wanglab/gogpt-training-data huggingface dataset:
Protein: Pentatricopeptide repeat-containing protein At1g62720 (Q9SI78)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Pentatricopeptide repeat-containing protein At4g21190
Sequence:
MRRSTTISIASKANKFLNLCLLQKGNPVIVPFISRFWGRTFSTKRSSMNLEEEIDLFCKMIQSRPLPSIVDFSKVLSKIAKSKNYDLVISLFHHMEVCGIGHDLYSYNIVINCLCRCSRFVIALSVVGKMMKFGYEPDVVTVSSLINGFCQGNRVFDAIDLVSKMEEMGFRPDVVIYNTIIDGSCKIGLVNDAVELFDRMERDGVRADAVTYNSLVAGLCCSGRWSDAARLMRDMVMRDIVPNVITFTAVIDVFVKEGKFSEAMKLYEEMTRRCVDPDVFTYNSLINGLCMHGRVDEAKQMLDLMVTKGCLPDVVTYNTLINGFCKSKRVDEGTKLFREMAQRGLVGDTITYNTIIQGYFQAGRPDAAQEIFSRMDSRPNIRTYSILLYGLCMNWRVEKALVLFENMQKSEIELDITTYNIVIHGMCKIGNVEDAWDLFRSLSCKGLKPDVVSYTTMISGFCRKRQWDKSDLLYRKMQEDGLLPL
Protein: SAND domain-containing protein (Q18624)
Organism: Caenorhabditis elegans
Interaction partners:
- C2H2-type domain-containing protein
- BTB domain-containing protein
- C2H2-type domain-containing protein
- Bicarbonate transporter-like transmembrane domain-containing protein
Sequence:
MCDDDDFEFSTQPEFGSTSEMKNEEMLVPSDPNFEIDGRRVQENMYDQASELSYTYLDTPSEHIWTPIVPLNATTVPVTCGYVKGIMHLKLFRCPGIRQACIEYESQYLTPKQFTELGGKGRQKDWKACIRVENVSLRTLLENKTIDFYNHKSICHGQCQSRNYMNSTGRAPVNKRHLEDVLASGDDASEPTEQSSGQISEEPIKKRGRGRPAGKKNKAKLEINFVESEDQLVFEEFFQPAFSTRSPAPERPVCSPAQDIYSCLQNDPMSFWSQIKRSGFISQFCDDIIAGAINLKQSAMTQSLNQNSAFVLTRATFALGIQKPIVNRVQSIERNVNEQKKQNEMMEDQGKYQEDAQTEADDLDNQPRCSYLLEDL
Protein: tRNA ligase phosphodiesterase domain-containing protein (Q57XG4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDAQVGVVQQPVTTSSTIWVGECQCPKWKKSTHRAVEQNLTTSLECGGERDALLDVACGSGIDIDSFLREKWIRVAFTSSFGSNSRVRVRARRVRIGSHEFVVVERNVFGCDDSVYRKDNKLWEGLPRGQACVFVESGDRAGFIPIGRLQGLRKFNSFDGPYGIRGRQPVSAVAMEAIDGDCGHISAFVHTGERYWLVGNKDTHLLVSFSVPEKDIFSNTAEGGAITNEGDKPLQGANYSPPSLAVRIARLWGQTLRALPDEKSFGLHEFLSSNRYTACFDAVLQDCGHLVDYGEDELLQFYALTQSGESLAEGLCVDPVSAIVNLQSFGLRVVPFHSEQCSSVPEILDLGTDEYSQYGGQVARRLNCRGAVMYGLDAQGIVVRLWKLPSHAYVVERAAQEAIVTHRLSGTVLRDKLRRKLDRLPKEIRRCVTEWSSARLEPLLNLAAWLHIMGKVTPEVGLDGLQEVRRSWITLQQQLVKHTKDMREHLQLYEPPVAEAAINNPDVIMCVGPQGCGKSTFCRAFCVLLQKVGQKPRWINQDEVGGRNEFIEAIRRAKESDCTHILIDKMNLDDAARNADYASFNLKTITVAWVHPCDVDVMVSTCLERVCHRGNAHRTFRGTVSPGKKRKMMTIIRGCVQRCEPPTTGIVIEANVLDPPAITIESVWKGLCRHTMSELPDIKDLSVADALEIARRYELLLSHSSRPFNCGIIKVVNSELLVALVPADYLEGKKMRKELDISTIYLGDRSHFDLTLLSELQTLEGTSIQVAPVRIASDAKATAIEIRNNNEFPCQNAHPHITIATAPGVPAKYSNELLSKVSTETSDIKVMEVSPDVSISGVFQFVR
Protein: Snaclec jerdonibitin subunit alpha (TJ-GPIb-bp subunit alpha) (D1MGU0)
Organism: Protobothrops jerdonii (Jerdon's pitviper) (Trimeresurus jerdonii)
