wanglab/gogpt-training-data huggingface dataset:
Protein: Nucleoprotein (Nucleocapsid protein) (Protein N) (P03466)
Organism: Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)
Function: Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the host nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals that are responsible for the active RNP import into the nucleus through cellular importin alpha/beta pathway. Later in the infection, nclear export of RNPs are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that nucleoprotein binds directly host exportin-1/XPO1 and plays an active role in RNPs nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmasks nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04070}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04070, ECO:0000269|PubMed:9770415, ECO:0000269|PubMed:9971805}.
Interaction partners:
Sequence:
MASQGTKRSYEQMETDGERQNATEIRASVGKMIGGIGRFYIQMCTELKLSDYEGRLIQNSLTIERMVLSAFDERRNKYLEEHPSAGKDPKKTGGPIYRRVNGKWMRELILYDKEEIRRIWRQANNGDDATAGLTHMMIWHSNLNDATYQRTRALVRTGMDPRMCSLMQGSTLPRRSGAAGAAVKGVGTMVMELVRMIKRGINDRNFWRGENGRKTRIAYERMCNILKGKFQTAAQKAMMDQVRESRNPGNAEFEDLTFLARSALILRGSVAHKSCLPACVYGPAVASGYDFEREGYSLVGIDPFRLLQNSQVYSLIRPNENPAHKSQLVWMACHSAAFEDLRVLSFIKGTKVLPRGKLSTRGVQIASNENMETMESSTLELRSRYWAIRTRSGGNTNQQRASAGQISIQPTFSVQRNLPFDRTTIMAAFNGNTEGRTSDMRTEIIRMMESARPEDVSFQGRGVFELSDEKAASPIVPSFDMSNEGSYFFGDNAEEYDN
Protein: DNA replication complex GINS protein PSF3 (Partner of Sld five 3) (Q12146)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as part of the GINS complex which plays an essential role in the initiation of DNA replication by binding to DNA replication origins and facilitating the assembly of the DNA replication machinery.
Subcellular location: Nucleus {ECO:0000269|PubMed:12730134}.
Interaction partners:
- DNA replication licensing factor MCM2
- DNA replication complex GINS protein PSF1
- DNA polymerase epsilon subunit B
- DNA replication complex GINS protein SLD5
- Minichromosome maintenance protein 5
- Topoisomerase 1-associated factor 1
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM7
- DNA replication licensing factor MCM6
- DNA replication complex GINS protein PSF2
Sequence:
MGYYDIDDVLADGTEFPCKFQYDIPGLGYLENNPGRPITKNTKLSLPLWLARILAIVGGDEALVDEEPVPFVELLPPDMFSTKVMNAIKTDPVALDLHSINSHFFSLAIKWIMLFSEKELANVVSELLLQRAQELNHHASSLSIDLNADSTGKNSANTNIATSTFLLKLEEMEKEIYKKSHESYKDTKRWMFKK
Protein: Uncharacterized protein C577.11 (Q9USQ8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:16823372}. Golgi apparatus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- D-aminoacyl-tRNA deacylase
- Uncharacterized protein C17C9.11c
Sequence:
MQQDLFGSDSICPISSDDVLKATDPNFESWRERIVQDALKIVEQIPKWKHLGNHDGVALYEKAPAYTGHTWYGRVSKHTRSLKTFKKGLLYEHIKKEADYDPLVFSAHQLETIIEDEIEIWMYKYKTPWFFRNRVYRQLVVSVMLDPDSFIVLQTPVTYPGSSSGGGNGVVALYDSVDFVSKKLDGDGKEEGVLWICAVRNDYGSMFSGLFSDTTFTKSLVRQVKLYNEWLNRTYPRKG
