wanglab/gogpt-training-data huggingface dataset:
Protein: Coatomer subunit gamma (Gamma-coat protein) (Gamma-COP) (Q0WW26)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}.
Interaction partners:
- Coatomer subunit delta
- Coatomer subunit alpha-2
- Coatomer subunit alpha-1
- Coatomer subunit beta-1
- Coatomer subunit beta-2
- Coatomer subunit epsilon-2
- Coatomer subunit beta'-1
- Coatomer subunit epsilon-1
- ARF guanine-nucleotide exchange factor GNL1
- Coatomer subunit beta'-2
Sequence:
MAQPLVKKDDDHDDELEYSPFMGIEKGAVLQEARVFNDPQVDPRRCSQVITKLLYLLNQGESFTKVEATEVFFSVTKLFQSKDTGLRRMVYLIIKELSPSSDEVIIVTSSLMKDMNSKIDMYRANAIRVLCRIIDGTLLTQIERYLKQAIVDKNPVVSSAALVSGLHLLKTNPEIVKRWSNEVQEGIQSRSALVQFHALALLHQIRQNDRLAVSKLVGSLTRGSVRSPLAQCLLIRYTSQVIRDMANHGQSGERPFYEFLESCLRHKAEMVILEAARAITELDGVTSRELTPAITVLQLFLSSPRPVLRFAAVRTLNKVAMTHPMAVTNCNIDMESLISDQNRSIATLAITTLLKTGNESSVERLMKQITNFMSDIADEFKIVVVDAIRSLCVKFPLKYRSLMTFLSNILREEGGFEYKRAIVDSIVTIIRDIPDAKESGLLHLCEFIEDCEFTYLSTQILHFLGIEGPNTSDPSKYIRYIYNRVHLENATVRAAAVSTLAKFGFMVESLKPRITVLLKRCIYDSDDEVRDRATLYLSVLGGDGTVDTDKESKDFLFGSLEVPLVNMETSLKNYEPSEEAFDINSVPKEVKSQPLAEKKAQGKKPTGLGAPPAAPASGFDGYERLLSSIPEFAAFGKLFKSSLPVELTEAETEYAVNVVKHIFDSHVVFQYNCTNTIPEQLLERVNVIVDASEAEEFSEVTSKALNSLPYDSPGQAFVVFEKPAGVPAVGKFSNTLTFVVKEVDPSTGEAEDDGVEDEYQLEDLEVVAGDYMVKVGVSNFRNAWESMDEEDERVDEYGLGQRESLGEAVKAVMDLLGMQTCEGTETIPLNARSHTCLLSGVYIGNVKVLVRAQFGMDSSKDIAMKLTVRAEDVSVAEAIHEIVASG
Protein: Rhomboid domain containing 1 (C9J1R4)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MQRRSRGINTGLILLLSQIFHVGINNIPPVTLATLALNIWFFLNPQKPLYSSCLSVEKCYQQKDWQRLLLSPLHHADDWHLYFNMASMLWKGINLERRLGSRWFAYVITAFSVLTGVVYLLLQFAVAEFMDEPD
Protein: EMILIN-2 (Elastin microfibril interface-located protein 2) (Elastin microfibril interfacer 2) (Protein FOAP-10) (Q9BXX0)
Organism: Homo sapiens (Human)
Function: May be responsible for anchoring smooth muscle cells to elastic fibers, and may be involved not only in the formation of the elastic fiber, but also in the processes that regulate vessel assembly. Has cell adhesive capacity.
Subcellular location: Secreted, extracellular space, extracellular matrix. Note=Found mainly at the interface between amorphous elastin and microfibrils.
