wanglab/gogpt-training-data huggingface dataset:
Protein: Disintegrin and metalloproteinase domain-containing protein 29 (ADAM 29) (Q811Q4)
Organism: Mus musculus (Mouse)
Function: May be involved in spermatogenesis and fertilization. Seems to be a non catalytic metalloprotease-like protein (By similarity).
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MNMIEALLSMRVLFLTQVFGIFLCFPGLTKAGHLHYHSSIEVVIPMKVTEKTRGMNLPNWISYSLKLGGQRYIIHMKIKNLFLTRHLPVFTYSDQDSLLEDYPFVQDDCYYQGYVEGDSESLVSLSSCFGGFHGLLEINNIVYEIMPKKFSRKFEHLVYKVDINKTESRGSSLMQDNITCQVELQKSGNPILKQSSFEDWWTHTKIVELVVVVDKTLYDHYGNYTVMLSDLYSVINIVDTIYEVIGIKILLVGVEVWNKKNLIVIDDVSKSLRLYCRWKASNFLHRLKHDVSHLFIYRHLRGLSGIGSTGGICDPKRSCAVVTFIDRTLNLRAIGVAHHLGHNLGMKHDEDICKCSYSKCIMHMDSPPIPKFSNCSYNYFWSYTVKNTRCLMENMYTKDIFDRTRCGNGVVEDKEQCDCGSLRNCTNDLCCMSNCTLSTGSSCAFGLCCKNCQFLPSGTLCRKRDNICDLPEWCNGTSHECPDDAYVEDGIPCGVSAYCYEKQCNDRNEHCRQIFGQNAKTASVHCYREINTKGDRFGHCGLQGPTYIKCKSNDALCGRIQCDNVVQIPNMKDHSTIHFALVKNVSCWGTDYHTGTSLTDIGDVKDGTECEQNHICINRHCVHISTLDSNCTPAFCNYRGICNNKHHCHCNFHWDPPNCMIRGHGGSVDSGLPPKTNKKKHFFYLLLLQLIILACLLSCLLWLLFNIKGSKRKPQVQPTPVKTKKVSKKVPSQKPSPVPSPSLPQLRMPSRSASPTSSIKSTN
Protein: Sensor for unfolded proteins in the ER ire1 [Includes: Serine/threonine-protein kinase (EC 2.7.11.1); Endoribonuclease (EC 3.1.26.-) (Serine/threonine-protein kinase 4)] (O94537)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Endoplasmic reticulum (ER) membrane-resident kinase/endoribonuclease involved in unfolded protein response (UPR). Initiates the selective decay of a subset of ER-localized-mRNAs that is required to survive ER stress. Rather than relying on a transcriptional program to up-regulate genes that enhance ER protein folding capacity as in S.cerevisiae, S.pombe cells reduce the amount of specific proteins entering the organelle by decreasing the level of ER-targeted mRNAs using ire1-dependent mRNA degradation. The sole mRNA cleaved upon ire1 activation that escapes decay is the ER chaperone bip1 mRNA which is more stable and hence is present at an increased steady-state after ire1 cleavage. Promotes ER stress-induced ER-phagy and via up-regulation of the protein level of the ER-phagy receptor epr1 (Ref.5).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-pass type I membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- tRNA ligase 1
- Endoplasmic reticulum chaperone BiP
- ERAD-associated E3 ubiquitin-protein ligase hrd1
- Metacaspase-1
Sequence:
MKSLKGRLLFLRKFVFFSLLILLFAHGASSSSSSFNYFDKRTNGKANNELALFSPTADSPSSVDGVLELPSAENVFAESSLYNAFIVATVDGSLHSYDRITGQELWSLFTNANPGLSYTKDENSLLSSKFLSQSNFKSYNSTHGEFYSDSTLNISYLSDDDTVWFVEPIDGGILYAFNLQTGLVRLPHSIKDLVHASPIRLLNNNVFVGSKNTTLFTIDVSNGDIVSQYPSGHRYETHHSVHNLGTKRDSVPSGADSDLSFKDPSGKKLSESLDLLDDFNYQVTVSNKSFVDIARTEYFITIYSDSNVILDLVYIDWTPTKNEIMYESFHSSSFDSKLALSSYDSSLHIVDTHSKFIKQNIPLMSPAATVFDIVTLPHNKKIDKSQTPAKFPTSVLLRQPIDTYLETMFPQIARNKTEHVYINHIGNAWFAMSERHYPLVSLAPEASFLYYNGFYIPLNSIFGLHSLMATPKPFFALPGLPGYDIPSYVESEGSTKTLPSIGKKPIPLLDPNPISSTPISITFWVIMFLSVSFTIVTFFSILRIRSSEVRPLKSQKNTVSINNKIDTSKRRRKGKRRKRVSDEHSASSNFNEIESQASFEQNQTLDILSENIVEIQDKSTDPLQKSLDSSLKSHLPEATVIQNTDGSVTVNSLTVYPEVIGYGSHGTIVYRGVYEDREVAVKRVLMEFYDLASREITLLQQSDNHPNIVRYYCKQKSDQFLYIVIELCKCNLSDLIEKPIAYDDLFKSIDLVSLLYQIAFGVSHLHSLDLVHRDLKPQNILLVVNNSPNLSKTRVRALISDFGLSKKLDFNQSSLRNTTFEAAGSYGWRSPEILSGSLSQQSKEIQVKTREGRIRQASHATDIFALGCIFYYTLTGGMHPFGSHYDCEGNILKGNYCLVHLQSLGECGVLAADLIEDMIAFEPSKRPTIEVVLNHPLFWDYAKKLDFLIDVSDRFEVEERDPPSPLLQMLENNSKSVIGENWTTCLHSSLVDNLGKYRKYDGSKILDILRVLRNKRHHYQDLPESVRRVLGDLPDGFTSYFVEKFPMLLLHCYHLVKDVLYEESQFKRYLEY
Protein: SSD domain-containing protein (O16530)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- SKN-1 Dependent Zygotic transcript
Sequence:
MKSVKKTHDVSDNTWFVRIIHWFFQKCSAVICYCPWTCIILTIMLTLVLSLKIPFTRMQNDISDFTPFGARSRVELEKYRKFFNNHGEPKAIYAFITSKVGDNMLGISQLNDTVHVLDTISRDFYLKTSQGPKNFEEYCSGFCLLNEPVKHFYSGMLISGQHGTDFSHLDLGYPITTVLGTKLYMDPNFFGVKVTTSNNKVESIADGNTKLFGDHTKQEPNNIREVSLVVLQFRSELGDEVTPEDLRNYEHQILDYIHDEYQSEHINVYILTDSYITEEIVRAGLTLLPFLVIGFTIMAVFSSITFVVSAYYTKQLNFYKPILAVMACVCPFMACGASLGAMFFIGFRFGSILCVTPFLVLAIGVDDSYLMANAWQRITCHRRKHARFESVNVELKNRITEMFIETGPSITITTITNALAFGIGATTPAAEIQLFSIGNALAVITDFVFTITFYGALMAVVGRYEIEQELKTQKPLPESESPSETSSTGSMRSSELDDCKFRRMIANVCKFLTNTWVCSVVLGLLAVYWYICIVGTVNIKSELSPNKLFLAESNIVEIFKQRKSHIIPYYSACWVLVENPGDINNPNQRAKLEELIESFEALPSANGRYSTKFWLRDYEDFLKQSEEIDLPMEEEEDEELAIQFTVNGSQVVTPSQPFGQGNELRQFLEWPEFSFWKGFIQVNESTYQMSKFLVTTAYHGSDLVDWSNRAKLLNEWRSVADQDKFKSLNVTVYEEDAKFLDLIETMSPVAIQSALWTFASMFLVAALFISHPPTLFVATFSILSTSLGVFGIMSWWGADLDPIMMSATVMSIGFSVDIPSHVSYHFYQTAKDTSDIRRRLQMTIEAVGFPIFEASLSTSLCVMSLFFVDLNMAQIFAKCMLLVVVIGMVHGMLVMPVIFALLDTVPRKLKPRKQHLASTVTVVTVVP
Protein: Propanediol dehydratase medium subunit (EC 4.2.1.28) (Diol dehydratase medium subunit) (DDH medium subunit) (Propanediol utilization protein PduD) (O31041)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Part of the PduCDE complex that catalyzes the dehydration of 1,2-propanediol (1,2-PD) to propionaldehyde. Required for S.typhimurium growth on 1,2-PD as the sole carbon and energy source (Probable). This subunit is directly targeted to the bacterial microcompartment (BMC) dedicated to 1,2-PD degradation, and is also responsible for targeting the other 2 subunits (pduC and pduE).
