wanglab/gogpt-training-data huggingface dataset:
Protein: Ras-related protein Rab6 (Protein warthog) (O18334)
Organism: Drosophila melanogaster (Fruit fly)
Function: Protein transport. Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER). Mediates membrane trafficking during egg chamber growth and organization, possibly upstream of exocyst component Sec5. Also during oogenesis, plays a role, together with BicD but independently of Sec5, in the polarization of the oocyte microtubule cytoskeleton, in the localization of oskar mRNA and in the anterodorsal secretion of grk. Required for anterograde opsin transport through the ER-Golgi complex. Plays a role, together with Rich, in regulating CadN transport in photoreceptor cells which is required for the formation of normal synaptic connections between axons from the inner photoreceptor cells in the eye and postsynaptic cells in the brain medulla layer M6. Necessary for proper development of bristle shafts of macrochaete and microchaete on the head, thorax and scutellum. Modulates Notch signaling. As a key regulator of vesicular traffic, plays a critical role in the regulation of actin organization and is required for normal rates of phagocytic uptake during phagocytosis involved in defense against viral and fungal infection.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:17827179, ECO:0000269|PubMed:21835342, ECO:0000269|PubMed:22000105}. Synapse {ECO:0000269|PubMed:17827179, ECO:0000269|PubMed:21835342, ECO:0000269|PubMed:22000105}. Perikaryon {ECO:0000269|PubMed:17827179, ECO:0000269|PubMed:21835342, ECO:0000269|PubMed:22000105}. Note=Colocalizes with Rich at the Golgi apparatus. During oogenesis, first accumulates transiently in a central position during stages 7-8, then is uniformly distributed at the beginning of stage 9 to end up juxtaposed to the entire oocyte cortex. {ECO:0000269|PubMed:17827179, ECO:0000269|PubMed:21835342, ECO:0000269|PubMed:22000105}.
Interaction partners:
- Rab GDP dissociation inhibitor
- Protein bicaudal D
- ADP-ribosylation factor-like protein 1
- FI04457p
- Vacuolar protein sorting-associated protein 39 homolog
- Guanine nucleotide exchange factor subunit Rich
- Vacuolar protein sorting-associated protein 52 homolog
- Vacuolar protein sorting-associated protein 53 homolog
- Syntaxin 16
- GRIP and coiled-coil domain containing 88 kDa
Sequence:
MSSGDFGNPLRKFKLVFLGEQSVGKTSLITRFMYDSFDNTYQATIGIDFLSKTMYLEDRTVRLQLWDTAGQERFRSLIPSYIRDSTVAVVVYDITNTNSFHQTSKWIDDVRTERGSDVIIMLVGNKTDLSDKRQVSTEEGERKAKELNVMFIETSAKAGYNVKQLFRRVAAALPGMDSTENKPSEDMQEVVLKDSPNETKDPEGGCAC
Protein: Galactosylceramide sulfotransferase (GalCer sulfotransferase) (EC 2.8.2.11) (3'-phosphoadenosine-5'-phosphosulfate:GalCer sulfotransferase) (3'-phosphoadenylylsulfate:galactosylceramide 3'-sulfotransferase) (Cerebroside sulfotransferase) (Q99999)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of a sulfate group to position 3 of non-reducing beta-galactosyl residues in glycerolipids and sphingolipids, therefore participates in the biosynthesis of sulfoglycolipids. Catalyzes the synthesis of galactosylceramide sulfate (sulfatide), a major lipid component of the myelin sheath and of monogalactosylalkylacylglycerol sulfate (seminolipid), present in spermatocytes. Seems to prefer beta-glycosides at the non-reducing termini of sugar chains attached to a lipid moiety. Also acts on lactosylceramide, galactosyl 1-alkyl-2-sn-glycerol and galactosyl diacylglycerol (in vitro).