Protein: Putative cystathionine beta-lyase (CBL) (EC 4.4.1.13) (Beta-cystathionase) (Cysteine lyase) (Cysteine-S-conjugate beta-lyase) (P9WQ83)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Cystathionine gamma-synthase
- O-succinylhomoserine sulfhydrylase
- cysteine-S-conjugate beta-lyase
- Probable O-acetylhomoserine sulfhydrylase MetC
- Methionine synthase
- Probable cystathionine beta-synthase Rv1077
- O-acetylserine sulfhydrylase
- L-cysteine desulfhydrase Cds1
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Putative thiosulfate sulfurtransferase SseB
Sequence:
MIPNPLEELTLEQLRSQRTSMKWRAHPADVLPLWVAEMDVKLPPTVADALRRAIDDGDTGYPYGTEYAEAVREFACQRWQWHDLEVSRTAIVPDVMLGIVEVLRLITDRGDPVIVNSPVYAPFYAFVSHDGRRVIPAPLRGDGRIDLDALQEAFSSARASSGSSGNVAYLLCNPHNPTGSVHTADELRGIAERAQRFGVRVVSDEIHAPLIPSGARFTPYLSVPGAENAFALMSASKAWNLGGLKAALAIAGREAAADLARMPEEVGHGPSHLGVIAHTAAFRTGGNWLDALLRGLDHNRTLLGALVDEHLPGVQYRWPQGTYLAWLDCRELGFDDAASDEMTEGLAVVSDLSGPARWFLDHARVALSSGHVFGIGGAGHVRINFATSRAILIEAVSRMSRSLLERR
Protein: CED-5 (Dedicator of cytokinesis protein 1) (G5EEN3)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Cell death abnormality protein 12
- Cell death abnormality protein 2
- Ras-related protein ced-10
- Cell death protein 6
- ABC transporter ced-7
- Cell death abnormality protein 1
- CRAL-TRIO domain-containing protein
- Rac-like GTPase
- Bifunctional arginine demethylase and lysyl-hydroxylase psr-1
- Cell division control protein 42 homolog
Sequence:
MATTGFYYAIVQYTFEDPLPSCDAPRLELFIGDRICVYGQHGEWGYGRKFDEKNGKCGIFPLAYVQIVQKSMFVSTSDGYLVVDEISRVINEWWTKIKELMVETTRIGSFEDLMDSFNELLIIKTKIESGGIPIEELSKLRLRVSKLVDRGNTILGQDVVIRNEEGVPLDVESLSLLRTYEAHISSKGRVGSLMREKPENVTINDSFSLLLSIKSVELHCKYSCEISISLYDLDKKMFTTDSYTFLWNSGSGKHTDLNLKALFTDFAKEDIQKKYLMVTRVVHVSPIESSNATMRKHGHHEATIPKTFYCRQSYASDIMEMSSIFLAGVGHEAKERVIFLNREPELPLSLKAYHATNRIPKNLSNDMETKLLISTQLVPGNVSQIKARHPHLFSRCPAAILRRADRTAVSIEDSRNEMYITLMQAELSGKSSDRNIEARLHVVESNGHVMENVFETISVTGSQLSTVYKSIVVYHTDKPMWTEPIKIALPSCASHDVYLRILFYSKKAYDKPKPEKGPFAIAHVQLIRSSALLCDGEHDLAVYKIDNPGSHFDESNVHYMNLPDTRRTLKESIGSAKPHSQGFSLSDKSFVMISTHSCSSMLTQNEHLLNVLRWRVNCVNLTSSLVALAQPIGDTEHEMIRFFSHLLDALFEIWHDRETSEKVVFDVIVAVLRICEEPRHYPQAAKIFEVYLKRFSFTSAALKILKCLNHYVISDSEDSNEKARNAFKVMGPLFKLVVVSKKCGIKFEEFDDFEKTYKQYLREFMKSLVALMSEKKAKMTVQNTALKSIPTIIDLLNESDSVSPENLCGFIVDLMNNFGSNIVTRERLNFIAQIVETRFFSLSICREQLLIPCLQIALDIIQIDNMATEKGEFADRAAECASIIAAILERLFADAKSGEGNAERELTSFILMVYRPLVQAMIRVIHDDKHTDDDARGHFFSVILALLDKMSAQMFSEYVEERSSDIDKRDFLMEMVQMIRDLLNRNAFPSTWKDMIMLQNKVIHKSLRFVMSAVQTFFSNDKFCVEMWREYMVTVVSFVTQEGLNSKHEWMKNEDEDMRIQLRKAAAKDLRSMWFRLTPSQKLNYIPSMIGSFLKVSLVDDDETREATIPIFFDMMQTEYNTSASRSFTEFASELVSQLDTNVDQHSATKGFKEHFRQLSITLCQSDKELMANGGEELIERIDRLLTALIEYHEVASKSLVECVDSLMSRTVQLMRYYNQYSHKELYVKYIYKLYDLHTSYGNKIEAAKTLLRHATMLTFDDDALPQWLIARSLNRHRELHRQLKEDLMEEAGNLFSKGEDWEDALIVYNQLVPVYQNIIMDYDKLAGLLQKIAQLYTSISRTERAYFYYYLVAFYGQGFPAYLNGHKFVFRSEKLEMHGEFMQRIMKMYDNPEKIMKTDPCPHLVDSPGRYIQVFNIDPIGTGCSFENNPEVKPVIKKYFRYYNIQTFEYSKVEERKDTKWTSIDPSSEFMRNWLVRRRIKTADSLPTDLRFTEIVELSDPIYVTPLQNAVEQMRKKNKELNETAASAESNPNFDLKLLSRDILGVVSAAVMGGVKNYEVFFTEACRNICECGEQSVIMELSSLIIEQVEILEYCCYVHASRCQGEARAINTMLADSFDSHRRYVEENFGKTRSRLPTHANIRLSSFDSDSINDGMMTMKSGKAAVLGNAVANLIYSNKRSSGPGTPVNLSSRSAPSFDNISSKLRSSLAISKLAPPPRPPNPISPINRGPSSNYEGIRMRAHSHQASTVSLNHMSVAPPLPPRPDRPDMDPNRTLKRKN
Protein: Olfactory receptor 5H1 (HTPCRX14) (A6NKK0)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MEEENATLLTEFVLTGFLYQPQWKIPLFLAFLVIYLITIMGNLGLIAVIWKDPHLHIPMYLLLGNLAFVDAWISSTVTPKMLNNFLAKSKMISLSECKIQFFSFAISVTTECFLLATMAYDRYVAICKPLLYPAIMTNGLCIRLLILSYVGGILHALIHEGFLFRLTFCNSNIVHHIYCDTIPLSKISCTDSSINFLMVFIFSGSIQVFSIVTILVSYTFVLFAILKKKSDKGVRKAFSTCGAHLFSVSLYYGPLLFIYVGPASPQADDQDMVEPLFYTVIIPLLNPIIYSLRNKQVTVSFTKMLKKHVKVSY
Protein: Putrescine hydroxycinnamoyltransferase 1 (OsPHT1) (EC 2.3.1.-) (BAHD-like hydroxycinnamoyl transferase HCT3) (Hydroxycinnamoyltransferase 3) (OsHCT3) (Q5SMM8)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Hydroxycinnamoyl transferase that catalyzes the transfer of an acyl from p-coumaryol-CoA to putrescine, to produce coumaroyl putrescine.
Interaction partners:
- 4-coumarate--CoA ligase 2
- Hydrolase, alpha/beta fold family protein, putative, expressed
- 4-coumarate--CoA ligase-like 9
- beta-ketoacyl-[acyl-carrier-protein] synthase III
- Os12g0262700 protein
- Nitrate reductase
- Nitrate reductase
- Nitrate reductase 1
- Os01g0315700 protein
- Probable 5'-adenylylsulfate reductase 1, chloroplastic
Sequence:
MAVEIVKSSMVTAGEATPEHRIWLSNLDLLVARSHTPTVYVYRRTGPDSDAAFFSPDVLKAALSKVLVPFYPLAGRLAQDSAGRPEISCTGEGVLFVTARSGATIDDLGDLAPSDELRRMLVPAADVAAASILAMFQVTFFRCGGVCLGAAIHHTAADGLAALDFVNTWAAIARDVAGDGEAAAAAVQRPWLDRTLLRARSPPAVRFDHAEYSRRRGGGSKLPFDSAILPMSKNQLNALKGAGAGAGKRLSTFTAVVAHVWRCACKARGLAVAGTEAATRLYMTADARTRLHPPLPRGYLGNAIFRASAVSKVSDIVAAGPLGAVAEKVSAATARLDDGYVRSLLDHLEQTAAAASGGAAGLRKGEWVMPESDLWVISWQGLPLYDADFGWGRPAFMGRACLQFSGLVYLVPGRDDGDGRLDVVVAMDPESLAKFKDVFYEELKC
Protein: Amylo-1,6-glucosidase, 4-alpha-glucanotransferase (F7CSZ6)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
XAMSAYNSHEEGRLVYRYGGEPVGSFVQPCLRPLMPAIAHALFMDITHDNECPIVHRSAYDALPSTTVVSMACCASGSTRGYDELVPHQISVVAEERFYTKWNPGASPADTGDVNVHSGIIAARCAINRLHQELGAKGFIQVYVDQVDEDIVAVTRHSPSIHQSVVAVSRTAFRNPKTSFYSKEVPQMCIPGNLRPHQ
Protein: Ubiquitin-like modifier-activating enzyme 5 (Ubiquitin-activating enzyme 5) (ThiFP1) (UFM1-activating enzyme) (Ubiquitin-activating enzyme E1 domain-containing protein 1) (Q9GZZ9)
Organism: Homo sapiens (Human)
