wanglab/gogpt-training-data huggingface dataset:
Protein: Glutamate receptor ionotropic, kainate 2 (GluK2) (Glutamate receptor 6) (GluR-6) (GluR6) (P42260)
Organism: Rattus norvegicus (Rat)
Function: Ionotropic glutamate receptor. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. Modulates cell surface expression of NETO2 (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:17486098, ECO:0000269|PubMed:22509486, ECO:0000269|PubMed:8163463}; Multi-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane {ECO:0000269|PubMed:17486098}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Glutamate receptor ionotropic, kainate 5
- Glutamate receptor ionotropic, kainate 4
- Glutamate receptor ionotropic, kainate 1
- Disks large homolog 4
- Glutamate receptor ionotropic, kainate 3
- Neuropilin and tolloid-like protein 2
- Glutamate receptor ionotropic, NMDA 1
- Glutamate receptor ionotropic, NMDA 2A
- Voltage-dependent calcium channel gamma-2 subunit
- Glutamate receptor 4
Sequence:
MKIISPVLSNLVFSRSIKVLLCLLWIGYSQGTTHVLRFGGIFEYVESGPMGAEELAFRFAVNTINRNRTLLPNTTLTYDTQKINLYDSFEASKKACDQLSLGVAAIFGPSHSSSANAVQSICNALGVPHIQTRWKHQVSDNKDSFYVSLYPDFSSLSRAILDLVQFFKWKTVTVVYDDSTGLIRLQELIKAPSRYNLRLKIRQLPADTKDAKPLLKEMKRGKEFHVIFDCSHEMAAGILKQALAMGMMTEYYHYIFTTLDLFALDVEPYRYSGVNMTGFRILNTENTQVSSIIEKWSMERLQAPPKPDSGLLDGFMTTDAALMYDAVHVVSVAVQQFPQMTVSSLQCNRHKPWRFGTRFMSLIKEAHWEGLTGRITFNKTNGLRTDFDLDVISLKEEGLEKIGTWDPASGLNMTESQKGKPANITDSLSNRSLIVTTILEEPYVLFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDVNGQWNGMVRELIDHKADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKPNGTNPGVFSFLNPLSPDIWMYILLAYLGVSCVLFVIARFSPYEWYNPHPCNPDSDVVENNFTLLNSFWFGVGALMQQGSELMPKALSTRIVGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSRRQSVLVKSNEEGIQRVLTSDYAFLMESTTIEFVTQRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHMMKEKWWRGNGCPEEESKEASALGVQNIGGIFIVLAAGLVLSVFVAVGEFLYKSKKNAQLEKRSFCSAMVEELRMSLKCQRRLKHKPQAPVIVKTEEVINMHTFNDRRLPGKETMA
Protein: Cytosolic 10-formyltetrahydrofolate dehydrogenase (10-FTHFDH) (FDH) (EC 1.5.1.6) (Aldehyde dehydrogenase family 1 member L1) (FBP-CI) (P28037)
Organism: Rattus norvegicus (Rat)
Function: Cytosolic 10-formyltetrahydrofolate dehydrogenase that catalyzes the NADP(+)-dependent conversion of 10-formyltetrahydrofolate to tetrahydrofolate and carbon dioxide. May also have an NADP(+)-dependent aldehyde dehydrogenase activity towards formaldehyde, acetaldehyde, propionaldehyde, and benzaldehyde.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:1848231, ECO:0000269|PubMed:3392008}.
