wanglab/gogpt-training-data huggingface dataset:
Protein: F-box/WD repeat-containing protein 8 (F-box and WD-40 domain-containing protein 8) (Q8BIA4)
Organism: Mus musculus (Mouse)
Function: Substrate-recognition component of a Cul7-RING ubiquitin-protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The Cul7-RING(FBXW8) complex mediates ubiquitination and consequent degradation of GORASP1, acting as a component of the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain. The Cul7-RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading to its degradation, thereby affecting cell proliferation and differentiation. Associated component of the 3M complex, suggesting that it mediates some of 3M complex functions (By similarity).
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P0DL28}. Golgi apparatus {ECO:0000250|UniProtKB:P0DL28}. Cytoplasm, cytosol {ECO:0000269|PubMed:23142081}. Note=Localizes to the cytosol when phosphorylated at Ser-86, promoting IRS1 ubiquitination. {ECO:0000269|PubMed:23142081}.
Interaction partners:
- S-phase kinase-associated protein 1
- Cullin-7
- E3 ubiquitin-protein ligase RBX1
- Cullin-1
- Obscurin-like protein 1
- Coiled-coil domain-containing protein 8 homolog
- Glomulin
- F-box only protein 4
- S-phase kinase-associated protein 2
- F-box/WD repeat-containing protein 1A
Sequence:
MDDHNLEEFRRHWQEELAQSQALRRRRRLEAGERRSPRRPEAGARGEPASGYLGLAQGLLEGAGRPPAPRPGRGGDRKDTSSRSRSPPDRDATEPEPLVDQLIRDLNELDDVPFFDVRLPYELAINIFQYLNRRELGLCAQVSKTWKVIAEDEVLWYRLCRQEGHLPHSRFSDYTCWKLILQECLAKEHTLRANWKNRKGAVSELEHVPDAVLCDVRSHDGVVIAGYTSGDVRVWDTRTWDYVAPFLESESEEEDPGMQPYVSFVRINSSLAVAAYEDGILNIWDLRTGRFPIFRFEHDARIQALALSQEKPIVATASAFDVVMLYPNEEGHWHVASEFEVQKLVDYLEIVPNTGRYPVAIATAGDLVYLLKADDSARTLHYVYGQPATCLDVSASQVAFGVKSLGWVYEGNKILVYSLEAERCLSKLGNALGDFTCVNIRDSPPNLMVSGNMDRRVRIHDLRSDKIALSLSAHQLGVSAVQMDDWKVVSGGEEGLVSVWDYRMNQKLWEVHSRHPVRYLSFNSHSLITANVPYEKVLRNSDLDNFACHRRHRGLIHAYEFAVDQLAFQSPLPVCRLPRDIMAGYSYDLALSFPHDSI
Protein: Left-right determination factor 2 (Endometrial bleeding-associated factor) (Left-right determination factor A) (Protein lefty-2) (Protein lefty-A) (Transforming growth factor beta-4) (TGF-beta-4) (O00292)
Organism: Homo sapiens (Human)
Function: Required for left-right (L-R) asymmetry determination of organ systems in mammals. May play a role in endometrial bleeding.
Subcellular location: Secreted.