Function: Snaclec that dose-dependently inhibits platelet aggregation induced by ristocetin or low-dose thrombin, but not by high-dose thrombin. Binds to GPIbalpha (GP1BA). In vivo, also dose-dependently induces thrombocytopenia of mice and platelet counts remains at very low level even after 18 hours intravenous injection.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MGRFIFVSFGLLVVFLSLSGTGADCPFDWSSFRQYCYRVFKQLKTWEDAERFCSEQVKGARLVSIESYREAVFVAQLLSENIKATKSHVWIGLSVENKGQQCSSKWSDGSSVSYENLVKPFSKKCFVLKKESEFHKWFNVYCGQQHLFMCKFLRPR
Protein: Heat shock cognate 70 kDa protein 2 (HSC70-2) (Q557E0)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May function in protein folding and assembly, and disassembly of protein complexes.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Interaction partners:
- DnaJ homolog subfamily A member 1 homolog
- Heat shock protein
- Heat shock cognate 90 kDa protein
- Luminal-binding protein 1
- J domain-containing protein
- J domain-containing protein
- GrpE protein homolog, mitochondrial
- J domain-containing protein
- J domain-containing protein
- Co-chaperone HscB C-terminal oligomerisation domain-containing protein
Sequence:
MSSSIGIDLGTTYSCVGVWQNDRVEIIANDQGNRTTPSYVAFNETERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFSDPVIQSDMKHWPFKVIAKEGDKPHLQVEFKGEVKTFSPEEVSSMVLLKMKETAEAYLGKTINNAVITVPAYFNDSQRQATKDAGAIAKLNVQRIINEPTAAAIAYGLEKKSQGERNILIFDLGGGTFDVSLLTIEDGVFEVKATAGDTHLGGEDFDNRLVNHFVDEFKRKHKKDLMTNQRALRRLRTACERAKRTLSSSAQASIEIDSLFEGIDFYTSITRARFEELCADLFRGCLDPVDKVLKDSKLDKKTIHEIVLVGGSTRIPKVQQLLQDHFNGKELNKSINPDEAVAYGAAVQAAILSNEGGAKVADILLLDVAPLSMGLETAGGVMTTLIPRNTTIPCKKNQTFSTYSDNQTGVLVQVYEGERAMTRDNNLLGKFELTNIPPAPRGVPQIEVTFDIDANGILNVSAEDKSTGNKHKITITNDKGRLTAEQIEKMVKDAEMFKAQDEAQREVVESKNKLENYAYTVRSTIKDDKIAAKLSKEDRKTVEEKSDEAINWLHANDSATKEEYEKAMKDLEAVCSPIISKVYGQQGGENPGNFSGAKTTEEDLD
Protein: Phototropic-responsive NPH3 family protein NPY2 (MAB4/ENP/NPY1-like proten 3) (Protein NAKED PINS IN YUC MUTANTS 2) (O80970)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). May play an essential role in auxin-mediated organogenesis and in root gravitropic responses.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21490067}. Cytoplasm, cytosol {ECO:0000269|PubMed:21490067}. Note=Polar localization at the cell periphery almost identical to PIN proteins polarity, in the upper side of the plasma membrane of root epidermis (PubMed:21490067). Weakly observed in the cytosol of the root tip quiescent center (QC) and in columella initial cells, sometimes close to the basal side of the plasma membrane (PubMed:21490067). {ECO:0000269|PubMed:21490067}.
