wanglab/gogpt-training-data huggingface dataset:
Protein: GATA-binding factor 2 (GATA-2) (Transcription factor NF-E1b) (P23824)
Organism: Gallus gallus (Chicken)
Function: Transcriptional activator which probably serves as a general switch factor for cell-specific development. It binds to DNA sites with the consensus sequence 5'-[AT]GATA[AG]-3' within regulatory regions of genes.
Subcellular location: Nucleus.
Interaction partners:
- Rhombotin-2
- T-cell acute lymphocytic leukemia protein 1 homolog
- LIM domain-binding protein 1
- Runt-related transcription factor
- Zinc finger protein, FOG family member 1.
- Paired like homeobox 2B
- Nuclear transcription factor Y subunit beta
- CCAAT/enhancer-binding protein beta
Sequence:
MEVATDQPRWMTHHAVLNGQHPESHHPGLAHNYMEPAQLLPPDEVDVFFNHLDSQGNPYYANSAHARARVSYSQAHARLTGSQMCRPHLIHSPGIPWLDSSKAALSAHHHNPWTVNPFTKTPLHPSAAGAPGAISVYPGSSTSSTASVSSLTPASHSGSHLFGFPPTPPKEVSPDPNSTSAASPSSSAGARQEDKDSIKYQVSLSEGMKMESASPLRSSLTSMGAQPSTHHPIPTYPSYVPAAHDYSSSLFHPGSFLGGPASSFTPKPRSKARSCSEGRECVNCGATATPLWRRDGTGHYLCNACGLYHKMNGQNRPLIKPKRRLSAARRAGTCCANCQTTTTTLWRRNANGDPVCNACGLYYKLHNVNRPLTMKKEGIQTRNRKMSNKSKKSKKGSECFEELSKCMQEKSSPFSAAALASHMAPMGHLPPFSHSGHILPTPTPIHPSSSISFGHPHPSSMVTAMG
Protein: Vesicular inhibitory amino acid transporter (Solute carrier family 32 member 1) (Vesicular GABA and glycine transporter) (Vesicular GABA transporter) (mVGAT) (mVIAAT) (O35633)
Organism: Mus musculus (Mouse)
Function: Antiporter that exchanges vesicular protons for cytosolic 4-aminobutanoate or to a lesser extend glycine, thus allowing their secretion from nerve terminals. The transport is equally dependent on the chemical and electrical components of the proton gradient. May also transport beta-alanine (By similarity). Acidification of GABAergic synaptic vesicles is a prerequisite for 4-aminobutanoate uptake.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:O35458}; Multi-pass membrane protein {ECO:0000255}. Presynapse {ECO:0000269|PubMed:19052203}. Note=Presents in glycine-, GABA- or GABA- and glycine-containing boutons. {ECO:0000250|UniProtKB:O35458}.
Interaction partners:
- Vesicular glutamate transporter 1
- Vesicular glutamate transporter 2
- Vesicular acetylcholine transporter
- Glutamate decarboxylase 2
- Vesicular glutamate transporter 3
- Synaptic vesicular amine transporter
- Gephyrin
- Glutamate decarboxylase 1
- Chromaffin granule amine transporter
- Synaptotagmin-1
Sequence:
MATLLRSKLTNVATSVSNKSQAKVSGMFARMGFQAATDEEAVGFAHCDDLDFEHRQGLQMDILKSEGEPCGDEGAEAPVEGDIHYQRGGAPLPPSGSKDQAVGAGGEFGGHDKPKITAWEAGWNVTNAIQGMFVLGLPYAILHGGYLGLFLIIFAAVVCCYTGKILIACLYEENEDGEVVRVRDSYVAIANACCAPRFPTLGGRVVNVAQIIELVMTCILYVVVSGNLMYNSFPGLPVSQKSWSIIATAVLLPCAFLKNLKAVSKFSLLCTLAHFVINILVIAYCLSRARDWAWEKVKFYIDVKKFPISIGIIVFSYTSQIFLPSLEGNMQQPSEFHCMMNWTHIAACVLKGLFALVAYLTWADETKEVITDNLPGSIRAVVNLFLVAKALLSYPLPFFAAVEVLEKSLFQEGSRAFFPACYGGDGRLKSWGLTLRCALVVFTLLMAIYVPHFALLMGLTGSLTGAGLCFLLPSLFHLRLLWRKLLWHQVFFDVAIFVIGGICSVSGFVHSLEGLIEAYRTNAED
Protein: RNA replication polyprotein (223 kDa protein) (ORF1 protein) [Cleaved into: Helicase (EC 3.6.4.13)] [Includes: Viral methyltransferase (EC 2.1.1.-); Putative Fe(2+) 2-oxoglutarate dioxygenase (EC 1.14.11.-); Protease (EC 3.4.22.-); RNA-directed RNA polymerase (EC 2.7.7.48)] (Q65652)
Organism: Blueberry scorch virus (BBScV)
Function: RNA-directed RNA polymerase involved in viral RNA replication.