Function: E1-like enzyme which specifically catalyzes the first step in ufmylation. Activates UFM1 by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a UFM1-E1 thioester and free AMP. Activates UFM1 via a trans-binding mechanism, in which UFM1 interacts with distinct sites in both subunits of the UBA5 homodimer. Trans-binding also promotes stabilization of the UBA5 homodimer, and enhances ATP-binding. Transfer of UFM1 from UBA5 to the E2-like enzyme UFC1 also takes place using a trans mechanism. Ufmylation is involved in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress. Ufmylation is essential for erythroid differentiation of both megakaryocytes and erythrocytes (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18442052, ECO:0000269|PubMed:26872069}. Nucleus {ECO:0000269|PubMed:18442052}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:30990354}. Golgi apparatus {ECO:0000269|PubMed:26872069}. Note=Localizes mainly in the cytoplasm, while it localizes to the nucleus in presence of SUMO2 (PubMed:18442052). Interaction with GABARAPL2 promotes localization to the endoplasmic reticulum membrane (PubMed:30990354). {ECO:0000269|PubMed:18442052, ECO:0000269|PubMed:30990354}.
Interaction partners:
- Ubiquitin-fold modifier 1
- Ubiquitin-fold modifier-conjugating enzyme 1
- Gamma-aminobutyric acid receptor-associated protein-like 2
- E3 UFM1-protein ligase 1
- NEDD8-conjugating enzyme Ubc12
- Ufm1-specific protease 2
- NEDD8-activating enzyme E1 catalytic subunit
- DDRGK domain-containing protein 1
- Ufm1-specific protease 1
- Protein boule-like
Sequence:
MAESVERLQQRVQELERELAQERSLQVPRSGDGGGGRVRIEKMSSEVVDSNPYSRLMALKRMGIVSDYEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITTVENFQHFMDRISNGGLEEGKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSENAVSGHIQLIIPGESACFACAPPLVVAANIDEKTLKREGVCAASLPTTMGVVAGILVQNVLKFLLNFGTVSFYLGYNAMQDFFPTMSMKPNPQCDDRNCRKQQEEYKKKVAALPKQEVIQEEEEIIHEDNEWGIELVSEVSEEELKNFSGPVPDLPEGITVAYTIPKKQEDSVTELTVEDSGESLEDLMAKMKNM
Protein: Myeloid/lymphoid or mixed-lineage leukemia translocated to 3 isoform 1 (A0A0S2Z448)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00376}.
Interaction partners:
Sequence:
MASSCAVQVKLELGHRAQVRKKPTVEGFTHDWMVFVRGPEHSNIQHFVEKVVFHLHESFPRPKRVCKDPPYKVEESGYAGFILPIEVYFKNKEEPRKVRFDYDLFLHLEGHPPVNHLRCEKLTFNNPTEDFRRKLLKAGGDPNRSIHTSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSTSFSKPHKLMKEHKEKPSKDSREHKSAFKEPSRDHNKSSKESSKKPKENKPLKEEKIVPKMAFKEPKPMSKEPKPDSNLLTITSGQDKKAPSKRPPISDSEELSAKKRKKSSSEALFKSFSSAPPLILTCSADKKQIKDKSHVKMGKVKIESETSEKKKSTLPPFDDIVDPNDSDVEENISSKSDSEQPSPASSSSSSSSSFTPSQTRQQGPLRSIMKDLHSDDNEEESDEVEDNDNDSEMERPVNRGGSRSRRVSLSDGSDSESSSASSPLHHEPPPPLLKTNNNQILEVKSPIKQSKSDKQIKNGECDKAYLDELVELHRRLMTLRERHILQQIVNLIEETGHFHITNTTFDFDLCSLDKTTVRKLQSYLETSGTS
Protein: Probable E3 ubiquitin-protein ligase LUL1 (EC 2.3.2.27) (Probable RING-type E3 ubiquitin transferase LUL1) (Protein LOG2-LIKE UBIQUITIN LIGASE 1) (RING finger protein 370) (Q9LYW5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates (in vitro).