Interaction partners:
- Structural maintenance of chromosomes flexible hinge domain-containing protein 1
Sequence:
MWQPRRPWPRVPWRWALALLALVGAGLCHAGPQPGYPARPSARNKNWCAYIVNKNVSCSVLEGSESFIQAQYNCAWNQMPCPSALVYRVNFRPRYVTRYKTVTQLEWRCCPGFRGGDCQEGPKDPVKTLRPTPARPRNSLKKATDNEPSQFSEPRKTLSPTGTAQPSWGVDPKEGPQELQEKKIQVLEEKVLRLTRTVLDLQSSLAGVSENLKHATQDDASRTRAPGLSSQHPKPDTTVSGDTETGQSPGVFNTKESGMKDIKSELAEVKDTLKNKSDKLEELDGKVKGYEGQLRQLQEAAQGPTVTMTTNELYQAYVDSKIDALREELMEGMDRKLADLKNSCEYKLTGLQQQCDDYGSSYLGVIELIGEKETSLRKEINNLRARLQEPSAQANCCDSEKNGDIGQQIKTLDQKIERVAEATRMLNGRLDNEFDRLIVPEPDVDFDAKWNELDARINVTEKNAEEHCFYIEETLRGAINGEVGDLKQLVDQKIQSLEDRLGSVLLQMTNNTGAELSPPGAAALPGVSGSGDERVMMELNHLKDKVQVVEDICLLNIQGKPHGMEGALPNREDRAVRDSLHLLKSLNDTMHRKFQETEQTIQKLQQDFSFLYSQLNHTENDVTHLQKEMSNCRAGENAGMGRFTKVGEQERTVDTLPSPQHPVAHCCSQLEERWQRLQSQVISELDACKECTQGVQREVSMVEGRVSHMEKTCSKLDSISGNLQRIKEGLNKHVSSLWNCVRQMNGTLRSHSRDISGLKNSVQQFYSHVFQISTDLQDLVKFQPSAKAPSPPPPAEAPKEPLQPEPAPPRPSGPATAEDPGRRPVLPQRPPEERPPQPPGSTGVIAETGQAGPPAGAGVSGRGLPRGVDGQTGSGTVPGAEGFAGAPGYPKSPPVASPGAPVPSLVSFSAGLTQKPFPSDGGVVLFNKVLVNDGDVYNPSTGVFTAPYDGRYLITATLTPERDAYVEAVLSVSNASVAQLHTAGYRREFLEYHRPPGALHTCGGPGAFHLIVHLKAGDAVNVVVTGGKLAHTDFDEMYSTFSGVFLYPFLSHL
Protein: Potassium voltage-gated channel subfamily E member 2 (MinK-related peptide 1) (MiRP1) (Minimum potassium ion channel-related peptide 1) (Potassium channel subunit beta MiRP1) (P63161)
Organism: Rattus norvegicus (Rat)
Function: Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1. Associated with KCNH2/HERG is proposed to form the rapidly activating component of the delayed rectifying potassium current in heart (IKr). May associate with KCNQ2 and/or KCNQ3 and modulate the native M-type current. May associate with HCN1 and HCN2 and increase potassium current (By similarity). Interacts with KCNQ1; forms a heterooligomer complex leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current (By similarity). KCNQ1-KCNE2 channel associates with Na(+)-coupled myo-inositol symporter in the apical membrane of choroid plexus epithelium and regulates the myo-inositol gradient between blood and cerebrospinal fluid with an impact on neuron excitability.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14679187, ECO:0000269|PubMed:19219384}; Single-pass type I membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000250|UniProtKB:Q9D808}; Single-pass membrane protein {ECO:0000255}. Note=Colocalizes with KCNB1 at the plasma membrane. {ECO:0000269|PubMed:19219384}.
Interaction partners:
- Potassium voltage-gated channel subfamily KQT member 1
- Potassium voltage-gated channel subfamily E member 3
- Voltage-gated inwardly rectifying potassium channel KCNH2
- Potassium voltage-gated channel subfamily E regulatory subunit 4
- Sodium channel protein type 5 subunit alpha
- A-kinase anchoring protein 9
- Potassium voltage-gated channel subfamily E regulatory subunit 5
- Potassium voltage-gated channel subfamily A member 5
- A-type voltage-gated potassium channel KCND3
- Sodium channel regulatory subunit beta-4
Sequence:
MTTLANLTQTLEDAFKKVFITYMDSWRRNTTAEQQALQARVDAENFYYVILYLMVMIGMFAFIVVAILVSTVKSKRREHSQDPYHQYIVEDWQQKYRSQILHLEDSKATIHENLGATGFTVSP
Protein: Iron-sulfur clusters transporter ABCB7, mitochondrial (ATP-binding cassette sub-family B member 7, mitochondrial) (H2LNR5)
Organism: Oryzias latipes (Japanese rice fish) (Japanese killifish)
Function: Exports glutathione-coordinated iron-sulfur clusters such as [2Fe-2S]-(GS)4 cluster from the mitochondria to the cytosol in an ATP-dependent manner allowing the assembly of the cytosolic iron-sulfur (Fe/S) cluster-containing proteins and participates in iron homeostasis (By similarity). May play a role in iron and lipid metabolism.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P40416}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P40416}. Mitochondrion {ECO:0000269|PubMed:19046159}.