Interaction partners:
Sequence:
MALTYRSPVEEVLTLFEPTAQSLIASAAVSAFQRHEKDNFEWFRYSVPAFAKEHLSKAGIYLSPYAGFPHSHPVCKTLENYILYVVVPSIVNSTFFFVGIKDFKINFLKSRFDKLNMISALNRYVSSADKIRYGNDFVIRAGVEHRALKRHRGLVDSPTLKALMPNVKSGSKLFLHDELHYWSKEELIGFLEICEPEVLLGTVIYPPELLIGSDCSLNPWCYEYEVKKKKLLFYPDGVRSEGYEQPLSGGYLLQTSRIKLPNAGIYCVDLLCSRFAHHLFSITRGDLITPDNRSFGPFEAVHSGALAGISRGKPNFYPVSQHTILRVYRYLRSLKKPDKQSAMAKFSQIVHEPCGRAVKFMEEFSDLIINTGTLRTVINPEQVKLFFGNLGRCMPPCFASKLKGTRTVCLDEFISMLRPLSVDVTLETISMHSMTMVVTTWSQEAEEGVDLPKIFEEKWEGKQSLDRTEAPYLGLAPFVDYKIQWRLQFNIPKFLNQLAELFVNSCSVNGGVRSMSIPAYLRRLATCRSCVGRAMLCCLTEVDIASLRVVVRNRYPYTEDFYRCRRRWFLRIGAQRRPSFYIEDAKHLERLGQFEEEQFQRPMSRRSLYTLASVSMNGTDDPFCSDCFYDPVPVARAKIVPTPTVIVERALEPLAIDTGTTSDAPCDAPGATCLRGAQAVVCACGLSMAVSAVPYAELKMDFYPDALKGRDAAWYSKEDREYKYNGGSHLCRGWPKWLQLWMQANGVDETYDCMLAQRYGAQGKIGFHADNEEIFMRGAPVHTVSMDGNADFGTECAAGRQYTTLRGNVQFTMPSGFQETHKHAVRNTTAGRVSYTFRRLAKKDESRVIEEVVEVETKDMGFSSSLFGVQIIVDEPCDGVEETFNVQCVPGDGNCFWHSLGSFTGLTVECMKAGIKNFACGPEGAEKLSRQLEPNVWAEDEALCAACAHLGVDLVIFDEDQGFKMLYRYPGNKREALLRLKGSHFEPLEPKEMCVVKAIAQAVKRSPMDVLRVALKKMGEDFKEQICRGKGVMLDVFMVLAKIFDVSACVLQGTEQIMINPKGRIKGLFRMTTDHLSYDGVPDKVKHSEVNVYKHDVALQIEDLIELRELSSLVEYTPSFSRAKLLADCLHDGSTGVMCSELYNDKGHLCPEGRETTRVTIGVLLGTFGCGKSRLFKEILFKLCGKSVCYISPRKALCDSFDDEIRKARGNMGERGIKHYKSLTFEKAILQASKLHKGSLVIIDEIQLYPPGYLDLLLLLAGPTMKYFALGDPCQSDYDSEKDRTILGSVRSDVFELLDGIEYKFNILSRRFQSSLFRGRLPCLMYEEDLEAGAPLRLIDGLESIDTSAAYSRCCLVSSFEEKKIVNAYFGERTKCLTFGESTGMTFDVGCVLITSISAHTSEQRWITALSRFRKDIVFVNAASVAWDTLQSVYANRWLGRFLNRSARQEDLRRMLPGTPLFVEGFQKNLLGADEGKRECKLEGDPWLKTMVDLLQVEDMEDIEIAKEVLQDEWCKTHLPQCELESVRARWVHKILAKEFREKRMGCLVSEQFTDQHSKQMGKHLTNSAERFETIYPRHRAADTVTFIMAVRKRLSFSCPIKESAKLNQALPYGPFLLKEFLKRVPLKPMHDRKMMEQAKFDFEEKKTSKSAATIENHSNRSCRDWLIDVGLVFSKSQLCTKFDNRFRDAKRAQTIVCFQHAVLCRFAPYMRYIEKKLNEVLPSKYYIHSGKGLEELNRWVIEGRFEGVCTESDYEAFDASQDHYIVAFEICLMRYLGLPNDLIEDYKFIKTHLGSKLGNFAIMRFSGEASTFLFNTMANMLFTFLQYDLKGNERICFAGDDMCANGRLHVSSKHKNFMSKLKLKAKVSNTMNPTFCGWNLSSDGIFKKPQLVLERLCIAKETNNLANCIDNYAIEVSFAYLMGERAKQRMDEEEVEAFYNCVRIIVKSKHLLKSDVATIYQTARVD
