wanglab/gogpt-training-data huggingface dataset:
Protein: UDP-glucose 4-epimerase 2 (AtUGE2) (EC 5.1.3.2) (UDP-galactose 4-epimerase 2) (Q9T0A7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the interconversion between UDP-glucose and UDP-galactose. Cooperates with UGE3 in pollen development and with UGE4 in cell wall carbohydrate biosynthesis and growth.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16644739}.
Interaction partners:
- ADP-glucose phosphorylase
- UDP-sugar pyrophosphorylase
- UTP--glucose-1-phosphate uridylyltransferase 1
- UTP--glucose-1-phosphate uridylyltransferase 2
- Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM1
- Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM3
- Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM2
- UDP-sulfoquinovose synthase, chloroplastic
- Putative UDP-glucose 6-dehydrogenase
- Galactinol synthase 10
Sequence:
MAKSVLVTGGAGYIGSHTVLQLLEGGYSAVVVDNYDNSSAASLQRVKKLAGENGNRLSFHQVDLRDRPALEKIFSETKFDAVIHFAGLKAVGESVEKPLLYYNNNIVGTVTLLEVMAQYGCKNLVFSSSATVYGWPKEVPCTEESPISATNPYGRTKLFIEEICRDVHRSDSEWKIILLRYFNPVGAHPSGYIGEDPLGVPNNLMPYVQQVAVGRRPHLTVFGTDYKTKDGTGVRDYIHVMDLADGHIAALRKLDDLKISCEVYNLGTGNGTSVLEMVAAFEKASGKKIPLVMAGRRPGDAEVVYASTEKAERELNWKAKNGIEEMCRDLWNWASNNPYGYNSSSNGSSS
Protein: Tubulin gamma-1 chain (Gamma-1-tubulin) (Gamma-tubulin complex component 1) (GCP-1) (P23258)
Organism: Homo sapiens (Human)
Function: Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome. Pericentriolar matrix component that regulates alpha/beta chain minus-end nucleation, centrosome duplication and spindle formation.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:24107630, ECO:0000269|PubMed:35849559, ECO:0000269|PubMed:9566967, ECO:0000269|PubMed:9566969}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:30723163}. Note=Localizes to mitotic spindle microtubules. {ECO:0000269|PubMed:30723163}.
Interaction partners:
- Gamma-tubulin complex component 6
- Gamma-tubulin complex component 5
- Gamma-tubulin complex component 4
- Gamma-tubulin complex component 3
- Gamma-tubulin complex component 2
- Mitotic-spindle organizing protein 1
- Mitotic spindle organizing protein 2B
- Protein NEDD1
- Tubulin gamma-2 chain
- Centrosomal P4.1-associated protein
Sequence:
MPREIITLQLGQCGNQIGFEFWKQLCAEHGISPEGIVEEFATEGTDRKDVFFYQADDEHYIPRAVLLDLEPRVIHSILNSPYAKLYNPENIYLSEHGGGAGNNWASGFSQGEKIHEDIFDIIDREADGSDSLEGFVLCHSIAGGTGSGLGSYLLERLNDRYPKKLVQTYSVFPNQDEMSDVVVQPYNSLLTLKRLTQNADCVVVLDNTALNRIATDRLHIQNPSFSQINQLVSTIMSASTTTLRYPGYMNNDLIGLIASLIPTPRLHFLMTGYTPLTTDQSVASVRKTTVLDVMRRLLQPKNVMVSTGRDRQTNHCYIAILNIIQGEVDPTQVHKSLQRIRERKLANFIPWGPASIQVALSRKSPYLPSAHRVSGLMMANHTSISSLFERTCRQYDKLRKREAFLEQFRKEDMFKDNFDEMDTSREIVQQLIDEYHAATRPDYISWGTQEQ
Protein: Replication protein E1 (EC 3.6.4.12) (ATP-dependent helicase E1) (P03116)
Organism: Bovine papillomavirus type 1
Function: ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1-E2 complex binds to the replication origin which contains binding sites for both proteins. During the initial step, a dimer of E1 interacts with a dimer of protein E2 leading to a complex that binds the viral origin of replication with high specificity. Then, a second dimer of E1 displaces the E2 dimer in an ATP-dependent manner to form the E1 tetramer. Following this, two E1 monomers are added to each half of the site, which results in the formation of two E1 trimers on the viral ori. Subsequently, two hexamers will be created. The double hexamer acts as a bi-directional helicase machinery and unwinds the viral DNA and then recruits the host DNA polymerase to start replication.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04000, ECO:0000269|PubMed:8382303}.