Interaction partners:
- Nucleotide binding protein 1
- Nucleotide binding protein 2
- ATP-binding cassette sub-family E member 1
- ATP-binding cassette sub-family F member 1
- ATP-binding cassette, sub-family B
- Iron-sulfur cluster transfer protein NUBPL
- Mitochondrial potassium channel ATP-binding subunit
Sequence:
MAPMLVSLNCGIRVQRRTLTLLIRQTSSYHIWDKSCINNGTNYQRRRTYALNSLHPQRTASWSTNRTENRRQILEAAKHLQVTDKRTCWHGNAGGRLNADPKNVLKEVHSAKILSAMLSYVWPKDRPDLRARVAVSLGLLAGAKLTNVMVPFMFKYAVDELNQMSGHMLNLNDAPSTVATMTTAVLIGYGVSRAGSALFNELRNTVFGKVAQSSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLGPTVFEMFLVSAILYYKCGGEFAAVALGTLSAYTIFTILVTQWRTRFRIEMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAERYDGYLKLYESSSLKTTSTLAMLNFGQSAIFSVGLTAIMLLASKGIAAGNMTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLNVDTKIKEKDLAPPLAVTPQDATIRFEDVYFEYMEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYISGQNIRDVSLESLRKALGVVPQDAVLFHNNIFYNLQYGNINATPEEVYQVARLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSITEENIMTSMKEMVKDRTSVFIAHRLSTIVDADEILVLSQGKVAERGTHQALLDTPGSLYAELWNAQNSKILNSRKSSSAPAAERLSQKEEERKKLQEEILNSVKGCGNCSC
Protein: Protein ABHD1 (EC 3.1.1.-) (Alpha/beta hydrolase domain-containing protein 1) (Abhydrolase domain-containing protein 1) (Lung alpha/beta hydrolase 1) (Q96SE0)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Guanine nucleotide-exchange factor SEC12
Sequence:
MLSSFLSPQNGTWADTFSLLLALAVALYLGYYWACVLQRPRLVAGPQFLAFLEPHCSITTETFYPTLWCFEGRLQSIFQVLLQSQPLVLYQSDILQTPDGGQLLLDWAKQPDSSQDPDPTTQPIVLLLPGITGSSQETYVLHLVNQALRDGYQAVVFNNRGCRGEELRTHRAFCASNTEDLETVVNHIKHRYPQAPLLAVGISFGGILVLNHLAQARQAAGLVAALTLSACWDSFETTRSLETPLNSLLFNQPLTAGLCQLVERNRKVIEKVVDIDFVLQARTIRQFDERYTSVAFGYQDCVTYYKAASPRTKIDAIRIPVLYLSAADDPFSPVCALPIQAAQHSPYVALLITARGGHIGFLEGLLPWQHWYMSRLLHQYAKAIFQDPEGLPDLRALLPSEDRNS
Protein: Transcription factor MUTE (Basic helix-loop-helix protein 45) (AtbHLH45) (bHLH 45) (Transcription factor EN 20) (bHLH transcription factor bHLH045) (Q9M8K6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor. Together with FMA and SPCH, regulates the stomata formation. Required for the differentiation of stomatal guard cells, by promoting successive asymmetric cell divisions and the formation of guard mother cells. Promotes the conversion of the leaf epidermis into stomata.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:17183267}.
