wanglab/gogpt-training-data huggingface dataset:
Protein: Fructose-1,6-bisphosphatase class 2 (FBPase class 2) (EC 3.1.3.11) (D-fructose-1,6-bisphosphate 1-phosphohydrolase class 2) (Q6M6E7)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Function: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate. Is essential for growth on gluconeogenic carbon sources. Also displays a low activity toward glucose 6-phosphate, and fructose 6-phosphate, glycerol 3-phosphate, ribulose 1,5-bisphosphate and myo-inositol-monophosphate are not significant substrates.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Transketolase
- Fructose-bisphosphate aldolase
- Transaldolase
- Glucose-6-phosphate isomerase
- ATP-dependent 6-phosphofructokinase
- Fructose-1-phosphate kinase and related fructose-6-phosphate kinase
- Fructose-1-phosphate kinase and related fructose-6-phosphate kinase
- mannose-6-phosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase
- Glucose-6-phosphate 1-dehydrogenase
Sequence:
MNLKNPETPDRNLAMELVRVTEAAALASGRWVGRGMKNEGDGAAVDAMRQLINSVTMKGVVVIGEGEKDEAPMLYNGEEVGTGFGPEVDIAVDPVDGTTLMAEGRPNAISILAAAERGTMYDPSSVFYMKKIAVGPEAAGKIDIEAPVAHNINAVAKSKGINPSDVTVVVLDRPRHIELIADIRRAGAKVRLISDGDVAGAVAAAQDSNSVDIMMGTGGTPEGIITACAMKCMGGEIQGILAPMNDFERQKAHDAGLVLDQVLHTNDLVSSDNCYFVATGVTNGDMLRGVSYRANGATTRSLVMRAKSGTIRHIESVHQLSKLQEYSVVDYTTAT
Protein: Beta-1,3-galactosyltransferase bre-5 (EC 2.4.1.-) (Bacillus thuringiensis toxin-resistant protein 5) (Bt toxin-resistant protein 5) (Q95US5)
Organism: Caenorhabditis elegans
Function: Transfers N-acetylgalactosamine onto mannose groups of carbohydrate substrates. Required for susceptibility to pore-forming crystal toxins in conjunction with bre-1, bre-2, bre-3, and bre-4. Involved in resistance to the nematotoxic C.cinerea galectin Cgl2.
Subcellular location: Golgi apparatus membrane {ECO:0000255, ECO:0000305}; Single-pass type II membrane protein {ECO:0000255, ECO:0000305}.
Interaction partners:
- Beta-1,4-N-acetylgalactosaminyltransferase bre-4
- Beta-1,4-mannosyltransferase bre-3
- Galactoside 2-alpha-L-fucosyltransferase
Sequence:
MFLCVRILKRKYHELSSFQKLLIFTITIFLLWVLGVVDKFRETSFGDFSWPLETRNLQLRSKFTKYPQCKFSGNGQKIIIIIIKSSAKNGPMRESVRKTWGVFRMIDGVEVMPIFIVGRVENMEIMRRIDVESEKYKDILAISDIDSYRNNTLKLFGAIDYAANPNQCSSPDFTFLVDDDYLVHIPNLVKFAKTKQKEELVYEGFVFDTSPFRLKIHKHSISLNEYPFSRYPPYVSAGAVFLTSETIARFRNSIRKLKMFPFDDVFTGILAKTVNVAATHNENFIFWCRRVSQKEWDDGVIAVHGYARKDLEYEYSQLNGFE
Protein: Protocadherin-11 (Q8CH63)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
PFRLRPVFSNQFLLETAAFLDFESTREYAIKLLAADAGKPPLNQSSMLLIKVKDENDNAPVFTQSFISLSVPENNSPGAQLTKISATDADSGQNAEISYMLGFDAPPEFNLDQRTGILTAVKKLDREKQEKYYFTVLAQDNGIPPLMSNATVFVTVLDQNDNSPIFTHNEYNFYVPESLPKHGTVGLITVTDPDYGENSAVTLSILDVNDQFTIDPQSGVIRPNISFDRERQESYTFYVKAEDGGRVSRSSTARVTINVVDVNDNKPIFIDPPSNYSFEWVLPSTNPGTVVFKVVAIDDDIGMNAEVLYSIVGGNTKGLFMIEQTSGNITLKEKCMVSDLGLHRVIVKANDLGQPDSLFNVVNVNFFINESVPNATLIYELVRRSIDAPANQNTETTSASSPTTDYVKIMVAIVAGTITVVLVIFITAVVRSPQP
Protein: Hexon-interlacing protein (Protein IX) (P03281)
Organism: Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Function: Structural component of the virion that acts as a cement protein on the capsid exterior and forms triskelion structures consisting of three molecules that stabilize three hexon trimers at the center of each icosahedral facet and fixes the peripentonal hexons. Dispensable for assembly. During virus entry, recruits the anterograde motor kinesin-1 to the capsid docked at the nuclear pore complex thereby subjecting the docked capsid to a pulling force. The resulting tension leads to capsid disruption, dispersion of capsid fragments toward cell periphery and eventually viral DNA entry into the host nucleus.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04050, ECO:0000269|PubMed:20798312, ECO:0000269|PubMed:25071205}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04050, ECO:0000305|PubMed:20798312}. Note=Located in the canyons between the hexons on the outer surface of the capsid. Forms a sort of hairnet on the outer side of the virion. Present in 240 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04050, ECO:0000269|PubMed:20798312, ECO:0000269|PubMed:25071205}.
