNVLELRILSKAGNKVPPGMRSPLNYGFITYDDPEAVQKCLANCPLYFPENSPDGQKLNVEEKKPRVRNDMVPRQQIGGNNLNNNMGRLGGNNGPQSRPMGNNNGSGGGMMRNNAVGNNLRQGGGGGNGAPRLGGGGGFGQRQDNRTGGGNNQSNGPLRGAGNGQSGGGNYGRR
Protein: Sno oncogene, isoform B (Sno oncogene, isoform C) (Sno oncogene, isoform D) (Sno oncogene, isoform G) (SnoN) (Q00G30)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Mothers against decapentaplegic homolog
- Mothers against decapentaplegic homolog
- Protein mothers against dpp
- Smrter, isoform G
- Integrator complex subunit 8
- receptor protein serine/threonine kinase
- E3 ubiquitin-protein ligase Smurf1
- Fizzy-related protein homolog
Sequence:
MTEYVTPMISTVLKKYQTSATKSLQGPGHALTTAGVLDIVTNGRSESPGLNGKCQASPPVVALIKKEILSSPEPQDLHHHECSTRGTPPQIYSPATPPRELSQPILSVADAGCGELYETKLEGKTIGCFSVGGEMRLCLPQFLNNVLNDFSLEQINRIFDELGIYCSQCTHDQLVEFKAAKILPSDVKASGLITRTDAERLCAALLHRSDRNSYVPIESLAKGALSFHVYHKCFGKCEGICTPDMYSYQKPTCIKCLECDGWFSPQKFVGHVHRKFENHTCHWGFDSRNWHDYLHVALDVENREKYQIILDQLKEVELKEMHKAQRELEHKKRKAEMLMDDGMLGSGPVLGLAGHPHGLVGALAPPPPPPMKQPQMDIPSGKKQLQQLKGATVAASALEYQYQVMYAHCVQKEREREREHLPHSHPLPRQHRAVLVATTPYPHLPQYPTPPTLNSSSAFRPWGPDTTKAFLHAYGATLSSLPYACQEPPELQNPERVVRSTDKRYAERTYQPNVALAPRKSILSKERDKDRERMEREVMERQRLREKETDHQVVHIKQERSQTPTPPTASPPDGVVLPLDVVEPPHPSSSGSNSPLPAHLPAAPATAPPNAGGAPPTPTNLRNMRSPEEFSAGGSNEITSSTSPHHQQSSHHQVVQPTAGAPPPSQHIIATVNQHAKLLPSSSSLPNGNGSSSLAATNNEPSRIRINKNLMSQQPVVAVSGMTPHHHQHHPTHMHHFSHGYYKSQASSPTQSSSAGLNLSTHSSNVVSSPHHATQPKTHHSSVGSGNHGLQNGKPHLGSEFELSTDTDDTDSLNGEPDSSAMLPPWEQAVESLRETRPKDRERVLLILQRLLQENDQYRYNNIQLSELLHKQDAHIADLTEQLQRYRRQFEEQVCKVDLRKMPFKHQTRLENVVEAGRGEAEEDEELEEDEMEDRANNNNQQELSPLIKAPANGLRRSVTPPNCCASEGGDCEKPDEPESKRIKLQVGEKAEDKQVENEESPSNGTESHDLEKLEKNDDKTDPTNNPKSPQPSQISSDDEMEEDDEDEDEEDEDEEVQVEAPHSSALATPPTATTPLSPDSAATAGQLFDSSNSSDESSMKKAQMSACHALEKMSSNVGSDENNQRLAEESQEDEAEEDPEEEDSDDDEMPLQQRQQQQRQRVAPQNVLSGPSVAGHHPAPAHPPMATKASKKQTPPAPPTAAATTTASATTNCELQIKKEIA
Protein: MIOREX complex component 10 (Mitochondrial organization of gene expression protein 10) (Q05648)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of MIOREX complexes, large expressome-like assemblies of ribosomes with factors involved in all the steps of post-transcriptional gene expression.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:23022099}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MLSFRSLTSTFGFVSRFQIRRLGTSLSIQNLEVQDGRWKGKLATEKKTNREHKSVDTNIKTMKMLKNPKNSTRYLRRSFVPNHRKQENGRDILEDSLSKDHLKVKSCITITTGEGYDLKRCMKLLTMQGLQPTNLIPDEIVSFSYQDNGNKGDVMILGQNGSIVSWGFSESSVRNCIVPIVKAASLNPLNGEDFETEDMDYVEIEGEQDFDKLSSLDNKVTPRIACESFLSGDLIIINSLDSDQGMLDKAAFSSGLSRSTNLAVLEEAMEKHISKTRTITENISKGTKLNLRSSDALKSIGRLFLIRGKLNLYSELIETPDLYWSEPQLEEIFKNVSRYLDIGPRINILNSKLDYSTDECRALISLLNERNSTFLEWIIIYLIAFELCFEIYHFYQKYSSYCSEPTNDDLDATK
Protein: Protein cordon-bleu (E7F568)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays an important role in the reorganization of the actin cytoskeleton. Binds to and sequesters actin monomers (G actin). Nucleates actin polymerization by assembling three actin monomers in cross-filament orientation and thereby promotes growth of actin filaments at the barbed end. Can also mediate actin depolymerization at barbed ends and severing of actin filaments. Promotes formation of cell ruffles. Regulates neuron morphogenesis and increases branching of axons and dendrites (By similarity). Required for normal embryonic development, including normal development of laterality, normal body size and shape, as well as normal brain, heart and kidney development. Required for normal development of stereocilia and kinocilia in sensory hair cells of neuromasts in the posterior lateral line organ, and thus also for balance keeping and normal swimming behavior.