Interaction partners:
- Excitatory amino acid transporter 1
- Glial fibrillary acidic protein
- Excitatory amino acid transporter 2
- Delta-1-pyrroline-5-carboxylate synthase
- Aquaporin-4
Sequence:
MKIAVIGQSLFGQEVYCQLRKEGHEVVGVFTIPDKDGKADPLGLEAEKDGVPVFKFPRWRARGQALPEVVAKYQALGAELNVLPFCSQFIPMEVINAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFTIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRFLFPEGIKGMVQAVRLIAEGTAPRCPQSEEGATYEGIQKKETAKINWDQPAEAIHNWIRGNDKVPGAWTEACGQKLTFFNSTLNTSGLSTQGEALPIPGAHRPGVVTKAGLILFGNDDRMLLVKNIQLEDGKMMPASQFFKGSASSDLELTEAELATAEAVRSSWMRILPNVPEVEDSTDFFKSGAASVDVVRLVEEVKELCDGLELENEDVYMATTFRGFIQLLVRKLRGEDDESECVINYVEKAVNKLTLQMPYQLFIGGEFVDAEGSKTYNTINPTDGSVICQVSLAQVSDVDKAVAAAKEAFENGLWGKINARDRGRLLYRLADVMEQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGATIPINQARPNRNLTLTKKEPVGVCGIVIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNILPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCALSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEESIHNQFVQKVVEEVEKMKIGNPLERDTNHGPQNHEAHLRKLVEYCQRGVKEGATLVCGGNQVPRPGFFFQPTVFTDVEDHMYIAKEESFGPIMIISRFADGDVDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFINTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRIKTVTFEY
Protein: Defective proboscis extension response 6, isoform D (M9PES4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPIAHPLPLCVAWLLLLVVIVMSDMTNGGVQGPIEGYNSLDDLLTTTPTPGQAALLLPTAPTAAYTHPKWMEPYFDPSTPRNVTALMGKSAYLSCRVRNLANKTVSWIRHRDIHILTVGSYTYTSDQRFQATHHQDTEDWTLQIKWAQKRDAGMYECQISTQPVRSYFVRLNVVVPTATILGGPDLHVDKGSTINLTCTVKFSPEPPAYIFWYHHEEVINYDSSRGGVSVITEKGDVTTSFLLIQNADLADSGKYSCAPSNADVASVRVHVLNDSQPHSRRAKIRS
Protein: Oleosin (A6MGW7)
Organism: Lilium longiflorum (Trumpet lily)
Subcellular location: Lipid droplet {ECO:0000269|PubMed:17468126}. Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Surface of oil bodies. Oleosins exist at a monolayer lipid/water interface. {ECO:0000305}.
Interaction partners:
Sequence:
MAERQTGTGPGPVTRTHRHHAPASGGACSNLLRRIQDHVPNSTQLVGFLTLLISGGILLLLTGLTATSAAMGFVLFAPLILLTSPVWIPLVTIFFLLTAGFLSTCGFGVAALAGGTWLYRYLSGRHPLGSERVDYARSRIADTASHVKDYAREYGGYLQSRVKDAAPGA
Protein: Hexahomomethionine N-hydroxylase (EC 1.14.14.42) (Cytochrome P450 79F2) (Q9FUY7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the conversion of the long chain elongated methionines penta- and hexahomomethionine to their corresponding aldoximes 8-methylthiooctanaldoxime and 9-methylthiononanaldoxime.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11226190}; Single-pass membrane protein {ECO:0000269|PubMed:11226190}.