Subcellular location: Bacterial microcompartment {ECO:0000269|PubMed:10498708, ECO:0000269|PubMed:11844753, ECO:0000269|PubMed:12923081, ECO:0000269|PubMed:21821773, ECO:0000269|PubMed:26283792}. Note=Probably located inside the BMC shell. {ECO:0000305|PubMed:10498708, ECO:0000305|PubMed:21821773}.
Interaction partners:
- Propanediol dehydratase large subunit
- Propanal dehydrogenase
- Propanediol dehydratase small subunit
- Bacterial microcompartment shell protein PduB
- Propanediol dehydratase-reactivating factor small subunit
- 1-propanol dehydrogenase PduQ
- Propanediol dehydratase-reactivating factor large subunit
- Corrinoid adenosyltransferase PduO
- Bacterial microcompartment shell protein PduK
- Phosphate propanoyltransferase
Sequence:
MEINEKLLRQIIEDVLRDMKGSDKPVSFNAPAASTAPQTAAPAGDGFLTEVGEARQGTQQDEVIIAVGPAFGLAQTVNIVGLPHKSILREVIAGIEEEGIKARVIRCFKSSDVAFVAVEGNRLSGSGISIGIQSKGTTVIHQQGLPPLSNLELFPQAPLLTLETYRQIGKNAARYAKRESPQPVPTLNDQMARPKYQAKSAILHIKETKYVVTGKNPQELRVAL
Protein: Spermatid nuclear transition protein 1 (STP-1) (TP-1) (P17306)
Organism: Sus scrofa (Pig)
Function: Plays a key role in the replacement of histones to protamine in the elongating spermatids of mammals. In condensing spermatids, loaded onto the nucleosomes, where it promotes the recruitment and processing of protamines, which are responsible for histone eviction.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P10856}. Chromosome {ECO:0000250|UniProtKB:P10856}. Note=Loaded onto the nucleosomes of condensing spermatids. {ECO:0000250|UniProtKB:P10856}.
Interaction partners:
- Nuclear transition protein 2
- Protamine-2
- Acrosin
- Stimulated by retinoic acid 8
- Testis expressed metallothionein like protein
Sequence:
MSTSRKLKSHGMRRGKNRAPHKGVKRGGSKRKYRKGSLKSRKRCDDANRNYRSHL
Protein: Protein yippee-like 2 (Q96QA6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:15556292}.
Interaction partners:
Sequence:
MVKMTRSKTFQAYLPSCHRTYSCIHCRAHLANHDELISKSFQGSQGRAYLFNSVVNVGCGPAEERVLLTGLHAVADIYCENCKTTLGWKYEHAFESSQKYKEGKYIIELAHMIKDNGWD
Protein: Transmembrane reductase CYB561D2 (EC 7.2.1.3) (Cytochrome b561 domain-containing protein 2) (Q9WUE3)
Organism: Mus musculus (Mouse)
Function: Transmembrane reductase that may use ascorbate as an electron donor in the cytoplasm and transfer electrons across endoplasmic reticulum membranes to reduce monodehydro-L-ascorbate radical and iron cations Fe(3+) in the lumen of that compartment.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17938141}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53TN4}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:17938141}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53TN4}.
Interaction partners:
- GATOR1 complex protein NPRL2
Sequence:
MALSVETESHIYRALRTASGAAAHLVALGFTIFVAVLARPGSSLFSWHPVLMSLAFSFLMTEALLMFSPESSLLRSLSRKVRARCHWVLQLLALLCALLGLGLVILHKEQLGKAHLTTRHGQAGLLAVLWAGLQCSGGMGLLYPKLLPRWPLAKLKLYHATSGLVGYLLGSASLLLGMFSLWFTATVTGGAWYLAVLCPILTSLVIMNQVSNAYLYRKRIQP
Protein: Protein enhancer of rudimentary (Q94554)
Organism: Drosophila virilis (Fruit fly)
Function: Acts as an enhancer of the rudimentary gene. Has a role in pyrimidine biosynthesis and the cell cycle.