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- 2-hydroxyacylsphingosine 1-beta-galactosyltransferase
- Galactocerebrosidase
- Sialidase-2
- Sialidase-4
- Alpha-galactosidase A
- Sialidase-1
- Sialidase-3
- Leucine-rich repeats and immunoglobulin-like domains protein 3
Sequence:
MLPPQKKPWESMAKGLVLGALFTSFLLLVYSYAVPPLHAGLASTTPEAAASCSPPALEPEAVIRANGSAGECQPRRNIVFLKTHKTASSTLLNILFRFGQKHRLKFAFPNGRNDFDYPTFFARSLVQDYRPGACFNIICNHMRFHYDEVRGLVPTNAIFITVLRDPARLFESSFHYFGPVVPLTWKLSAGDKLTEFLQDPDRYYDPNGFNAHYLRNLLFFDLGYDNSLDPSSPQVQEHILEVERRFHLVLLQEYFDESLVLLKDLLCWELEDVLYFKLNARRDSPVPRLSGELYGRATAWNMLDSHLYRHFNASFWRKVEAFGRERMAREVAALRHANERMRTICIDGGHAVDAAAIQDEAMQPWQPLGTKSILGYNLKKSIGQRHAQLCRRMLTPEIQYLMDLGANLWVTKLWKFIRDFLRW
Protein: SD06673p (Q960D2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSACAAADALAMPPPPPPATTSAAYQFLHPSKKSELNSINSRLQNIALDAEEPPSDISTISTNTVRNAGRPSRELHGMVHSTPKSGSVEPLRHRPLDDNILLEIDHYLDDNNAHRWQRHDHHLHHRSDDHLRNERAGKEGHPGTSSLPSMRLASSSSGAVSVEAARVDRSSLNENKIISLSELWGKSSLTKTVLDNNSPNRPLCSSSLKEEQLRRQHLEKMVHTLQSHLLEYQQRISVAIEVDRSKDAALTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQSRFDALQNELSQAVNLATRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVDYQQEKLKARIEELEKENNTLTNQKEMLQEYHQKQKARADSLESHRKSLQETLANLTETETNLKKKLDIQQKSLKQYYQQQMENVVAKKMQEFQDQLDKNEEHLKNEARERERLIAERAVKQLEMINEKNNQELNLIQEKHNEEVELYRLQLANASKKIDEMDLKLSCYKTKRADIAEKLHGVMEAQWQQALAILTTPSQNSIIQSSDTEASESPELNNARMYPETPKSSKSQRSNNTEKNNLDVVGKRDPPSPMDKLQAYIELLLSKSPSDFDRLDEILAMTSKQGSKQSKPKSGSGNSKPPPWKC
Protein: H-2 class II histocompatibility antigen, A-F beta chain (P06346)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
AAVVVLMVLSSPGTEGGNSERHFVSQFKGECYFTNGTQRIRSVDRYIYNREEYLRFDSDVGEYRAVTELGRSDAEYYNKQYLERTRAELDTVCRHNYEGVETPTSLRRLEQPNVVISLSRTEALNHHNTLVCSVTDFYPAKIKVRWFRNGQEETVGVSSTQLIRNGDWTFQVLVMLEMAPRRGEVYTCHVEHPSLKSPITVEWRAQSESARSKMLSGIGGCVLGVIFLGLGLFIRYRSQKGPRGPPPAGLLQ
Protein: Kaposi's sarcoma-associated herpesvirus cyclin homolog (Q98147)
Organism: Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Interaction partners:
Sequence:
MATANNPPSGLLDPTLCEDRIFYNILEIEPRFLTSDSVFGTFQQSLTSHMRKLLGTWMFSVCQEYNLEPNVVALALNLLDRLLLIKQVSKEHFQKTGSACLLVASKLRSLTPISTSSLCYAAADSFSRQELIDQEKELLEKLAWRTEAVLATDVTSFLLLKLVGGSQHLDFWHHEVNTLITKALVDPKTGSLPASIISAAGCALLVPANVIPQDTHSGGVVPQLASILGCDVSVLQAAVEQILTSVSDFDLRILDSY
Protein: phosphoinositide 5-phosphatase (EC 3.1.3.36) (Q54D97)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Phosphatidylinositol-3-phosphatase SAC1
- 1-phosphatidylinositol 4-kinase
- Rac guanine nucleotide exchange factor B
- Uncharacterized protein
- SAC domain-containing protein