Interaction partners:
- Methylthioalkylmalate synthase 3, chloroplastic
- Methylthioalkylmalate synthase 1, chloroplastic
- Dihomomethionine N-hydroxylase
- Transcription factor MYB28
- UDP-glycosyltransferase 74C1
- Transcription factor MYB76
- Transcription factor MYB29
- S-alkyl-thiohydroximate lyase SUR1
- Cytosolic sulfotransferase 18
- Methionine aminotransferase BCAT4
Sequence:
MMMKISFNTCFQILLGFIVFIASITLLGRIFSRPSKTKDRCRQLPPGRPGWPILGNLPELIMTRPRSKYFHLAMKELKTDIACFNFAGTHTITINSDEIAREAFRERDADLADRPQLSIVESIGDNYKTMGTSSYGEHFMKMKKVITTEIMSVKTLNMLEAARTIEADNLIAYIHSMYQRSETVDVRELSRVYGYAVTMRMLFGRRHVTKENMFSDDGRLGKAEKHHLEVIFNTLNCLPGFSPVDYVDRWLGGWNIDGEEERAKVNVNLVRSYNNPIIDERVEIWREKGGKAAVEDWLDTFITLKDQNGNYLVTPDEIKAQCVEFCIAAIDNPANNMEWTLGEMLKNPEILRKALKELDEVVGKDRLVQESDIRNLNYLKACCRETFRIHPSAHYVPPHVARQDTTLGGYFIPKGSHIHVCRPGLGRNPKIWKDPLAYEPERHLQGDGITKEVTLVETEMRFVSFSTGRRGCVGVKVGTIMMAMMLARFLQGFNWKLHRDFGPLSLEEDDASLLMAKPLLLSVEPRLASNLYPKFRP
Protein: Yuri gagarin, isoform B (Q9V435)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Tropomyosin-1, isoforms 9A/A/B
- LIM and SH3 domain protein Lasp
- Calmodulin-related protein 97A
- Myosin heavy chain 95F
- AT09290p
- Dynamin
- Cortactin, isoform A
- Proteasome inhibitor PI31 subunit
- PFTAIRE-interacting factor 1A, isoform H
- Eukaryotic translation initiation factor 3 subunit M
Sequence:
MASRQAGFVLDAKSMGLNPSRPASSPPPPPSSASQMCRQVQPTGTSASHPHQESTLKASSPDRCTASTEAMSTEHYRCLIQKLRDTNGDAGDMSFELNSIFLKRLDEIDCLDEHEGDDMHTCQLRLVTFQEWVDFLLHVNSVILGNVSDLEKEAYSKIVACCQSVQVRQQHTLEENRRLREDICAIIERVQHSPHCTDFDFNGISLETLTVNQLRGVGKDPAHAECESEKMSESMKSLVGEIAAKHDEIGELKSQINALDEVVHTARQKLLLKDQCIAQLNQQLHEITRCIESRDQAKMEESPNDTLTADAITSDMLENLSIHDTQESEMLRLLNAELNDLLDLHNKQEFQTIEIRRKRVSCFIEKLVSEREDTLKKLESIRSHLTILQSDLDQSCLISVDPESGPCDLDADAQMLEALRRRLLNLSQLNRELHGKYQRLDTESKIKISELEARIESESSVLQRNSDVLREIAELICSLGSKEFSYNEIYDESSKENPFCTTIADMFARKFEQEQNQVEINGQLSCQIKGLQENLKDRDNQISQLQSMINSYSDFSENNRLKEEMHVLKQKNCDLSRQLRDLPSLLKNQENQSVELCTKYESLMASFEDQCQELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQQKSAQLEMEKMRTLVRKMQSHLQLDDIRHRESIQRMNETTESLREELRTISENCQQMQIRLNQQTEVNQQQEQIIDSFRKWKDAQVRADEAMRLCAKRAEEHIHMLLDENRTLAEDYRNLFRDYKLLETEIKRVKQAVNCASSSAISCPPPKSGGLTNPEAGNDMARRLQNLTSTSQRIFNQNQTMNDQYCNSLISGSPAGIGQPVAQSILRRTRSSQDQS
Protein: Frizzled-4 (Q95Y45)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MMHSLGIILLFIPLATGSIFDQAVKGKCIPIDIELCKDLPYNYTYFPNTILHNDQHTLQTHTEHFKPLMKTKCHPHIHFFICSVFAPMCPIGMPQAVTSCKSVCEQVKADCFSILEEFGIGWPEPLNCAQFPDPPELCMKPTEDEITGGFSAPRLPTKGSSSSSSKPTGCPSDLVDVDPHDPKSHCAFACQSNVMFSTDNKRMVRSWSIWFAAANAGVALFSFLTFAIDRKRFRFPERCVFYLSLCIFISSLPYLTPLFIDAPIRSCHALGNGRSYLSIGTFDNSYCLASFLLNYFFSTAAALWWLMFSFTLYLSGGRKWVPEGIEACSSYVHFVAWGLSSLATIIVLIFNKVDASELTALCSVGNLNSIALLWFVIVPRTICIVIGTCFIVGGFASMCRERISFRTRGTDTSKLEKLMVKMGFFCALFILPNVIELVCQCYKFMILTQWTRMTIDCKQQSGACHRPTPPQAEIYMTAVISSLATGFSCLMWVLSAKTVHAWKNFIFCGMCSSAPVKVKPNRAINTSIARATNCSATTTTGIHANGDESSEFMETQ
Protein: Cadherin 6 (Cadherin-6 isoform X1) (Cadherin-6 precursor) (Q5WN09)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU003318}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU003318}.