Interaction partners:
- Protein ENHANCED DISEASE RESISTANCE 2-like
- Calmodulin binding protein PICBP
- IQ domain-containing protein IQM3
- Protein LIGHT-DEPENDENT SHORT HYPOCOTYLS 10
Sequence:
MKFMKIGSKLDSFKTDGNNVRYVENELASDISVDVEGSRFCLHKFPLLSKCACLQKLLSSTDKNNIDDIDISGIPGGPTAFETCAKFCYGMTVTLSAYNVVATRCAAEYLGMHETVEKGNLIYKIDVFLSSSLFRSWKDSIIVLQTTKPFLPLSEDLKLVSLCIDAIATKACVDVSHVEWSYTYNKKKLAEENNGADSIKARDVPHDWWVEDLCELEIDYYKRVIMNIKTKCILGGEVIGEALKAYGYRRLSGFNKGVMEQGDLVKHKTIIETLVWLLPAEKNSVSCGFLLKLLKAVTMVNSGEVVKEQLVRRIGQQLEEASMAELLIKSHQGSETLYDVDLVQKIVMEFMRRDKNSEIEVQDDEDGFEVQEVRKLPGILSEASKLMVAKVIDSYLTEIAKDPNLPASKFIDVAESVTSIPRPAHDALYRAIDMFLKEHPGITKGEKKRMCKLMDCRKLSVEACMHAVQNDRLPLRVVVQVLFFEQVRAAASSGSSTPDLPRGMGRELRSCGTYGSSRSVPTVMEDEWEAVATEEEMRALKSEIAALKLQEESGRKSMDRAGVTAISKIRSLIMSKKIFGKKVQLQSKGGGEKNNGGGGGGSDSSESLGSMNAAEETAKTATPSRNLTRRVSVS
Protein: tRNA acetyltransferase TAN1 (EC 2.3.-.-) (P53072)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable tRNA acetyltransferase required for the formation of the modified nucleoside N(4)-acetylcytidine in serine and leucine tRNAs. Binds RNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- tRNA
- RNA cytidine acetyltransferase
- tRNA pseudouridine synthase 4
- tRNA-dihydrouridine
- tRNA
- Repressor of RNA polymerase III transcription MAF1
- tRNA pseudouridine synthase 1
- Uncharacterized protein YGL230C
- tRNA
Sequence:
MGEKRNRNGKDANSQNRKKFKVSSGFLDPGTSGIYATCSRRHERQAAQELQLLFEEKFQELYGDIKEGEDESENDEKKDLSIEDQIKKELQELKGEETGKDLSSGETKKKDPLAFIDLNCECVTFCKTRKPIVPEEFVLSIMKDLADPKNMVKRTRYVQKLTPITYSCNAKMEQLIKLANLVIGPHFHDPSNVKKNYKFAVEVTRRNFNTIERMDIINQVVKLVNKEGSEFNHTVDLKNYDKLILVECFKSNIGMCVVDGDYKTKYRKYNVQQLYESKFRKDEDKSVKQ
Protein: LD16982p (Q7K115)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MESRSDIHRQLAASLTDELVKPLKIVVEGHHKARKAVESNVDKAARVLGEWRASEAKAKKASHTAARENEKLQDAMLDVRIQKSPSIALLHQGPNKQAAEKELKSAEKDCVKLDNKRKKAEEAVKRADVEYYTLCVRSERARVDWEMAVLRGSAQLQSSEQQRLGNMHNFAQQYARLISDMNPILGGLSTRLQPQLDACNVAKDMQVVRHIRRNSEGPSEQLLPDFYCEHTTLAMNRERRKHALIKLLQLVKTDLERERRSRDGLRGLSQSLNHQEHQNITDKLYHIRSMLTYLEGARLKLHSALLELDHKPRATHPLAQHIHITRDRTGLQQSILKVPNWLKNNDKSQTQQSTSMLAHDITDITTNHEDELPDENCSHLHSSSHSNNNSNGSCTDVSSVVKPFNRSKSNIETNFTSQPKIISTTNAAIAVSVKSKTLANLQDGHHNNQQHHHHHHNHHSDRGQADGGSNQQDSDFDEFSSQDEDDEPQQPQQQPQPLQSQQQQQQPLLQNPTINGQVQTQHFYQNAQELQKGQKNGSVPILGRCKALYSYTPKLYDELELSPGDIIEVHAKQDDGWWLGALRNHIGIFPATYVEECA
Protein: DNA-binding protein (Q61491)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MMRILSLPTENAVTYYDVLVSFTQEEWALLDPSQKSLYKDVMLETYRNLTAIGYNWEEDNIEEDCENSGRPTRHLQRDGPSNTGEKPFECIQYDGAFARNHHQLHKDTGSFMSYTDRQIHRRPHTEEKVYDGNQCGKTFSCHNHFEIRKGTYTGEKPYECNQCGKAFARNSNLLDHKRIHTGEKPYKCKQCGKDFTHHSTLHIHKRIHTREKTYKCNQCMTIAHLQCHKITHTGEKLCEYNQCWKAFAYHKTLQIHERTHTGEKLYQCNQCAKAFPYHRTLQIHERTHTGEKPYECNQCGKAFACLRNLQNHKTTHTGEKPYECNQCGRAFRQYVYLQCHERIHTGEKPFECNQCGKAFAHHSTLQRHKRTHTGEKPYECNQCGKAFACPRYLQIHKRTHTGEKPYECNQCGKAFACYQSFQIHKRTHTGEKPYECNQCGKAFACNRYLQIHKRTHTGERPYECNQCGKAFTCRSNLQIHKRTHTGEKPYECNQCGKAFTQFFPLKRHEITHTKEKPYECNQCGKAFTRHSTLQIHKRTHTGEKPV