Interaction partners:
Sequence:
MANDKGSNWDSGLGCSYLLTEAECESDKENEEPGAGVELSVESDRYDSQDEDFVDNASVFQGNHLEVFQALEKKAGEEQILNLKRKVLGSSQNSSGSEASETPVKRRKSGAKRRLFAENEANRVLTPLQVQGEGEGRQELNEEQAISHLHLQLVKSKNATVFKLGLFKSLFLCSFHDITRLFKNDKTTNQQWVLAVFGLAEVFFEASFELLKKQCSFLQMQKRSHEGGTCAVYLICFNTAKSRETVRNLMANTLNVREECLMLQPAKIRGLSAALFWFKSSLSPATLKHGALPEWIRAQTTLNESLQTEKFDFGTMVQWAYDHKYAEESKIAYEYALAAGSDSNARAFLATNSQAKHVKDCATMVRHYLRAETQALSMPAYIKARCKLATGEGSWKSILTFFNYQNIELITFINALKLWLKGIPKKNCLAFIGPPNTGKSMLCNSLIHFLGGSVLSFANHKSHFWLASLADTRAALVDDATHACWRYFDTYLRNALDGYPVSIDRKHKAAVQIKAPPLLVTSNIDVQAEDRYLYLHSRVQTFRFEQPCTDESGEQPFNITDADWKSFFVRLWGRLDLIDEEEDSEEDGDSMRTFTCSARNTNAVD
Protein: 2S seed storage albumin protein (2S albumin) (To-A1) [Cleaved into: 2S albumin small chain; 2S albumin large chain] (P86783)
Organism: Taraxacum officinale (Common dandelion) (Leontodon taraxacum)
Function: This is a 2S seed storage protein. Has antifungal activity. Inhibits spore germination in H.sativum (IC(50)=62.5 ug/ml) and P.betae (IC(50)=62.5 ug/ml). Inhibits growth of H.sativum, V.albo-atrum and P.infestans.
Interaction partners:
Sequence:
PVSRQQCSQRIQGERFNQCRSQMQDGQLQSCCQELQNVEEQCQC
Protein: Leucine-rich repeat protein (LRRP), putative (Q382S6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MQQLAETLIMEQHVEALSLPEVELDDEGLITLFTLITRRDHLGSPNTNWETCDNENQALQESGPAAASEAAPNDAQTENKESASPEAGAALTPVGKSSPTKTLWFGVRCLDLSRCKVTDPTNVFSLFRCPVLEVLVLPPSNQLGDVHLRGILEGCPHLHTIDISGNTALTTACVKYIGRHSTIKVLRLENCPGIDQLDLPNVEVLFSSLSYVIKLHAPELRRLPVPVVHSRVLFNFKAPRLREITLKGIVVDRGTLDSLKETAGEDSACEPKLARSVLSSCDKSAYSDGQKQSTAATMQLLCAGFIDCTFTAESEVREFTKKQKALLRFSLHGCKGVVDANLTRLPATLMDLDVSDAARLTNRGLEIIATTLPQLIRLNLKNAGPQISNEGIRLLRGLVNLEVLNLLRLPQILPEVVSAVANDLPWLRKLYHETAVVGPRSVVAATSAPVHLDVLREDDEDTTRNAVGECAKELLQLRNETALAFWMDAQLPKPTSLIPPRTAAADSIDLNAPNPPLTANTTFYEAACRKLSRSGNGSAFGSQRRAITPRNADAAANQNEESEKVNVLVVSSGDDSPLMASMSGGVEGVNADCGDVDDKSFSTAPDQLRAMENALDEKNRLVIEKKPLGPWDEEDLVEKHRRIA
Protein: Conserved serine rich protein (O05574)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- SAF domain-containing protein
- 5-formyltetrahydrofolate cyclo-ligase
- Chaperone protein DnaJ 2
- Possible iron-regulated short-chain dehydrogenase/reductase
- UTP--glucose-1-phosphate uridylyltransferase