Interaction partners:
Sequence:
MSHTILLVQPGARPETRTYCDYESVNECMEGVCKIYEEHLKRRNPNTPTITYDISQLFDFIDTLIDISCLVYQKSTNTYAPYNKDWIKEKIYVLLRQAAFSPNA
Protein: Pre-mRNA-processing factor 17 (O43071)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions in the second step of pre-mRNA splicing. Involved in splicing intron which are longer than 200 nucleotides.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Pre-mRNA-splicing factor ATP-dependent RNA helicase prp16
- Pre-mRNA-splicing factor cwf18
- Pre-mRNA-splicing factor cwf4
- Pre-mRNA-splicing factor cwf17
- Pre-mRNA-splicing factor cwf15
- Small nuclear ribonucleoprotein F
- Pre-mRNA-splicing factor cwf14
- Pre-mRNA-splicing factor cwf7
- Pre-mRNA-splicing factor spp42
- Small nuclear ribonucleoprotein Sm D3
Sequence:
MLVANYSSDSEEQENSQSPNIQPLLHTENLAPAVVDNVKDDLIVSKGGNSRELARNVPVNEMVQPALGPANPFVTKEQDSIKNSITGYAEREYVPNFVFNQEYYANTHAIYGKRNFDDNEATTSTDLKRKSQKIKERREDPGDPSILEGDGAYKGPWAGYGSEQSSSPLEYSEYEEVESLDVKSEKDTESNNLGQNELLKEQLATPEVETHRSKEETILHKDRLFDYQNRSYMHVPNDVGINLSEEPGEQTCYIPKKHIFTWKGHTKGISCLRFFPISGHLLLSGSMDNQIKIWEVYHDRSLLRTFQGHARPIRDLSFSQDGRSFLSTSFDKTIKLWDTELGKCLNCFNSDRLTNCVKFQVDPDKPNEFLAGTADKRILQFDIRSPDIVQAYDHHLGGINSITFLENGKRFVTTSDDSSMRFWEYGTPVPIKFVADIAMHSMPRVALRPNGKSIACQSLDNCIYVYSAYEKYRQNKKKVFKGYSCSGYSLEVGFSPDGRFVFSGDSSGNACFWDWKTCKLMAKLPAHSGPVQSMAFHPQETSKVATSSIVDGSIKYWD
Protein: Uncharacterized protein (Q54PZ3)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Kinesin-related protein 8
- Coiled-coil domain-containing protein 87
- Kinesin-related protein 13
- Kinesin-related protein 10
- Probable serine/threonine-protein kinase mps1
- SAP domain-containing protein
- Uncharacterized protein
Sequence:
MIGNEIIIINKDNCNYNHYLSSKIIEKYYNQINPLIIKYDNILQSLEDNNDDDNNDENDTNKNQHQQLNKEIIELIENKIGQQKEREQILIEKKSNLLIEINKLIQSLDLTPNKFEIDNEIQSDYNTLIQSTLLKTPKLLKQINHLNNFNINLKNVFIKLNNNNNNNNNNNNNNNNNKVYSELMKLYKELGIDLSDNKDTEYVSSSFIEIGISVSNKRIDEIENEIKKLQDIRNSIMDKINDSKSIALNLKNQLELESTIENNENNELNQILNKLKLNDDDDGDDCSKNKLEMKSLIQILYKIEGIIKTFELMKEKRLKQINNQINSIERDYQQLSIPLNDETRLNFKLKRNKLPPPSIPSLSLINLLTQESNHLTNLKKLKFKDSFQSKFKSLQSLWDQLCIPLNQRNLKDLLLNNNNNNDNNNNNDEIDYSNEINYYNIETLEIIDKEIKLLNELLDSMKSILNKVKRREWIKSEMKNFETSASDPSRFKGSSIRLLEEAKFRKTIAREYPILTTDLVKELAEWENQNQKSFLYFGNSYLELMNTEQDRPDFHLLHLKLVTKKDPENISDSPMVSYSSTTSSPTTTTTSSPTSSPTTSTINVQQQPQEQPQQTQQNIRPTTPTTPQRPTTPLSKKPSPLTKKPSSSSSSPSSSFTTSPTTPKIPTLSKASSSLNLSPTSVGNNSSSGGGGKIPSLSKTMSSVNLTTTTINSNPTVNKPTPSKKESPILITPSKPKSSPTTSSSSSSVNMTSKSPLTTTTTNKK
Protein: Tumor necrosis factor receptor superfamily member 10A (Death receptor 4) (TNF-related apoptosis-inducing ligand receptor 1) (TRAIL receptor 1) (TRAIL-R1) (CD antigen CD261) (O00220)
Organism: Homo sapiens (Human)
Function: Receptor for the cytotoxic ligand TNFSF10/TRAIL. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Promotes the activation of NF-kappa-B.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22240897}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000269|PubMed:19090789, ECO:0000269|PubMed:22240897}. Cytoplasm, cytosol {ECO:0000269|PubMed:22240897}. Note=Palmitoylation is required for association with membranes. {ECO:0000269|PubMed:22240897}.