Interaction partners:
Sequence:
MSTNSFDGSIVSSYLTTRMPPWAGVRQNVMGSSIDGRPVLPANSTTLTYETVSGTPLETAASAAASAAAATARGIVTDFAFLSPLASSAASRSSARDDKLTALLAQLDSLTRELNVVSQQLLDLRQQVSALKASSPPNAV
Protein: Utrophin (A0A1W2P7C0)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004202}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Postsynapse {ECO:0000256|ARBA:ARBA00034110}.
Interaction partners:
Sequence:
MIGLNFSLRELLTKFEKDIQAEIDAHNDIFKSIDGNRQKMVKALGNSEEATMLQHRLDDMNQRWNDLKAKSASIRAHLEASAEKWNRLLASLEELIKWLNMKDEELKKQMPIGGDVPALQLQYDHCKVLRRELKEKEYSVLNAVDQARVFLADQPIEAPEEPRRNPQSKTELTPEERAQKIAKAMRKQSSEVREKWENLNAVTSNWQKQVGKALEKLRDLQGAMDDLDADMKEVEAVRNGWKPVGDLLIDSLQDHIEKTLAFREEIAPINLKVKTMNDLSSQLSPLDLHPSLKMSRQLDDLNMRWKLLQVSVDDRLKQLQEAHRDFGPSSQHFLSTSVQLPWQRSISHNKVPYYINHQTQTTCWDHPKMTELFQSLADLNNVRFSAYRTAIKIRRLQKALCLDLLELNTTNEVFKQHKLNQNDQLLSVPDVINCLTTTYDGLEQLHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLMSLSKGLLEEKYRCLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFIDWMHLEPQSMVWLPVLHRVAAAETAKHQAKCNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHKLHYPMVEYCIPTTSGEDVRDFTKVLKNKFRSKKYFAKHPRLGYLPVQTVLEGDNLETPITLISMWPEHYDPSQSPQLFHDDTHSRIEQYATRLAQMERTNGSFLTDSSSTTGSVEDEHALIQQYCQTLGGESPVSQPQSPAQILKSVEREERGELERIIADLEEEQRNLQVEYEQLKEQHLRRGLPVGSPPDSIVSPHHTSEDSELIAEAKLLRQHKGRLEARMQILEDHNKQLESQLHRLRQLLEQPDSDSRINGVSPWASPQHSALSYSLDTDPGPQFHQAASEDLLAPPHDTSTDLTDVMEQINSTFPSCSSNVPSRPQAM
Protein: RanBP-type and C3HC4-type zinc finger-containing protein 1 (SHANK-associated RH domain-interacting protein) (X1WDE8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- RanBP-type and C3HC4-type zinc finger-containing protein 1
- RanBP-type and C3HC4-type zinc finger-containing protein 1
- Uncharacterized protein.
- Receptor
- Tumor necrosis factor receptor superfamily, member 1a.
- Receptor-interacting serine-threonine kinase 2.
- Lymphotoxin-alpha
- X-linked inhibitor of apoptosis.
- Tnf receptor-associated factor 5.