Interaction partners:
- Cadherin 18, type 2
- Catenin beta-1
Sequence:
MRTWIVLLLWACAHISVNAIALSRGPVRRKSKEIEGRQDKGLLRRSKRGWMWKQFFLQEEYTGSEHQYIGKLHSDMDRGDGTVMYVLTGEGAGTIFVIDANSGDLHATRSLDREEKPSYSLRAQAVNRKTGIPLEPETEFIVKLHDINDNEPKFDKEVYTASVPEGSHIGTFVTQVTAQDADDEMFGYSAKLAYSIKEGHPYFSVEPNTGIIRTALGPTDMDREQREHYQVVIEAKDMAGQKGGLIGSTTVNISLTDINDNAPHFKQGIYQFSVPELTKVGSSVGRIEAEDADIGRNAEMSYSITGGDSLDVFDISTDRNTQEGILTVKKPLDYEKKKSYTLQIEVKNTHPYSHYMSQDTKDKATIRISVEDVDEPPQFEKISYILEVKEDAAVGTMIGSVSAVDPDMRRSPVKYSIDRHTDVDRIFGIYAGNGSIFLQKPLDREEFAWHNISVIASEFRHLDNPEQTSRVPVYIRVLDVNDNPPVLASFYETFVCENAKAGQKIQTISAVDPDEPVGGHRFLFSLAPESSVRANFSVRDNGDNTAGIFTRRSGFGRMHKSTHLVAVVISDGHFPMQSSTGTLTIRVCTCDRDGNMEMCNAEALTSSAGLSTGALVAILLCILILLLIVVLFAALKRQKKKEPLIISKEDVRDNVVSYNDEGGGEEDTQAFDIGALRHPEVMEDSKLRRDILPSESLYPPPPLRRTIVPARENADVRDFINQRVEENDGNPTAPPYDSLATYAYEGNGSVAESLSSLGSVSSEGEQDYNYLSEWGPRFRKLADMYGGEDSDWDS
Protein: Ubiquilin 1 (Ubiquilin-1 isoform 2) (A0A287B231)
Organism: Sus scrofa (Pig)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAENGESGSPPSSQDSAAAAEGAGAPAAAASAEPKIMKVTVKTPKEKEEFAVPENSSVQQFKEEISKRFKSHTDQLVLIFAGKILKDQDTLSQHGIHDGLTVHLVIKTQNRPQDHSAQQTNTSGSNATTSSAPSSNSTSGSATSNPFGLGGLGGLAGLSSLGLNTTNFSELQSQMQRQLMSNPEMMVQIMENPFVQSMLSNPDLMRQLIMANPQMQQLIQRNPEISHMLNNPDIMRQTLELARNPAMMQEMMRNQDRALSNLESIPGGYNALRRMYTDIQEPMLSAAQEQFGGNPFASLVSNTSSGEGSQPSRTENRDPLPNPWAPQASQSSSASSGTTSAVGGTSGSAASGTTGQNSTAPNLGPGVGASMFNTPGMQSLLQQITENPQLMQNMLSAPYMRSMMQSLSQNPDLAAQMQNPDTLSAMSNPRAMQALLQIQQGLQTLATEAPGLIPGFTPGLGALGSTGSSSGTNGSNSAPSENPSPTAGTTEPGHQQFIQQMLQALAGVNPQLQNPEVRFQQQLEQLSAMGFLNREANLQALIATGGDINAAIERLLGSQPS
Protein: Eukaryotic translation initiation factor 4E (O97266)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Polyadenylate-binding protein-interacting protein 1, putative
- RNA helicase
- Eukaryotic translation initation factor 4 gamma
- RNA helicase
- Eukaryotic translation initiation factor 3 subunit B
Sequence:
MKYLTFNKNNRDAIDLSEKLEATKIDLSNPLLLQYNWVIWEQVSDNKIKQSNNYKDYTRPLAKFNSVQKFWQLWNRLPQPSDLLAQRSMTRFSEDGIFRIVDALMIFRDNIQPMWEDPANSGGGHFEYKILPKDYPYSQIDEFWNNLVLAIIGCSLKHYDLITGIRLVDKLSTTRYGYIRIEIWYTTITDESVKNYLRKDLEEHMCNRIDGSTIFPPRVKSLSHIHR
Protein: Allene oxide cyclase 2, chloroplastic (EC 5.3.99.6) (Q9LS02)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the production of 12-oxo-phytodienoic acid (OPDA), a precursor of jasmonic acid.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:12777050}.