Sequence:
MPTYSYECTQCANRFDVVQAFTDDALTTCERCSGRLRKLFNAVGVVFKGTGFYRTDSRESGKKSKSQTNGSSTSESTKSSGSSGSSGSSESKASGSTEKSTSSTTAAAAV
Protein: Uncharacterized protein (Q54K22)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Glucose-6-phosphate isomerase
- Fructose-bisphosphate aldolase
- Probable phosphoglucomutase-2
- Phosphoglucomutase-1
- glucose-6-phosphate 1-epimerase
- Glucokinase
- Galactokinase
- Transketolase
- Glucose-6-phosphate 1-dehydrogenase
- Probable transaldolase
Sequence:
MSKRQTKNSPPLVGNSSPTSQSSQSPEISKKKLKKIEQKANRPKILVERPLSNLKFGGLVVFFICLVIFYIYLRINPLYDSGNNSNNLNNNNDNNNTNINIIDDIKSMKKIENGLKDIAKYKEWNEECKNKTIAVGYNTNLDLVVDAIELMDKLKLKSSIHNRPMSKEVIKSLDDFEQTFSHYFKSGSAAERMIENEDTFSAILAAALQSESKQFYTGGNAGIMANRLVADGCRVYLGGIIGKKLKELLSPSVSIIGYQSENGEEFDEIHLIMEYNKQSRWGSISPPRSNRFIISRDNTNSHLMTMESFHQEIEKKQPDLLLLSGLHLLTEEAQERRVNDMVNLLKQIPYNNNPSNFLNHPSLNVPIHLELASIASPSYINLLAKKIIPFVDSVGLNEQELGFIYVSTGGKKFSLDDFKEPSVNVVVNALLHIMEISFHYATTTTTSTTADRNVDDNILGDFGIPTMSKQRLLTRIHFHYLSFHLIITKSYSQWSPKLTSASVAASSIEATFQACRFNSVELLLPLSVEVDYRYTPGATKSIIIDPSSPVTTWQDSGYEFHLAPVLVCKSPLKTVGLGDSISTMGFLYQTIKSNEN
Protein: Protein ATP11, mitochondrial (P32453)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential for the assembly of the mitochondrial F1-F0 complex. May interact with the alpha and/or beta subunits of F1-ATPase.
Subcellular location: Mitochondrion.
Interaction partners:
- Protein ATP12
- ATP synthase subunit alpha
- ATP synthase subunit beta, mitochondrial
- mRNA-binding protein PUF3
- Mitochondrial ATPase complex subunit ATP10
- ATP synthase assembly factor FMC1, mitochondrial
- ATP synthase subunit gamma, mitochondrial
- Mitochondrial inner membrane protease ATP23
Sequence:
MWRLTRKIGTRIHISNQLSPIFNKAIGTVPVFRFYSSSPEQKYRKKLLEEAQKQGFNSIEELKNHLKETIESKKREFNKIDPLKELEDYQQKTQMENNNSKHLMTKSRSPLDPSAPKVPFKTLDSFLDVGKLKDLSKQEVEFLWRARWAQKDNTLCAVIPVSVYDKMMANARNNPIFVLPLPRQVQSEDAKPNEEQGMELHYIQWQFVGPQTTHCMMTSLAEYKLHQEFARPHTTLQFHSDLVKDKGIVFMNGHVEPDTNVNVQDAQLLLLNVQRFYGAMGEETPVAKQRVQLLRDFSKASPGFTVEKLISLSQSMEN
Protein: Isocitrate lyase (ICL) (EC 4.1.3.1) (Isocitrase) (Isocitratase) (Q6Z6M4)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in storage lipid mobilization during the growth of higher plant seedling.