Interaction partners:
- Nodal homolog
- Left-right determination factor 1
- Activin receptor type-2B
- Protein Cripto
- Transforming growth factor beta-3 proprotein
- Cryptic protein
- Transforming growth factor beta-1 proprotein
- Zinc finger protein ZIC 3
- Pituitary homeobox 2
- POU domain, class 5, transcription factor 1
Sequence:
MWPLWLCWALWVLPLAGPGAALTEEQLLGSLLRQLQLSEVPVLDRADMEKLVIPAHVRAQYVVLLRRSHGDRSRGKRFSQSFREVAGRFLASEASTHLLVFGMEQRLPPNSELVQAVLRLFQEPVPKAALHRHGRLSPRSAQARVTVEWLRVRDDGSNRTSLIDSRLVSVHESGWKAFDVTEAVNFWQQLSRPRQPLLLQVSVQREHLGPLASGAHKLVRFASQGAPAGLGEPQLELHTLDLRDYGAQGDCDPEAPMTEGTRCCRQEMYIDLQGMKWAKNWVLEPPGFLAYECVGTCQQPPEALAFNWPFLGPRQCIASETASLPMIVSIKEGGRTRPQVVSLPNMRVQKCSCASDGALVPRRLQP
Protein: Cyclin-dependent kinase 2-associated protein 2 (CDK2-associated protein 2) (DOC-1-related protein) (DOC-1R) (O75956)
Organism: Homo sapiens (Human)
Function: Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin. Inhibits cell cycle G1/S phase transition by repressing CDK2 expression and activation; represses CDK2 activation by inhibiting its interaction with cyclin E and A. Plays a role in regulating the self-renewal of embryonic stem cells (ESCs) and in maintaining cell survival during terminal differentiation of ESCs (By similarity). Regulates microtubule organization of metaphase II oocytes (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10082655}. Nucleus {ECO:0000269|PubMed:10082655, ECO:0000269|PubMed:33283408}. Note=Accumulates in immature oocytes in the nucleus. During the first meiotic division, accumulates in the cytoplasm and localizes in dots in the vicinity of the chromosomes in a region enriched in microtubules. {ECO:0000250|UniProtKB:Q9CPY4}.
Interaction partners:
Sequence:
MSYKPIAPAPSSTPGSSTPGPGTPVPTGSVPSPSGSVPGAGAPFRPLFNDFGPPSMGYVQAMKPPGAQGSQSTYTDLLSVIEEMGKEIRPTYAGSKSAMERLKRGIIHARALVRECLAETERNART
Protein: DNA polymerase III subunit delta' (EC 2.7.7.7) (P28631)
Organism: Escherichia coli (strain K12)
Function: Part of the beta sliding clamp loading complex, which hydrolyzes ATP to load the beta clamp onto primed DNA to form the DNA replication pre-initiation complex. DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The gamma complex (gamma(3),delta,delta') is thought to load beta dimers onto DNA by binding ATP which alters the complex's conformation so it can bind beta sliding clamp dimers and open them at one interface. Primed DNA is recognized, ATP is hydrolyzed releasing the gamma complex and closing the beta sliding clamp ring around the primed DNA.
Interaction partners:
- DNA polymerase III subunit delta
- DNA polymerase III subunit chi
- Beta sliding clamp
- DNA polymerase III subunit psi
- DNA polymerase III subunit tau
- DNA polymerase III subunit alpha
- Thymidylate kinase
- DNA polymerase III subunit epsilon
- Endolytic murein transglycosylase
- Aminodeoxychorismate lyase
Sequence:
MRWYPWLRPDFEKLVASYQAGRGHHALLIQALPGMGDDALIYALSRYLLCQQPQGHKSCGHCRGCQLMQAGTHPDYYTLAPEKGKNTLGVDAVREVTEKLNEHARLGGAKVVWVTDAALLTDAAANALLKTLEEPPAETWFFLATREPERLLATLRSRCRLHYLAPPPEQYAVTWLSREVTMSQDALLAALRLSAGSPGAALALFQGDNWQARETLCQALAYSVPSGDWYSLLAALNHEQAPARLHWLATLLMDALKRHHGAAQVTNVDVPGLVAELANHLSPSRLQAILGDVCHIREQLMSVTGINRELLITDLLLRIEHYLQPGVVLPVPHL
Protein: Methylcrotonyl-CoA carboxylase subunit 1 (E9PG35)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAASAVSVLLVAAERNRWHRLPSLLLPPRTWVWRQRTMKYTTATDEAYSIGPAPSQQSYLSMEKIIQVAKTSAAQAIHPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEGYHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRKKLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPRADPSTRIETGVRQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFEAGNVHTDFIPQHHKQLLLSRKAAAKESLCQAALGLILKEKAMTDTFTLQAHDQFSPFSSSSGRRLNISYTRNMTLKDGKNNVAIAVTYNHDGSYSMQIEDKTFQVLGNLYSEGDCTYLKCSVNGVASKAKLIILENTIYLFSKEGSIEIDIPVPKYLSSVSSQET
Protein: Zinc-finger homeodomain protein 3 (AtZHD3) (Homeobox protein 21) (AtHB-21) (Zinc finger homeodomain transcription factor 4) (O64722)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Putative transcription factor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. Note=Interactions with MIF proteins prevent nuclear subcellular location and leads to a scattered repartition throughout the cytoplasm. {ECO:0000250}.