Interaction partners:
- Transcription factor ICE1
- Transcription factor SCREAM2
- Protein EPIDERMAL PATTERNING FACTOR 2
- Protein EPIDERMAL PATTERNING FACTOR 1
- EPIDERMAL PATTERNING FACTOR-like protein 9
- Protein BREAKING OF ASYMMETRY IN THE STOMATAL LINEAGE
- LRR receptor-like serine/threonine-protein kinase ERL1
- LRR receptor-like serine/threonine-protein kinase ERL2
- Mitogen-activated protein kinase kinase kinase YODA
- Subtilisin-like protease SBT1.2
Sequence:
MSHIAVERNRRRQMNEHLKSLRSLTPCFYIKRGDQASIIGGVIEFIKELQQLVQVLESKKRRKTLNRPSFPYDHQTIEPSSLGAATTRVPFSRIENVMTTSTFKEVGACCNSPHANVEAKISGSNVVLRVVSRRIVGQLVKIISVLEKLSFQVLHLNISSMEETVLYFFVVKIGLECHLSLEELTLEVQKSFVSDEVIVSTN
Protein: Histone H2A-beta (H2A.2) (P04910)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Histone H2B-alpha
- Histone H4
- Histone H3.1/H3.2
- Histone H2A-alpha
- Histone H3.3
- Histone H2A.Z
- DNA repair protein crb2
- BRCT-containing protein 1
- Histone acetyltransferase mst1
- FACT complex subunit spt16
Sequence:
MSGGKSGGKAAVAKSAQSRSAKAGLAFPVGRVHRLLRKGNYAQRVGAGAPVYLAAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGHVTIAQGGVVPNINAHLLPKQSGKGKPSQEL
Protein: Protein DETOXIFICATION 21 (AtDTX21) (Multidrug and toxic compound extrusion protein 21) (MATE protein 21) (Q8W488)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein DETOXIFICATION 42
- Patatin-like protein 1
- F18B13.24 protein
Sequence:
MAGGGGELTAALLKKTAENGGEEKDELGLKQKVWIESKKLWIVAAPAIFTRFSTFGVSIISQSFIGHLGPIELAAYSITFTVLLRFSNGILLGMASALETLCGQAYGAKQNHMLGIYLQRSWIVLTGCTICLTPVYIFSGPILLALGQEERIVRVARIIALWVIGINFSFVPSFTCQMFLQAQSKNKIIAYVAAVSLGVHVFLSWLLMVHFNFGITGAMTSTLVAFWLPNIAQLLFVTCGGCKDTWRGFSMMAFKDLWPVFKLSMSSGGMLCLELWYNSILVLLTGNLKNAEVALDALAICLNINGLEMMIALGFLAAASVRVSNELGSGNPKGAKFATLTAVFTSLSLGIVLFFVFLFLRGRVSYIFTTSEAVAAEVADLSPLLAFSILMNSVQPVLSGVAVGAGWQGYVTYVNLACYYLVGIPIGIILGYVVGLQVKGVWIGMLFGIFVQTCVLTVMTLRTDWDQQVSTSLRRLNRWVVPESRDVNQVSSEE
Protein: Zinc finger CCCH-type containing 18 (E7ERS3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDVAESPERDPHSPEDEEQPQGLSDDDILRDSGSDQDLDGAGVRASDLEDEESAARGPSQEEEDNHSDEEDRASEPKSQDQDSEVNELSRGPTSSPCEEEGDEGEEDRTSDLRDEASSVTRELDEHELDYDEEVPEEPAPAVQEDEAEKAGAEDDEEKGEGTPREEGKAGVQSVGEKESLEAAKEKKKEDDDGEIDDGEIDDDDLEEGEVKDPSDRKVRPRPTCRFFMKDVVTPLSTLLPPISNSIPFRGQVKGNCTWGMNCRFIHPGVNDKGNYSLITKADPFPPNGAPPLGPHPLMPANPWGGPVVDEILPPPPPEPPTESAWERGLRHAKEVLKKATIRKEQEPDFEEKRFTVTIGEDEREFDKENEVFRDWNSRIPRDVRDTVLEPYADPYYDYEIERFWRGGQYENFRVQYTETEPYHNYRERERERERENRQRERERERERDRERERRQRERERERERERDKERQRRKEEWERERAKRDEKDRQHRDRDREKEREKEKGKPKPRSPQPPSRQAEPPKKEAATTGPQVKRADEWKDPWRRSKSPKKKLGVSVSPSRARRRRKTSASSASASNSSRSSSRSSSYSGSGSSRSRSRSSSYSSYSSRSSRHSSFSGSRSRSRSFSSSPSPSPTPSPHRPSIRTKGEPAPPPGKAGEKSVKKPAPPPAPPQATKTTAPVPEPTKPGDPREARRKERPARTPPRRRTLSGSGSGSGSSYSGSSSRSRSLSVSSVSSVSSATSSSSSAHSVDSEDMYADLASPVSSASSRSPAPAQTRKEKGKSKKEDGVKEEKRKRDSSTQPPKSAKPPAGGKSSQQPSTPQQAPPGQPQQGTFVAHKEIKLTLLNKAADKGSRKRYEPSDKDRQSPPPAKRPNTSPDRGSRDRKSGGRLGSPKPERQRGQNSKAPAAPADRKRQLSPQSKSSSKVTSVPGKASDPGAASTKSGKASTLSRREELLKQLKAVEDAIARKRAKIPGKA
Protein: RNase E specificity factor CsrD (Regulator of CsrB and CsrC decay CsrD) (P13518)