Subcellular location: Glyoxysome {ECO:0000269|PubMed:15944756}.
Interaction partners:
- Malate synthase
- alanine--glyoxylate transaminase
- Aconitate hydratase
- Citrate synthase
- Citrate synthase
- Citrate synthase
- Peroxisomal
- glycerate dehydrogenase
- Os04g0107500 protein
- Os04g0106400 protein
Sequence:
MSSPFSVPSLIMEEEGRFEAEVAEVEAWWGTDRFRLTKRPYTARDVALLRGTLRQSYASGDMAKKLWRTLRAHQANGTASRTFGALDPVQVAMMAKHLDTVYVSGWQCSSTHTSTNEPGPDLADYPYDTVPNKVEHLFFAQLYHDRKQREARMSMSRAERAHEPYVDYLKPIIADGDTGFGGATATVKLCKLFVERGAAGVHLEDQSSVTKKCGHMAGKVLVAVSEHVNRLVAARLQFDIMGVETVLVARTDAVAATLIQTNVDARDHQFILGATNPRLRNRSLAAVLSDAMSAGKNGRELQAIEDEWLATAQLKTFSDCVRDAIASLNATDADKQRKLQEWSAATSHDKCVPLEQARDIAAGLGVTSLFWDWDLPRTREGFYRFRGSVAAAVVRGRAFAPHADVLWMETSSPNIAECTAFAEGVRAASPGAMLAYNLSPSFNWDASGMTDADMSEFIPRVARLGYVWQFITLAGFHADALVTDTFARDFARRGMLAYVERIQREERSNGVETLQHQKWSGANFYDRVLKTVQGGISSTAAMGKGVTEEQFKGSWTGPGSESSSHVLAKSRM
Protein: Charged multivesicular body protein 4b (Chromatin-modifying protein 4b) (CHMP4b) (Q9D8B3)
Organism: Mus musculus (Mouse)
Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Plays a role in the endosomal sorting pathway. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. When overexpressed, membrane-assembled circular arrays of CHMP4B filaments can promote or stabilize negative curvature and outward budding. CHMP4A/B/C are required for the exosomal release of SDCBP, CD63 and syndecan.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9H444}. Late endosome membrane {ECO:0000250|UniProtKB:Q9H444}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H444}. Midbody {ECO:0000250|UniProtKB:Q9H444}. Nucleus envelope {ECO:0000250|UniProtKB:Q9H444}. Note=Recruited to the nuclear envelope by CHMP7 during late anaphase. Localizes transiently to the midbody arms immediately before abscission. {ECO:0000250|UniProtKB:Q9H444}.
Interaction partners:
- Programmed cell death 6-interacting protein
- Charged multivesicular body protein 2a
- Charged multivesicular body protein 3
- Charged multivesicular body protein 6
- Charged multivesicular body protein 7
- Charged multivesicular body protein 2b
- Vacuolar protein sorting-associated protein 4B
- Vacuolar-sorting protein SNF8
- Tumor susceptibility gene 101 protein
- Charged multivesicular body protein 4c
Sequence:
MSVFGKLFGAGGGKAGKGGPTPQEAIQRLRDTEEMLSKKQEFLEKKIEQELTAAKKHGTKNKRAALQALKRKKRYEKQLAQIDGTLSTIEFQREALENANTNTEVLKNMGYAAKAMKAAHDNMDIDKVDELMQDIADQQELAEEISTAISKPVGFGEEFDEDELMAELEELEQEELDKNLLEISGPETVPLPNVPSVALPSKPAKKKEEEDDDMKELENWAGSM
Protein: Matrix protein (F4YH96)
Organism: Henipavirus hendraense
Subcellular location: Virion {ECO:0000256|ARBA:ARBA00004328}.