Interaction partners:
- GLABROUS1 enhancer-binding protein-like 3
- Protein S-acyltransferase 21
- Protein BASIC PENTACYSTEINE7
- Homeobox-leucine zipper protein ATHB-21
Sequence:
MEIASQEDPIPINTSYGNSGGGHGNMNHHHHANSAPSSLNITTSNPLLVSSNSNGLGKNHDHSHHHHVGYNIMVTNIKKEKPVVIKYKECLKNHAATMGGNAIDGCGEFMPSGEEGSIEALTCSVCNCHRNFHRRETEGEEKTFFSPYLNHHQPPPQQRKLMFHHKMIKSPLPQQMIMPIGVTTAGSNSESEDLMEEEGGGSLTFRQPPPPPSPYSYGHNQKKRFRTKFTQEQKEKMISFAERVGWKIQRQEESVVQQLCQEIGIRRRVLKVWMHNNKQNLSKKSNNVSNNVDLSAGNNDITENLASTNP
Protein: Putative nitronate monooxygenase (EC 1.13.12.16) (Nitroalkane oxidase) (P47177)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the oxidation of alkyl nitronates to produce the corresponding carbonyl compounds and nitrites.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- tRNA modification GTPase MSS1
Sequence:
MYFLNQLIFQDVSVMSVDKREDMSRSFQKCLNLRYPIIQAPMAGVTTIEMAAKACIAGAIASLPLSHLDFRKVNDIEKLKLMVSQFRDQVADESLEGNLNLNFFCHDIVDKPTDLQTANWAKLYRKSMNVPIDMNEIKFDNGNVSFKAFEKENALQDFFQYLSDGFRPKIISFHFGHPSKSTIEYLQKIGILIFVTATSVREVRLLARLGINGIVCQGYEAGGHRGNFLVNDPKDDENLSTVQLVKRTVDELAEMKNKGLIHATPFVIAAGGIMDSKDISYMLSQQADAVQVGTAFLGCSESNASKNFSSPFTRETTTKMVNIISGKPARTISTPFIEKVIANFQGEELPPYGYMYSAFKQVRKKYPELANFILAGQGFQNVQSGITTDKKIETMGARLKIDGK
Protein: Protein RecA (Recombinase A) (P42443)
Organism: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)
Function: Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage (By similarity). Probably involved in base excision repair.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00268}.
Interaction partners:
- DNA polymerase I
- LexA repressor
- Regulatory protein RecX
- CinA-like protein
- DNA repair protein RadA
- DNA repair protein RecN
- HTH cro/C1-type domain-containing protein
- DNA 3'-5' helicase
- Recombination protein RecR
- RNA 2',3'-cyclic phosphodiesterase
Sequence:
MSKDATKEISAPTDAKERSKAIETAMSQIEKAFGKGSIMKLGAESKLDVQVVSTGSLSLDLALGVGGIPRGRITEIYGPESGGKTTLALAIVAQAQKAGGTCAFIDAEHALDPVYARALGVNTDELLVSQPDNGEQALEIMELLVRSGAIDVVVVDSVAALTPRAEIEGDMGDSLPGLQARLMSQALRKLTAILSKTGTAAIFINQVREKIGVMYGNPETTTGGRALKFYASVRLDVRKIGQPTKVGNDAVANTVKIKTVKNKVAAPFKEVELALVYGKGFDQLSDLVGLAADMDIIKKAGSFYSYGDERIGQGKEKTIAYIAERPEMEQEIRDRVMAAIRAGNAGEAPALAPAPAAPEAAEA
Protein: RH49505p (Q8SWZ8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQRVAIIGGTGMTGECAVDHALQKGLSVKLLYRSEKTVPERFKSKVELVKGDVTNYEDVQRVIEGVDAVAVILGTRNKLEATTELSRGTENLIKAMKEAKLTKFSIVMSSFLLRPLNEVPTVFHRLNEEHQRMLDLTKACDLDWIAILPPHIADEPATAYTVLHEEAPGRLVSKYDLGKFIIDSLEQPEHYRKVCGIGKSPKSA
Protein: DNA replication licensing factor MCM7 (EC 3.6.4.12) (Q7ZVL6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365012}.