Organism: Escherichia coli (strain K12)
Function: Serves as a specificity factor required for RNase E-mediated decay of the small global regulatory RNAs CsrB and CsrC, it is probably not a nuclease. Nor does its activity involve c-di-GMP, despite its domain composition. Positively modulates motility gene expression, is also required for curli expression.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Signal transduction histidine-protein kinase BarA
- Ribonuclease E
- Carbon storage regulator
- Response regulator UvrY
- Probable diguanylate cyclase DgcT
- Probable diguanylate cyclase CdgI
- Probable diguanylate cyclase DgcI
- Probable cyclic di-GMP phosphodiesterase PdeN
- Probable cyclic di-GMP phosphodiesterase PdeI
- Probable diguanylate cyclase DgcJ
Sequence:
MRLTTKFSAFVTLLTGLTIFVTLLGCSLSFYNAIQYKFSHRVQAVATAIDTHLVSNDFSVLRPQITELMMSADIVRVDLLHGDKQVYTLARNGSYRPVGSSDLFRELSVPLIKHPGMSLRLVYQDPMGNYFHSLMTTAPLTGAIGFIIVMLFLAVRWLQRQLAGQELLETRATRILNGERGSNVLGTIYEWPPRTSSALDTLLREIQNAREQHSRLDTLIRSYAAQDVKTGLNNRLFFDNQLATLLEDQEKVGTHGIVMMIRLPDFNMLSDTWGHSQVEEQFFTLTNLLSTFMMRYPGALLARYHRSDFAALLPHRTLKEAESIAGQLIKAVDTLPNNKMLDRDDMIHIGICAWRSGQDTEQVMEHAESATRNAGLQGGNSWAIYDDSLPEKGRGNVRWRTLIEQMLSRGGPRLYQKPAVTREGQVHHRELMCRIFDGNEEVSSAEYMPMVLQFGLSEEYDRLQISRLIPLLRYWPEENLAIQVTVESLIRPRFQRWLRDTLMQCEKSQRKRIIIELAEADVGQHISRLQPVIRLVNALGVRVAVNQAGLTLVSTSWIKELNVELLKLHPGLVRNIEKRTENQLLVQSLVEACSGTSTQVYATGVRSRSEWQTLIQRGVTGGQGDFFASSQPLDTNVKKYSQRYSV
Protein: Bifunctional diterpene synthase, chloroplastic (Copalyl diphosphate synthase) (EC 5.5.1.12) (Miltiradiene synthase) (SmMDS) (EC 4.2.3.131) (Terpene synthase 4) (SmTPS4) (G9MAN7)
Organism: Selaginella moellendorffii (Spikemoss)
Function: Bifunctional diterpene cyclase that catalyzes the successive two-step type-B (protonation-initiated cyclization) and type-A (ionization-initiated cyclization) reactions of geranylgeranyl diphosphate (GGDP) producing successively (+)-copalyl diphosphate and miltiradiene.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
Sequence:
MAKVLFSSFQQTGISGSLKSGQLSGVFINGTNLKSNAHAKRFRKNSTSSITIRCCASNSPTLENTKLAGAPEKRQKKKQLPYQGILHVPGDRVEELDTRETSLLVAEVKGWLMKLASGKGEISPSAYDTAWVARIASESDSSLPEFPEALEWIINSQLPDGSWGDDRHLQLYDRVLSTLSCLVTLKTWDIGHNSIAQGTKFLRENMIKLKQDDGDLLSGFEVTFPMMLHEAKQLGLDIPYETEFTRLLEISTKKKLAKIPLDKLHSAPTTLLYSLEGLQDLEIDWQKILKLQSKDGSFLSSPSSTACVYLKTKDRKSLQYLQNAMEDQNYAVPCHYPIDLFESLWVVDTIERLGIDVFFRDEIKAVLDYVYSFWTNEGIGWGSTCLVNDIDDTAMAFRILRMHGYNVSPDAFNQFWLPGDKFCCFVGELSHGVSEMLNLHRASQVDFPNEAILTKTFKYSHDYLLNVDSAHMDKWATKKNLMGEVAFELANPFHDCLPRIYNNAYIKHYGMDDLWIAKTIYRLPLVNNKVFLELANRYAQQCQLYQPAELTKLVNWWHSSRFEDIPSTRLTANIDMLPYIYYVICATFHEQEFAQLRVFFSKACCLNTLFDDLMDCATSIEELDRLQNVIERWDISLSHELPLEYRIPFQEFYNTVLVMTEAASKIHKNLSPEFICKYLSGIYTKLIKSEIADARWKIEGYIPSFEEYMENAEVSISTWVHVLMSILFCGEPLTEEILNTIYDSRPLKLDRIICRLCNDIQTYKIEMKLGQPTQGVSCYMKEHPGATEEDALVYLQSLLEKTKRELNESYFITHENDLPKNIKRFNFEMVRMMLITYNETRQVDLFRNPDNELKDMIKFCLETYRTL
Protein: Histone 24 (Histone H1.1) (P10771)
Organism: Caenorhabditis elegans