Interaction partners:
Sequence:
MDFSVSDNLDDPIEGVSDFSPTSWENGGYLDKVEAEIDKHGSMIPKYKIYTPGANERKFNNYMYMICYGFVEDVERSPESGKRKKIRTIAAYPLGVGKSTSHPQDLLEELCSLKVTVRRTAGATEKIVFGSSGPLHHLLPWKKILTGGSIFNAVKVCRNVDQIQLEKQQSLRIFFLSITKLNDSGIYMIPRTMLEFRRNNAIAFNLLVYLKIDADLAKAGIQGSFDKDGTKVASFMLHLGNFVRRAGKYYSVEYCKRKIDRMKLQFSLGSIGGLSLHIKINGVISKRLFAQMGFQKNLCFSLMDINPWLNRLTWNNSCEISRVAAVLQPSVPREFMIYDDVFIDNTGKILKG
Protein: Protein Rev (ART/TRS) (Anti-repression transactivator) (Regulator of expression of viral proteins) (P04616)
Organism: Human immunodeficiency virus type 1 group M subtype B (isolate BH10) (HIV-1)
Function: Escorts unspliced or incompletely spliced viral pre-mRNAs (late transcripts) out of the nucleus of infected cells. These pre-mRNAs carry a recognition sequence called Rev responsive element (RRE) located in the env gene, that is not present in fully spliced viral mRNAs (early transcripts). This function is essential since most viral proteins are translated from unspliced or partially spliced pre-mRNAs which cannot exit the nucleus by the pathway used by fully processed cellular mRNAs. Rev itself is translated from a fully spliced mRNA that readily exits the nucleus. Rev's nuclear localization signal (NLS) binds directly to KPNB1/Importin beta-1 without previous binding to KPNA1/Importin alpha-1. KPNB1 binds to the GDP bound form of RAN (Ran-GDP) and targets Rev to the nucleus. In the nucleus, the conversion from Ran-GDP to Ran-GTP dissociates Rev from KPNB1 and allows Rev's binding to the RRE in viral pre-mRNAs. Rev multimerization on the RRE via cooperative assembly exposes its nuclear export signal (NES) to the surface. Rev can then form a complex with XPO1/CRM1 and Ran-GTP, leading to nuclear export of the complex. Conversion from Ran-GTP to Ran-GDP mediates dissociation of the Rev/RRE/XPO1/RAN complex, so that Rev can return to the nucleus for a subsequent round of export. Beside KPNB1, also seems to interact with TNPO1/Transportin-1, RANBP5/IPO5 and IPO7/RANBP7 for nuclear import. The nucleoporin-like HRB/RIP is an essential cofactor that probably indirectly interacts with Rev to release HIV RNAs from the perinuclear region to the cytoplasm.
Subcellular location: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04077}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04077}. Note=The presence of both nuclear import and nuclear export signals leads to continuous shuttling between the nucleus and cytoplasm. {ECO:0000255|HAMAP-Rule:MF_04077}.