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Inositol 5-phosphatase 4
- Phosphatidylinositol 4-kinase
- 1-phosphatidylinositol 4-kinase
- 1-phosphatidylinositol-5-phosphate 4-kinase
Sequence:
MADNTFRIFITTQSFIIKRDSLHSKALVINRRDPSKIDIIQPDQIDQSLRSERSVYCVLGIFRLVNECYLVVVTESDIAANFQFQGQPNVIRKIRCTDFISFQTGRGHISIGGGGGGGGSGNGESKEDDRPYVQVMNLLNSGHFYWTPPNSSFDITRTYQSQCLEPKSDLPVWERVDKRFYWNKYLQKDFIAYRLYDWCFPIIQGFVVSDHLGHIQGKNVVYTLISRRSRFRAGTRFVTRGIDDDGNVANFCESEQILSIESYGVLAFLQIRGSVPVFWNQSSPQMSDLKIKMSNLSKIGKISKKKITIARNTQATTPAFQLHLKEQTKKYGNIVIVNLLSKLKSGECDLVNAYEEQIRILRSPQVFYNHFDLNEQTKGNRMDPLDSLINYIDNQSISGGGGTTGGVSEKIVGYFFQNSNGQIISKQNGIIRTNCKDCLDRTNIVQSRVSWVLFESQLRKLGLFRGHDSIGSYPRVSQTLKTTWADNGDALSIQYAGSGSLKSTLTREGDYGIMGMLADGKKTMTRFYINNFKDPGRQDVLDLLLGLHKSMVVNNSNNGNGGNGGNGSGHDDNIRKQVQDRVKEYSKKEWRNVFVGTYNVGGVHSSYFDLVQWLRPDGANCPTPDFYVLGLQEVVELTAGQILATDSSIGKQWEDAIERALPKVSPNVKYIKLQSSQLVGLLMAIYVREDAIHYFREVQIQNVKCGMNGLAGNKGGIGVRLLFSDTSFTFVTAHFAAGQSNVEDRISDFREIDSTLAFGRQGQFKVSDSDYSFWLGDFNFRIDLPDEEIRRCVYDQQFPKLYNYDQLRKCMEAGRVFNGYREETIAFPPTYKYDLNSTQYDTSQKQRSPAWTDRIVWSNKVHHDLRQLYYHRQEILASDHRPVSSYFQLEVTKIDKDKERTLRQELYEQKSSQFITTSQSTNNLINTTNQNGKDGANLITKEFEQLTLIKQSASTPNLQKGRSNTTNIQYQITSTNQISNTNNNTIQQQQHHQELVNVTTTRKNSLNSNNNNNNNNINNSNNTLVASGGSNGVPPRKLSSGRPLPMLPQPIQIPPTQQQQQQQQQQQQQQQQETVNLQKMTGSGGGRKISSSPSSSFNNTNSIGSSSSPSGAHSPIFDDQFDPRKGRSSPVPQSFNENNNSNQSKMELLIPNQNSTQYQQQQQQQQQQQQQQQQQQQQQQQQQQQQPQYNSNLYNSGPPPLQPIHQSNLNPNSNYNQQLQQPPPQPINHDLQLIDSWGNSSNGYQSREPPPLQPIPQSVYQSQPPPLQPIPQSVYQPTNFALQQPLQPMMSPPPLLYSNQKAVYNIPVPSPYNQQQQQPQQPYQQPYQQPYQQPYQQNLYNQPPPLNNSYNNYNNQNNNNNNQNNNNTYNNPYLGSILD
Protein: Peroxisome assembly protein 12 (Peroxin-12) (Peroxisome assembly factor 3) (PAF-3) (O88177)
Organism: Rattus norvegicus (Rat)
Function: Component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling (By similarity). The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane (By similarity). PEX12 also regulates PEX5 recycling by activating the E3 ubiquitin-protein ligase activity of PEX10 (By similarity). When PEX5 recycling is compromised, PEX12 stimulates PEX10-mediated polyubiquitination of PEX5, leading to its subsequent degradation (By similarity).
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:9354782}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Peroxisome biogenesis factor 10
- Peroxisomal membrane protein PEX13
- Peroxisomal membrane protein PEX14
- Peroxisome biogenesis factor 2
- Peroxisomal targeting signal 1 receptor
- Peroxisomal ATPase PEX6
- Peroxisomal biogenesis factor 3
- Peroxisomal biogenesis factor 19
- Peroxisomal targeting signal 1 receptor.