Interaction partners:
- Protein GLUTAMINE DUMPER 1
- Zinc finger CCCH domain-containing protein 34
- Small ribosomal subunit protein mS81
- Protein GLUTAMINE DUMPER 2
- SAUR-like auxin-responsive protein family
- C3HC4-type RING finger protein
- C3HC4-type RING finger protein
- Protein DA1-related 2
- Protein SMALL AUXIN UP-REGULATED RNA 51
- DNA-binding protein BIN4
Sequence:
MGNLISLIFCCGRRQRSNIPPAMETAPLELPPNRFVFAAVPPYLNPNPNYVDQYPGNCLPPPVTEPPMLPYNFNHLHHYPPNSYQLPHPLFHGGRYPILPPPTYVHQKAVTIRNDVNLKKKTLTLIPDPENPNRLLVSFTFDASMPGRITVVFFATEDAECNLRATKEDTLPPITFDFGEGLGQKFIQSSGTGIDLTAFKDSELFKEVDTDVFPLAVKAEATPAEEGKSGSTNVQITQVVYTKEKGEIKIEVVKQILWVNKRRYELLEIYGIENTVDGSDEGKECVVCLSEPRDTTVLPCRHMCMCSGCAKALRFQTNLCPVCRQPVEMLLEINKNG
Protein: High-affinity branched-chain amino acid transport system permease protein LivH (LIV-I protein H) (P0AEX7)
Organism: Escherichia coli (strain K12)
Function: Part of the binding-protein-dependent transport system for branched-chain amino acids. Probably responsible for the translocation of the substrates across the membrane.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Leucine-specific-binding protein
- High-affinity branched-chain amino acid transport system permease protein LivM
- High-affinity branched-chain amino acid transport ATP-binding protein LivG
- Leu/Ile/Val-binding protein
- High-affinity branched-chain amino acid transport ATP-binding protein LivF
- Histidine/lysine/arginine/ornithine transport ATP-binding protein HisP
- sn-glycerol-3-phosphate transport system permease protein UgpA
- sn-glycerol-3-phosphate-binding periplasmic protein UgpB
Sequence:
MSEQFLYFLQQMFNGVTLGSTYALIAIGYTMVYGIIGMINFAHGEVYMIGSYVSFMIIAALMMMGIDTGWLLVAAGFVGAIVIASAYGWSIERVAYRPVRNSKRLIALISAIGMSIFLQNYVSLTEGSRDVALPSLFNGQWVVGHSENFSASITTMQAVIWIVTFLAMLALTIFIRYSRMGRACRACAEDLKMASLLGINTDRVIALTFVIGAAMAAVAGVLLGQFYGVINPYIGFMAGMKAFTAAVLGGIGSIPGAMIGGLILGIAEALSSAYLSTEYKDVVSFALLILVLLVMPTGILGRPEVEKV
Protein: Membrane-anchored protein 1 (Q10268)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for correct cell separation at high temperatures.
Subcellular location: Cell membrane; Multi-pass membrane protein. Cell tip.
Interaction partners:
- Metal-binding regulatory protein cuf1
- Copper transport protein ctr4
- Uncharacterized protein C140.04
- Uncharacterized protein C2D10.19c
- Metal homeostasis factor atx1
Sequence:
MIRNTLAFLAILFLLIPTALLIIGSVSVPSTRMTLAKVEGTEFGIFGTCTGNGTDCTETSFGYNASSSLIDDFYYKGDKRLVLSKVLITHIISAFLSFLSAIFVFFSIFLVNQAVNIINIIVVFITTLLTCLAFAIELVLFLPHNTWQSYVTAGAIGSDLIAILALCLRSVSISRIGQKSARLEHVDTMNSSYSSYKTDVKYPLALDDKLSSVPTLPKFHDALTSTSEFGPPSDSGDTVGTTQYPGDIKYATGYESTVASPVPSRVAKLSSRDTPSIIADYDEFRKSESSPSRSSVLSTSKPEVHETEGYCPHKTGNRPGFPSLNIPRTRPTTAGIANTQFDLEPYRNRQAGSISSEGTDSRFFDVENQVSVAQTPSVKPEMFPKTARPFAAIHANASSTQLRNTENITHPGIPNHFAKTTSSVFDEPPATRMPQTRSPVNDHSSFPSDLPIKGEMSTNMTGAPRVGSRNNSSNDLHAQAGMLKNVGNGPRNAPRNNSSNNLHAQGGMPMNMRGPRGAPRNNSSGDLHIQSGMPMNGRNGPRDTSRNNSSSDLYAQSGMHPNMNNGHRGAPRNNSSNDLHAHGGMPVNMRGPRNTSRNNSSSEFNAQIPMNLRNGPRNASRSNSSTDLFGQSGIPGNSRGMPTSPNSRNNSALDLSMHGIPLANNSRQFKRPSYGNMSRPSFELNGSRNPSHGSLNTAHAGMGYGPRSMMRDPQNLSNVPPVSNTLDQLSGNADFELPVRGNRNNRRGPGGNRMIR