Protein: Protein AsmA (P28249)
Organism: Escherichia coli (strain K12)
Function: Involved in the inhibition of assembly of mutant ompF proteins. In general, could be involved in the assembly of outer membrane proteins.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
- Probable phospholipid transport protein YdbH
- AsmA family protein YicH
- AsmA family protein YhjG
- Intermembrane phospholipid transporter YhdP
- Outer membrane porin F
- Penicillin-binding protein activator LpoB
- Outer membrane porin C
- Cell division protein ZapB
- Phosphotransferase RcsD
- Protein YdgA
Sequence:
MRRFLTTLMILLVVLVAGLSALVLLVNPNDFRDYMVKQVAARSGYQLQLDGPLRWHVWPQLSILSGRMSLTAQGASQPLVRADNMRLDVALLPLLSHQLSVKQVMLKGAVIQLTPQTEAVRSEDAPVAPRDNTLPDLSDDRGWSFDISSLKVADSVLVFQHEDDEQVTIRNIRLQMEQDPQHRGSFEFSGRVNRDQRDLTISLNGTVDASDYPHDLTAAIEQINWQLQGADLPKQGIQGQGSFQAQWQESHKRLSFNQISLTANDSTLSGQAQVTLTEKPEWQLRLQFPQLNLDNLIPLNETANGENGAAQQGQSQSTLPRPVISSRIDEPAYQGLQGFTADILLQASNVRWRGMNFTDVATQMTNKSGLLEITQLQGKLNGGQVSLPGTLDATSINPRINFQPRLENVEIGTILKAFNYPISLTGKMSLAGDFSGADIDADAFRHNWQGQAHVEMTDTRMEGMNFQQMIQQAVERNGGDVKAAENFDNVTRLDRFTTDLTLKDGVVTLNDMQGQSPVLALTGEGMLNLADQTCDTQFDIRVVGGWNGESKLIDFLKETPVPLRVYGNWQQLNYSLQVDQLLRKHLQDEAKRRLNDWAERNKDSRNGKDVKKLLEKM
Protein: T. brucei spp.-specific protein (Q384V8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MQRYRGKQFEGVGTHDRMSSIMSMQGPKSQDIRAPYGNDEDLVRRGSSVSCCTSSLMQSGVGRRRQLSTGIRSPPVEFPMFEREIRTTQNHMNATPRSRMLRSPFPPNERGNENESTPLSAAGSSNSGNSEKNNLDEFVTCEPVEVVNGMNRVCVYVPSSKGAETPRSGALKITFPAPERSMGTASYPSPPVMRFQPLYSPSLPYTVPSPVQEALRSLLEEAAQRQQLGIGTSRRQSFVCNTGVQTEPGTEVESIAPGQTVESDDTHSNRAQENEQAPLSCGVSSPVCLSGTLSSMSSPRSPREPRPLMKVGETERDEGDSKVDTKPAPGEQQEQKDQARNEEREREGTKEQRNVGSAAPSVMSVSSAAESSPTEPLNAATTAEQPRGASACVFIDLHGICSAKNGKAAAGPPIRVHVTNPIPGTNTSGTGHDTNMDNVDYPMKSGLMLNQQSERCRKLASQMLGHETANPQPTALSTAPWYLRTSLVVEPNEFKSLLRNSWRWSSGEHGGPDNVGAHVSSSTEPYGHTADIAQNVYNSEVKGPRPTAPDSLVEGPSRSPSHASGAPRPKAQRSKASDGKHRGSRRRGSHSSTRTTRSKDSAALRTRRVSAPDGLTEDGPLAMSVSDSCTQRSKGPDAVIDIRGDLNPSITRAPPPSSPSVGVEPSVSPANQRNAETEQHPAAEVRRKQKTRCCCTG