- RING-type E3 ubiquitin transferase
Sequence:
MSTSTGCSTVLMSVRVSVRPLPVGSDSLRLQLSMNPNRAGLFTLTLRHTDRGGRSVSLAEFDLRSVQYELKSPRCHELRLLKPPHDCLSFSFRSEQEAQEWATVVMSSLRESHRVASICQEGLQYVKSGEKSAVLSLSMKEELCVELSRAIEAGDAQAAARYATDLAQQQMTLSIQPAPRDTDDKDISLAVIVEDASSSCCVTVKIHPHVTVASLKQQMFVEYGFHPRVQRWIISQCLCSDSRSVSSYGVCRDGDTAFLYLLSAGHASLSQQQENGLSVPTAAPANASLSAPAGGGSSGHDWRAYSTLPPRFSHASTGSGGSEKPSVTDIINLEMLQLGGSKLKSSNTQSGWPCPSCTFINKSTRPGCEICSTDRPNPPHHTHLQQEKSRRSNQ
Protein: Latent-transforming growth factor beta-binding protein 1 (LTBP-1) (Transforming growth factor beta-1-binding protein 1) (TGF-beta1-BP-1) (Q14766)
Organism: Homo sapiens (Human)
Function: Key regulator of transforming growth factor beta (TGFB1, TGFB2 and TGFB3) that controls TGF-beta activation by maintaining it in a latent state during storage in extracellular space. Associates specifically via disulfide bonds with the Latency-associated peptide (LAP), which is the regulatory chain of TGF-beta, and regulates integrin-dependent activation of TGF-beta. Outcompeted by LRRC32/GARP for binding to LAP regulatory chain of TGF-beta.
Subcellular location: Secreted {ECO:0000269|PubMed:16157329}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:16157329, ECO:0000269|PubMed:8617200}.
Interaction partners:
- Transforming growth factor beta-1 proprotein
- Fibrillin-1
- Transforming growth factor beta-3 proprotein
- Transforming growth factor beta-2 proprotein
- Thrombospondin-1
- ADAMTS-like protein 2
- Fibronectin
- A disintegrin and metalloproteinase with thrombospondin motifs 10
- Latent-transforming growth factor beta-binding protein 2
- Latent-transforming growth factor beta-binding protein 3
Sequence:
MAGAWLRWGLLLWAGLLASSAHGRLRRITYVVHPGPGLAAGALPLSGPPRSRTFNVALNARYSRSSAAAGAPSRASPGVPSERTRRTSKPGGAALQGLRPPPPPPPEPARPAVPGGQLHPNPGGHPAAAPFTKQGRQVVRSKVPQETQSGGGSRLQVHQKQQLQGVNVCGGRCCHGWSKAPGSQRCTKPSCVPPCQNGGMCLRPQLCVCKPGTKGKACETIAAQDTSSPVFGGQSPGAASSWGPPEQAAKHTSSKKADTLPRVSPVAQMTLTLKPKPSVGLPQQIHSQVTPLSSQSVVIHHGQTQEYVLKPKYFPAQKGISGEQSTEGSFPLRYVQDQVAAPFQLSNHTGRIKVVFTPSICKVTCTKGSCQNSCEKGNTTTLISENGHAADTLTATNFRVVICHLPCMNGGQCSSRDKCQCPPNFTGKLCQIPVHGASVPKLYQHSQQPGKALGTHVIHSTHTLPLTVTSQQGVKVKFPPNIVNIHVKHPPEASVQIHQVSRIDGPTGQKTKEAQPGQSQVSYQGLPVQKTQTIHSTYSHQQVIPHVYPVAAKTQLGRCFQETIGSQCGKALPGLSKQEDCCGTVGTSWGFNKCQKCPKKPSYHGYNQMMECLPGYKRVNNTFCQDINECQLQGVCPNGECLNTMGSYRCTCKIGFGPDPTFSSCVPDPPVISEEKGPCYRLVSSGRQCMHPLSVHLTKQLCCCSVGKAWGPHCEKCPLPGTAAFKEICPGGMGYTVSGVHRRRPIHHHVGKGPVFVKPKNTQPVAKSTHPPPLPAKEEPVEALTFSREHGPGVAEPEVATAPPEKEIPSLDQEKTKLEPGQPQLSPGISTIHLHPQFPVVIEKTSPPVPVEVAPEASTSSASQVIAPTQVTEINECTVNPDICGAGHCINLPVRYTCICYEGYRFSEQQRKCVDIDECTQVQHLCSQGRCENTEGSFLCICPAGFMASEEGTNCIDVDECLRPDVCGEGHCVNTVGAFRCEYCDSGYRMTQRGRCEDIDECLNPSTCPDEQCVNSPGSYQCVPCTEGFRGWNGQCLDVDECLEPNVCANGDCSNLEGSYMCSCHKGYTRTPDHKHCRDIDECQQGNLCVNGQCKNTEGSFRCTCGQGYQLSAAKDQCEDIDECQHRHLCAHGQCRNTEGSFQCVCDQGYRASGLGDHCEDINECLEDKSVCQRGDCINTAGSYDCTCPDGFQLDDNKTCQDINECEHPGLCGPQGECLNTEGSFHCVCQQGFSISADGRTCEDIDECVNNTVCDSHGFCDNTAGSFRCLCYQGFQAPQDGQGCVDVNECELLSGVCGEAFCENVEGSFLCVCADENQEYSPMTGQCRSRTSTDLDVDVDQPKEEKKECYYNLNDASLCDNVLAPNVTKQECCCTSGVGWGDNCEIFPCPVLGTAEFTEMCPKGKGFVPAGESSSEAGGENYKDADECLLFGQEICKNGFCLNTRPGYECYCKQGTYYDPVKLQCFDMDECQDPSSCIDGQCVNTEGSYNCFCTHPMVLDASEKRCIRPAESNEQIEETDVYQDLCWEHLSDEYVCSRPLVGKQTTYTECCCLYGEAWGMQCALCPLKDSDDYAQLCNIPVTGRRQPYGRDALVDFSEQYTPEADPYFIQDRFLNSFEELQAEECGILNGCENGRCVRVQEGYTCDCFDGYHLDTAKMTCVDVNECDELNNRMSLCKNAKCINTDGSYKCLCLPGYVPSDKPNYCTPLNTALNLEKDSDLE
Protein: Fatty acyl-CoA reductase (EC 1.2.1.84) (O46038)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MHHPLSGEMEEFFEDSEIFVTGGSGVVGKALVEKLLRSCNVRRIYVLLRPRKQLTAEQRLVRLRQATVFHVLAVQKPEELDKIVAVPGDVSLPGLGIDPSMMQRMKGVSLVYHCAATVRFDEPLREAVRLNVGGTLEALKFAETLPQLRAFIHVSTFYSNPYLTRVEPKEYTWLSTCVLPGCTLYNAISFGYLMAPCPRLIMGFPNTYTFTKNLAESLVNDYRHRLPVIVYRPSIVLFAVEDPSPGFSPSLMGAMGLFALVGAGILKTVYLGKDIRLDITPQDIGIKSMLCYTKMGYDIYRRGPPADLPVFLSSSCTHVPHTFTQIAEQMDTLDLWRDVAFEKNLMIPGCHYTDKRWAYQFLVFTKQILPALILDLLLRIFGQKPVLMSAVRKAYQTLEVMQPFMFNNWDSPGVSDMETLSKHGEGSAFNFDAFNHPDIHGLVIQSCSNMLHSIRTHLLREDPKTLERSKRILRM
Protein: COUP transcription factor 2 (COUP-TF2) (Apolipoprotein A-I regulatory protein 1) (ARP-1) (COUP transcription factor II) (COUP-TF II) (COUPb) (Nuclear receptor subfamily 2 group F member 2) (Ovalbumin upstream promoter beta nuclear receptor) (O09018)
Organism: Rattus norvegicus (Rat)
Function: Ligand-activated transcription factor. Activated by high concentrations of 9-cis-retinoic acid and all-trans-retinoic acid, but not by dexamethasone, cortisol or progesterone (in vitro). Regulation of the apolipoprotein A-I gene transcription. Binds to DNA site A. May be required to establish ovary identity during early gonad development.
Subcellular location: Nucleus.
Interaction partners:
- Nuclear receptor corepressor 2
- SRY-box transcription factor 18
- Nuclear receptor corepressor 1
- Hepatocyte nuclear factor 1-beta
Sequence:
MAMVVSTWRDPQDEVPGSQGSQASQAPPVPGPPPGAPHTPQTPGQGGPASTPAQTAAGSQGGPGGPGSDKQQQQQHIECVVCGDKSSGKHYGQFTCEGCKSFFKRSVRRNLSYTCRANRNCPIDQHHRNQCQYCRLKKCLKVGMRREAVQRGRMPPTQPTHGQFALTNGDPLNCHSYLSGYISLLLRAEPYPTSRFGSQCMQPNNIMGIENICELAARMLFSAVEWARNIPFFPDLQITDQVALLRLTWSELFVLNAAQCSMPLHVAPLLAAAGLHASPMSADRVVAFMDHIRIFQEQVEKLKALHVDSAEYSCLKAIVLFTSDACGLSDVAHVESLQEKSQCALEEYVRSQYPNQPTRFGKLLLRLPSLRTVSSSVIEQLFFVRLVGKTPIETLIRDMLLSGSSFNWPYMAIQ
Protein: N-acylneuraminate cytidylyltransferase A (EC 2.7.7.43) (CMP-sialic acid synthetase 1) (Q0E671)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalyzes the activation of N-acetylneuraminic acid (NeuNAc) to cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-NeuNAc), a substrate required for the addition of sialic acid. Also has activity towards N-glycolylneuraminic acid (Neu5Gc). Has weak activity towards 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN).
Subcellular location: Nucleus {ECO:0000269|PubMed:22351762}.