Protein: Polyadenylate-binding protein 1-like 2 (RNA-binding motif protein 32) (RNA-binding protein 32) (Q5JQF8)
Organism: Homo sapiens (Human)
Interaction partners:
- Polyadenylate-binding protein-interacting protein 1
- Polyadenylate-binding protein 2
- Eukaryotic translation initiation factor 4 gamma 1
- Eukaryotic translation initiation factor 4E
- Eukaryotic initiation factor 4A-II
- Eukaryotic initiation factor 4A-I
Sequence:
MASLYVGDLHPEVTEAMLYEKFSPAGPILSIRICRDKITRRSLGYAYVNYQQPVDAKRALETLNFDVIKGRPVRIMWSQRDPSLRKSGVGNVFIKNLGKTIDNKALYNIFSAFGNILSCKVACDEKGPKGYGFVHFQKQESAERAIDVMNGMFLNYRKIFVGRFKSHKEREAERGAWARQSTSADVKDFEEDTDEEATLR
Protein: Alkaline/neutral invertase CINV2 (EC 3.2.1.26) (Alkaline/neutral invertase I) (A/N-INVI) (Cytosolic invertase 2) (Q67XD9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cytosolic invertase that may cleave sucrose into glucose and fructose, and that is involved in the regulation of root growth. May regulate sugar-mediated root development by controlling sucrose catabolism in root cells.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9LQF2}.
Interaction partners:
- Sucrose synthase 4
- AT1G06500 protein
- Sucrose synthase 3
- Beta-fructofuranosidase, insoluble isoenzyme CWINV1
- TCP-1/cpn60 chaperonin family protein
- Probable pectinesterase 66
- At5g49410
- Sucrose synthase 1
- Sucrose synthase 6
- Beta-fructofuranosidase, insoluble isoenzyme CWINV3
Sequence:
MEEGHKEPLVLRVEGSHCSLSEMDDFDLTRALEKPRQLKIERKRSFDERSMSELSTGYVRQDSILEMAHSPGSRSMVDTPLSVRNSFEPHPMVAEAWEALRRSMVFFRGQPVGTIAAYDHASEEVLNYDQVFVRDFVPSALAFLMNGEPDIVKNFLLKTLQLQGWEKRVDRFKLGEGVMPASFKVLHDPVRKTDTIIADFGESAIGRVAPVDSGFWWIILLRAYTKSTGDLTLSETPECQRGMRLILSLCLSEGFDTFPTLLCADGCSMVDRRMGVYGYPIEIQALFFMALRCALSMLKPDEEGRDFIERIVKRLHALSFHMRSYFWLDFQQLNDIYRYKTEEYSHTAVNKFNVMPDSIPDWVFDFMPLRGGYFVGNVSPARMDFRWFSLGNCVSILSSLATPDQSMAIMDLLEHRWEELVGEMPLKICYPCIESHEWRIVTGCDPKNTRWSYHNGGSWPVLLWTLTAACIKTGRPQIARRAIDLIESRLHRDCWPEYYDGKQGRYVGKQARKYQTWSIAGYLVAKMMLEDPSHIGMISLEEDKQMKPVIKRSASWTC
Protein: P-selectin (CD62 antigen-like family member P) (Granule membrane protein 140) (GMP-140) (Leukocyte-endothelial cell adhesion molecule 3) (LECAM3) (Platelet activation dependent granule-external membrane protein) (PADGEM) (CD antigen CD62P) (P16109)
Organism: Homo sapiens (Human)
Function: Ca(2+)-dependent receptor for myeloid cells that binds to carbohydrates on neutrophils and monocytes. Mediates the interaction of activated endothelial cells or platelets with leukocytes. The ligand recognized is sialyl-Lewis X. Mediates rapid rolling of leukocyte rolling over vascular surfaces during the initial steps in inflammation through interaction with SELPLG.