Interaction partners:
Sequence:
MAGRSGDSDEDLLKAVRLIKFLYQSNPPPNPEGTRQARRNRRRRWRERQRQIHSISERILSTYLGRSAEPVPLQLPPLERLTLDCNEDCGTSGTQGVGSPQILVESPTVLESGAKE
Protein: SET domain-containing protein (O17186)
Organism: Caenorhabditis elegans
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
Interaction partners:
- SPK domain-containing protein
- MYND-type domain-containing protein
- JmjC domain-containing protein
- Histone-lysine N-methyltransferase set-18
- MYND-type domain-containing protein
- Histone-lysine N-methyltransferase set-17
Sequence:
MPIIGKEWFTDVAKQQPMVLYEDISQGCERFVVPVYSNPRFFMDSSLFENFKYTSRIIDVAGQLACRSASPTFMCQCAGQCSTNCECSSGVFGEGGTVENMELLMWDTVRECNEYCNCALWCGNRVAQKGAMYPVEIFARDPWCGWGVRASVDIAFGTFIGEYAGELIDDEEAMDRHDSTFLFETKVGSETLTIDAKYSGNYTRFINHSCAPNVKVANISWDYDKIQLIHMCFFTDKAIRKGEELTIDYGEAWWANKKFPCLCKSSECRYQFGNDQRT
Protein: Eukaryotic translation initiation factor 2A (eIF-2A) (P53235)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions in the early steps of protein synthesis of a small number of specific mRNAs. Acts by directing the binding of methionyl-tRNAi to 40S ribosomal subunits. In contrast to the eIF-2 complex, it binds methionyl-tRNAi to 40S subunits in a codon-dependent manner, whereas the eIF-2 complex binds methionyl-tRNAi to 40S subunits in a GTP-dependent manner. Specifically associates with both 40S subunits and 80S ribosomes.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 5B
- Small ribosomal subunit protein eS19A
- Small ribosomal subunit protein eS8A
- Small ribosomal subunit protein eS1A
- Small ribosomal subunit protein RACK1
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein eS6A
- Small ribosomal subunit protein eS17A
- Small ribosomal subunit protein eS30A
Sequence:
MSSQFFLKTSQDIELFQSYPTFEQSNTNSKDFPVISSVLSPCGRFLALSTKENVKVFTGPCLDNVLLTMKLSDVYDLHFSPAGNYLSTWERASIQDPNHKNVKVWYLNKPFKKDCVSEDIVPAYEYQAKSQSGWFLQFSKLDNYGLRLFKHDLKIVKLSSANADNFDFQSPFAVLSDDETSQHFTTYLISPAEHPTICTFTPEKGGKPAQLIIWALSEGKITKKIASKTFFKADSCQLKWNPLGNAILCLAITDFDSSNKSYYGENTLYLLSFQGVNGTLGGNSVRVSLTTGPVHDFTWSPTSRQFGVIAGYMPATISFFDLRGNVVHSLPQQAKNTMLFSPSGHYILIAGFGNLQGSVEILDRLDKFKCVSKFDATNTSVCKWSPGGEFIMTATTSPRLRVDNGVKIWHVSGSLVFVKEFKELLKVDWRSPCNYKTLENKDEAFFENHIINNWEPLPDSTTSSLDPKISNKSELQIHSSVQEYISQHPSREASSNGNGSKAKAGGAYKPPHARRTGGGRIVPGVPPGAAKKTIPGLVPGMSANKDANTKNRRRRANKKSSETSPDSTPAPSAPASTNAPTNNKETSPEEKKIRSLLKKLRAIETLKERQAVGDKLEDTQVLKIQTEEKVLKDLEKLGWKDE
Protein: Peptide YY (PYY) (PYY-I) (Peptide tyrosine tyrosine) [Cleaved into: Peptide YY(3-36) (PYY-II)] (P10082)
Organism: Homo sapiens (Human)
Function: This gut peptide inhibits exocrine pancreatic secretion, has a vasoconstrictory action and inhibitis jejunal and colonic mobility.
Subcellular location: Secreted.
Interaction partners:
- Neuropeptide Y receptor type 2
- Neuropeptide Y receptor type 1
- Neuropeptide Y receptor type 5
- Pro-neuropeptide Y
- Pancreatic polypeptide prohormone
- Appetite-regulating hormone
- Neuropeptide Y receptor type 4-2
- Pro-glucagon
- Pro-opiomelanocortin
- G-protein coupled receptor 83
Sequence:
MVFVRRPWPALTTVLLALLVCLGALVDAYPIKPEAPREDASPEELNRYYASLRHYLNLVTRQRYGKRDGPDTLLSKTFFPDGEDRPVRSRSEGPDLW
Protein: Guanylyl cyclase-activating protein 1 (GCAP 1) (Guanylate cyclase activator 1A) (P43080)
Organism: Homo sapiens (Human)
Function: Stimulates retinal guanylyl cyclase when free calcium ions concentration is low and inhibits guanylyl cyclase when free calcium ions concentration is elevated. This Ca(2+)-sensitive regulation of retinal guanylyl cyclase is a key event in recovery of the dark state of rod photoreceptors following light exposure (By similarity). May be involved in cone photoreceptor light response and recovery of response in bright light (By similarity).