Protein: Pyruvate dehydrogenase E1 component alpha subunit, putative (EC 1.2.4.1) (Q388X3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Pyruvate dehydrogenase E1 component subunit beta
- Dihydrolipoamide acetyltransferase, putative
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoamide dehydrogenase, putative
- Dihydrolipoamide dehydrogenase, point mutation
- Dihydrolipoyl dehydrogenase
- Dihydrolipoamide dehydrogenase, putative
- 3-methyl-2-oxobutanoate dehydrogenase
- Glucose-6-phosphate isomerase
- Pyruvate kinase
Sequence:
MLKCVSRVFLGAKTVPLNPHVPFKLHTAGRDDLPPIPTTATYEPEKIKENLAMMIRIRRVEALADQSYKLKKIRGFCHLCIGQEAIPVGMENVLSRGDPVVTGYRDHGLFMTRGGTIEELFAELFGREGGCSKGKGGSMHMYRVKENFYGGNGIVGAQAPLGAGLAWRYALENRDKPSNVAVTFYGDGAANQGQVFEAMNIAALQRIPVIFCCENNHYGMGTREDRAAYQPQMYRRGDYIPGLRVDGMDVLAVQEGTRWAKEWCLAGKGPVVLEMDSYRYMGHSMSDPDSQYRTKNDIQEVRRTRDCIEKMKEFVVSEGIMTVEEIKQMEKDVKKEVDKELPPAEKQAITPLKELFTDIYCGEQYEHRTTQGTVYAKP
Protein: Poly(A) RNA polymerase GLD2-A (EC 2.7.7.19) (PAP-associated domain-containing protein 4-A) (Q641A1)
Organism: Xenopus laevis (African clawed frog)
Function: Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific RNAs, forming a poly(A) tail. In contrast to the canonical nuclear poly(A) RNA polymerase, it only adds poly(A) to selected cytoplasmic mRNAs during oocyte maturation. Plays a central role during oocyte maturation by mediating polyadenylation of dormant mRNAs, which contain 5'AAUAAA-3' sequence in their 3'UTR. In immature oocytes, polyadenylation of poly(A) tails is counteracted by the ribonuclease parn. During maturation parn is excluded from the ribonucleoprotein complex, allowing poly(A) elongation and activation of mRNAs. May not play a role in replication-dependent histone mRNA degradation (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15987818}.
Interaction partners:
Sequence:
MYPNSPSLGRIPLPLPCEQQQQASGYSDKLPVSAAPELLSPEQFIQASLNIQKHANLSRMLMNGNVLTVPPVSSPPWAYLNHSPLISPGSPSSSFQNRKRRSDEGNVSYDVKRQRFHSPQEQTVNHQAVPLRGDLRCSYPGSPAFPLLQSPSPPVLKEHVSNSGDCWLYDHIDTTLPVAEDKLSQQILDLFQALQQQVCDIKKKDICRAELQREIQQIFPQSRLYLVGSSLNGFGTRISDADLCLVLKEEPMNQHTEATQILGLLHKLFYTRLSYIERLQFIRAKVPIVKFRDKVSGAEFDLNVNNVVGIRNTFLLRTYAYLESRVRPLVLVIKKWANHHGINDASRGTLSSYTLVLMVLHYLQTLPEPILPSLQKKYPECFDLSMQLNLVHHAPRNIPPYLSKNETPLGDLLLGFLKYFAVEFDWSKDIISVREGKALPRSDDYLWRNKYICVEEPFDGTNTARAVYERQKFDMIRAEFLKAWGALRDDRDLYSLLPVTAIVKKMNSL
Protein: T-complex protein 1 subunit beta (TCP-1-beta) (CCT-beta) (Q54ES9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit eta
- Uncharacterized protein
- Uncharacterized protein
- T-complex protein 1 subunit gamma
- Uncharacterized protein
Sequence:
MSSQLAPIPILNQNASEERGEIARLSSFVGAIAITDLVKTTLGPKGMDKILISASNPNELIITNDGATILTKIYIDNPAAKILVDISRTQDDEVGDGTTSVCVLAGELLREGERLVQQKVHPQTIISGWRLALETARAALQSSTQDHSSDKVKFREDLLNIARTTLSSKILHTEKDHFANMVVDAVLRLNGNTNLDNIHIIKKSGGSLRESYLDEGFILEKKIGVGCPKRLENPKILIANTAMDTDKIKIFGGKVVVDSMTELAKMEDAEKEKMLNKCKKIVDHGINCFVNRQLVYNLPEQYFAEHGVMSIEHADFDGIERLALVTGAEIVSTFDHPELVKIGTCKLIEEVMIGEDKVIRFSGIPSGEACTIVLRGATSHILEEAERSIHDALCVLAVTVAETRTVLGAGCSEMIMSKAVDELAAITPGKKAMAIESFAKALRQIPTIIANNAGYDSSELVSQLKAAHHQGDKKAGLNMRDGCIGNAEELGVIESFKVKQQVLVSAHEAAEMIMRVDDILRAAPRQRSNLQH
Protein: Dematin (Dematin actin-binding protein) (Erythrocyte membrane protein band 4.9) (Q08495)
Organism: Homo sapiens (Human)
Function: Membrane-cytoskeleton-associated protein with F-actin-binding activity that induces F-actin bundles formation and stabilization. Its F-actin-bundling activity is reversibly regulated upon its phosphorylation by the cAMP-dependent protein kinase A (PKA). Binds to the erythrocyte membrane glucose transporter-1 SLC2A1/GLUT1, and hence stabilizes and attaches the spectrin-actin network to the erythrocytic plasma membrane. Plays a role in maintaining the functional integrity of PKA-activated erythrocyte shape and the membrane mechanical properties. Also plays a role as a modulator of actin dynamics in fibroblasts; acts as a negative regulator of the RhoA activation pathway. In platelets, functions as a regulator of internal calcium mobilization across the dense tubular system that affects platelet granule secretion pathways and aggregation. Also required for the formation of a diverse set of cell protrusions, such as filopodia and lamellipodia, necessary for platelet cell spreading, motility and migration. Acts as a tumor suppressor and inhibits malignant cell transformation.
Subcellular location: Cytoplasm. Cytoplasm, cytosol. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton. Cell membrane. Membrane {ECO:0000250}. Endomembrane system. Cell projection {ECO:0000250}. Note=Localized at the spectrin-actin junction of erythrocyte plasma membrane. Localized to intracellular membranes and the cytoskeletal network. Localized at intracellular membrane-bounded organelle compartment in platelets that likely represent the dense tubular network membrane. Detected at the cell membrane and at the parasitophorous vacuole in malaria-infected erythrocytes at late stages of plasmodium berghei or falciparum development.
Interaction partners:
- Beta-adducin
- Alpha-adducin
- Gamma-adducin
- Protein 4.1
- Tropomodulin-1
- Protein 4.2
- Tropomodulin-2
- Tropomodulin-3
- Glycophorin-C
- Ankyrin-1
Sequence:
MERLQKQPLTSPGSVSPSRDSSVPGSPSSIVAKMDNQVLGYKDLAAIPKDKAILDIERPDLMIYEPHFTYSLLEHVELPRSRERSLSPKSTSPPPSPEVWADSRSPGIISQASAPRTTGTPRTSLPHFHHPETSRPDSNIYKKPPIYKQRESVGGSPQTKHLIEDLIIESSKFPAAQPPDPNQPAKIETDYWPCPPSLAVVETEWRKRKASRRGAEEEEEEEDDDSGEEMKALRERQREELSKVTSNLGKMILKEEMEKSLPIRRKTRSLPDRTPFHTSLHQGTSKSSSLPAYGRTTLSRLQSTEFSPSGSETGSPGLQNGEGQRGRMDRGNSLPCVLEQKIYPYEMLVVTNKGRTKLPPGVDRMRLERHLSAEDFSRVFAMSPEEFGKLALWKRNELKKKASLF