Subcellular location: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cell projection, ruffle {ECO:0000250}. Cytoplasm. Cytoplasm, cytosol. Note=Detected throughout the neuron cell body, as well as in axons and dendrites (By similarity). Colocalizes with the actin cytoskeleton. Recruited to the cell membrane via interaction with pacsin1. Detected at the apical surface of cells at the basis of forming cilia, but not in the cilia themselves. {ECO:0000250}.
Interaction partners:
- Junction mediating and regulatory protein, p53 cofactor.
- Amine oxidase
- Leiomodin 2
Sequence:
MNLGDATTRPPVGRRMKAQAPPPPRPPQPAPRRIFRNAVPDGGGSSGGDCKENMLRSYVDLHISLPTGYQTTINVDGRKALMDLLVDLCSQYHLNPAYHTLELLSPDAQPVSFKPNALLGALDVSCALIKERVLEDRVIRKPPPKVPEKTVRLVVNYHRSQKAVVRVNPLAPLQTLVPVICQKCEFDPAHVLLFKDNINHQQLDLDKSLSDLGIRELYVLDQTLVLQPKMASTPALNYSAESLRSNSLSGSEKKGLLGFLKFNRRKSKGMSVVASGPCVEARPSTLGQSQSVMNISKMSPKVELKKRRAPAPPPAPTQTLPPTSQISLGSPSSHNLLKKRKAPAPPPTPPPSTPEPDISTYVPTATVQEHYIPASVERTPRASTPADDSDLSHSIEDSEPARSICSSSSGDDAAAVGSSSSSLAEEPVTHRADVIAPFTTSTPEPEPKPEYEPELKKEASPRSTPELEPGPRPEVPAAEDLEVEMELKMEETENNRHSGIAWLHSAHESVLERRVQQEVETVSVASSESFADHGYAASEDMAEESGPVSPSERMQSVSPMDIMSLNSDSTLPVKQSKESSSDSDEGCATWGSRQSSGHIQDGQKSIKRQNGYEEDPEITAQIHLTLADLDANLADLNHSDGASVFVDDEIPVSIVDMDIPVTAIDEVLDDDQCSASECESVLLRSTQSISSKPCTPCGVIQNKNNNACLTEEKHRSPFPDIEKQLQTATLTVIDKPTIQSPTSKKPSQDAKITDNMEQKTTFNSEAKSKSETVELTSQKDTVLQKSQSFVRPDVQSVQKERTSSTRVLPTQGKITLSSFSRFGMKTFTVIPPKPAVSQTKPAGSLVTGAIKIDEQGNMVTQRQISSGPEKNNTPSVDTTRADKTPLVKAKAFWSTTEKQEKLTTAKTEPIVNNGDTDVFKASAVTGSFKLSPPEETHKEVIIVERKPISGVASKPSFSENHAEKRDLSFLIPSRRTSSQYVASVIAKNNKNSSIPKTKIDTTPAPLSISGVQNPVNQLLNNEVKPTSIHKPAVTVKPTENPVPSFRPKCLQSYVAEKPTSSERISTLHGGDKTKSLDSQPLSIKIQPFPHVSAHIKSFSEEATSINNFPDTSSARQTPTDTTHPPLAKKPELHKSEIPSEPNQGNVFGPVKKFKPVIFKPVQQETSIHSSLMEAIQSGEGIERLRKVSDLPTSCTVKKPSYNDPENERSALLSAIRASSTSAKLKKTKSVASKELEQLRKVEEDRNVHTEVISPRPTSPDFVPPLPPSFSPPPPPPPPLAPAKPPVVLPPGGNPEAAREALLEAIRSGSGAQQLRKVPVTQTRRQVNGRLGTIQATSPLSYGH
Protein: Galactocerebrosidase (GALCERase) (EC 3.2.1.46) (Galactocerebroside beta-galactosidase) (Galactosylceramidase) (Galactosylceramide beta-galactosidase) (P54803)
Organism: Homo sapiens (Human)
Function: Hydrolyzes the galactose ester bonds of glycolipids such as galactosylceramide and galactosylsphingosine. Enzyme with very low activity responsible for the lysosomal catabolism of galactosylceramide, a major lipid in myelin, kidney and epithelial cells of small intestine and colon.