Subcellular location: Membrane; Lipid-anchor {ECO:0000250|UniProtKB:P46065}. Photoreceptor inner segment {ECO:0000269|PubMed:9620085}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:9620085}. Note=Present at higher levels in cone than in rod outer segments (PubMed:9620085). Subcellular location is not affected by light or dark conditions. {ECO:0000269|PubMed:9620085}.
Interaction partners:
- Retinal guanylyl cyclase 1
- Retinal guanylyl cyclase 2
- Guanylyl cyclase-activating protein 2
- Guanylyl cyclase-activating protein 3
- Protein RD3
- Translation factor GUF1, mitochondrial
- Calcium-binding protein 1
- Aryl-hydrocarbon-interacting protein-like 1
- Cyclic nucleotide-gated channel alpha-1
- Cyclic nucleotide-gated channel beta-1
Sequence:
MGNVMEGKSVEELSSTECHQWYKKFMTECPSGQLTLYEFRQFFGLKNLSPSASQYVEQMFETFDFNKDGYIDFMEYVAALSLVLKGKVEQKLRWYFKLYDVDGNGCIDRDELLTIIQAIRAINPCSDTTMTAEEFTDTVFSKIDVNGDGELSLEEFIEGVQKDQMLLDTLTRSLDLTRIVRRLQNGEQDEEGADEAAEAAG
Protein: Uncharacterized protein (Q585V1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDEQNSESSDVGGLLEVLEECALGDWDVSADELLLKSLMTMQAKLSARFDSIRGMVDSLYDEARTASIQLQNAMNSFAVLSQRQFVQNRVSAEDEGSERETEPSKSDEGESEDRERGLGDVEVRVARMCQECVDLSYRVLKKRTMPLLDEDSSLSEYGSGDDESEGSSAEVRRPSCSENLFMSPITSRKFLSDPYGGYFDNTVGKADFTSGGRRRLGGSTGRMGRGSRQNPSTRLGGPTTVRPAAPPPLPPTPPPVQMAKAKGTLPPPPPPMPTGKLKAPPPPPPPFASIAGKTRAPLPPPPPAPTGKTQAPAAPPPAPTGKTQAPAAPPPAPTGKTQAPAAPPPAPTGKTQAPAAPPPAPTGKTQAPAAPPPAPTGKTQAPTAPPPAPTGKTQAPAAPPPAPTGKTQAPAAPPPAPTGKTQAPAAPRVAAQTQKQQAKKGVAAFLDSSDSSDGSEAKPCAGAVVRPGLAAPSLVRENSTLPSPAPVLSMKRPPAASSGKGKVALFDSSSDSDEENSGVRAATFTEKDDQQFPKGGVGAGDLARKGSPRGVPSRATSGSRVGPTDQQKLISPVGSPRSRRPIFSSSSGSSPEATPPRASIKQTGCRGAALGVSSTAQVGGGNNQSTTAKPLPTTFQSVERSVPASPPPPEGVRARSEAAPAQSPDAAANVMPIVKTETQPQGDDKEQHTAAPLKVIPNVAFSKRKISDSDSDN
Protein: Small ribosomal subunit protein uS5 (40S ribosomal protein S2) (Q8IL02)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Ribosomal protein S27a, putative
- 60S acidic ribosomal protein P0
- 40S ribosomal protein S7
- 40S ribosomal protein S17, putative
- 60S ribosomal protein L30e, putative
- 40S ribosomal protein S4
- 40S ribosomal protein S19
- 40S ribosomal protein S9, putative
- 40S ribosomal protein S8
- 60S ribosomal protein L13, putative
Sequence:
MEDRGGFSRGFGRGVRGTRGRGGRGARGRGRGSAEDDLKNWVPVTKLGRLVKEGKIVSIEEIYLHSLPIKEYQIIDYFFQPNECSHPLKDDVVKIMPVQKQTRAGQRTRFKAFVAIGDGNGHCGLGVKCAKEVATAIRGAIISAKLSLIPVRRGYWGNKIGDPHTVPMKVSGKCGSVRIRLVPAPRGTQIVGAPTTKKMLNFAGIKDCFSSSCGKTKTKGNFLRAIFNALSKTYGYLTPDLWKVTNFDKSPYEEWSDFLETYQNLKGIKGTV