Interaction partners:
- Allene oxide synthase, chloroplastic
- 12-oxophytodienoate reductase 3
- 12-oxophytodienoate reductase 2
- 12-oxophytodienoate reductase 1
- Putative 12-oxophytodienoate reductase-like protein 1
- Lipoxygenase 3, chloroplastic
- Lipoxygenase 4, chloroplastic
- Lipoxygenase 2, chloroplastic
- Lipoxygenase 6, chloroplastic
- Jasmonate O-methyltransferase
Sequence:
MASSAVSLQSISMTTLNNLSCNQQFHRSSLLGSSKSFQNLGISSNGSDFSYPSSFTAKKNLTASRALSQNGNIENPRPSKVQELSVYEINELDRHSPKILKNAFSLMFGLGDLVPFTNKLYTGDLKKRVGITAGLCVVIEHVPEKKGERFEATYSFYFGDYGHLSVQGPYLTYEDSFLAITGGAGIFEGAYGQVKLQQLVYPTKLFYTFYLKGLANDLPLELTGTPVPPSKDIEPAPEAKALEPSGVISNYTN
Protein: DNA-directed RNA polymerase (EC 2.7.7.6) (Q95NZ8)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- rRNA adenine N
- Probable dimethyladenosine transferase-N
- DNA-directed RNA polymerase I subunit rpa2
- Non-histone chromosomal protein 6 homolog
Sequence:
MIRLGQNLRSISKVKLQSFNNYKYSSSNNNNNNNNINSNINNIKINEYSNLRKIIEDGQENSNRLDKLKELFPDKEDLSSPLEYLDSEQRLNETKQKLIDLEKSFVEDLAKLNKARVVAQSYLLDGEDGIENDTDWKSDVKEISDDEKNLRKIQTLLEFEAIDDAVTRYRDLMLDSKGKSFVTSFKSIRDVLMQWNEGLTEKVQKDLATKDQDAAWVTILKTVSVQKCILKSLNIIVGKSVLKDRYDFATNIIIETIGVSVYAEYKSLIVKKKEPKTYKKISKLIPNSALKKFYNLSTDNLDVIVLPPESKDIFSIGEFLVSQVFKHCTIQESLGEDGSKQSPAFTIQSHYANGVRTTKVIPHKNIFKLIEAGHEIRETGGARLFPMVIKPLPWITPTEGPYLHYKVPIMRTNGSAMQLRTLVDSDMSLIYRALNILGETPWVINRDLYNVILEAWANGGNIGDIPKRTDFEYPEISDDMLFDHEARKELYKKEQRIKSLNFNLHSLRCDTNYKLEVARKFLDHTLYFPHNIDFRGRSYPIPPHLNHLGSDFCRSLLKFEKSLPLGEKGLEWLKIHVANLYGVDKIPLNERLAFTERNMENIFDSVDSPLNGNKWWLKADNPWQTLAACMELTKAIRSGKPAEFLSNLPIHQDGTCNGLQHYAALGGDVWGAEKVNLLPSDCPQDVYSSVAQLVEQIVEEDAKNGDEIAQFFLGKVDRKLVKQTVMTSVYGVTYIGAREQIENAILEKFSDLDLDEDFIFKSSTYITKNTFASLNNMFVGARSIMKWMSDCATLIAKSGHCVTWNTPLGLPVVQPYKKGGKYNIRTLECDFIVVHNDDLLQVDSNRQRSAFPPNFIHSLDSTHMFLTAMTCYDQGITYSSVHDSYWTHASTVDRMNDILRNEFVELHKQPILERLLEWFQVRYPDIKFPKLPKKGELDINKVKESRYFFH
Protein: SR-related and CTD-associated factor 8 (RNA-binding motif protein 16) (Q63623)
Organism: Rattus norvegicus (Rat)
Function: Anti-terminator protein required to prevent early mRNA termination during transcription. Together with SCAF4, acts by suppressing the use of early, alternative poly(A) sites, thereby preventing the accumulation of non-functional truncated proteins. Mechanistically, associates with the phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit (POLR2A), and subsequently binds nascent RNA upstream of early polyadenylation sites to prevent premature mRNA transcript cleavage and polyadenylation. Independently of SCAF4, also acts as a positive regulator of transcript elongation.