Interaction partners:
- Tumor necrosis factor ligand superfamily member 10
- FAS-associated death domain protein
- Tumor necrosis factor ligand superfamily member 6
- Tumor necrosis factor receptor superfamily member 25
- Tumor necrosis factor receptor superfamily member 10B
- Caspase-8
- Tumor necrosis factor
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- CASP8 and FADD-like apoptosis regulator
- Receptor-interacting serine/threonine-protein kinase 1
Sequence:
MAPPPARVHLGAFLAVTPNPGSAASGTEAAAATPSKVWGSSAGRIEPRGGGRGALPTSMGQHGPSARARAGRAPGPRPAREASPRLRVHKTFKFVVVGVLLQVVPSSAATIKLHDQSIGTQQWEHSPLGELCPPGSHRSEHPGACNRCTEGVGYTNASNNLFACLPCTACKSDEEERSPCTTTRNTACQCKPGTFRNDNSAEMCRKCSRGCPRGMVKVKDCTPWSDIECVHKESGNGHNIWVILVVTLVVPLLLVAVLIVCCCIGSGCGGDPKCMDRVCFWRLGLLRGPGAEDNAHNEILSNADSLSTFVSEQQMESQEPADLTGVTVQSPGEAQCLLGPAEAEGSQRRRLLVPANGADPTETLMLFFDKFANIVPFDSWDQLMRQLDLTKNEIDVVRAGTAGPGDALYAMLMKWVNKTGRNASIHTLLDALERMEERHAREKIQDLLVDSGKFIYLEDGTGSAVSLE
Protein: Villin-1 (Q62468)
Organism: Mus musculus (Mouse)
Function: Epithelial cell-specific Ca(2+)-regulated actin-modifying protein that modulates the reorganization of microvillar actin filaments. Plays a role in the actin nucleation, actin filament bundle assembly, actin filament capping and severing. Binds phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA); binds LPA with higher affinity than PIP2. Binding to LPA increases its phosphorylation by SRC and inhibits all actin-modifying activities. Binding to PIP2 inhibits actin-capping and -severing activities but enhances actin-bundling activity. Regulates the intestinal epithelial cell morphology, cell invasion, cell migration and apoptosis. Protects against apoptosis induced by dextran sodium sulfate (DSS) in the gastrointestinal epithelium. Appears to regulate cell death by maintaining mitochondrial integrity. Enhances hepatocyte growth factor (HGF)-induced epithelial cell motility, chemotaxis and wound repair. Upon S.flexneri cell infection, its actin-severing activity enhances actin-based motility of the bacteria and plays a role during the dissemination.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, microvillus {ECO:0000250}. Cell projection, lamellipodium. Cell projection, ruffle {ECO:0000250}. Cell projection, filopodium tip. Cell projection, filopodium. Note=Rapidly redistributed to ruffles and lamellipodia structures in response to autotaxin, lysophosphatidic acid (LPA) and epidermal growth factor (EGF) treatment (By similarity). Relocalized in the tip of cellular protrusions and filipodial extensions upon infection with S.flexneri in primary intestinal epithelial cells (IEC) and in the tail-like structures forming the actin comets of S.flexneri. Redistributed to the leading edge of hepatocyte growth factor (HGF)-induced lamellipodia. {ECO:0000250}.