Subcellular location: Lysosome.
Interaction partners:
- Arylsulfatase A
- Acid ceramidase
- Lysosomal acid glucosylceramidase
- Alpha-galactosidase A
- Sphingomyelin phosphodiesterase
- 2-hydroxyacylsphingosine 1-beta-galactosyltransferase
- Non-lysosomal glucosylceramidase
- Ceramide glucosyltransferase
- Ceramide kinase
- Prosaposin
Sequence:
MAEWLLSASWQRRAKAMTAAAGSAGRAAVPLLLCALLAPGGAYVLDDSDGLGREFDGIGAVSGGGATSRLLVNYPEPYRSQILDYLFKPNFGASLHILKVEIGGDGQTTDGTEPSHMHYALDENYFRGYEWWLMKEAKKRNPNITLIGLPWSFPGWLGKGFDWPYVNLQLTAYYVVTWIVGAKRYHDLDIDYIGIWNERSYNANYIKILRKMLNYQGLQRVKIIASDNLWESISASMLLDAELFKVVDVIGAHYPGTHSAKDAKLTGKKLWSSEDFSTLNSDMGAGCWGRILNQNYINGYMTSTIAWNLVASYYEQLPYGRCGLMTAQEPWSGHYVVESPVWVSAHTTQFTQPGWYYLKTVGHLEKGGSYVALTDGLGNLTIIIETMSHKHSKCIRPFLPYFNVSQQFATFVLKGSFSEIPELQVWYTKLGKTSERFLFKQLDSLWLLDSDGSFTLSLHEDELFTLTTLTTGRKGSYPLPPKSQPFPSTYKDDFNVDYPFFSEAPNFADQTGVFEYFTNIEDPGEHHFTLRQVLNQRPITWAADASNTISIIGDYNWTNLTIKCDVYIETPDTGGVFIAGRVNKGGILIRSARGIFFWIFANGSYRVTGDLAGWIIYALGRVEVTAKKWYTLTLTIKGHFTSGMLNDKSLWTDIPVNFPKNGWAAIGTHSFEFAQFDNFLVEATR
Protein: Probable sarcosine oxidase (EC 1.5.3.1) (Q9SJA7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Probable low-specificity L-threonine aldolase 2
- Low-specificity L-threonine aldolase 1
- Glycine dehydrogenase
- Glycine dehydrogenase
- Serine--glyoxylate aminotransferase
- Serine hydroxymethyltransferase 1, mitochondrial
- Serine hydroxymethyltransferase 6
- Serine hydroxymethyltransferase 3, chloroplastic
- Serine hydroxymethyltransferase 7
- Serine hydroxymethyltransferase 2, mitochondrial
Sequence:
MEYSDDGRFDVIVVGAGVMGSSAAYQLAKRGQKTLLLEQFDFLHHRGSSHGESRTIRATYPEDYYYSMVSESTRLWAAAQSEIGYKVHFPTQQFDMGPADQQSLLSVVATCQKHGLAHRVMDSHAVSEHFSGRISIPENWIGVSTELGGIIKPTKAVSMFQTLAIGHGAILRDNTKVANIKRDGESGEGVIVCTVKGDKFYGKKCIVTAGAWISKLVKTVAGIDFPVEPLETTVCYWRIKEGHEEKFTIDGEFPTFASYGAPYVYGTPSLEYPGLIKVAVHGGYWCDPDKRPWGPGVKLEELKEWIKERFGGMVDSEGPVATQLCMYSMTPDEDFVIDFLGGEFGRDVVVGGGFSGHGFKMAPAVGRILADMAMEVEAGGGGVEMKQFSLRRFEDNPKGNAKEYPDQVILDVPLKH
Protein: Calvin cycle protein CP12, chloroplastic (CP12 domain-containing protein) (Chloroplast protein 12) (A6Q0K5)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Acts as a linker essential in the assembly of a core complex of PRK/GAPDH. Coordinates the reversible inactivation of chloroplast enzymes GAPDH and PRK during darkness in photosynthetic tissues.