Protein: Invariant surface glycoprotein (Q38A30)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSTFAVLNGVIILAVFVVTAACLDDQKPIREGGKALSGEAAKHLCRIKQISELLGSRAEFELIRDGSKFTSERQVLRNVQDKITEGVKGINELFGRHCRRVSLGIEGGGSDMLSNPNCEDSDKKEGTGEATDQGSGTLSEEGIIQCEHGNFLRDFLIRGALEAYRSQMEQWEKKKPTEGNKTSTEVKGDESSKKHEDQCQQMGYSVHGACTVSEQKWRQHLEEAVKLMEGIIVVKKEDVCGVSKEGETQK
Protein: Oxidation resistance protein 1 (B7Z0T6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MFDPNVSDPLVIEHGPESYGVIAPMELVVNAAIFHDIAHMRVAGGAGQGLNSASGDAEKPEIYYPKPVLVEEDSKELPEQQSLLGEDGNKRLDAEIGSLEIADDQESLCSSTGRDGDAFPKAFDRERVEDSSMEAKDSAKTDALDDEDKKAGLGLSSTRSTLEERRKSLLDHHWAIPSKDRSSEDEGDNESNVTVDSGARVQDPHSANSSVSGVPLSQPPVAAAAAAAAVAPASAVVPLPPSGIDLEHLEQLSKQSCYDSGIDIREPVPNVQPIPKKTVYSDADIVLSSDWVPPKTIVPTHFSESPPRSTILGQSLDAGTGGAGGVRKKTSSVSFSVDDEAAQQAQAQSAALAVTDKQADKKNKMLKRLSYPLTWVEGLTGEGGAVPPGGVGSGSLNKSGDTDSAPNTGDSNQSVFSKVFSRRSSIGTFIRPHSSEGTSSSTKLKEAKQAPKLDYRSMVSMDDKPELFISVDKLIPRPARACLDPPLYLRLRMGKPIGKAIPLPTSVMSYGKNKLRAEYWFSVPKNRVDELYRFINTWVKHLYGELDEEQIKARGFELIQEDTEWTKSGTTKAGMGGGSQDGEEISDLTRESWEVLSMSTDEYRKTSLFATGSFDLDFPIPDLIGKTEILTEEHREKLCSHLPARAEGYSWSLIFSTSQHGFALNSLYRKMARLESPVLIVIEDTEHNVFGALTSCSLHVSDHFYGTGESLLYKFNPSFKVFHWTGENMYFIKGNMESLSIGAGDGRFGLWLDGDLNQGRSQQCSTYGNEPLAPQEDFVIKTLECWAFV
Protein: BclA protein (Q81JD7)
Organism: Bacillus anthracis
Interaction partners:
Sequence:
MSNNNYSNGLNPDESLSASAFDPNLVGPTLPPIPPFTLPTGPTGPTGPTGPTGPTGPTGPTGPTGPTGPTGDTGTTGPTGPTGPTGPTGPTGDTGTTGPTGPTGPTGPTGPTGPTGPTGDTGTTGPTGPTGPTGPTGPTGDTGTTGPTGPTGPTGPTGPTGPTGPTGPTGPTGPTGPTGPTGPTGDTGTTGPTGPTGPTGPTGPTGDTGTTGPTGPTGPTGPTGPTGPTGPTGATGLTGPTGPTGPSGLGLPAGLYAFNSGGISLDLGINDPVPFNTVGSQFGTAISQLDADTFVISETGFYKITVIANTATASVLGGLTIQVNGVPVPGTGSSLISLGAPIVIQAITQITTTPSLVEVIVTGLGLSLALGTSASIIIEKVA
Protein: G-patch domain and KOW motifs-containing protein homolog 1 (Protein mos-2 homolog) (Q21924)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9C801}.