Interaction partners:
- Espin
- Leucine-rich repeat-containing G-protein coupled receptor 5
- Mucin-2
- Homeobox protein CDX-2
- Chromogranin-A
- Olfactomedin-4
Sequence:
MTKLNAQVKGSLNITTPGIQIWRIEAMQMVPVPSSTFGSFFDGDCYVVLAIHKTSSTLSYDIHYWIGQDSSQDEQGAAAIYTTQMDDYLKGRAVQHREVQGNESETFRSYFKQGLVIRKGGVASGMKHVETNSCDVQRLLHVKGKRNVLAGEVEMSWKSFNRGDVFLLDLGKLIIQWNGPESNRMERLRGMALAKEIRDQERGGRTYVGVVDGEKEGDSPQLMAIMNHVLGPRKELKAAISDSVVEPAAKAALKLYHVSDSEGKLVVREVATRPLTQDLLKHEDCYILDQGGLKIFVWKGKNANAQERSGAMSQALNFIKAKQYPPSTQVEVQNDGAESPIFQQLFQKWTVPNRTSGLGKTHTVGSVAKVEQVKFDALTMHVQPQVAAQQKMVDDGSGEVQVWRIEDLELVPVESKWLGHFYGGDCYLLLYTYLIGEKQHYLLYIWQGSQASQDEIAASAYQAVLLDQKYNDEPVQIRVTMGKEPPHLMSIFKGRMVVYQGGTSRKNNLEPVPSTRLFQVRGTNADNTKAFEVTARATSLNSNDVFILKTPSCCYLWCGKGCSGDEREMAKMVADTISRTEKQVVVEGQEPANFWMALGGKAPYANTKRLQEENQVITPRLFECSNQTGRFLATEIFDFNQDDLEEEDVFLLDVWDQVFFWIGKHANEEEKKAAATTVQEYLKTHPGNRDLETPIIVVKQGHEPPTFTGWFLAWDPFKWSNTKSYDDLKAELGNSGDWSQIADEVMSPKVDVFTANTSLSSGPLPTFPLEQLVNKSVEDLPEGVDPSRKEEHLSTEDFTRALGMTPAAFSALPRWKQQNIKKEKGLF
Protein: tRNA-splicing endonuclease subunit Sen34 (EC 4.6.1.16) (Q0E8E7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- tRNA splicing endonuclease subunit 54
- tRNA splicing endonuclease subunit 15, isoform A
- tRNA-intron lyase
- Ribonuclease Z, mitochondrial
- Probable arginine--tRNA ligase, mitochondrial
- 2'-phosphotransferase
Sequence:
MYLTLLNGTGFVFNVDDYMELRSKHRIMGAPVGTANTKGWSPNQSTLPVELSKFETQLLLDENIAKLVDKSKDLKAKPTAEKLEECKADFESRLLGQEEALKTEKLRETERYMDKILTGKRKKLLKQGKNELAAALTDKDVLLEMSVNFKFDRQNALLEVHCEHPTDHSAQIVTGPIVHTNSLKYRVFKDLWRRGKYVTSGDAFGADFLVYPGDPMIYHASHIVILHEQPVIKPLELIAKVRLSVIVNKSCVFAYEMENNEEEIHYQTVAWCNLGK
Protein: Protein trichome birefringence-like 26 (O04621)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the O-acetylation of mannan. May act as a bridging protein that binds pectin and other cell wall polysaccharides. Probably involved in maintaining esterification of pectins (By similarity).
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Tubulin beta-4 chain
- At5g50410
- At5g38130
- Jacalin-related lectin 23
- Regulator of G-protein signaling 1
- Probable serine/threonine-protein kinase WNK10
- Myrosinase-binding protein 1
- GDSL esterase/lipase At1g54020
- Serine/threonine-protein kinase WNK8
- Guanine nucleotide-binding protein subunit beta
Sequence:
MEQQLTLVLLDSPKGAKYVETFEEAASSSSSSSSSSVPSCTDHRHRTFVKFFLYFSLVALAYYFIISSLAVSPIPPTLPQSSPGNVSSAKCDLFTGDWIPDPTGPLYTNVTCRHIQDFQNCLLNGRPDVNYLFWRWKPRDCDLPRFSPSQFLASVKNKWWAFIGDSIARNHVQSLICILSQVEEVEEIYHDKEFRSKIWRFPSHNFTLSVIWSPFLLKSETSSNSDIQLYLDQLDHKWTVQYPKFDYVVISGGKWFLKTTIFHENNVVTGCHYCQGRNNLTDLGYDYSYRKTLNLLRDFVLNSTHKPLVLFRTTTPDHFENGEWNTGGYCNRTMPFKEGQANMKTVDDVMRDVELEVFQKFGKGFGLGSNIRLLDTTGMSLLRPDGHPGPYRHPNPFAGVKNKSNVQNDCLHWCLPGPIDSWNDVMVETTLNRERELYDLTG
Protein: Syntaxin-binding protein 2 (MUSEC1) (Protein unc-18 homolog 2) (Munc18-2) (Unc18-2) (Protein unc-18 homolog B) (Unc-18B) (Q64324)
Organism: Mus musculus (Mouse)
Function: Involved in intracellular vesicle trafficking and vesicle fusion with membranes. Contributes to the granule exocytosis machinery through interaction with soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins that regulate membrane fusion. Regulates cytotoxic granule exocytosis in natural killer (NK) cells (By similarity).