Interaction partners:
Sequence:
MAPKDYTAEKEKCKRFLQEFYTEDDSGKKIFKYGAQLVSLAHREQVALLVDLDDVAEEDPDLVESVCENAKRYTALFADAIHELLPEYREREAVVKDALDVYIEHRLMMEVRGRDPADTRDHRKQYPPELMRRFEVYFRPPATLKPRVVRDVKADSIGQLVTVRGIVTRATEVKPMMAVATYTCDQCGAETYQPIASPSFTPLIMCPSQECVTNKSGGRLYLQTRGSKFIKFQELRIQEHSDQVPVGNIPRSMTIYARGENTRVAQPGDHVAVSGVFLPLLRSGFRQAVQGLLSETYLECHSITLMNKTEDDELGTEELSDEELRQITEEDFYEKLAGSIAPEIYGHEDVKKALLLLLVGGVEQAPRGMKIRGNINICLMGDPGVAKSQLLSYIDRLAPRSQYTTGRGSSGVGLTAAVMRDPVTGEMTLEGGALVLADLGVCCIDEFDKMADADRTAIHEVMEQQTISIAKAGIMTSLNARCSILAAANPAYGRYNPRKSIEQNIQLPAALLSRFDLLWLIQDRPDAESDLRLAQHITYVHQHCRQPPTHFTPIDMKLMRRYISKCKQKQPVVPESLSDYITAAYVEMRKEARVSKDTTFTSARTLLSILRLSTALARLRMVSVVEKEDVNEAMRLMEMSKDSLQADRSSSSRAQRPADVIFSLLRELCGESAGRSVRVSAAEQRCVSRGFTPAQFQAALQEYEELNVWQINQARTRITFV
Protein: Uncharacterized WD repeat-containing protein C25H1.08c (O13982)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Ribosome assembly protein rrb1
- Ankyrin repeat-containing protein P16F5.05c
- Large ribosomal subunit protein uL16A
- Large ribosomal subunit protein uL16B
- Uncharacterized NOC2 family protein C1142.04
- Uncharacterized NOC2 family protein C1B3.09c
- Ribosome assembly factor mrt4
- Ribosome biogenesis protein rlp24
- Nucleolar complex-associated protein 3
- Importin subunit beta-2
Sequence:
MAEEEENQELYIAENEVEEVIKDNDKLMDQGVTEDEAEQEQNDTMNNMVMDMSVQGFFEHKDSVFSVSINPVHSNLCASGGGDDLGYIWDITTGEQICQLTGHKDSIVAIDWSFDGTYIATGGMDSQVRLWKSSTGFEFITAFETVDEIVWLSWHPKGLFLAAGCNDGSIWMWSLPSGKVVQVMYGHTAPVNAGKFIPPGVGKRLATVDDSGTLIVWNPATGAPECRMSSDDHRFDPGNEETAAGWTSFDCNAEGNVLFLGGSSGKVKVVNINSSHILASLEAQTESVEAIALCTALPICACASVDGTVALYDSASLKFRKSLPHEQAVIDCKFLPNTPYLLTACADCVIRKWDVRSGQLLGEYTGHQEPILCMAITPDGKRVVTGSDDTELLVFDCEH
Protein: M protein (Q6V4L4)
Organism: Streptococcus pyogenes
Subcellular location: Secreted, cell wall {ECO:0000256|PROSITE-ProRule:PRU01372}; Peptidoglycan-anchor {ECO:0000256|PROSITE-ProRule:PRU01372}.