- Peroxisomal targeting signal 2 receptor
Sequence:
MAEHGAHITTASVADDQPSIFEVVAQDSLMTAVRPALQHVVKVLAESNPAHYGFFWRWFDEIFTLLDFLLQQHYLSRTSASFSEHFYGLKRIVAGSSPQLQRPASAGLPKEHLWKSAMFLVLLPYLKVKLEKLASTLREEDEYSIHPPSSHWKRFYRVFLAAYPFVTMTWEGWFLTQQLRYILGKAEHHSPLLKLAGVRLGRLTAQDIQAMEHRLVEASAMQEPVRSIGKKIKSALKKAVGGVALSLSTGLSVGVFFLQFLDWWYSSENQETIKSLTALPTPPPPVHLDYNSDSPLLPKMKTVCPLCRKARVNDTVLATSGYVFCYRCVFNYVRSHQACPITGYPTEVQHLIKLYSPEN
Protein: Secretin (P09910)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Hormone involved in different processes, such as regulation of the pH of the duodenal content, food intake and water homeostasis (By similarity). Exerts its biological effects by binding to secretin receptor (SCTR), a G-protein coupled receptor expressed in the basolateral domain of several cells (By similarity). Acts as a key gastrointestinal hormone by regulating the pH of the duodenal content (By similarity). Secreted by S cells of the duodenum in the crypts of Lieberkuehn and regulates the pH of the duodenum by (1) inhibiting the secretion of gastric acid from the parietal cells of the stomach and (2) stimulating the production of bicarbonate (NaHCO(3)) from the ductal cells of the pancreas. Production of bicarbonate is essential to neutralize the pH and ensure no damage is done to the small intestine by the gastric acid. In addition to regulating the pH of the duodenal content, plays a central role in diet induced thermogenesis: acts as a non-sympathetic brown fat (BAT) activator mediating prandial thermogenesis, which consequentially induces satiation (By similarity). Mechanistically, secretin released by the gut after a meal binds to secretin receptor (SCTR) in brown adipocytes, activating brown fat thermogenesis by stimulating lipolysis, which is sensed in the brain and promotes satiation. Also able to stimulate lipolysis in white adipocytes (By similarity). Also plays an important role in cellular osmoregulation: released into the systemic circulation in response to hyperosmolality and acts at different levels in the hypothalamus, pituitary and kidney to regulate water homeostasis (By similarity). Also plays a role in the central nervous system, possibly by acting as a neuropeptide hormone: required for hippocampal synaptic function and neural progenitor cells maintenance (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:3626755}.
Interaction partners:
Sequence:
HSDGTFTSELSRLRESARLQRLLQGLV
Protein: PQ loop repeat containing 2 isoform 1 (PQ loop repeat containing 2, isoform CRA_b) (A0A024RAA1)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MDQALSLWFLLGWIGGDSCNLIGSFLADQLPLQTYTAVYYVLADLVMLTLYFYYKFRTRPSLLSAPINSVLLFLMGMACATPLLSAAGPVAAPREAFRGRALLSVESGSKPFTRQEVIGFVIGSISSVLYLLSRLPQIRTNFLRKSTQGISYSLFALVMLGNTLYGLSVLLKNPEEGQSEGSYLLHHLPWLVGSLGVLLLDTIISIQFLVYRRSTAASELEPLLPS
Protein: Arrestin-C (Cone arrestin) (C-arrestin) (cArr) (Retinal cone arrestin-3) (X-arrestin) (P36575)
Organism: Homo sapiens (Human)
Function: May play a role in an as yet undefined retina-specific signal transduction. Could bind to photoactivated-phosphorylated red/green opsins.
Subcellular location: Photoreceptor inner segment {ECO:0000250|UniProtKB:Q9EQP6}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:Q9EQP6}.