Interaction partners:
- N-acetylneuraminic acid synthase a.
- Cytidine monophosphate-N-acetylneuraminic acid hydroxylase
- N-acetylneuraminic acid phosphatase.
- N-acetylneuraminic acid synthase b.
- exo-alpha-sialidase
- Uncharacterized protein
- exo-alpha-sialidase
- Alpha-2,8-sialyltransferase 8E
- Sialidase-1
- Inorganic pyrophosphatase 1a.
Sequence:
MDAVNENGKRAMKDDSHGNSTSPKRRKSRHISALILARGGSKGIPLKNIKMLAGVPLIGWVIRAAVDSNVFNSVWVSTDHEEIAKVALAWGAKVHKRSPEVSQDSSSSLDTIREFSRQHREVDVICNIQATSPCLHPKHLTEAVELITKQGYDSVFSVVRRHNFRWKEVEKGGDCSTEPMNLNPACRPRRQDWSGELCENGSFYFAKKELIEQGLLQGGKKTYYEMKPEYSVDIDVDIDWPVAEQRVLRFGYFGKDKPEVVRLLLCNVSGCLTDGQIYTSASGEEMVSINIRDQIGISMLKKEGVKVILLETYPIAKALAVRLSERMGCPLLHHMDDKLKEVERIMVEEKLEWKEVAYLGNDEADVKCLELAGLSGVPVDAPTVALNHTKYTCHNAAGHGAVREFAEHILLLKKKAKSQMEQDRICRDAF
Protein: Dynamin-1-like protein drp-1 (EC 3.6.5.5) (Dynamin-related protein drp-1) (Q8WQC9)
Organism: Caenorhabditis elegans
Subcellular location: Mitochondrion {ECO:0000269|PubMed:10619028, ECO:0000269|PubMed:21949250}. Mitochondrion outer membrane {ECO:0000269|PubMed:10619028}. Cytoplasm, cytosol {ECO:0000269|PubMed:21949250}. Note=Localized to sites of mitochondrial scission (PubMed:10619028). May be recruited to the mitochondrial surface by a ced-9/egl-1 complex (PubMed:21949250). {ECO:0000269|PubMed:10619028, ECO:0000269|PubMed:21949250}.
Interaction partners:
- FIS1-related protein fis-1
- Transmembrane GTPase fzo-1
- FIS1-related protein fis-2
- E3 ubiquitin-protein ligase parkin
- Serine/threonine-protein kinase pink-1, mitochondrial
- Endoplasmic reticulum transmembrane protein
- Mitochondrial fission factor
- Mitoferrin
- Actin
- Intersectin-1
Sequence:
MENLIPVVNKLQDVFATLGRKEDQIQLPQIVVVGSQSAGKSSVLENLVGRDFLPRGTGIVTRRPLILQLNHVALDDESKRRRSNGTLLTDDWAMFEHTGSKVFTDFDAVRKEIEDETDRVTGVNKGISLLPISLKIYSHRVVSLSLVDLPGITKIPVGDQPVNIEEQIREMILLYISNPSSIILAVTPANQDFATSEPIKLAREVDAGGQRTLAVLTKLDLMDQGTDAMDVLMGKVIPVKLGIIGVVNRSQQNILDNKLIVDAVKDEQSFMQKKYPTLASRNGTPYLAKRLNMLLMHHIRNCLPALKARVSIMNAQCQSDLVAFGEPVEDKNRTLLQIITRFATAYTSTIEGTARNIETTELCGGARICYIFHDTFGRSLESVNPLENLTQLDILTAIRNATGPRPALFVPEVSFELLVKRQIQRLEEPSLRCVELVHEEMQRMVQHCGFTTQQEMIRFPRLYDKINEVVSGVLKERLKPTNELVENLVAIELAYINTKHPEFTEANLVTLLKEELLLDDRHGRSRNRHASTGERAVSAHGEQQLQPVPGVNGVDLNAVLQQQQQQSQNQRASNGFLGLFGNAAASSKTSPQEKQSANFLPEVPETQLGRKLTSREQRDVAIIERLIRNYFIIVRKNIQDSVPKAIMALLVNFVRDNLQSELVRQLYKPDEMDDLLAETEDMAQRRRDTLETMKALQQASVIISEVRETQVW
Protein: Histone-lysine N-methyltransferase ASHH3 (EC 2.1.1.-) (ASH1 homolog 3) (Protein SET DOMAIN GROUP 7) (Q945S8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Histone methyltransferase.
Subcellular location: Nucleus {ECO:0000250}. Chromosome, centromere {ECO:0000250}. Note=Associates with centromeric constitutive heterochromatin. {ECO:0000250}.