Subcellular location: Plastid, chloroplast {ECO:0000250}.
Interaction partners:
Sequence:
MMLTKSVVISRPAVRPVSTRRAVVVRASGQPAVDLNKKVQDAVKEAEDACAKGTSADCAVAWDTVEELSAAVSHKKDAVKADVTLTDPLEAFCKDAPDADECRVYED
Protein: Uncharacterized protein YhiJ (P37627)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Acetyl-CoA:oxalate CoA-transferase
- Uncharacterized symporter YidK
Sequence:
MKIGTVAGTNDSTTTIATNDMVQEHVTNFTKELFGYIANGIGDDISSIARTMLGEVVEKIDDWQIERFQQSIQDDKISFTIQTDHSEKYSMLSGMRAHILRRNNNYQFIVTINSKNYGCSLDNTDINWCSIVYLLNNMTVNDNANDVAVTESYKPIWNWKISQYNVSDIKFETMIKPQFADRIYFSNCLPVDPTSTRPTYFGDTDGSVGAVLFALFATGHLGIMAEGENFLSQLLNIEDEVLNVLLRENFNEQLNTNVNTIISILNRRDIILESLQPYLVINKDAVTPCTFLGDQTGDRFSNICGDQFIIDLLKRIMSINENVHVLAGNHETNCNGNYMQNFTRMKPLDEDTYSGIKDYPVCFYDPKYKIMANHHGITFDDQRKRYIIGPITVSIDEMTNALDPVELAAIINKKHHAIINGKKFKTSRAISCRSFNRYFSVSTDYRPKLEALLACSQMLGINQVVAHNGNGGRERIGETGTVLGLNARDSKHAGRMFSMHNCQINPGAGPEITTPWKSYQHEKNRNGLMPLIRRRTMLQL
Protein: Serpin I2 (Myoepithelium-derived serine protease inhibitor) (Pancpin) (Pancreas-specific protein TSA2004) (Peptidase inhibitor 14) (PI-14) (O75830)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Cilia- and flagella-associated protein 337
- Carboxypeptidase B
Sequence:
MDTIFLWSLLLLFFGSQASRCSAQKNTEFAVDLYQEVSLSHKDNIIFSPLGITLVLEMVQLGAKGKAQQQIRQTLKQQETSAGEEFFVLKSFFSAISEKKQEFTFNLANALYLQEGFTVKEQYLHGNKEFFQSAIKLVDFQDAKACAEMISTWVERKTDGKIKDMFSGEEFGPLTRLVLVNAIYFKGDWKQKFRKEDTQLINFTKKNGSTVKIPMMKALLRTKYGYFSESSLNYQVLELSYKGDEFSLIIILPAEGMDIEEVEKLITAQQILKWLSEMQEEEVEISLPRFKVEQKVDFKDVLYSLNITEIFSGGCDLSGITDSSEVYVSQVTQKVFFEINEDGSEAATSTGIHIPVIMSLAQSQFIANHPFLFIMKHNPTESILFMGRVTNPDTQEIKGRDLDSL
Protein: P-element somatic inhibitor, isoform C (A1ZAK8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- 14-3-3 protein zeta
- Poly
- RAC serine/threonine-protein kinase
Sequence:
MSDFQQQGINQSQALAQAIQRAKQIAAKIQPSQQGGGTAGPSPPSSGGGPGFKRINDDGDSGPESKRSLGSPEYANNSSNMSSGSGGGGGGGGGPGGASITQAIAQAAAVAARLAASAGTSCEEQIRLPESVAGAFMGRSSNDTITHIQAESGVKVQVMQDQDRVIMLRGQRDTVTKGREMIQNMANRAGGGQVEVLLTINMPPPGPSGYPPYQEIMIPGAKVGLVIGKGGDTIKQLQEKTGAKMIIIQDGPNQELIKPLRISGEAQKIEHAKQMVLDLIAQKDAQGQQQGGRGGGGGGGGPGMGFNNFNNGNGGESTEVFVPKIAVGVVIGKGGDMIRKIQTECGCKLQFIQGKNDEMGDRRCVIQGTRQQVDDAKRTIDGLIENVMQRNGMNRNGNGGGGGPGGDSGNSNYGYGYGVNHAQGGREEITFLVPASKCGIVIGRGGETIKLINQQSGAHTEMDRNASNPPNEKLFKSKGTTDQVEAARQMISEKINMELNVISRKPIGGGPGGGGGNSGGGQNNSHHNQQQGGYGGQNQMQGGDPNSGAGYQQQPWGGPYGQQGWDPSGQQQQMAMANQGGSAAGGASGGQDYSAQWIEYYKQMGCHREAEMIEQQMKAKQAGGSSGPVQQQQPQQQQQSQQQTGGAGAGGADYSAQWAEYYRSVGKIEEAEAIEKTLKNKQQNGSGGQSSTPNPSQGGSGQQQPNPAAAAAAAAAAAAAAGGYGQSMTPTQYAQYSQYYAAAAAAGGQPQGAPQPGGGQSGGPPGNYPGNYPGAGYGGYPGAPGQQQQKSHKNDNH
Protein: Ferredoxin (P83524)
Organism: Alkekengi officinarum var. franchetii (Japanese lantern) (Physalis franchetii)
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:9862138}.