Interaction partners:
- Rhodopsin
- Short-wave-sensitive opsin 1
- Beta-adrenergic receptor kinase 1
- Retinol-binding protein 3
- Mitogen-activated protein kinase kinase kinase 5
- Recoverin
- Beta-2 adrenergic receptor
- Neurabin-2
- Photoreceptor-specific nuclear receptor
- Cone-rod homeobox protein
Sequence:
MSKVFKKTSSNGKLSIYLGKRDFVDHVDTVEPIDGVVLVDPEYLKCRKLFVMLTCAFRYGRDDLEVIGLTFRKDLYVQTLQVVPAESSSPQGPLTVLQERLLHKLGDNAYPFTLQMVTNLPCSVTLQPGPEDAGKPCGIDFEVKSFCAENPEETVSKRDYVRLVVRKVQFAPPEAGPGPSAQTIRRFLLSAQPLQLQAWMDREVHYHGEPISVNVSINNCTNKVIKKIKISVDQITDVVLYSLDKYTKTVFIQEFTETVAANSSFSQSFAVTPILAASCQKRGLALDGKLKHEDTNLASSTIIRPGMDKELLGILVSYKVRVNLMVSCGGILGDLTASDVGVELPLVLIHPKPSHEAASSEDIVIEEFTRKGEEESQKAVEAEGDEGS
Protein: LD25711p (Rho GTPase activating protein at 18B, isoform B) (Rho GTPase activating protein at 18B, isoform F) (Rho GTPase activating protein at 18B, isoform H) (RhoGAP18B-PA) (Q9VWL9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAGDTENKRGYRTIFRSISQVFYANAKNSSNTNSSSSNNNNNIINYNNNTIENNNEGIGQLTVTLTSITPPTATWTSTSPTISTCTTASASAGSSTASLSPLASRSARSAENISCSECGNPDPYHGQDMELAKGQALTPEVPAVPVPAASADQNQKLRASSMLDLTSNHRHQNGLRIVPVTDILRAQQIQEDNEVQQTQQSTILQRYKSVSIGNLLDLPGEDDKKSIKNRMRMKFAVNSNVFRINRSPKSEKKSRSRRGQVNSLYLDEQKYPLFAAPLSALELNMTDHPNVPRFVVDVCAYIEQPECIEQDGLYRASGNKVLVDELRKKLTHVYDPRWLKTDDIHTLTSLHKQFFRELTSPLITQEAYERLGRSLNDDAAIERMSLAFDDMPEPNRSTLRFLIRHLTRVAAASASNRMPSTNLAIVWGPCLLSANQIQLDIGRMNMLAKVLIENYDRIFHPDNERLVC
Protein: Proteasome subunit alpha type-4 (Macropain subunit PRE6) (Multicatalytic endopeptidase complex subunit PRE6) (Proteasome component PRE6) (Proteinase YSCE subunit PRE6) (P40303)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Proteasome subunit alpha type-2
- Proteasome subunit beta type-1
- Proteasome subunit beta type-2
- 26S proteasome regulatory subunit 8 homolog
- Proteasome subunit alpha type-5
- 26S proteasome regulatory subunit 4 homolog
- 26S proteasome regulatory subunit RPN9
- Proteasome subunit beta type-5
- 26S proteasome regulatory subunit 6B homolog
- 26S proteasome regulatory subunit RPN7
Sequence:
MSGYDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRITPSKVSKIDSHVVLSFSGLNADSRILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSGGVRPFGVSTLIAGFDPRDDEPKLYQTEPSGIYSSWSAQTIGRNSKTVREFLEKNYDRKEPPATVEECVKLTVRSLLEVVQTGAKNIEITVVKPDSDIVALSSEEINQYVTQIEQEKQEQQEQDKKKKSNH
Protein: NEDD4-binding protein 2 (N4BP2) (EC 3.-.-.-) (BCL-3-binding protein) (Q86UW6)
Organism: Homo sapiens (Human)
Function: Has 5'-polynucleotide kinase and nicking endonuclease activity. May play a role in DNA repair or recombination.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- NADH dehydrogenase 1 beta subcomplex subunit 7
Sequence:
MPRRRKNLGGNPFRKTANPKEVVVSSVASREEPTTTLPSMGETKVDQEELFTSISEIFSDLDPDVVYLMLSECDFKVENAMDCLLELSATDTKIEESSSQSFVASENQVGAAESKIMEKRPEEESEDSKMDSFLDMQLTEDLDSLIQNAFEKLNSSPDDQVYSFLPSQDVNSFNDSSEFINPDSSNMTPIFSTQNMNLNGENLENSGSTLSLNPLPSHSVLNESKCFIKDNTLALESNYPEDSLLSSSLNVASDSIAGCSSLNQKQKELLESECVEAQFSEAPVDLDASEPQACLNLPGLDLPGTGGDQKSTRVSDVFLPSEGFNFKPHKHPELPTKGKDVSYCPVLAPLPLLLPPPPPPPMWNPMIPAFDLFQGNHGFVAPVVTTAAHWRSVNYTFPPSVISHTSPTKVWRNKDGTSAYQVQETPVSQVVRKKTSYVGLVLVLLRGLPGSGKSFLARTLQEDNPSGVILSTDDYFYINGQYQFDVKYLGEAHEWNQNRAKEAFEKKISPIIIDNTNLQAWEMKPYVALSQKHKYKVLFREPDTWWKFKPKELARRNIHGVSKEKITRMLEHYQRFVSVPIIMSSSVPEKIERIELCAYSCEDRSTSPRDDEDIISEKEENILSLSLKHLEFTEEKNLDVTKETMLPENVAYLSNADLNKRRKEISDMNPSIQSALILETPHMYFSDSESKLQATDKSENEQIEMVAVKGYSKTDTDSSMERVSPSTCCSENNQEDCDLANSGPLQNEKSSPGEIVEERATVTKKAFGKQKSKSTLEKFPRHELSNFVGDWPVDKTIGQRTKRNRKTEKTSSVQSDKKYNYPQSHKLVNSVSVNTDCVQQRGSPHESVEDGRKSQCDDASEPLNSYKYDAYKNIDKNSFNIMGDWPSSDSLAQREHRSRMPKTGLSEPNLEIGTNDKMNEISLSTAHEACWGTSSQKLKTLGSSNLGSSEMLLSEMTCESQTCLSKKSHGQHTSLPLTFTNSAPTVSGVVEPQTLAECQEQMPKRDPGKEVGMCTQTEPQDFALLWKIEKNKISISDSIKVLTGRLDGFKPKVFNINTKSDVQEAIPYRVMYDKSTFVEESELTSADESENLNILCKLFGSFSLEALKDLYERCNKDIIWATSLLLDSETKLCEDTEFENFQKSCDGSQIGPFSLGLNLKEIISQRGTLENSNSPVPEFSHGIGISNADSQSTCDAERGNSEQAEMRAVTPENHESMTSIFPSAAVGLKNNNDILPNSQEELLYSSKQSFPGILKATTPKDMSETEKNLVVTETGDNIHSPSHFSDIFNFVSSTSNLELNEEIYFTDSLEIKRNENFPKDYVKFSDEEEFMNEDEKEMKEILMAGSSLSAGVSGEDKTEILNPTPAMAKSLTIDCLELALPPELAFQLNELFGPVGIDSGSLTVEDCVVHIDLNLAKVIHEKWKESVMERQRQEEVSCGKFMQDPSLVGHTGLDNPEQKSSQRTGKKLLKTLTASEMLPLLDHWNTQTKKVSLREIMSEEIALQEKHNLKRETLMFEKDCATKLKEKQLFKIFPAINQNFLVDIFKDHNYSLEHTVQFLNCVLEGDPVKTVVAQEFVHQNENVTSHTGQKSKEKKPKKLKETEETPSELSFQDFEYPDYDDYRAEAFLHQQKRMECYSKAKEAYRIGKKNVATFYAQQGTLHEQKMKEANHLAAIEIFEKVNASLLPQNVLDLHGLHVDEALEHLMRVLEKKTEEFKQNGGKPYLSVITGRGNHSQGGVARIKPAVIKYLISHSFRFSEIKPGCLKVMLK
Protein: T cell receptor beta, variable 1 (A0A0B4J1G7)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MWQFCILCLCVLMASVATDPTVTLLEQNPRWRLVPRGQAVNLRCILKNSQYPWMSWYQQDLQKQLQWLFTLRSPGDKEVKSLPGADYLATRVTDTELRLQVANMSQGRTLYCTCSA
Protein: SR-CI (Q5ELT0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEFFWTLAVIVIYCIGHIHGRCERSIDLDNGSINYRQRNIVRFRCNRGYTLQGTVMQTCDRDGRLRGEKPFCASRGCARPEDPENGHVENLSLRADVVCHDGYVLVGGRTAYCDGERWSTQLGSCRRSNHTRDHSCDFESEDQCGWEAETTFRRPWKRVSTVSDIHSLRTGPRHDHTFKNESGGHYMRMETQMGAYGSYHLLSPIYPRSLTLKTACCFRFHYFMFGAGVDNLVVSVKPVSMPMATMWNRFRANCSKFEISGQQGTQWLEHTISIDEMQEDFQVIFTATDARSQFGDIAIDDVKLMTGSECGTNGFSTTTEPTAPTGSNEQPLVYDMMSCSGRCGTSMSASNITNNGIVMGCGCNDECLSDETCCLNYLEECTKELLTTTEDDISSLPPTVTSTSTSTTRKSTTTTTTSTTTTSTTTTKRPTTTTTTTKATTTKRTTTTKKPTTTSTTPKPTTTTSTTPKSTTSTTSTTSTTPTTTTTINVFTTKKTTIMIPTSSTEKTTGIITTMKTRKRITWNVDPQDIEGHMDTSGSTPNPALVVLYLLLGIVLVVVLANVVNRWIIPITGSKTSSEKAVRFKKAFDSLKKQRKRNSMDDQPLCDSDNDDVEYFEEMGVDIRHRTDL
Protein: Vacuolar protein sorting-associated protein 5 (Carboxypeptidase Y-deficient protein 10) (Vacuolar protein-targeting protein 5) (Q92331)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Plays a role in vesicular protein sorting. Required for retention of late Golgi membrane proteins and vacuolar biogenesis. Component of the membrane-associated retromer complex which is essential in endosome-to-Golgi retrograde transport. The VPS5-VPS17 subcomplex may assemble onto the membrane to promote vesicle formation.