Subcellular location: Nucleus {ECO:0000269|PubMed:9528809}. Nucleus matrix {ECO:0000269|PubMed:9528809}. Note=Detected in granular nuclear foci which correspond to sites of active transcription. {ECO:0000250|UniProtKB:Q9UPN6}.
Interaction partners:
- Pre-mRNA cleavage complex 2 protein Pcf11
- Probable helicase senataxin
- DNA-directed RNA polymerase subunit
- Transcription initiation factor TFIID subunit 2
- Transmembrane protein 242
- Regulation of nuclear pre-mRNA domain-containing protein
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
- Regulation of nuclear pre-mRNA domain-containing protein
- WD repeat domain 33
- Tubby-related protein 4
Sequence:
MEAVKTFNSELYSLNDYKPPISKAKMTQITKAAIKAIKFYKHVVQSVEKFIQKCKPEYKVPGLYVIDSIVRQSRHQVGQEKDVCAPRFSNNIISTFQNLYRCPGDDKSKIVRVLNLWQKNNVFKSEIIQPLLDMAAGIPPPVVTPVLASTTVAMSNTPGTPVTPVTPANVVQGLPDPWVSQITNTDTLAAVAQILQSPQGQQLQQLIQTLQIQQQKPQPSILQALDAGLVVQLQALTAQLTAAAAAANTLTPLDQGVSFNKKLMDRFDFGEDSEHSEESKKEIPTPQLSHVSESVNNSIFHQIAEQLQQQNLEQLRQQLLEQQQPQKVTPQDSQEGAFGSEHSASPSQGSSQQHFLEPEANLDDSIDIQQQDMDIDEGQDVVEEEIFEPEAKKVAVRSRSRTHSRSRSRSPRKRRSRSRSGSRKRKHRKRSRSRSRERKRKSSRSYSSERRAREREKERQKKGLPPVRSKTLSVCSTTLWVGQVDKKATQQDLTNLFEEFGQIESINMIPPRGCAYVCMVHRQDSFRALQKLSSGSYKIGSKVIKIAWALNKGVKTEYKQFWDVDLGVTYIPWEKVKVDDLDGFAEGGMIDQETVNAEWETVKTSEPVKETVQTTQSPAAVEKETVVTTQSEVFPPPVTMLQIPVAPTVPAVSLVPPAFPVSMPVPPPGFSPIPPPPFLRASFNPSQPPPGFMPPPVPPPVVPPPAIPPVVPTSLVQPPLSMTPETVKDVGFGSLVLPGGSVAGNLAPSTLPAGNVFNPPSKAEPEEKVPHLTEHQIPSGENTRPVIPSDIPSSAPMLAQPPGASNTSGILCVQRPNVSSNSEILGVRPANVSNSAAIMGAQPPNMLNNSGILGIQPPNVSSGSGLLGVLPPNLPNNSGLVGLQPPNVTNPAGLLGTQPPIGPQNLPPLTIPAQRMPALPMLDIRPGLIAQAPGPRFPLLQPGIPPQRGIPPPSVLDAALHPPPRGPFPPGDLFSQPERPFLAPGRPNIDSVPNPDKRIPLGNDNIQQEGDRDYRFPPIETREGINRPPPVDVRDVVGRPIDPREGPGRPPLDGRDHFGRPPVDMRETLVRPGLDHLGRRDHFGFPPEKPWGPRDFDEREHRVLPVFGGPKGLHEERGRFRAGNYRFDPRSGPWNRGFGQEVHRDFDDRRRPWERQRDRDDRDFDFCREINGNRLGRDRIQNTWVPPPHARVFDYFEGATSQRKGENVPQVNGGNTERHAPPPPLPVQKDPELYEKLASSGDADKEESGTAAGVESEAVVESTETEGT
Protein: Flap endonuclease 1 (FEN-1) (EC 3.1.-.-) (Cell death-related nuclease 1) (Flap structure-specific endonuclease 1) (Q9N3T2)
Organism: Caenorhabditis elegans