Interaction partners:
Sequence:
RKLKTGTASVAVALTVVGAGLASQTEVKADQPVDHHRYTEANNAVLQGRTVSARALLHEINKNGQLRSENEELKADLQKKEQELKNLNDDVKKLNDEVALERLKNERHVHDEEVELERLKNERHDHDKKEAERKALEDKLADKQEHLDGALRYINEKEAERKEKEAEQKKLKEEKQISDASRQGLRRDLDASREAKKQVEKDLANLTAELDKAKEEKQISDASRQGLRRDLDASREAKKQVEKDLANLTAELDKVKEEKQISDASRQGLRRDLDASREAKKQVEKALEEANSKLAALEKLNKELEESKKLTEKEKAELQAKLEAEAKALKEKLAKQAEELAKLRAEKASDSQTPDAKPGNKAVPGKGQAPQAGTKPNQNKAPMKETKRQLPSTGETT
Protein: 3',5'-cyclic-AMP phosphodiesterase, isoform F (EC 3.1.4.53) (Learning/memory process protein) (Protein dunce) (cAMP-specific phosphodiesterase, isoform F) (Q8IRU4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes (By similarity). Vital for female fertility. Required for learning/memory (By similarity).
Interaction partners:
Sequence:
MLNKNSASSQSLPRVHSFFNMIPSIMQDDLALTILNDRDNMFSIKSQRSHGEDLIVTPFAQILASLRSVRNNLLSLTNVPASNKSRRPNQSSSASRSGNPPGAPLSQGEEAYTRLATDTIEELDWCLDQLETIQTHRSVSDMASLKFKRMLNKELSHFSESSRSGNQISEYICSTFLDKQQEFDLPSLRVEDNPELVAANAAAGQQSAGQYARSRSPRGPPMSQISGVKRPLSHTNSFTGERLPTFGVETPRENELGTLLGELDTWGIQIFSIGEFSVNRPLTCVAYTIFQSRELLTSLMIPPKTFLNFMSTLEDHYVKDNPFHNSLHAADVTQSTNVLLNTPALEGVFTPLEVGGALFAACIHDVDHPGLTNQFLVNSSSELALMYNDESVLENHHLAVAFKLLQNQGCDIFCNMQKKQRQTLRKMVIDIVLSTDMSKHMSLLADLKTMVETKKVAGSGVLLLDNYTDRIQVLENLVHCADLSNPTKPLPLYKRWVALLMEEFFLQGDKERESGMDISPMCDRHNATIEKSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEENRDYYQSMIPPSPPPSGVDENPQEDRIRFQVTLEESDQENLAELEEGDESGGESTTTGTTGTTAASALSGAGGGGGGGGGMAPRTGGCQNQPQHGGM
Protein: Lectin 11 (MtLec11) (Agglutinin LEC11) (A0A396GS61)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Function: May be involved in arbuscular mycorrhizal (AM) symbiosis with AM fungi.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MHYSHFYFIINNTNMTINAIPKLFATKNSISLSIVIFMYLLILVANVKSDSSFNFPNFQPEALKKLGFANDATLKNGVIQLTKKDAYGDPLKHSAGQFGLLKPIRLFDQTTGKVASFVTEFTFSVNSNGRQDHGDGFAFFMASPKFKIPNKNKSEGGFLGMFTRETALYTKEIVLVEFDSFANEWDPNPSSNLGIGSHLGIDVNSIKSVANALWLNDFDDITVGKARIEYDSSDKNLKVLVTYSEKGAFNGDSSLVYNIDLTTFLPEMIEIGFSASTGDLVETHDILSWSFTSNM
Protein: Fibrillarin (M0QXL5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
GRGGFGGGRGRGGGFRGNQSGKNVMVEPHRHEGVFICRGKEDALVTKNLVPGESVYGEKRVSISEGDDKIEYRAWNPFRSKLAAAILGGVDQIHIKPGAKVLYLGAASGTTVSHVSDIVGPDGLVYAVEFSHRSGRDLINLAKKRTNIIPVIEDARHPHKYRMLIAMVDVIFADVAQPDQTRIVALNAHTFLRNGGHFVISIKANCIDSTASAEAVFASEVKKMQQENMKPQEQLTLEPYERDH
Protein: Xylan O-acetyltransferase 4 (EC 2.3.1.-) (Protein trichome birefringence-like 10) (OsTBL10) (A0A0P0XXR9)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Xylan acetyltransferase required for 2-O- and 3-O-monoacetylation of xylosyl residues in xylan. Catalyzes the 2-O-acetylation of xylan, followed by nonenzymatic acetyl migration to the O-3 position, resulting in products that are monoacetylated at both O-2 and O-3 positions (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q2QYU2}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MTKPQQQSPPSTTATTTTSPPPPPPSTPPPASSSSSSLAKLPLRLHSLASSSRSLLSALRRSPVTTLVAAFFLLALFMYGEDVRTLAELSIDDYLYPDADFYNVSALPPLLLPPPTCDLSRGRWVFDNTSLPAYREKECTFLTKQVSCLANGRPDDLWQYWRWQPNNCSLPTFDARRFMEKMRGKRMMFVGDSLNRNQWESLVCLVQPILSKGRKKIVKRGSFNIFYAKEYRATLEFYWAPFLVESNSDNPNFHHIDQRIISPERIESHANNWKDVDYLIFNTYIWWMNNEDIKVRRPNSTSWSDHDEVPRIETYGRVFKTWSTWLEQNVDPARTSVFFMTISPLHNSPAQWGNPNGIKCVKETLPVLNYTKPLDLNHDMRMYDLVAKVAKNMKNVPVSLIDITRMSDYRKDAHTSLYSIRQGKLLTPEQKADPQKYADCIHWCLPGVPDVWNQILYTRILSKSSPPSPHPPLPPQ