Interaction partners:
- Probable pre-mRNA-splicing factor ATP-dependent RNA helicase mog-4
- Probable pre-mRNA-splicing factor ATP-dependent RNA helicase mog-1
- BUD13 homolog
- Septin and tuftelin-interacting protein 1 homolog
- Large ribosomal subunit protein mL54
- Pre-mRNA-splicing factor 8 homolog
- Splicing factor 3B subunit 3
- Probable ribosome biogenesis protein RLP24
- RNA-binding protein 5
- PWI domain-containing protein
Sequence:
MVEQTTSEPAAGSMPKISFGVKKREENKVQAPAKAVVIEVDLDSDEEREKNEMERAAKRRKVMHFEDGTVQGDIDKPKEAAVIPMVVEHDWRTQKLIEKEKAGTLTEEERAKLALVLPNGIDGENEEESGKGEKIVVEDGRGDTEDADYSAIPIESFGLAILRGCNWKDGDGIGKNPQKVALKLPNRRPPGLGLGATPKNPVGKNKNTGESSKAEEEKLEEIKVGSFIKVVDGRNKGVYGKVEGRDDDSNSLFIRTAIGGKTMKVSQIVAVAVSAKEYERDSKCLNKSEYDKEKDRLETERKKLESQPPSTSTSQSSKDYKSKSSSSKHDKNSSEYERNDKMWARTDLLVRFIDEDFKRGSLYEQKVRIVDVAGDNDVTIEDDRGNTHYNIRQSWLETVIPREIGEKLMIVAGKRSGQLAVMLDKDKRKEKVTARLVATNDVVTAYFEDVCSVKIRHEEDYE
Protein: Glutamine sensor PIB2 (Phosphatidylinositol 3-phosphate-binding protein 2) (P53191)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as an intracellular glutamine sensor that directly activates the TORC1 signaling pathway, to promote cell growth when glutamine is available. May play a role in repressing NPR1 activity independently of TORC1 signaling.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:26510498, ECO:0000269|PubMed:29698392}; Peripheral membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- GTP-binding protein GTR1
- GTP-binding protein GTR2
- Protein MEH1
- Serine/threonine-protein kinase TOR1
- Protein SLM4
- Target of rapamycin complex 1 subunit KOG1
- Target of rapamycin complex 1 subunit TCO89
- Protein PAR32
- Protein LST4
Sequence:
MTALHSVSKTPAIKEEEEDGDERDGRGVPLGPRNHDYRGRKGDEESGADTVTSPITFEKKKIAPRASTHSEQSILSSISLKSMVNQHRQQQLQQESSTGAGTGFVDRKQQIQSPAMVSILRKNSAEENVRSSHSSKLGEGQIDGRKASASKEIGKTLPFTDDQRSNPELDPTNSVVDVSRGKNTKSKTVFNELEDDADDDDEVRQKNLTTQALRKLSSFKMNASSNLRLSKENKAKESSSSSTSSVSSSSTSKVENIVDKLTTTNSSSMSQLRFGNTNVIIDSVNHAAKPPHQQMLRKPSLEFLPQPASSTNLNFNSNKHKSNVRQISNPKKPLYIPAVLRKVSETNITNDDLLNATLSSYYKKASNLEHGFNPSKSQSASVQNANNLRIISSQSSVQSNTSSILESYKNKISSYLFPNSIPNSDRINLIPTISNRNSARVNPPTKDHWIPDSKRNSCRYCHKPFTLWERKHHCRHCGDIFCQDHLRHWLYLDSQANFIMINELNNGGINGGGTLCKICDDCLVEYENLSTTNHNANTNEDNINVEEGEDDDNDNRKKLRNYYKNRQMNALFRPKKGGSSQEHATVDRDTTTPIQVKSNDEEADNENTGGEQEEGNDVLGSVIGSVPANWNWSSF
Protein: Pleiotropic regulator 1 (O43660)
Organism: Homo sapiens (Human)
Function: Involved in pre-mRNA splicing as component of the spliceosome. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing.
Subcellular location: Nucleus {ECO:0000269|PubMed:11101529, ECO:0000269|PubMed:20176811, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770}. Nucleus speckle {ECO:0000269|PubMed:11544257}.