Interaction partners:
- Syntaxin-11
- Syntaxin-3
- Syntaxin-19
- Vesicle-associated membrane protein 8
- Vesicle-associated membrane protein 2
- Syntaxin-2
- Syntaxin-1A
- Protein unc-13 homolog D
- Syntaxin-4
- Synaptosomal-associated protein 23
Sequence:
MAPLGLKAVVGEKILSGVIRSVKKDGEWKVLIMDHPSMRILSSCCKMSDILAEGITIVEDINKRREPIPSLEAIYLLSPTEKSVQALIADFQGTPTFTYKAAHIFFTDTCPEPLFSELGRSRLAKAVKTLKEIHLAFLPYEAQVFSLDAPHSTYNLYCPFRAGERGRQLDALAQQIATLCATLQEYPSIRYRKGPEDTAQLAHAVLAKLNAFKADTPSLGEGPEKTRSQLLIMDRAADPVSPLLHELTFQAMAYDLLDIEQDTYRYETTGLSESREKAVLLDEDDDLWVELRHMHIADVSKKVTELLKTFCESKRLTTDKANIKDLSHILKKMPQYQKELNKYSTHLHLADDCMKHFKGSVEKLCSVEQDLAMGSDAEGEKIKDAMKLIVPVLLDASVPPYDKIRVLLLYILLRNGVSEENLAKLIQHANVQSYSSLIRNLEQLGGTVTNSAGSGTSSRLERRERMEPTYQLSRWSPVIKDVMEDVVEDRLDRKLWPFVSDPAPVPSSQAAVSARFGHWHKNKAGVEARAGPRLIVYIVGGVAMSEMRAAYEVTRATEGKWEVLIGSSHILTPTRFLDDLKTLDQKLEGVALP
Protein: Secernin-2 (Q96FV2)
Organism: Homo sapiens (Human)
Interaction partners:
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 2/3 complex subunit 4
- NCK-interacting protein with SH3 domain
Sequence:
MASSSPDSPCSCDCFVSVPPASAIPAVIFAKNSDRPRDEVQEVVFVPAGTHTPGSRLQCTYIEVEQVSKTHAVILSRPSWLWGAEMGANEHGVCIGNEAVWTKEPVGEGEALLGMDLLRLALERSSSAQEALHVITGLLEHYGQGGNCLEDAAPFSYHSTFLLADRTEAWVLETAGRLWAAQRIQEGARNISNQLSIGTDISAQHPELRTHAQAKGWWDGQGAFDFAQIFSLTQQPVRMEAAKARFQAGRELLRQRQGGITAEVMMGILRDKESGICMDSGGFRTTASMVSVLPQDPTQPCVHFLTATPDPSRSVFKPFIFGMGVAQAPQVLSPTFGAQDPVRTLPRFQTQVDRRHTLYRGHQAALGLMERDQDRGQQLQQKQQDLEQEGLEATQGLLAGEWAPPLWELGSLFQAFVKRESQAYA
Protein: Chitinase 5 (EC 3.2.1.-, EC 3.2.1.14) (LP08894p) (Q9VFR3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- N-acetyl-D-glucosamine kinase
- beta-N-acetylhexosaminidase
- Knickkopf
- beta-N-acetylhexosaminidase
- chitin synthase
Sequence:
MVRYIPLLLLGVLCSWPAATVASDQASRIVCYFSNWAVYRTGIGRYGLEDVPADLCTHIIYSFIGVNDKSWDVLVIDPELDVDQGGFSKFTQLKKSNPNVKLEIAVGGWAEGGSKYSQMVAVRDRRQSFIRSVVRFMKQYNFDGFDLDWEYPGATDRGGNYGDKDKFLYFVEELRRAFDREGRGWEITMAVPVAKFRLNEGYHVPELCEALDAIHAMTYDLRGNWAGFADVHSPLYKRKHDQYAYEKLNVNDGLALWEEMGCPANKLVVGVPFYGRTFTLSNSNKNYNMGTYINKEAGGGAPGPYTNASGFLAYYEICTEVMDKSKGWTVEWDDAGMVPYTYKDTQWVGYENEASIQIKMDFIKQRGYAGAMTWAIDMDDFHGMCGRKNGLTQILYDNMKNYRVPEPTRQTTPRPEWAKPPATPPNPDEGAVVAPTTSTTKRPKPKPKPTSSPLSPTSAPGPVPTVGSSTPKPTTKKPKKPKKTTTTTTTTPAPEKSTEEPEEVVYPVDPVEPTDPEQPMGPQFDPNEIDCTNRDFVPHPNCRKYFRCVHGKPVEFECKEGTAFHTVLNVCDWIENSDRYYCSRMKNKEKGNEAH
Protein: Rho guanine nucleotide exchange factor 19 (Ephexin-2) (Q8IW93)
Organism: Homo sapiens (Human)
Function: Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase.