Subcellular location: Cytoplasm. Golgi apparatus membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Vacuolar protein sorting-associated protein 29
- Vacuolar protein sorting-associated protein 17
- Carboxypeptidase Y-deficient protein 8
- Vacuolar protein sorting-associated protein 35
- Sorting nexin-3
- Vacuolar protein sorting-associated protein 27
- Vacuolar protein sorting/targeting protein VPS10
- Sorting nexin-41
- Protein MUK1
- Sorting nexin MVP1
Sequence:
MDYEDNLEAPVWDELNHEGDKTQSLVSNSIESIGQISTNEERKDNELLETTASFADKIDLDSAPEWKDPGLSVAGNPQLEEHDNSKADDLINSLAPEQDPIADLKNSTTQFIATRESGGALFTGNANSPLVFDDTIYDANTSPNTSKSISGRRSGKPRILFDSARAQRNSKRNHSLKAKRTTASDDTIKTPFTDPLKKAEKENEFVEEPLDDRNERRENNEGKFTASVEKNILEQVDRPLYNLPQTGANISSPAEVEENSEKFGKTKIGSKVPPTEKAVAFKVEVKDPVKVGELTSIHVEYTVISESSLLELKYAQVSRRYRDFRWLYRQLQNNHWGKVIPPPPEKQSVGSFKENFIENRRFQMESMLKKICQDPVLQKDKDFLLFLTSDDFSSESKKRAFLTGSGAINDSNDLSEVRISEIQLLGAEDAAEVLKNGGIDAESHKGFMSISFSSLPKYNEADEFFIEKKQKIDELEDNLKKLSKSLEMVDTSRNTLAASTEEFSSMVETLASLNVSEPNSELLNNFADVHKSIKSSLERSSLQETLTMGVMLDDYIRSLASVKAIFNQRSKLGYFLVVIENDMNKKHSQLGKLGQNIHSEKFREMRKEFQTLERRYNLTKKQWQAVGDKIKDEFQGFSTDKIREFRNGMEISLEAAIESQKECIELWETFYQTNL
Protein: Cellulose synthase (EC 2.4.1.12) (P93155)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361116}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361116}.