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA (By similarity). Can associate and cooperate with cps-6 to promote stepwise DNA fragmentation, utilizing the endonuclease activity of cps-6 and both of its own 5'-3' exonuclease activity and gap-dependent endonuclease activity. May play a critical role in switching the state of cells from DNA replication/repair to DNA degradation during apoptosis.
Subcellular location: Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03140}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03140}. Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03140}. Note=Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage. {ECO:0000255|HAMAP-Rule:MF_03140}.
Interaction partners:
- Proliferating cell nuclear antigen
- DNA ligase 1
- DNA replication ATP-dependent helicase/nuclease DNA2
- DNA polymerase delta catalytic subunit
- exodeoxyribonuclease III
- Double-strand break repair protein mre-11
- DNA mismatch repair protein
- Probable DNA polymerase delta small subunit
- DNA replication licensing factor MCM2
- Endonuclease G, mitochondrial
Sequence:
MGIKGLSQVIADNAPSAIKVNEMKAFFGRTVAIDASMCLYQFLIAVRQDGSQLQSEDGETTSHLMGMLNRTVRMFENGVKPVYVFDGKPPDMKGGELEKRSERRAEAEKALTEAKEKGDVKEAEKFERRLVKVTKQQNDEAKRLLGLMGIPVVEAPCEAEAQCAHLVKAGKVFGTVTEDMDALTFGSTVLLRHFLAPVAKKIPIKEFNLSLALEEMKLSVEEFIDLCILLGCDYCGTIRGVGPKKAVELIRQHKNIETILENIDQNKYPPPEDWPYKRARELFLNPEVTKPEEVELTWKEADVEGVIQFLCGEKNFNEERIRNALAKLKTSRKSGTQGRIDSFFGNSTKVTCVTAATKRKAEEAEKAKKGAKKGGPPKKRAK
Protein: Cellular tumor antigen p53 (Tumor suppressor p53) (P10360)
Organism: Gallus gallus (Chicken)
Function: Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MAEEMEPLLEPTEVFMDLWSMLPYSMQQLPLPEDHSNWQELSPLEPSDPPPPPPPPPLPLAAAAPPPLNPPTPPRAAPSPVVPSTEDYGGDFDFRVGFVEAGTAKSVTCTYSPVLNKVYCRLAKPCPVQVRVGVAPPPGSSLRAVAVYKKSEHVAEVVRRCPHHERCGGGTDGLAPAQHLIRVEGNPQARYHDDETTKRHSVVVPYEPPEVGSDCTTVLYNFMCNSSCMGGMNRRPILTILTLEGPGGQLLGRRCFEVRVCACPGRDRKIEEENFRKRGGAGGVAKRAMSPPTEAPEPPKKRVLNPDNEIFYLQVRGRRRYEMLKEINEALQLAEGGSAPRPSKGRRVKVEGPQPSCGKKLLQKGSD
Protein: Poly(rC)-binding protein 3 (Alpha-CP3) (PCBP3-overlapping transcript) (PCBP3-overlapping transcript 1) (P57721)
Organism: Homo sapiens (Human)
Function: Single-stranded nucleic acid binding protein that binds preferentially to oligo dC.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14612387}.