Subcellular location: Cell membrane {ECO:0000269|PubMed:28011641}; Single-pass type I membrane protein {ECO:0000305|PubMed:28011641}.
Interaction partners:
- von Willebrand factor
- Platelet glycoprotein Ib alpha chain
- P-selectin glycoprotein ligand 1
- Sorting nexin-17
- Signal transducer CD24
- CD44 antigen
- Complement C3
- L-selectin
- Tumor necrosis factor receptor superfamily member 5
- Golgi apparatus protein 1
Sequence:
MANCQIAILYQRFQRVVFGISQLLCFSALISELTNQKEVAAWTYHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYLNKVLPYYSSYYWIGIRKNNKTWTWVGTKKALTNEAENWADNEPNNKRNNEDCVEIYIKSPSAPGKWNDEHCLKKKHALCYTASCQDMSCSKQGECLETIGNYTCSCYPGFYGPECEYVRECGELELPQHVLMNCSHPLGNFSFNSQCSFHCTDGYQVNGPSKLECLASGIWTNKPPQCLAAQCPPLKIPERGNMTCLHSAKAFQHQSSCSFSCEEGFALVGPEVVQCTASGVWTAPAPVCKAVQCQHLEAPSEGTMDCVHPLTAFAYGSSCKFECQPGYRVRGLDMLRCIDSGHWSAPLPTCEAISCEPLESPVHGSMDCSPSLRAFQYDTNCSFRCAEGFMLRGADIVRCDNLGQWTAPAPVCQALQCQDLPVPNEARVNCSHPFGAFRYQSVCSFTCNEGLLLVGASVLQCLATGNWNSVPPECQAIPCTPLLSPQNGTMTCVQPLGSSSYKSTCQFICDEGYSLSGPERLDCTRSGRWTDSPPMCEAIKCPELFAPEQGSLDCSDTRGEFNVGSTCHFSCDNGFKLEGPNNVECTTSGRWSATPPTCKGIASLPTPGVQCPALTTPGQGTMYCRHHPGTFGFNTTCYFGCNAGFTLIGDSTLSCRPSGQWTAVTPACRAVKCSELHVNKPIAMNCSNLWGNFSYGSICSFHCLEGQLLNGSAQTACQENGHWSTTVPTCQAGPLTIQEALTYFGGAVASTIGLIMGGTLLALLRKRFRQKDDGKCPLNPHSHLGTYGVFTNAAFDPSP
Protein: H2-M beta chain (Q31101)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
GGFVAHVESTCVLNDAGTPQDFTYCVSFNKDLLACWDPDVGKIVPCEFGVLSRLAEIISNILNEQESLIQRLQNGLQDCATHTQPFWDVLTHRTRPPSVRVAQTAPFNTREPVMLACYVWSFYPADVTITWMKNGQLVPSHSNKEKTAQPNGDWTYQTVSYLALTPSYGDVYTCVVQHSGTSEPIRGDW
Protein: Probable methylcrotonoyl-CoA carboxylase beta chain, mitochondrial (MCCase subunit beta) (EC 6.4.1.4) (3-methylcrotonyl-CoA carboxylase 2) (3-methylcrotonyl-CoA carboxylase non-biotin-containing subunit) (3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta) (P34385)
Organism: Caenorhabditis elegans
Function: Carboxyltransferase subunit of the 3-methylcrotonyl-CoA carboxylase, an enzyme that catalyzes the conversion of 3-methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for leucine and isovaleric acid catabolism.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q9HCC0}.