Protein: Aminopeptidase N (AP-N) (rAPN) (EC 3.4.11.2) (Alanyl aminopeptidase) (Aminopeptidase M) (AP-M) (Kidney Zn peptidase) (KZP) (Microsomal aminopeptidase) (CD antigen CD13) (P15684)
Organism: Rattus norvegicus (Rat)
Function: Broad specificity aminopeptidase which plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. Also involved in the processing of various peptides including peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. May also be involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis and promote cholesterol crystallization. May have a role in amino acid transport by acting as binding partner of amino acid transporter SLC6A19 and regulating its activity (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:2564389}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P15144}. Note=Also found as a soluble form. {ECO:0000250|UniProtKB:P15144}.
Interaction partners:
- Reticulon-4 receptor
- Cytosol aminopeptidase
- Glutathione hydrolase 6
- Glutathione hydrolase 7
- Glutamate--cysteine ligase catalytic subunit
- Glutathione hydrolase 5 proenzyme
- Glutamate--cysteine ligase regulatory subunit
- Glutathione synthetase
- Putative glutathione-specific gamma-glutamylcyclotransferase 2
- N-acetyltransferase family 8 member 2
Sequence:
MAKGFYISKTLGILGILLGVAAVCTIIALSVVYAQEKNRNAENSAIAPTLPGSTSATTSTTNPAIDESKPWNQYRLPKTLIPDSYQVTLRPYLTPNEQGLYIFKGSSTVRFTCNETTNVIIIHSKKLNYTNKGNHRVALRALGDTPAPNIDTTELVERTEYLVVHLQGSLVKGHQYEMDSEFQGELADDLAGFYRSEYMEGGNKKVVATTQMQAADARKSFPCFDEPAMKASFNITLIHPNNLTALSNMLPKDSRTLQEDPSWNVTEFHPTPKMSTYLLAYIVSEFKYVEAVSPNRVQIRIWARPSAIDEGHGDYALQVTGPILNFFAQHYNTAYPLEKSDQIALPDFNAGAMENWGLVTYRESALVFDPQSSSISNKERVVTVIAHELAHQWFGNLVTVDWWNDLWLNEGFASYVEFLGADYAEPTWNLKDLIVLNDVYRVMAVDALASSHPLSSPANEVNTPAQISELFDSITYSKGASVLRMLSSFLTEDLFKKGLSSYLHTFQYSNTIYLDLWEHLQQAVDSQTAIKLPASVSTIMDRWILQMGFPVITVNTSTGEIYQEHFLLDPTSKPTRPSDFNYLWIVPIPYLKNGKEDHYWLETEKNQSAEFQTSSNEWLLLNINVTGYYQVNYDENNWRKIQNQLQTDLSVIPVINRAQIIHDSFNLASAGKLSITLPLSNTLFLASETEYMPWEAALSSLNYFKLMFDRSEVYGPMKRYLKKQVTPLFAYFKIKTNNWLDRPPTLMEQYNEINAISTACSSGLEECRDLVVGLYSQWMNNSDNNPIHPNLRSTVYCNAIAFGGEEEWNFAWEQFRKATLVNEADKLRSALACSNEVWILNRYLSYTLNPDYIRKQDATSTIVSIANNVVGQTLVWDFVRSNWKKLFEDYGGGSFSFANLIQGVTRRFSSEFELQQLEQFKEDNSATGFGSGTRALEQALEKTKANIKWVKENKDVVLKWFTENS