Interaction partners:
Sequence:
MGEGDAFWAPSVLPHSTLSTLSHHPQPQFGRRMESKVSEGGLNVTLTIRLLMHGKEVGSIIGKKGETVKKMREESGARINISEGNCPERIVTITGPTDAIFKAFAMIAYKFEEDIINSMSNSPATSKPPVTLRLVVPASQCGSLIGKGGSKIKEIRESTGAQVQVAGDMLPNSTERAVTISGTPDAIIQCVKQICVVMLESPPKGATIPYRPKPASTPVIFAGGQAYTIQGQYAIPHPDQLTKLHQLAMQQTPFPPLGQTNPAFPGEKLPLHSSEEAQNLMGQSSGLDASPPASTHELTIPNDLIGCIIGRQGTKINEIRQMSGAQIKIANATEGSSERQITITGTPANISLAQYLINARLTSEVTGMGTL
Protein: Sphingosine 1-phosphate receptor 4 (S1P receptor 4) (S1P4) (Endothelial differentiation G-protein coupled receptor 6) (Sphingosine 1-phosphate receptor Edg-6) (S1P receptor Edg-6) (O95977)
Organism: Homo sapiens (Human)
Function: Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. May be involved in cell migration processes that are specific for lymphocytes.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein subunit alpha-12
- Sphingosine 1-phosphate receptor 1
- Guanine nucleotide-binding protein subunit alpha-13
- Sphingosine kinase 2
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-15
- Sphingosine kinase 1
- Guanine nucleotide-binding protein subunit alpha-11
Sequence:
MNATGTPVAPESCQQLAAGGHSRLIVLHYNHSGRLAGRGGPEDGGLGALRGLSVAASCLVVLENLLVLAAITSHMRSRRWVYYCLVNITLSDLLTGAAYLANVLLSGARTFRLAPAQWFLREGLLFTALAASTFSLLFTAGERFATMVRPVAESGATKTSRVYGFIGLCWLLAALLGMLPLLGWNCLCAFDRCSSLLPLYSKRYILFCLVIFAGVLATIMGLYGAIFRLVQASGQKAPRPAARRKARRLLKTVLMILLAFLVCWGPLFGLLLADVFGSNLWAQEYLRGMDWILALAVLNSAVNPIIYSFRSREVCRAVLSFLCCGCLRLGMRGPGDCLARAVEAHSGASTTDSSLRPRDSFRGSRSLSFRMREPLSSISSVRSI
Protein: Protein Wnt-7b (Q3L254)
Organism: Gallus gallus (Chicken)
Function: Ligand for members of the frizzled family of seven transmembrane receptors that functions in the canonical Wnt/beta-catenin signaling pathway (By similarity). Required for normal fusion of the chorion and the allantois during placenta development (By similarity). Required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P56706}. Secreted {ECO:0000250|UniProtKB:P56706}.
Interaction partners:
- Low-density lipoprotein receptor-related protein
- Frizzled-4
- Wnt inhibitory factor 1
- Porcupine O-acyltransferase.
- Frizzled-1
- Notum, palmitoleoyl-protein carboxylesterase.
- Cerberus
- Frizzled-3
- Frizzled-2
- Frizzled-6
Sequence:
MHRNFRKWIFYVFLCFGVIYVKLGALSSVVALGANIICNKIPGLAPRQRAICQSRPDAIIVIGEGAQMGINECQYQFRYGRWNCSALGEKTVFGQELRVGSREAAFTYAITAAGVAHAVTAACSQGNLSNCGCDREKQGYYNQEEGWKWGGCSADIRYGIEFSRRFVDAREIKKNARRLMNLHNNEAGRKVLEERMKLECKCHGVSGSCTTKTCWTTLPKFREIGYILKEKYNAAVQVEVVRASRLRQPTFLKIKQIKSYQKPMETDLVYIEKSPNYCEEDASTGSVGTQGRLCNRTSPNADGCDMMCCGRGYNTHQYTKVWQCNCKFHWCCFVKCNTCSERTEVFTCK