Function: Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures (Probable). Probably does not act as global transcriptional repressor. Acting in concert with chromobox protein homologs hpl-1 and hpl-2, involved in reproduction, somatic gonad development, male tail development, and vulval cell fate decisions; perhaps as a result of modulating expression of Hox genes mab-5 and egl-5. Plays a role in linking epigenetic regulation with the innate immune response.
Subcellular location: Nucleus {ECO:0000269|PubMed:22083954}. Chromosome {ECO:0000269|PubMed:22083954, ECO:0000305|PubMed:3202838}. Cytoplasm {ECO:0000269|PubMed:22083954}. Note=Cytoplasmic localization is observed after infection with Gram-positive bacterium B.thuringiensis. {ECO:0000269|PubMed:22083954}.
Interaction partners:
- Histone H3.3 type 2
- Chromobox protein homolog hpl-1
- Protein unc-119
- Pre-mRNA-splicing factor CWC22 homolog
- Histone H1.3
- Histone H2A.V
Sequence:
MSDSAVVAAAVEPKVPKAKAAKAAKPTKVAKAKAPVAHPPYINMIKEAIKQLKDRKGASKQAILKFISQNYKLGDNVIQINAHLRQALKRGVTSKALVQAAGSGANGRFRVPEKAAAAKKPAAAKKPAAAKKPAAAKKATGEKKAKKPAAAKPKKAATGDKKVKKAKSPKKVAKPAAKKVAKSPAKKAAPKKIAKPAAKKAAKPAAKA
Protein: Orf161 protein (Q8HCP5)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MLYGRMLRRIIRTMRFYFYGFHFGEGSNLRLLKRFMSHGKSLGLSYLSAAFGLPLHSTSDTGEDVRLIHLLNFRGEKRLPVHELLQSIENPYRLSISVIDGCRSGVLRTRGTCMQTGEEEENLECRLLRHNQGPLAQIETLNPRCDVHLFHFIISWKKRIN
Protein: Probable UDP-sugar transporter protein SLC35A4 (Solute carrier family 35 member A4) (Q96G79)
Organism: Homo sapiens (Human)
Function: Mediates the transport of CDP-ribitol. Does not exhibit CMP-sialic acid, UDP-galactose and UDP-N-acetylglucosamine transport activity.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:28167211, ECO:0000269|PubMed:38580077}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSVEDGGMPGLGRPRQARWTLMLLLSTAMYGAHAPLLALCHVDGRVPFRPSSAVLLTELTKLLLCAFSLLVGWQAWPQGPPPWRQAAPFALSALLYGANNNLVIYLQRYMDPSTYQVLSNLKIGSTAVLYCLCLRHRLSVRQGLALLLLMAAGACYAAGGLQVPGNTLPSPPPAAAASPMPLHITPLGLLLLILYCLISGLSSVYTELLMKRQRLPLALQNLFLYTFGVLLNLGLHAGGGSGPGLLEGFSGWAALVVLSQALNGLLMSAVMKHGSSITRLFVVSCSLVVNAVLSAVLLRLQLTAAFFLATLLIGLAMRLYYGSR
Protein: Glutathione hydrolase 5 proenzyme (EC 3.4.19.13) (Gamma-glutamyl transpeptidase-related enzyme) (GGT-rel) (Gamma-glutamyltransferase 5) (GGT 5) (EC 2.3.2.2) (Gamma-glutamyltransferase-like activity 1) (Gamma-glutamyltranspeptidase 5) (Leukotriene-C4 hydrolase) (EC 3.4.19.14) [Cleaved into: Glutathione hydrolase 5 heavy chain; Glutathione hydrolase 5 light chain] (P36269)
Organism: Homo sapiens (Human)
Function: Cleaves the gamma-glutamyl peptide bond of glutathione and glutathione-S-conjugate such as leukotriene C4. Does not cleaves gamma-glutamyl compounds such as gamma-glutamyl leucine. May also catalyze a transpeptidation reaction in addition to the hydrolysis reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Acts as a negative regulator of geranylgeranyl glutathione bioactivity by cleaving off its gamma-glutamyl group, playing a role in adaptive immune responses.