Interaction partners:
- Calmodulin-lysine N-methyltransferase
- Histone H3-like centromeric protein CENH3
- Histone-lysine N-methyltransferase ATXR5
- Histone-lysine N-methyltransferase ATXR6
- Protein SET DOMAIN GROUP 41
- Histone H3.1
- Histone H3-like 4
- Histone H3-like 5
- Histone H3-like 1
- Histone H3-like 3
Sequence:
MPASKKISDRNHLGQVFDKLLNQIGESEEFELPEWLNKGKPTPYIFIRRNIYLTKKVKRRVEDDGIFCSCSSSSPGSSSTVCGSNCHCGMLFSSCSSSCKCGSECNNKPFQQRHVKKMKLIQTEKCGSGIVAEEEIEAGEFIIEYVGEVIDDKTCEERLWKMKHRGETNFYLCEITRDMVIDATHKGNKSRYINHSCNPNTQMQKWIIDGETRIGIFATRGIKKGEHLTYDYQFVQFGADQDCHCGAVGCRRKLGVKPSKPKIASDEAFNLVAHELAQTLPKVHQNGLVNRHIDAGKSWNNLSQRDTCSRNCIGVVIRLSRPTSDRCFGLVRHFDEYSRKHSVMFEDGVTEFVDMSREDWEIV
Protein: Excitatory amino acid transporter 3 (Excitatory amino-acid carrier 1) (Sodium-dependent glutamate/aspartate transporter 3) (Solute carrier family 1 member 1) (P51907)
Organism: Rattus norvegicus (Rat)
Function: Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. Can also transport L-cysteine. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion. Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport. Plays an important role in L-glutamate and L-aspartate reabsorption in renal tubuli (By similarity). Plays a redundant role in the rapid removal of released glutamate from the synaptic cleft, which is essential for terminating the postsynaptic action of glutamate (By similarity). Contributes to glutathione biosynthesis and protection against oxidative stress via its role in L-glutamate and L-cysteine transport (By similarity). Negatively regulated by ARL6IP5.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11242046, ECO:0000269|PubMed:19720795, ECO:0000269|PubMed:9011753}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P43003}. Apical cell membrane {ECO:0000250|UniProtKB:P43005}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P43003}. Synapse, synaptosome {ECO:0000250|UniProtKB:P51906}. Early endosome membrane {ECO:0000250|UniProtKB:P51906}. Late endosome membrane {ECO:0000250|UniProtKB:P51906}. Recycling endosome membrane {ECO:0000250|UniProtKB:P51906}.
Interaction partners:
- Excitatory amino acid transporter 4
- PRA1 family protein 3
- Amino acid transporter heavy chain SLC3A1
- Glutamate receptor ionotropic, NMDA 2A
- Sodium-dependent neutral amino acid transporter B
- Disks large-associated protein 3
- Sodium- and chloride-dependent GABA transporter 1
Sequence:
MGKPTSSGCDWRRFLRNHWLLLSTVAAVVLGIVVGVLVRGHSELSNLDKFYFAFPGEILMRMLKLVILPLIISSMITGVAALDSNVSGKIGLRAVVYYFSTTVIAVILGIVLVVSIKPGVTQKVNEINRTGKTPEVSTVDAMLDLIRNMFPENLVQACFQQYKTKREEVKPASDPGGNQTEVSVTTAMTTMSENKTKEYKIVGLYSDGINVLGLIIFCLVFGLVIGKMGEKGQILVDFFNALSDATMKIVQIIMCYMPIGILFLIAGKIIEVEDWEIFRKLGLYMATVLSGLAIHSLVVLPLIYFIVVRKNPFRFALGMAQALLTALMISSSSATLPVTFRCAEEKNHVDKRITRFVLPVGATINMDGTALYEAVAAVFIAQLNGMDLSIGQIITISITATAASIGAAGVPQAGLVTMVIVLSAVGLPAEDVTLIIAVDWLLDRFRTMVNVLGDAFGTGIVEKLSKKELEQVDVSSEVNIVNPFALEPTILDNEDSDTKKSYVNGGFSVDKSDTISFTQTSQF
Protein: Rlm1p (A0A1D8PL95)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Mitogen-activated protein kinase MKC1
- Protein kinase C-like 1
- Transcription factor MBP1
- Mitogen-activated protein kinase HOG1
- Mitogen-activated protein kinase kinase kinase
- Extracellular signal-regulated kinase 1
- GTP-binding protein RHO1
- Transcriptional regulator SKO1
- Rho family guanine nucleotide exchange factor
- Transcriptional regulator
Sequence:
MGRRKIEIEPLTDDRNRTVTFVKRKAGLFKKAHELAVLCQVDLTVIIVGNNNKVYEYSTVEANEIFNAYNKTIKVRKQVHESKSPEYYSKFRKKRHLNEPLMNKSGSVVGTNTHLNDEDYDHNVHEAGDEDSEYESDDNSPQPKRHKRSESVKKEQNPKVFNSTQPPPPPPPPHISLNNVPTFTNPQNYKKQIDETNNTSAPPATGTKNEPTMQRPVLRVQIPNDAKSNTNNSHSGVNNSDGKDTARTVTAVDNSATNQNTQSSNTTSGTGTADTNSSQLNSNGNSNLVPANVPNTRFSGYSSFRSPDSRKPTLPLPLQTKSQTSSPASAVAPGLPLTGGSNAYFAGMQQSPVGGSYVNYPAQVYQQYQQFQNQLQLQEQQQQQQKQQSQPQPSSQSVGNQNAQLESAARFRSGLPTGTQFNNGEQTPISGLPSRYVNDMFPFPSPSNFLAPQDWPSGITPTTHLPQYFVNMPLSGIGSQQSQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQNAQQQSQVPVIPIQTQTSQQMASTTNHKSANLIPGFLQNPTQATGNSANASKSSDAGDGTNPTTAGSSSSADVNNTNNGPNKNT
Protein: Magnesium chelatase, putative (O69660)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MTQSASNPQAPPTQTPGAELPGYPPQAGGAPTAAPSGPHPHRAEAESARDALLALRAEVAKAVVGQDGVISGLVIALLCRGHVLLEGVPGVAKTLIVRAMSAALQLEFKRVQFTPDLMPGDVTGSLVYDARTAEFVFRPGPVFTNLLLADEINRTPPKTQAALLEAMEERQVSVEGEPKPLPNPFIVAATQNPIEYEGTYQLPEAQLDRFLLKLNVTLPARDSEIAILDRHAHGFDPRDLSAINPVAGPAELAAGREAVRHVLVANEVLGYIVDIVGATRSSPALQLGVSPRGATALLGTARSWAWLSGRDYVTPDDVKAMARPTLRHRVMLRPEAELEGATPDGVLDGILASVPVPR
Protein: Adapter protein unc-53 (Uncoordinated protein 53) (Q7YSI9)
Organism: Caenorhabditis elegans
Function: Involved in the migration and outgrowth of muscles, axons and excretory canals.
Interaction partners:
- SH3 domain-containing protein
- CRAL-TRIO domain-containing protein
- Netrin unc-6
Sequence:
MTTSNVELIPIYTDWANRHLSKGSLSKSIRDISNDFRDYRLVSQLINVIVPINEFSPAFTKRLAKITSNLDGLETCLDYLKNLGLDCSKLTKTDIDSGNLGAVLQLLFLLSTYKQKLRQLKKDQKKLEQLPTSIMPPAVSKLPSPRVATSATASATNPNSNFPQMSTSRLQTPQSRISKIDSSKIGIKPKTSGLKPPSSSTTSSNNTNSFRPSSRSSGNNNVGSTISTSAKSLESSSTYSSISNLNRPTSQLQKPSRPQTQLVRVATTTKIGSSKLAAPKAVSTPKLASVKTIGAKQEPDNSGGGGGGMLKLKLFSSKNPSSSSNSPQPTRKAAAVPQQQTLSKIAAPVKSGLKPPTSKLGSATSMSKLCTPKVSYRKTDAPIISQQDSKRCSKSSEEESGYAGFNSTSPTSSSTEGSLSMHSTSSKSSTSDEKSPSSDDLTLNASIVTAIRQPIAATPVSPNIINKPVEEKPTLAVKGVKSTAKKDPPPAVPPRDTQPTIGVVSPIMAHKKLTNDPVISEKPEPEKLQSMSIDTTDVPPLPPLKSVVPLKMTSIRQPPTYDVLLKQGKITSPVKSFGYEQSSASEDSIVAHASAQVTPPTKTSGNHSLERRMGKNKTSESSGYTSDAGVAMCAKMREKLKEYDDMTRRAQNGYPDNFEDSSSLSSGISDNNELDDISTDDLSGVDMATVASKHSDYSHFVRHPTSSSSKPRVPSRSSTSVDSRSRAEQENVYKLLSQCRTSQRGAAATSTFGQHSLRSPGYSSYSPHLSVSADKDTMSMHSQTSRRPSSQKPSYSGQFHSLDRKCHLQEFTSTEHRMAALLSPRRVPNSMSKYDSSAAALNASGMSRSMILLESLSPRPPRRHQSPADSCIITASPSAPRRSHSPRGPTARIPLSLASSPVHVNNNWGSYSARSRGGSSTGIYGETFQLHRLSDEKSPAHSAKSEMGSQLSLASTTAYGSLNEKYEHAIRDMARDLECYKNTVDSLTKKQENYGALFDLFEQKLRKLTQHIDRSNLKPEEAIRFRQDIAHLRDISNHLASNSAHANEGAGELLRQPSLESVASHRSSMSSSSKSSKQEKISLSSFGKNKKSWIRSSLSKFTKKKNKNYDEAHMPSISGSQGTLDNIDVIELKQELKERDSALYEVRLDNLDRAREVDVLRETVNKLKTENKQLKKEVDKLTNGPATRASSRASIPVIYDDEHVYDAACSSTSASQSSKRSSGCNSIKVTVNVDIAGEISSIVNPDKEIIVGYLAMPTSQSCWKDIDVSILGLFEVYLSRIDVEHQLGIDARDSILGYQIGELRRVIGDSTTMITSHPTDILTSSTTIRMFMHGAAQSRVDSLVLDMLLPKQMILQLVKSILTERRLVLAGATGIGKSKLAKTLAAYVSIRTNQSEDSIVNISIPENNKEELLQVERRLEKILRSKESCIVILDNIPKNRIAFVVSVFANVPLQNNEGPFVVCTVNRYQIPELQIHHNFKMSVMSNRLEGFILRYLRRRAVEDEYRLTVQMPSELFKIIDFFPIALQAVNNFIEKTNSVDVTVGPRACLNCPLTVDGSREWFIRLWNENFIPYLERVARDGKKTFGRCTSFEDPTDIVSEKWPWFDGENPENVLKRLQLQDLVPSPANSSRQHFNPLESLIQLHATKHQTIDNI
Protein: Retrotransposon hot spot (RHS) protein, putative (Q584M9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MWNSMRRFYTDGLHAARRFLKRLRGDEEGPTWTMNSSIEDVLLQRFAGLRDMKLHDLLNHHFGETLGTSNVSVGVFVQSPEDYIVNAKFLGRIQRLDEFQLLRAVIYLPRNRIEDIHQWEENATAQIREFVGPVAATKLDSALRIAKEARKRAHQTADGVELKGVYESIYNATWGYVESGHNDLPLGMKVVGNSDGEPELWTEEEVNVSHTPYDLCDPLPRHGNLEIAVLTSQEGWPYNSFSTPEHAIQEEAEEPGDYVFDGDVYIRREVMRVWYLVKHRLDLWLGPGVNKKQIPCVLVGTPGIGKSFGVGSFLLQRLLHYDSELLRNIAYFVKGRAYIFFRATNDHPGKVVFYEKEKDGLDAVEAFVVEKVLGYIIYDFWKDRHQPIPADLPGAWPVIVLTSPDPNNYKDWKEPRGCEFLCINCYEEVELKAAVAWRRLSKLEESKITEAHIINLENEWQKTLGWIKKVGPLARQVLEGEKRYKGRVREINEALAEISRGDDSHYMKVLNSRVQWRQDGTTYMLAKLVRVVTENGEECRNRAVSIDIEQKLRVWANTACMRDNYLRKVFRGKEERAADEFENVGVYAFTMGNVVQTIVTHLRYLPRVGEEMDSNVSVLASGNAVGRVPTSLRQFNPETTGQDIEVGCFYRPVQGNFPVVDAFFFVTEPAVDREGRAIITTTIVLLQATVAPTHHTTREKVDKFIKAMKQLFGEWDKLARNLKWELIYIQYSDSKPIEERQKCEPVGGRGDHTTELWNKINQFQVKMEGNIVKEITQDEPNAIAGGPAA
Protein: Olfactory receptor 4Q3 (Olfactory receptor 4Q4) (Olfactory receptor OR14-3) (Q8NH05)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
Sequence:
MKKEQDSNVTEFVLLGLSSSWELQLFLFLLFLFFYIAIVLGNLLIVVTVQAHAHLLQSPMYYFLGHLSFIDLCLSCVTVPKMLGDFLQQGKSISFSGCLAQIYFLHFLGASEMFLLTVMAYDRYVAICNPLRYLTVMNPQLCLWLVLACWCGGFIHSIMQVILVIQLPFCGPNELDNFYCDVPQVIKLACMDTYVVEVLVIANSGLLSLVCFLVLLFSYAIILITLRTHFCQGQNKVFSTCASHLTVVSLIFVPCVFIYLRPFCSFSVDKIFSLFYTVITPMLNPLIYTLRNTDMKTAMKKLRIKPCGIPLPC