Interaction partners:
- Cellulose synthase
- Cellulose synthase
- Cellulose synthase
- Cellulose synthase
Sequence:
MMESGVPVCHTCGEHVGLNVNGEPFVACHECNFPICKSCFEYDLKEGRKACLRCGSPYDENLLDDVEKATGDQSTMAAHLNKSQDVGIHARHISSVSTLDSEMAEDNGNSIWKNRVESWKEKKNKKKKPATTKVEREAEIPPEQQMEDKPAPDASQPLSTIIPIPKSRLAPYRTVIIMRLIILGLFFHYRVTNPVDSAFGLWLTSVICEIWFAFSWVLDQFPKWYPVNRETYIDRLSARYEREGEPDELAAVDFFVSTVDPLKEPPLITANTVLSILALDYPVDKVSCYISDDGAAMLTFESLVETADFARKWVPFCKKFSIEPRAPEFYFSQKIDYLKDKVQPSFVKERRAMKRDYEEYKIRINALVAKAQKTPDEGWTMQDGTSWPGNNPRDHPGMIQVFLGYSGARDIEGNELPRLVYVSREKRPGYQHHKKAGAENALVRVSAVLTNAPFILNLDCDHYVNNSKAVREAMCFLMDPQVGRDVCYVQFPQRFDGIDRSDRYANRNTVFFDVNMKGLDGIQGPVYVGTGCVFNRQALYGYGPPSMPSFPKSSSSSCSCCCPGKKEPKDPSELYRDAKREELDAAIFNLREIDNYDEYERSMLISQTSFEKTFGLSSVFIESTLMENGGVAESANPSTLIKEAIHVISCGYEEKTAWGKEIGWIYGSVTEDILTGFKMHCRGWRSIYCMPLRPAFKGSAPINLSDRLHQVLRWALGSVEIFLSRHCPLWYGFGGGRLKWLQRLAYINTIVYPFTSLPLIAYCSLPAICLLTGKFIIPTLSNLASVLFLGLFLSIIVTAVLELRWSGVSIEDLWRNEQFWVIGGVSAHLFAVFQGFLKMLAGIDTNFTVTAKAADDADFGELYIVKWTTLLIPPTTLLIVNMVGVVAGFSDALNKGYEAWGPLFGKVFFSFWVILHLYPFLKGLMGRQNRTPTIVVLWSVLLASVFSLVWVRINPFVSTADSTTVSQSCISIDC
Protein: Serine/threonine/tyrosine-interacting protein (Inactive tyrosine-protein phosphatase STYX) (Phosphoserine/threonine/tyrosine interaction protein) (Q8WUJ0)
Organism: Homo sapiens (Human)
Function: Catalytically inactive phosphatase. Acts as a nuclear anchor for MAPK1/MAPK3 (ERK1/ERK2). Modulates cell-fate decisions and cell migration by spatiotemporal regulation of MAPK1/MAPK3 (ERK1/ERK2). By binding to the F-box of FBXW7, prevents the assembly of FBXW7 into the SCF E3 ubiquitin-protein ligase complex, and thereby inhibits degradation of its substrates. Plays a role in spermatogenesis (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:23847209, ECO:0000269|PubMed:28007894}. Cytoplasm, cytosol {ECO:0000269|PubMed:23847209}. Note=Predominantly localizes to the nucleus. {ECO:0000269|PubMed:23847209, ECO:0000269|PubMed:28007894}.
Interaction partners:
- F-box/WD repeat-containing protein 7
Sequence:
MEDVKLEFPSLPQCKEDAEEWTYPMRREMQEILPGLFLGPYSSAMKSKLPVLQKHGITHIICIRQNIEANFIKPNFQQLFRYLVLDIADNPVENIIRFFPMTKEFIDGSLQMGGKVLVHGNAGISRSAAFVIAYIMETFGMKYRDAFAYVQERRFCINPNAGFVHQLQEYEAIYLAKLTIQMMSPLQIERSLSVHSGTTGSLKRTHEEEDDFGTMQVATAQNG
Protein: Protein transport protein SEC23 (Q95TD2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000256|RuleBase:RU365030}; Peripheral membrane protein {ECO:0000256|RuleBase:RU365030}; Cytoplasmic side {ECO:0000256|RuleBase:RU365030}. Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU365030}; Peripheral membrane protein {ECO:0000256|RuleBase:RU365030}; Cytoplasmic side {ECO:0000256|RuleBase:RU365030}.
Interaction partners:
Sequence:
MLGIGRGAAPGPQQQQHLPGQPAGAAAPVPPAHRFLQPIGQCDAALGDLLSELQRDPWPVPQGKRYLRSTGAALSIAVGLLECTYPNTGGRIMTFVGGPCSQGPGQVVDDELKHPIRSHHDIHKDNVRFMKKAIKHYDALALRAATNGHSVDIYSCALDQTGLLEMKQLCNSTGGHMVMGDSFNSSLFKQTFQRVFARDGRNDLKMAFNATLEVKCSRELKISGGIGSCVSLNVKSPSVSDVKIGMGNTVQWKLCTLNPSSTVAYFFEVVNQHAAPIPQGGRGCIQFITQYQHPSGQRRIRVTTLARKYVLA