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q9Z2A9}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9Z2A9}.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta-5
- Glutathione hydrolase 6
- Glutathione synthetase
- 5-oxoprolinase
- Aminopeptidase N
- Glutathione hydrolase 7
- Gamma-glutamylcyclotransferase
- Cytosol aminopeptidase
- Leukotriene C4 synthase
- Glutathione hydrolase 1 proenzyme
Sequence:
MARGYGATVSLVLLGLGLALAVIVLAVVLSRHQAPCGPQAFAHAAVAADSKVCSDIGRAILQQQGSPVDATIAALVCTSVVNPQSMGLGGGVIFTIYNVTTGKVEVINARETVPASHAPSLLDQCAQALPLGTGAQWIGVPGELRGYAEAHRRHGRLPWAQLFQPTIALLRGGHVVAPVLSRFLHNSILRPSLQASTLRQLFFNGTEPLRPQDPLPWPALATTLETVATEGVEVFYTGRLGQMLVEDIAKEGSQLTLQDLAKFQPEVVDALEVPLGDYTLYSPPPPAGGAILSFILNVLRGFNFSTESMARPEGRVNVYHHLVETLKFAKGQRWRLGDPRSHPKLQNASRDLLGETLAQLIRQQIDGRGDHQLSHYSLAEAWGHGTGTSHVSVLGEDGSAVAATSTINTPFGAMVYSPRTGIILNNELLDLCERCPRGSGTTPSPVSGDRVGGAPGRCWPPVPGERSPSSMVPSILINKAQGSKLVIGGAGGELIISAVAQAIMSKLWLGFDLRAAIAAPILHVNSKGCVEYEPNFSQEVQRGLQDRGQNQTQRPFFLNVVQAVSQEGACVYAVSDLRKSGEAAGY
Protein: Thioredoxin 2 (F1SKJ2)
Organism: Sus scrofa (Pig)
Interaction partners:
Sequence:
MVRSGIAAEAPLQARSHAGRWPSGQKPWMAQRLLLRRFLASVVSRKPSHSRWAPLASRALQTPQLSLSNLTGTPSQARSLYTTQVCTTTFNIQDGPDFQDRVVNSETPVVVDFHAQWCGPCKILGPRLEKVVAKQHGKVVMAKVDIDDHTDLAIEYEVSAVPTVLAIKNGDVVDKFVGIKDEDQLEAFLKKLIG
Protein: Thioredoxin domain-containing protein (Q389F2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Rhodanese domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- MICOS complex subunit MIC10
- Transmembrane protein
- Mitochondrial fission process protein 1
Sequence:
MTQNIIRRIFGNRELPENLSGSEYERYMQENFPKWIDEFEKGGFLEATKLPAIKSERDFLSKLIEHKDEIMVVKYWKHGCIPCLSLAEMYKQVSEQCKKENRRIAWYSVNTKDVSARSLVDYQLVNGTPTVQTFSRMKQVGKEIRAISAEELMRELSLREAALNTES