Interaction partners:
- Disheveled-associated activator of morphogenesis 1
- Transforming protein RhoA
- Rho guanine nucleotide exchange factor 35
Sequence:
MDCGPPATLQPHLTGPPGTAHHPVAVCQQESLSFAELPALKPPSPVCLDLFPVAPEELRAPGSRWSLGTPAPLQGLLWPLSPGGSDTEITSGGMRPSRAGSWPHCPGAQPPALEGPWSPRHTQPQRRASHGSEKKSAWRKMRVYQREEVPGCPEAHAVFLEPGQVVQEQALSTEEPRVELSGSTRVSLEGPERRRFSASELMTRLHSSLRLGRNSAARALISGSGTGAAREGKASGMEARSVEMSGDRVSRPAPGDSREGDWSEPRLDTQEEPPLGSRSTNERRQSRFLLNSVLYQEYSDVASARELRRQQREEEGPGDEAEGAEEGPGPPRANLSPSSSFRAQRSARGSTFSLWQDIPDVRGSGVLATLSLRDCKLQEAKFELITSEASYIHSLSVAVGHFLGSAELSECLGAQDKQWLFSKLPEVKSTSERFLQDLEQRLEADVLRFSVCDVVLDHCPAFRRVYLPYVTNQAYQERTYQRLLLENPRFPGILARLEESPVCQRLPLTSFLILPFQRITRLKMLVENILKRTAQGSEDEDMATKAFNALKELVQECNASVQSMKRTEELIHLSKKIHFEGKIFPLISQARWLVRHGELVELAPLPAAPPAKLKLSSKAVYLHLFNDCLLLSRRKELGKFAVFVHAKMAELQVRDLSLKLQGIPGHVFLLQLLHGQHMKHQFLLRARTESEKQRWISALCPSSPQEDKEVISEGEDCPQVQCVRTYKALHPDELTLEKTDILSVRTWTSDGWLEGVRLADGEKGWVPQAYVEEISSLSARLRNLRENKRVTSATSKLGEAPV
Protein: Ovarian cancer G-protein coupled receptor 1 (OGR-1) (G-protein coupled receptor 68) (GPR12A) (Sphingosylphosphorylcholine receptor) (Q15743)
Organism: Homo sapiens (Human)
Function: Proton-sensing receptor involved in pH homeostasis. May represents an osteoblastic pH sensor regulating cell-mediated responses to acidosis in bone. Mediates its action by association with G proteins that stimulates inositol phosphate (IP) production or Ca(2+) mobilization. The receptor is almost silent at pH 7.8 but fully activated at pH 6.8. Also functions as a metastasis suppressor gene in prostate cancer (By similarity).
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Mitogen-activated protein kinase kinase kinase 4
- Probable G-protein coupled receptor 132
Sequence:
MGNITADNSSMSCTIDHTIHQTLAPVVYVTVLVVGFPANCLSLYFGYLQIKARNELGVYLCNLTVADLFYICSLPFWLQYVLQHDNWSHGDLSCQVCGILLYENIYISVGFLCCISVDRYLAVAHPFRFHQFRTLKAAVGVSVVIWAKELLTSIYFLMHEEVIEDENQHRVCFEHYPIQAWQRAINYYRFLVGFLFPICLLLASYQGILRAVRRSHGTQKSRKDQIQRLVLSTVVIFLACFLPYHVLLLVRSVWEASCDFAKGVFNAYHFSLLLTSFNCVADPVLYCFVSETTHRDLARLRGACLAFLTCSRTGRAREAYPLGAPEASGKSGAQGEEPELLTKLHPAFQTPNSPGSGGFPTGRLA