Protein: cDNA, FLJ94117, highly similar to Homo sapiens actinin, alpha 3 (ACTN3), mRNA (B2R8Y4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MMMVMQPEGLGAGEGRFAGGGGGGEYMEQEEDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRPDKGKMRFHKIANVNKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDAEDIVNTPKPDEKAIMTYVSCFYHAFAGAEQAETAANRICKVLAVNQENEKLMEGYEKLASELLEWIRRTVPWLENRVGEPSMSAMQRKLEDFRDYRRLHKPPRIQEKCQLEINFNTLQTKLRLSHRPAFMPSEGKLVSDIANAWRGLEQVEKGYEDWLLSEIRRLQRLQHLAEKFRQKASLHEAWTRGKEEMLSQRDYDSALLQEVRALLRRHEAFESDLAAHQDRVEHIAALAQELNELDYHEAASVNSRCQAICDQWDNLGTLTQKRRDALERMEKLLETIDQLQLEFARRAAPFNNWLDGAVEDLQDVWLVHSVEETQSLLTAHDQFKATLPEADRERGAIMGIQGEIQKICQTYGLRPCSTNPYITLSPQDINTKWDMVRKLVPSRDQTLQEELARQQVNERLRRQFAAQANAIGPWIQAKVEEVGRLAAGLAGSLEEQMAGLRQQEQNIINYKTNIDRLEGDHQLLQESLVFDNKHTVYSMEHIRVGWEQLLTSIARTINEVENQVLTRDAKGLSQEQLNEFRASFNHFDRKRNGMMEPDDFRACLISMGYDLGEVEFARIMTMVDPNTAGVVTFQAFIDFMTRETAETDTTEQVVASFKILAGDKNYITPEELRRELPAKQAEYCIRRMVPYKGSGAPAGALDYVAFSSALYGESDL
Protein: Sucrose transport protein SUT2 (SUC4-like protein) (Sucrose permease 2) (Sucrose transporter 2) (OsSUT2) (Sucrose-proton symporter 2) (Q0ILJ3)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Responsible for the transport of sucrose into the cell, with the concomitant uptake of protons (symport system). May also transport other glucosides (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MPRRPSGGGGGAGPAAAAVRKVPLRKLLRAASVACGVQFGWALQLSLLTPYVQELGIPHAFASLVWLCGPLSGLLVQPLVGHLSDRIAPAASPLGRRRPFIAAGAASIAAAVLTVGFSADLGRIFGDSITPGSTRLGAIIVYLVGFWLLDVGNNATQGPCRAFLADLTENDPRRTRIANAYFSLFMALGNILGYATGAYSGWYKIFPFTVTPSCSISCANLKSAFLLDIIILVVTTCITVASVQEPQSFGSDEADHPSTEQEAFLWELFGSFRYFTLPVWMVLIVTALTWIGWFPFILFDTDWMGREIYRGSPDDPSITQSYHDGVRMGSFGLMLNSVLLGFTSIVLEKLCRKWGAGLVWGVSNILMALCFVAMLVITYVAKNMDYPPSGVPPTGIVIASLVVFTILGAPLAITYSIPYAMAASRVENLGLGQGLAMGILNLAIVIPQVIVSLGSGPWDQLFGGGNAPAFAVAAAASFIGGLVAILGLPRARIASRRRGHR
Protein: RAR-related orphan receptor C (A0A8I5ZN69)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004334}.
Interaction partners:
Sequence:
MIRLACKSYHVDFQKNILIYLQGLTDSAHELLAAKKTHTSQIEVIPCKICGDKSSGIHYGVITCEGCKGFFRRSQQCNVAYSCTRQQNCPIDRTSRNRCQHCRLQKCLALGMSRDAVKFGRMSKKQRDSLHAEVQKQLQQQQQREQVAKTPPAGSHGADTLTYTLGVPDGQLPLGASPDLPEASACPPGLLRASGSGPPYSNTLAKTEVQGASCHLEYSPERGKAEGRDSIYSTDGQLTLGRRGLQLGEPEQGSDSHCSPSFCSAPEAPYASLTDIEYLVQNVCKSYRETCQLRLEDLLRQRTNLFSREEVTSYQRKSMWEMWERCAHHLTEAIQYVVEFAKRLSGFMELCQNDQIILLKAGAMEVVLVRMCRAYNANNHTVFFEGKYGGVELFRALGCSELISSIFDFSHFLSALCFSEDEIALYTALVLINANRPGLQEKRRVEHLQYNLELAFHHHLCKTHRQGLLAKLPPKGKLRSLCSQHVEKLQDFQHLHPIVVQAAFPPLYKELFSTDIESSEGLSK
Protein: Oxidation resistance protein 1 (Meiotically up-regulated gene 63 protein) (O14284)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May be involved in protection from oxidative damage (By similarity). Has a role in meiosis.