Protein: Testicular secretory protein Li 66 (A0A140VK66)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEPGKRRTKDDTWKADDLRKHLWAIQSGGSKEERKHREKKLRKESEMDLPEHKEPRCRDPDQDARSRDRVAEVHTAKESPRGERDRDRQRERRRDAKDREKEKLKEKHREAEKSHSRGKDREKEKDRRARKEELRQTVAHHNLLGQETRDRQLLERAERKGRSVSKVRSEEKDEDSERGDEDRERRYRERKLQYGDSKDNPLKYWLYKEEGERRHRKPREPDRDNKHREKSSTREKREKYSKEKSNSFSDKGEERHKEKRHKEGFHFDDERHQSNVDRKEKSAKDEPRKRESQNGEHRNRGASSKRDGTSSQHAENLVRNHGKDKDSRRKHGHEEGSSVWWKLDQRPGGEETVEIEKEETDLENARADAYTASCEDDFEDYEDDFEVCDGDDDESSNEPESREKLEELPLAQKKEIQEIQRAINAENERIGELSLKLFQKRGRTEFEKEPRTDTNSSPSRASVCGIFVDFASASHRQKSRTQALKQKMRSTKLLRLIDLDFSFTFSLLDLPPVNEYDMYIRNFGKKNTKQAYVQCNEDNVERDIQTEEIETREVWTQHPGESTVVSGGSEQRDTSDAVVMPKIDTPRLCSFLRAACQVMAVLLEEDRLAAEPSWNLRAQDRALYFSDSSSQLNTSLPFLQNRKVSSLHTSRVQRQMVVSVHDLPEKSFVPLLDSKYVLCVWDIWQPSGPQKVLICESQVTCCCLSPLKAFLLFAGTAHGSVVVWDLREDSRLHYSVTLSDGFWTFRTATFSTDGILTSVNHRSPLQAVEPISTSVHKKQSFVLSPFSTQEEMSGLSFHIASLDESGVLNVWVVVELPKADIAGSISDLGLMPGGRVKLVHSALIQLGDSLSHKGNEFWGTTQTLNVKFLPSDPNHFIIGTDMGLISHGTRQDLRVAPKLFKPQQHGIRPVKVNVIDFSPFGEPIFLAGCSDGSIRLHQLSSAFPLLQWDSSTDSHAVTGLQWSPTRPAVFLVQDDTSNIYIWDLLQSDLGPVAKQQVSPNRLVAMAAVGEPEKAGGSFLALVLARASGSIDIQHLKRRWAAPEVDECNRLRLLLQEALWPEGKLHK
Protein: Phosphofurin acidic cluster sorting protein 2 (F8VW41)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAERGRLGLPGAPGALNTPVPMNLFATWEVDGSSPSCVPRLCSLTLKKLVVFKELEKELISVVIAVKMQYPHFLKREGNKLQIMLQRRKRYKNRTILGYKTLAAGSISMAEVMQHPSEGGQVLSLCSSIKEAPVKAAEIWIASLSSQPIDHEDSTMQAGPKAKSTDNYSEEEYESFSSEQEASDDAVQGQDLDEDDFDVGKPKKQRRSIVRTTSMTRQQNFKQKVVALLRRFKVSDEVLDSEQDPAEHIPEAEEDLDLLYDTLDMEHPSDSGPDMEDDDSVLSTPKPKLRPYFEGLSHSSSQTEIGSIHSARSHKEPPSPADVPEKTRSLGGRQPSDSVSDTVALGVPGPREHPGQPEDSPEAEASTLDVFTERLPPSGRITKTESLVIPSTRSEGKQAGRRGRSTSLKERQAARPQNERANSLDNERCPDARSQLQIPRKTVYDQLNHILISDDQLPENIILVNTSDWQGQFLSDVLQRHTLPVVCTCSPADVQAAFSTIVSRIQRYCNCNSQPPTPVKIAVAGAQHYLSAILRLFVEQLSHKTPDWLGYMRFLVIPLGSHPVARYLGSVDYRYNNFFQDLAWRDLFNKLEAQSAVQDTPDIVSRITQYIAGANCAHQLPIAEAMLTYKQKSPDEESSQKFIPFVGVVKVGIVEPSSATSGDSDDAAPSGSGTLSSTPPSASPAAKEASPTPPSSPSVSGGLSSPSQGVGAELMGLQVDYWTAAQPADRKRDAEKKDLPVTKNTLKCTFRSLQVSRLPSSGEAAATPTMSMTVVTKEKNKKVMFLPKKAKDKDVESKSQCIEGISRLICTARQQQNMLRVLIDGVECSDVKFFQLAAQWSSHVKHFPICIFGHSKATF