Interaction partners:
- SNW domain-containing protein 1
- Protein BUD31 homolog
- Pre-mRNA-splicing factor SYF2
- Pre-mRNA-splicing factor SPF27
- Small nuclear ribonucleoprotein F
- Spliceosome-associated protein CWC15 homolog
- Cell division cycle 5-like protein
- Pre-mRNA-splicing factor RBM22
- Splicing factor YJU2
- Pre-mRNA-splicing factor SYF1
Sequence:
MVEEVQKHSVHTLVFRSLKRTHDMFVADNGKPVPLDEESHKRKMAIKLRNEYGPVLHMPTSKENLKEKGPQNATDSYVHKQYPANQGQEVEYFVAGTHPYPPGPGVALTADTKIQRMPSESAAQSLAVALPLQTKADANRTAPSGSEYRHPGASDRPQPTAMNSIVMETGNTKNSALMAKKAPTMPKPQWHPPWKLYRVISGHLGWVRCIAVEPGNQWFVTGSADRTIKIWDLASGKLKLSLTGHISTVRGVIVSTRSPYLFSCGEDKQVKCWDLEYNKVIRHYHGHLSAVYGLDLHPTIDVLVTCSRDSTARIWDVRTKASVHTLSGHTNAVATVRCQAAEPQIITGSHDTTIRLWDLVAGKTRVTLTNHKKSVRAVVLHPRHYTFASGSPDNIKQWKFPDGSFIQNLSGHNAIINTLTVNSDGVLVSGADNGTMHLWDWRTGYNFQRVHAAVQPGSLDSESGIFACAFDQSESRLLTAEADKTIKVYREDDTATEETHPVSWKPEIIKRKRF
Protein: Large ribosomal subunit protein mL39 (39S ribosomal protein L39, mitochondrial) (MRP-L39) (MRP-L5) (Q9VUJ0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9NYK5}.
Interaction partners:
- Large ribosomal subunit protein uL22m
- Large ribosomal subunit protein uL1m
- Small ribosomal subunit protein mS31
- Small ribosomal subunit protein uS12m
- GM03767p
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein bL32m
- Large ribosomal subunit protein mL44
Sequence:
MSAATKLHKTSWCALRQLQQYRTKANFSGSSASLAKRNDLFNQEQRRQRDAVGRIDKIEVRYLGLPEDVTLVMNGNISTPFNCAQHLSEGHCKRSALALIDGSVPWDMHRPLQESCTLQLLNFHVSEPHVVNKAFWRTCSFMLGAALNRAFKPEANLQLHSFPGPNIKSGSFVHDIVLQTQNWEPGKEEMRALSAEMVKLAAQDLRIERLDVQQDLAQEMFKDSKYKSEQLPSISQQTNGRVTLYRLGDHIDISRGPMVASTSFLGKCVISAAHKVAEEGPSGAFYRIQGVALPSGFQLNHVAFGVLEERSKKPSPARLPNEPFEEQQQLQLS
Protein: X-box-binding protein 1 (F6ZM55)
Organism: Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis)
Interaction partners:
- Uncharacterized protein
Sequence:
MKMAPTATTHTVVISPSSKLVPVTMANQARTEVEFVGSPQQIPKYALGLFESNGNGPRKRKRLTHLTTEEKVMRRKLKNRVAAQTARDRKKVRMECLEDNIQKVQQQAKELLDVNMQLLERAEALERENRELRVRLGISSSHDTTVSSKREDVERIKLEFDDLVAQSEQTPDVIAVSLPECILSPDESADEFDHHMDIKRRLCEPRSDVAAKRLCLAKTECASPVPAVFGEHKLDRLSPQQQDAVNLMLIHSEKAKVKSQAPTSQMKPHIMRMISLDGSNKSVMNLSLKKESATKLQTPLDLSKNIKLQ
Protein: Peptidyl-prolyl cis-trans isomerase FKBP13, chloroplastic (PPIase FKBP13) (EC 5.2.1.8) (FK506-binding protein 1) (FK506-binding protein 13) (AtFKBP13) (Immunophilin FKBP13) (Rotamase) (Q9SCY2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Responsive of the major PPIase activity in the chloroplast thylakoid lumen. Regulates the accumulation of Rieske protein, an essential component of the photosynthetic electron transport chain.
Subcellular location: Plastid, chloroplast thylakoid lumen {ECO:0000269|PubMed:11719511}.