Interaction partners:
- Methylcrotonoyl-CoA carboxylase subunit alpha
- Propionyl-CoA carboxylase alpha chain, mitochondrial
- Isovaleryl-CoA dehydrogenase, mitochondrial
- Pyruvate carboxylase 1
- Enoyl-CoA hydratase
- Probable enoyl-CoA hydratase, mitochondrial
- Probable enoyl-CoA hydratase, mitochondrial
- Probable medium-chain specific acyl-CoA dehydrogenase 10, mitochondrial
- medium-chain acyl-CoA dehydrogenase
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MFRHVAQNLGSRNTSIQSYRLLRTRWERGYLKDLYHRRQILGADPAISRSSYPNCSVQVRNHHCSADKSTLQWAPIKTSIDNSSDDFAANTAEMKVLVEDLKAKISKIEQAGGEKAVKLHRSRGKMLARERIDGIVDAGSPFIEFSQLAGYEMYGKEEVPSGGILTGVGIVSGRVCVIVANDATVKGGTYYPITVKKHLRAQEIARENKLPCIYLVDSGGANLPRQADIFADSQHFGRIFYNQATMSSEGIPQLAVVMGSCTAGGAYVPAMSDQAIIVKGTGTVFLGGPPLVKAATGEEISAEELGGADLHCGESGVTDYYAHNDKHALYLARSCIAGLPPVEEHMTFNPNADEPLYPAEEIYGIVGSNLKKTYDVREVIARIVDGSRFHEFKERYGETLVTGFATIYGQRVGILANNGVLFAESAMKGSHFIELCCQRKIPLLFLQNITGFMVGRDAEAGGIAKHGAKLVTAVACAKVPKITVLVGGSYGAGNYGMCGRGYSPRYVFMWPNSRISVMGGEQAANVLSTVQKEKKKREGADWTDQQDLELRKPVEEKFEKEGHPYFASARLWDDGVIDPKDTRKVLGLAFQSTLQKPIPETKFGVFRM
Protein: Solute carrier family 22 member 3 (Extraneuronal monoamine transporter) (EMT) (Organic cation transporter 3) (OCT3) (O88446)
Organism: Rattus norvegicus (Rat)
Function: Mediates potential-dependent transport of a variety of organic cations. May play a significant role in the disposition of cationic neurotoxins and neurotransmitters in the brain. Mediates the transport of polyamine spermidine and might be involved in its disposition. Transports dopaminergic neuromodulators cyclo(his-pro) and salsolinol with lower efficency (By similarity). May contribute to the transport of cationic compounds in testis across the blood-testis-barrier (Probable).
Subcellular location: Cell membrane {ECO:0000269|PubMed:27659446}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:15817714}; Multi-pass membrane protein {ECO:0000305}. Basolateral cell membrane {ECO:0000250|UniProtKB:O75751}; Multi-pass membrane protein {ECO:0000305}. Mitochondrion membrane {ECO:0000269|PubMed:27659446}. Endomembrane system {ECO:0000269|PubMed:27659446}. Nucleus membrane {ECO:0000305|PubMed:27659446}. Nucleus outer membrane {ECO:0000305|PubMed:27659446}. Note=Localized to neuronal and glial plasma membranes (PubMed:27659446). Localized to the luminal/apical membrane of ciliated and brush epithelial cells in the airway (PubMed:15817714). Located to neuronal and glial endomembranes, including mitochondrial and nuclear membranes (PubMed:27659446). {ECO:0000269|PubMed:15817714, ECO:0000269|PubMed:27659446}.
Interaction partners:
- Choline transporter-like protein 4
- Choline transporter-like protein 1
- Choline transporter-like protein 2
- Choline transporter-like protein 3
- High affinity choline transporter 1
- Solute carrier family 22 member 2
- Choline transporter-like protein
- Solute carrier family 22 member 1
- Multidrug and toxin extrusion protein 1
- Cation-independent mannose-6-phosphate receptor
Sequence:
MPTFDQALRKAGEFGRFQRRVFLLLCLTGVTFAFLFVGVVFLGSQPDYYWCRGPRATALAERCAWSPEEEWNLTTPELHVPAERRGQGHCHRYLLEDTNTSSELSCDPLAAFPNRSAPLVPCSGDWRYVETHSTIVSQFDLVCGNAWMLDLTQAILNLGFLAGAFTLGYAADRYGRLIVYLISCFGVGITGVVVAFAPNFSVFVIFRFLQGVFGKGAWMTCFVIVTEIVGSKQRRIVGIVIQMFFTLGIIILPGIAYFTPSWQGIQLAISLPSFLFLLYYWVVPESPRWLITRKQGEKALQILRRVAKCNGKHLSSNYSEITVTDEEVSNPSCLDLVRTPQMRKCTLILMFAWFTSAVVYQGLVMRLGLIGGNLYMDFFISGLVELPGALLILLTIERLGRRLPFAASNIVAGVSCLVTAFLPEGIPWLRTTVATLGRLGITMAFEIVYLVNSELYPTTLRNFGVSLCSGLCDFGGIIAPFLLFRLAAIWLELPLIIFGILASVCGGLVMLLPETKGIALPETVEDVEKLGSSQLHQCGRKKKTQVSTSNV