Subcellular location: Mitochondrion {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- V-type proton ATPase subunit B
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit D
- Ceramide-binding protein svf1
- V-type proton ATPase subunit C
- V-type proton ATPase subunit E
- V-type proton ATPase subunit G
- Zinc finger chaperone zpr1
- DnaJ protein homolog xdj1
- V-type proton ATPase subunit F
Sequence:
MFNFTRQYSVKDGLITDELASHIVENLPARYASAETWKRIYSLQHDGASLQTMYLACEKEKARSGHPKGACILAVRDTDGDVFGVFIPDYLIPAPHYFGSEETFLWKYFPPKKYVHYPFVGNSNFVAYCTKSFLAFGGGNGRYSLWLDGSLEYAYSSRTPAFENNPLSYRGCPDQRIQIVDIELWVLE
Protein: Mce-family protein Mce1C (O07415)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Conserved integral membrane protein YrbE1A
- Mce-family protein Mce1A
- Conserved integral membrane protein YrbE1B
- Possible Mce-family lipoprotein LprK
- Mce-family protein Mce1B
- Mce-family protein Mce1F
- Mce-family protein Mce1D
- Probable ribonucleotide transport ATP-binding protein mkl
- Probable fatty-acid-CoA ligase FadD5
- Conserved hypothetical integral membrane protein YrbE2A
Sequence:
MRTLEPPNRMRIGLMGIVVALLVVAVGQSFTSVPMLFAKPSYYGQFTDSGGLHKGDRVRIAGLGVGTVEGLKIDGDHIVVKFSIGTNTIGTESRLAIRTDTILGRKVLEIEPRGAQALPPGGVLPVGQSTTPYQIYDAFFDVTKAASGWDIETVKRSLNVLSETVDQTYPHLSAALDGVAKFSDTIGKRDEQITHLLAQANQVASILGDRSEQVDRLLVNAKTLIAAFNERGRAVDALLGNISAFSAQVQNLINDNPNLNHVLEQLRILTDLLVDRKEDLAETLTILGRFSASFGETFASGPYFKVLLANLVPGQILQPFVDAAFKKRGISPEDFWRSAGLPAYRWPDPNGTRFPNGAPPPPPPVLEGTPEHPGPAVPPGSPCSYTPPADGLPRPWDPLPCANLTQGPFGGPDFPAPLDVATSPPNPDGPPPAPGLPIAGRPGEVPPNVPGTPVPIPQEAPPGARTLPLGPAPGPAPPPAAPGPPAPPGPGPQLPAPFINPGGTGGSGVTGGSEN
Protein: Extracellular calcium-sensing receptor (CaR) (CaSR) (hCasR) (Parathyroid cell calcium-sensing receptor 1) (PCaR1) (P41180)
Organism: Homo sapiens (Human)
Function: G-protein-coupled receptor that senses changes in the extracellular concentration of calcium ions and plays a key role in maintaining calcium homeostasis. Senses fluctuations in the circulating calcium concentration and modulates the production of parathyroid hormone (PTH) in parathyroid glands (By similarity). The activity of this receptor is mediated by a G-protein that activates a phosphatidylinositol-calcium second messenger system. The G-protein-coupled receptor activity is activated by a co-agonist mechanism: aromatic amino acids, such as Trp or Phe, act concertedly with divalent cations, such as calcium or magnesium, to achieve full receptor activation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15572418, ECO:0000269|PubMed:16740594, ECO:0000269|PubMed:17555508, ECO:0000269|PubMed:19789209, ECO:0000269|PubMed:20861236, ECO:0000269|PubMed:22114145, ECO:0000269|PubMed:22789683, ECO:0000269|PubMed:25104082, ECO:0000269|PubMed:25766501, ECO:0000269|PubMed:26386835, ECO:0000269|PubMed:8702647}; Multi-pass membrane protein {ECO:0000269|PubMed:20861236}.