Interaction partners:
- Thiol-disulfide oxidoreductase LTO1
- Peptidyl-prolyl cis-trans isomerase FKBP16-1, chloroplastic
- Peptidyl-prolyl cis-trans isomerase CYP38, chloroplastic
- Photosynthetic NDH subunit of lumenal location 5, chloroplastic
- Peptidyl-prolyl cis-trans isomerase CYP20-3, chloroplastic
- Thylakoid lumenal 17.4 kDa protein, chloroplastic
- Peptidyl-prolyl cis-trans isomerase FKBP17-2, chloroplastic
- Protein disulfide-isomerase LQY1, chloroplastic
- Thioredoxin-like protein HCF164, chloroplastic
- Peptidyl-prolyl cis-trans isomerase CYP59
Sequence:
MSSLGFSVGTCSPPSEKRKCRFLVNNSLNKAEAINLRNKQKVSSDPELSFAQLSSCGRREAIIGFGFSIGLLDNVSALAETTSCEFSVSPSGLAFCDKVVGYGPEAVKGQLIKAHYVGKLENGKVFDSSYNRGKPLTFRIGVGEVIKGWDQGILGSDGIPPMLTGGKRTLRIPPELAYGDRGAGCKGGSCLIPPASVLLFDIEYIGKA
Protein: V-type proton ATPase 116 kDa subunit a 2 (V-ATPase 116 kDa subunit a 2) (Lysosomal H(+)-transporting ATPase V0 subunit a 2) (TJ6) (Vacuolar proton translocating ATPase 116 kDa subunit a isoform 2) (Q9Y487)
Organism: Homo sapiens (Human)
Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Essential component of the endosomal pH-sensing machinery. May play a role in maintaining the Golgi functions, such as glycosylation maturation, by controlling the Golgi pH. In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation.
Subcellular location: Cell membrane; Multi-pass membrane protein. Endosome membrane. Note=In kidney proximal tubules, also detected in subapical vesicles. {ECO:0000250}.
Interaction partners:
- V-type proton ATPase subunit d 1
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit d 2
- V-type proton ATPase subunit F
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit S1
- V-type proton ATPase subunit D
- V-type proton ATPase subunit B, brain isoform
- V-type proton ATPase subunit E 1
- V-type proton ATPase subunit H
Sequence:
MGSLFRSETMCLAQLFLQSGTAYECLSALGEKGLVQFRDLNQNVSSFQRKFVGEVKRCEELERILVYLVQEINRADIPLPEGEASPPAPPLKQVLEMQEQLQKLEVELREVTKNKEKLRKNLLELIEYTHMLRVTKTFVKRNVEFEPTYEEFPSLESDSLLDYSCMQRLGAKLGFVSGLINQGKVEAFEKMLWRVCKGYTIVSYAELDESLEDPETGEVIKWYVFLISFWGEQIGHKVKKICDCYHCHVYPYPNTAEERREIQEGLNTRIQDLYTVLHKTEDYLRQVLCKAAESVYSRVIQVKKMKAIYHMLNMCSFDVTNKCLIAEVWCPEADLQDLRRALEEGSRESGATIPSFMNIIPTKETPPTRIRTNKFTEGFQNIVDAYGVGSYREVNPALFTIITFPFLFAVMFGDFGHGFVMFLFALLLVLNENHPRLNQSQEIMRMFFNGRYILLLMGLFSVYTGLIYNDCFSKSVNLFGSGWNVSAMYSSSHPPAEHKKMVLWNDSVVRHNSILQLDPSIPGVFRGPYPLGIDPIWNLATNRLTFLNSFKMKMSVILGIIHMTFGVILGIFNHLHFRKKFNIYLVSIPELLFMLCIFGYLIFMIFYKWLVFSAETSRVAPSILIEFINMFLFPASKTSGLYTGQEYVQRVLLVVTALSVPVLFLGKPLFLLWLHNGRSCFGVNRSGYTLIRKDSEEEVSLLGSQDIEEGNHQVEDGCREMACEEFNFGEILMTQVIHSIEYCLGCISNTASYLRLWALSLAHAQLSDVLWAMLMRVGLRVDTTYGVLLLLPVIALFAVLTIFILLIMEGLSAFLHAIRLHWVEFQNKFYVGAGTKFVPFSFSLLSSKFNNDDSVA
Protein: Duplicated homeodomain-like superfamily protein (MYB transcription factor) (Q9LFB6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- AT4g33900 family protein)
- Extracellular ligand-gated ion channel protein
- At1g13195
- AT5g37540/mpa22_p_70
- Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SEC
- Kelch repeat-containing protein At3g27220
- Myb-related protein 2
- 1,4-dihydroxy-2-naphthoyl-CoA thioesterase 1
- Receptor-like protein 54
- Telomere repeat-binding factor 3
Sequence:
MSSSTMYRGVNMFSPANTNWIFQEVREATWTAEENKRFEKALAYLDDKDNLESWSKIADLIPGKTVADVIKRYKELEDDVSDIEAGLIPIPGYGGDASSAANSDYFFGLENSSYGYDYVVGGKRSSPAMTDCFRSPMPEKERKKGVPWTEDEHLRFLMGLKKYGKGDWRNIAKSFVTTRTPTQVASHAQKYFLRQLTDGKDKRRSSIHDITTVNIPDADASATATTADVALSPTPANSFDVFLQPNPHYSFASASASSYYNAFPQWS
Protein: Caprin homolog (Q9I7D3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Lipid droplet {ECO:0000269|PubMed:16979555}.