Interaction partners:
Sequence:
ATYKVKLITPDGPVVFDCPDNEYILDAAEEQGHDLPYSCRAGSCSSCAGKVTAGTVDQSDGNFLDDDQVADGFVLTCVAYPQSDVTIETHKEEELTA
Protein: Cyclic nucleotide gated channel beta 1 (A0A1D5RLZ4)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MLGWVQRVLPQPPGTPQKTVETAGPQPETESKPEANPQPEPEPQQEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPVPEEAPPEVQALPPEEPMEGEGEAEAGPSLQETQVADPAQPTSQAQVAVAKVNRPSSWMLSWFWRGMQKVVPQPVCSNGGQNLAAGERDPDQGGAQIPEPCGTGDPGSAEASGTQDTE
Protein: MD-2-related lipid recognition domain-containing protein / ML domain-containing protein (F4J7G5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Nuclear pore complex protein NUP93A
- Patellin-2
- Mitochondrial phosphate carrier protein 3, mitochondrial
- Mitochondrial dicarboxylate/tricarboxylate transporter DTC
- Patellin-3
Sequence:
MSKFTGFSSLAISYFLLVSTIVAATDVHYCDNNEEYEVKVQGVDITPYPIARGEPATFRISANTDTEISSGKLVIEVSYFGWHIHSETHDLCDETSCPVAIGDFLVAHSQVLPGYTPPTEKRFNLVSIAYYEFHVEGSYSLKMKMLDGRKKELTCIKFSFDIGFGSSVADM
Protein: Transcriptional activator hap5 (P79007)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the CCAAT-bound heteromer, php5 is essential for DNA-binding activity. It is essential for transcription activation of cyc1. It is the linchpin that binds to the subunit association domains (SAD) of php2 and php3 to bring these proteins together.
Subcellular location: Nucleus.
Interaction partners:
- Transcriptional activator hap3
- Transcriptional activator hap2
- CCAAT-binding factor complex subunit php4
- DNA polymerase epsilon subunit D
- Iron-sensing transcriptional repressor
- Zinc finger protein rst2
- Monothiol glutaredoxin-4
- Transcriptional repressor tup11
Sequence:
MNSIPDSYSLKQGFPEGLGEYVDPSGNPNSQVRIGYGQDSVSRFQQPVPDVDPTAVNHYNASAPIEVASPFDNVTQGLVGSDAQALAEYWQKTIDTLEHDDQAVKTLHLPLARIKKVMKTDDDVKNKMISAEAPFLFAKGSEIFIAELTMRAWLHAKKNQRRTLQRSDIANAVSKSEMYDFLIDIISKDNNNSRASSSQAHMSATQVAAMGGMNGLQPFPTQAGLPNQGFPMPTGSQLPFSNQQSSQPSMQYSSHPSRMQQMQDIDQSMYKQQRLGSEYPQLQMSDNSGNVNQMNMQRPVMVAPYMAEHLYRYPPTHLESGSSAFRLQSSPMGYQMPQFQGNMRPNMQQSQMFDPSAYGMSRRPGSPRQFDQQQRLYSQPNAMMYQTQQGRQGNPMHQQFSQQQNPLSRYSQQPQ