Protein: Magnesium transporter NIPA1 (Non-imprinted in Prader-Willi/Angelman syndrome region protein 1) (Spastic paraplegia 6 protein) (Q7RTP0)
Organism: Homo sapiens (Human)
Function: Acts as a Mg(2+) transporter. Can also transport other divalent cations such as Fe(2+), Sr(2+), Ba(2+), Mn(2+) and Co(2+) but to a much less extent than Mg(2+) (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8BHK1}; Multi-pass membrane protein {ECO:0000255}. Early endosome {ECO:0000250|UniProtKB:Q8BHK1}. Note=Recruited to the cell membrane in response to low extracellular magnesium. {ECO:0000250|UniProtKB:Q8BHK1}.
Interaction partners:
- Gamma-tubulin complex component 5
- Cytoplasmic FMR1-interacting protein 1
- Spastin
- Insulin-like growth factor-binding protein 2
- Receptor expression-enhancing protein 1
- Spartin
- WASH complex subunit 5
- Atlastin-1
- Magnesium transporter NIPA2
- Kinesin heavy chain isoform 5A
Sequence:
MGTAAAAAAAAAAAAAGEGARSPSPAAVSLGLGVAVVSSLVNGSTFVLQKKGIVRAKRRGTSYLTDIVWWAGTIAMAVGQIGNFLAYTAVPTVLVTPLGALGVPFGSILASYLLKEKLNILGKLGCLLSCAGSVVLIIHSPKSESVTTQAELEEKLTNPVFVGYLCIVLLMLLLLIFWIAPAHGPTNIMVYISICSLLGSFTVPSTKGIGLAAQDILHNNPSSQRALCLCLVLLAVLGCSIIVQFRYINKALECFDSSVFGAIYYVVFTTLVLLASAILFREWSNVGLVDFLGMACGFTTVSVGIVLIQVFKEFNFNLGEMNKSNMKTD
Protein: DNA mismatch repair protein Mlh1 (MutL protein homolog 1) (P40692)
Organism: Homo sapiens (Human)
Function: Heterodimerizes with PMS2 to form MutL alpha, a component of the post-replicative DNA mismatch repair system (MMR). DNA repair is initiated by MutS alpha (MSH2-MSH6) or MutS beta (MSH2-MSH3) binding to a dsDNA mismatch, then MutL alpha is recruited to the heteroduplex. Assembly of the MutL-MutS-heteroduplex ternary complex in presence of RFC and PCNA is sufficient to activate endonuclease activity of PMS2. It introduces single-strand breaks near the mismatch and thus generates new entry points for the exonuclease EXO1 to degrade the strand containing the mismatch. DNA methylation would prevent cleavage and therefore assure that only the newly mutated DNA strand is going to be corrected. MutL alpha (MLH1-PMS2) interacts physically with the clamp loader subunits of DNA polymerase III, suggesting that it may play a role to recruit the DNA polymerase III to the site of the MMR. Also implicated in DNA damage signaling, a process which induces cell cycle arrest and can lead to apoptosis in case of major DNA damages. Heterodimerizes with MLH3 to form MutL gamma which plays a role in meiosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:21120944, ECO:0000269|PubMed:22753075, ECO:0000269|PubMed:30770470}. Chromosome {ECO:0000269|PubMed:26300262}. Note=Recruited to chromatin in a MCM9-dependent manner. {ECO:0000269|PubMed:26300262}.