Interaction partners:
- AT27578p
- FI04408p
- Fragile X messenger ribonucleoprotein 1 homolog
- ubiquitinyl hydrolase 1
- Eukaryotic translation initiation factor 4E1
Sequence:
MPSAANTATVTAAIATTVAASASNTNNNSVSKEKRSSIISLGGSVIPGTAVAAGAGVATTNGQSNSSAAATADGSQTDLASSNNNGNAAKSKANAVSAAAVVPEPYNPLKQLLVTIEHKIRNLEKRKTKLESYRAIQSSGKELSGDQASAVAKYDAVLANLEFARELAKHIQQQSKEAEKEQKKQARKDNLAKTIAETAKIREVLIIQNVLNCFNDDQVRSDFLNGENGAKKLENTELELLEKFFIETQTRRPETADDVSFIATAQKSAELFYSTINARPKSFGEVSFEKLRSLFQQIQDSGYLDKYYLVPLAENAVANSTDSGTGSGDGESGDLLNDGSGELDAELPSEPSARNSLEEGLDKLHLGVQAELDQHQSYQQQQERPSHLLEPQHQRAPSLEHQQNSMVQQVSTQVYQAAPQAGGTTTPVHVLYAPAPPAQQQPQQPPPHPHQLLSSPVNLQALQTGTAAPPAQQQQPHPTHFAPNVRAVEQNYFKQPPQHPQGPGIQAPQTPQQQQFMQHSRPLAEVLGTGRFHFLQDSELDNPEALAPPPPTNQGLVFEQQPQQPNHVEEPTQAILTLTFTNQSFPSQQPQPQQQGPQQQQQLFSPVLIHEQRQQPPQQQPQPMLIMPRLPTQQPQQPAPQGIGMQAGDVTSGFSYENAVVSYEQQIQQQLKQQQQQQQQQQQNLQQLDEPSSVNSSSSVGAGGDVENNEWHARNNDTNAAATAALTNVLKGETTQATPPAPPTKWSSEMNAMSSAASNGSSNTSHKQEWATPRDHSTGGGNSGYADNNESNNHWNNSQGDGRRNSGNYQRRGGDRDNRDRDQGGRGDERRNGGDRGNYRSRQYGNSSNTNGRNSGNSSGVYFRNNESGNGGGNNYYQNGGGGGGTYNKESRYESSGGGGGSYRGQRGGNQQRNVNGSYGGGRPMGDRGRGGAGNQGGGGGGYINRQNQSQRMPLGLENKN
Protein: 15-hydroxyprostaglandin dehydrogenase [NAD(+)] (15-PGDH) (EC 1.1.1.141) (Eicosanoid/docosanoid dehydrogenase [NAD(+)]) (EC 1.1.1.-, EC 1.1.1.232) (Prostaglandin dehydrogenase 1) (Q3T0C2)
Organism: Bos taurus (Bovine)
Function: Catalyzes the NAD-dependent dehydrogenation (oxidation) of a broad array of hydroxylated polyunsaturated fatty acids (mainly eicosanoids and docosanoids, including prostaglandins, lipoxins and resolvins), yielding their corresponding keto (oxo) metabolites. Decreases the levels of the pro-proliferative prostaglandins such as prostaglandin E2 (whose activity is increased in cancer because of an increase in the expression of cyclooxygenase 2) and generates oxo-fatty acid products that can profoundly influence cell function by abrogating pro-inflammatory cytokine expression. Converts resolvins E1, D1 and D2 to their oxo products, which represents a mode of resolvin inactivation. Resolvin E1 plays important roles during the resolution phase of acute inflammation, while resolvins D1 and D2 have a unique role in obesity-induced adipose inflammation.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Prostaglandin E synthase
Sequence:
MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVKCKAALDEQFEPQKTLFIQCDVADQEQLRDTFRKVVDHFGKLDILVNNAGVNNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEGGININMSSLAGLMPVAQQPVYCASKHGIVGFTRSAAMAANLMNSGVRLNAICPGFVDTPILKSIEKEENMGKYIEYMGPIKDMMKYYGILDPSMIANGLITLIEDDALNGAIMKITTSKGIHFQDYDTTPFHMKMQ