Interaction partners:
- Guanine nucleotide-binding protein subunit alpha-11
- Guanine nucleotide-binding protein G
- G-protein coupled receptor family C group 6 member A
- Parathyroid hormone
- Chorion-specific transcription factor GCMb
- Guanine nucleotide-binding protein G
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1
- Gamma-aminobutyric acid type B receptor subunit 1
Sequence:
MAFYSCCWVLLALTWHTSAYGPDQRAQKKGDIILGGLFPIHFGVAAKDQDLKSRPESVECIRYNFRGFRWLQAMIFAIEEINSSPALLPNLTLGYRIFDTCNTVSKALEATLSFVAQNKIDSLNLDEFCNCSEHIPSTIAVVGATGSGVSTAVANLLGLFYIPQVSYASSSRLLSNKNQFKSFLRTIPNDEHQATAMADIIEYFRWNWVGTIAADDDYGRPGIEKFREEAEERDICIDFSELISQYSDEEEIQHVVEVIQNSTAKVIVVFSSGPDLEPLIKEIVRRNITGKIWLASEAWASSSLIAMPQYFHVVGGTIGFALKAGQIPGFREFLKKVHPRKSVHNGFAKEFWEETFNCHLQEGAKGPLPVDTFLRGHEESGDRFSNSSTAFRPLCTGDENISSVETPYIDYTHLRISYNVYLAVYSIAHALQDIYTCLPGRGLFTNGSCADIKKVEAWQVLKHLRHLNFTNNMGEQVTFDECGDLVGNYSIINWHLSPEDGSIVFKEVGYYNVYAKKGERLFINEEKILWSGFSREVPFSNCSRDCLAGTRKGIIEGEPTCCFECVECPDGEYSDETDASACNKCPDDFWSNENHTSCIAKEIEFLSWTEPFGIALTLFAVLGIFLTAFVLGVFIKFRNTPIVKATNRELSYLLLFSLLCCFSSSLFFIGEPQDWTCRLRQPAFGISFVLCISCILVKTNRVLLVFEAKIPTSFHRKWWGLNLQFLLVFLCTFMQIVICVIWLYTAPPSSYRNQELEDEIIFITCHEGSLMALGFLIGYTCLLAAICFFFAFKSRKLPENFNEAKFITFSMLIFFIVWISFIPAYASTYGKFVSAVEVIAILAASFGLLACIFFNKIYIILFKPSRNTIEEVRCSTAAHAFKVAARATLRRSNVSRKRSSSLGGSTGSTPSSSISSKSNSEDPFPQPERQKQQQPLALTQQEQQQQPLTLPQQQRSQQQPRCKQKVIFGSGTVTFSLSFDEPQKNAMAHRNSTHQNSLEAQKSSDTLTRHEPLLPLQCGETDLDLTVQETGLQGPVGGDQRPEVEDPEELSPALVVSSSQSFVISGGGSTVTENVVNS
Protein: E3 ubiquitin-protein ligase XIAP (EC 2.3.2.27) (Baculoviral IAP repeat-containing protein 4) (RING-type E3 ubiquitin transferase XIAP) (X-linked inhibitor of apoptosis protein) (H0YZU0)
Organism: Taeniopygia guttata (Zebra finch) (Poephila guttata)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Caspase 7
- Caspase-3
- Caspase 9
- Direct IAP-binding protein with low pI
- Receptor-interacting serine/threonine-protein kinase 2
- Receptor-interacting serine/threonine-protein kinase 2-like
- Baculoviral IAP repeat containing 2
- Receptor interacting serine/threonine kinase 1
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 1
- TNF receptor-associated factor
Sequence:
MSHSDACASADTDGAREWAQERERQGTFVGFPQGCPVSVLALAQAGFVYTGEGDKVKCFSCHTTIEGWVPGDSALERHKKLAPNCKFITESAFLESDMDPVAQNYQNRTENGTSNSALPCALDDPDVETDYLLRTRQVVDMSDSLYPKNPAMCSEETRLKSFHNWPLNDQLTPQELANAGFYYTGVGDQVACFCCGGKLKNWEPSDRAWSEHKRHFPKCLFVQGQDIGNVSSESIPSELGISGLNNAQHPRNPSMTKYGKRLQTFLSWIYPVAKERLAEAGFYSVGNGDHVVCFHCGGGLQEWKENEDPWDQHAKWFPGCRFVSNEKGIEFINNVHLKDGCRDSTVNDLLQNPWVQSAIAMGFSLSEIRNTMEKRLQMTGESHTSVEDLVADLSAHTENTREEEPNEIPVEQDELIQLQNLYLSTEEKLRRLQEEKLCKICMAKDVSVVFIPCGHLVACKECAQLLNECPLCRSDIMKIQEIFMY