Interaction partners:
- DNA mismatch repair protein Mlh3
- PMS1 protein homolog 1
- Fanconi anemia group J protein
- RecQ-like DNA helicase BLM
- Exonuclease 1
- DNA mismatch repair protein Msh3
- DNA mismatch repair protein Msh2
- Mismatch repair endonuclease PMS2
- DNA mismatch repair protein Msh6
- Fanconi-associated nuclease 1
Sequence:
MSFVAGVIRRLDETVVNRIAAGEVIQRPANAIKEMIENCLDAKSTSIQVIVKEGGLKLIQIQDNGTGIRKEDLDIVCERFTTSKLQSFEDLASISTYGFRGEALASISHVAHVTITTKTADGKCAYRASYSDGKLKAPPKPCAGNQGTQITVEDLFYNIATRRKALKNPSEEYGKILEVVGRYSVHNAGISFSVKKQGETVADVRTLPNASTVDNIRSIFGNAVSRELIEIGCEDKTLAFKMNGYISNANYSVKKCIFLLFINHRLVESTSLRKAIETVYAAYLPKNTHPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILERVQQHIESKLLGSNSSRMYFTQTLLPGLAGPSGEMVKSTTSLTSSSTSGSSDKVYAHQMVRTDSREQKLDAFLQPLSKPLSSQPQAIVTEDKTDISSGRARQQDEEMLELPAPAEVAAKNQSLEGDTTKGTSEMSEKRGPTSSNPRKRHREDSDVEMVEDDSRKEMTAACTPRRRIINLTSVLSLQEEINEQGHEVLREMLHNHSFVGCVNPQWALAQHQTKLYLLNTTKLSEELFYQILIYDFANFGVLRLSEPAPLFDLAMLALDSPESGWTEEDGPKEGLAEYIVEFLKKKAEMLADYFSLEIDEEGNLIGLPLLIDNYVPPLEGLPIFILRLATEVNWDEEKECFESLSKECAMFYSIRKQYISEESTLSGQQSEVPGSIPNSWKWTVEHIVYKALRSHILPPKHFTEDGNILQLANLPDLYKVFERC
Protein: Cardinal (EC 1.11.1.-) (Q9VCW2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTDETTPLTDAVPSGSGYVVLPPYQGPERVFPGGVSPRARRNKMRQFQCCMGITFIAIVFTALCLALVFSDSLGGADGGPSFFFVVNGSDSELAPNRPLPDEPAAEWALQQAALGHHDGAQAVSAGIKALGDREILEEGLQPNEVNTPSFRHYRSLSTNPEARKLARRGYVENQATIDIAKRFNYTKQPGRSNIGWGPKIVLPDPTVLRLECDFNARYRRSTGVCNNKQHPRTYGASMVPYRRMVSPDYADGIAAPRVSHHGRLPPARQVSLKIHRSSYETDSNFTVMLAVFGQFMDHDITATSLTTSQEGESIDCCVAATREQHPECYPVDILPDDPYYKQYNISCMNFVRSAPAPTGRFGPRMQLNQATAFIDASVVYGNLEQRQNQLRSFINGSLRMFVTDDGRQLLPISSNPADGCNRVQMTRLGKYCFESGDDRANENLLLTSMHLLWARHHNYLARQLQEQNPHWEDERLYQEARKILGAQMAHITYNEFLPVLLGKNISEAKGLLPAKHNLNAPDTYDPEVDPSIANCFAAAAFRFAHTLLPGLFNISRDNSTPEAIELHKMLFNPFSLWAEHGIDHALMTAANTPVMQVDRFFSLEVTQKLFEGTAEDRVPLCGLDLVSLNIQRGRDHGIPSYPVFRRHCRLPTVDTWEEMSQAIDNATLDSIRQIYESPQDVDVYTGALSEPPLDGAIFGPLLSCMVSDQFLRLKLGDSHWYERKMGPQKFTKAQLAEIYKTSLAAIICRNSDGITRVREHVMQRLRDGGNPHVDCQDLEGFHFNFEPWSEKQQPQDLHSAGISRGSTSVRVMSKANHQAHNVTLHIDKGI
Protein: Interleukin-1 beta (IL-1 beta) (Catabolin) (P01584)
Organism: Homo sapiens (Human)
Function: Potent pro-inflammatory cytokine. Initially discovered as the major endogenous pyrogen, induces prostaglandin synthesis, neutrophil influx and activation, T-cell activation and cytokine production, B-cell activation and antibody production, and fibroblast proliferation and collagen production. Promotes Th17 differentiation of T-cells. Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-helper 1 (Th1) cells. Plays a role in angiogenesis by inducing VEGF production synergistically with TNF and IL6. Involved in transduction of inflammation downstream of pyroptosis: its mature form is specifically released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore. Acts as a sensor of S.pyogenes infection in skin: cleaved and activated by pyogenes SpeB protease, leading to an inflammatory response that prevents bacterial growth during invasive skin infection.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:15192144}. Secreted {ECO:0000269|PubMed:11728343, ECO:0000269|PubMed:15192144, ECO:0000269|PubMed:33883744}. Lysosome {ECO:0000269|PubMed:15192144}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:P10749}. Note=The precursor is cytosolic (PubMed:15192144). In response to inflammasome-activating signals, such as ATP for NLRP3 inflammasome or bacterial flagellin for NLRC4 inflammasome, cleaved and secreted (PubMed:24201029, PubMed:33377178, PubMed:33883744). Mature form is secreted and released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore (PubMed:33883744). In contrast, the precursor form is not released, due to the presence of an acidic region that is proteolytically removed by CASP1 during maturation (PubMed:33883744). The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10 (PubMed:32272059). {ECO:0000269|PubMed:15192144, ECO:0000269|PubMed:24201029, ECO:0000269|PubMed:32272059, ECO:0000269|PubMed:33377178, ECO:0000269|PubMed:33883744}.
Interaction partners:
- Interleukin-1 receptor type 2
- Caspase-1
- Interleukin-2
- Interleukin-1 alpha
- Myeloid differentiation primary response protein MyD88
- Interleukin-1 receptor type 1
- Interleukin-1 receptor accessory protein
- Interleukin-4
- Tumor necrosis factor
- Interleukin-5
Sequence:
MAEVPELASEMMAYYSGNEDDLFFEADGPKQMKCSFQDLDLCPLDGGIQLRISDHHYSKGFRQAASVVVAMDKLRKMLVPCPQTFQENDLSTFFPFIFEEEPIFFDTWDNEAYVHDAPVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFVQGEESNDKIPVALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKMEKRFVFNKIEINNKLEFESAQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS
Protein: Dual specificity protein phosphatase 19 (EC 3.1.3.16) (EC 3.1.3.48) (Protein phosphatase SKRP1) (Stress-activated protein kinase pathway-regulating phosphatase 1) (Q8K4T5)
Organism: Mus musculus (Mouse)
Function: Has a dual specificity toward Ser/Thr and Tyr-containing proteins.
Interaction partners:
- Dual specificity mitogen-activated protein kinase kinase 7
Sequence:
MHSLNQKIKAFSRDNLRKQCTRVTTLTGKKLIETWEDATVHVVETEPSGGGGCGYVQDLTLDLQVGVIKPWLLLGSQDAAHDLELLRKHKVTHILNVAYGVENAFLSEFTYKTISILDVPETNILSYFPECFEFIEQAKLKDGVVLVHCNAGVSRAAAIVIGFLMSSEEATFTTALSLVKEARPSICPNPGFMEQLRTYQVGKESNGGDKVPAEDTTHGL