wanglab/gogpt-training-data huggingface dataset:
Protein: Metabotropic glutamate receptor-like protein D (Q54L53)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Frizzled and smoothened-like protein B
- Frizzled and smoothened-like protein K
Sequence:
MKINSFLIILILLFISIKNSNGEPEKKFKLITLLAAHVQDLGFNNMVNRGHVEVSKAMKLEDSQAIVVVGYNDTIRILAPLVAVGDVDLVICSSQDHAQACRELATKYKGSSIKTQFLVRGSGEATSNLITYSYNYANANYISGYFAGLYTKTNKIGFLSPGAIDNNNDSFVYAFWYGAKRANPDISFYYYNIGNYLNPDKTVAATKDLLDMGCDMVADTLNDFSTGNTLIANNRKTAMGTSGFPQRDVYGEDVIYSYNYNWFKLFYPVAQSVYSGNTNNTNWYADFNLNETISFFGLSFSFTVPNETLTKFYEELDYLKRTPRLSHPYFCNDLMYEYAKKNHLTMSTNDSTHCLANSQFTRINAPFPGMTWLGNYEITLTEVYQSRPIQIAISSISSFFIVTVLVMMGLVVRFRKNPSIRSASPIFLNFILFGALIIYVGIIIWSSSINSASCNAQFWLVTLGFTTLIGSLVVKNVRIWLIFDNPELKLVKITNLQLVPWVGVCLVINIILMSILTSVGDLREVNAQGIDSLGKYEFMRICKMNSSGASTLYTILAYFAALLLIGVFVSWKIRIVDILEFNESKAIANTLYAISFCLFVIVPLMISPQDKQSEKIILCIAGLFIVTAAVLIIFVPKFYRVYIFGSGGTSDMFYKKKKQSPVATARAESTSKGSSGGGAGSGGATGGSGVKTNKRGNLVSGDFSDDTESSLSEPNKPVKVVAGAVLAEFTDDTISDLDNIDQPIEIITENGQDSNNNNNNEENKDNNIENNKISEEIKENLKNEENNDGDN
Protein: Uncharacterized transporter ESBP6 (P53918)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
Sequence:
MSTHSNDYFSASSGMVSETSSEVSSINSSQPVSFSKASIAAPVPCSDLHSTKSNDASRKLSISRTLTNRLNDIKKAVDDDNLQTEENSADVNKILESRFDVADAIRLQHNESVQSKLNIPVTHTTTAGASLSAPSSSAFSASSIQNDTTEHKASMDSKLMRNRLYPASTKHSGKDLEAQGITEFEPDEPTVKKVFTNKSTGQLELPPDGGYGWVVTFCVFLTMFSTWGCNASFGVDLAYYLNHDTYPGASKYDYALIAGLTVFLGQLLSPLVMALMRIIGLRTTMLFGDAVMLAAYLLASFTTKLWQLYVTQGFMVGCSISLIFVPATTVLPGWFLKKRAVAMGVSLLGTGAGGVVYGLATNKMLSDFGNTRWCLRIIGISCSISVLVAIALLKERNPTPAIGLKSPRAMFEQLKAMFSLKVITKPFVVLIALWFMFALFAYNMMVFTLSSYAISKGLSSHDASTLTAILNGSQSIGRPLMGLAGDKFGRANVTIVLTTLLTIYMFAFWIPAHTFVQLIFFSILVGSCVGVANVMNTVLIADMVKPEEFLPAWAFVNYCGAPFLLVCEVIAQALTVEKDKSNPYLHAQIFCGCCFIAALILISILREYSIRMKLTERQAMTNEKLKEWKASEYDTDSADEDWGKLKERKTKYDLLLGPGIKKYFLRMVYPMKV
Protein: RNA-binding protein 47 (RNA-binding motif protein 47) (A0AV96)
Organism: Homo sapiens (Human)
Function: Single-stranded RNA-binding protein that functions in a variety of RNA processes, including alternative splicing, RNA stabilization, and RNA editing. Functions as an enzyme-substrate adapter for the cytidine deaminase APOBEC1. With APOBEC1 forms an mRNA editing complex involved into cytidine to uridine editing of a variety of mRNA molecules. Through the binding of their 3'UTR, also stabilizes a variety of mRNAs and regulates the expression of genes such as the interferon alpha/beta receptor and interleukin-10. Also involved in the alternative splicing of several genes including TJP1. Binds the pre-mRNA (U)GCAUG consensus sequences in downstream intronic regions of alternative exons, regulating their exclusion and inclusion into mRNAs. Independently of its RNA-binding activity, could negatively regulate MAVS by promoting its lysosomal degradation (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:24038582, ECO:0000269|PubMed:24916387}. Cytoplasm {ECO:0000269|PubMed:24916387}.
Interaction partners:
Sequence:
MTAEDSTAAMSSDSAAGSSAKVPEGVAGAPNEAALLALMERTGYSMVQENGQRKYGGPPPGWEGPHPQRGCEVFVGKIPRDVYEDELVPVFEAVGRIYELRLMMDFDGKNRGYAFVMYCHKHEAKRAVRELNNYEIRPGRLLGVCCSVDNCRLFIGGIPKMKKREEILEEIAKVTEGVLDVIVYASAADKMKNRGFAFVEYESHRAAAMARRKLMPGRIQLWGHQIAVDWAEPEIDVDEDVMETVKILYVRNLMIETTEDTIKKSFGQFNPGCVERVKKIRDYAFVHFTSREDAVHAMNNLNGTELEGSCLEVTLAKPVDKEQYSRYQKAARGGGAAEAAQQPSYVYSCDPYTLAYYGYPYNALIGPNRDYFVKAGSIRGRGRGAAGNRAPGPRGSYLGGYSAGRGIYSRYHEGKGKQQEKGYELVPNLEIPTVNPVAIKPGTVAIPAIGAQYSMFPAAPAPKMIEDGKIHTVEHMISPIAVQPDPASAAAAAAAAAAAAAAVIPTVSTPPPFQGRPITPVYTVAPNVQRIPTAGIYGASYVPFAAPATATIATLQKNAAAAAAMYGGYAGYIPQAFPAAAIQVPIPDVYQTY
Protein: Epididymis luminal protein 35 (Epididymis secretory sperm binding protein Li 125m) (Heat shock protein 90kDa beta (Grp94), member 1, isoform CRA_b) (V9HWP2)
Organism: Homo sapiens (Human)
Subcellular location: Melanosome {ECO:0000256|ARBA:ARBA00004223}.
Interaction partners:
Sequence:
MRALWVLGLCCVLLTFGSVRADDEVDVDGTVEEDLGKSREGSRTDDEVVQREEEAIQLDGLNASQIRELREKSEKFAFQAEVNRMMKLIINSLYKNKEIFLRELISNASDALDKIRLISLTDENALSGNEELTVKIKCDKEKNLLHVTDTGVGMTREELVKNLGTIAKSGTSEFLNKMTEAQEDGQSTSELIGQFGVGFYSAFLVADKVIVTSKHNNDTQHIWESDSNEFSVIADPRGNTLGRGTTITLVLKEEASDYLELDTIKNLVKKYSQFINFPIYVWSSKTETVEEPMEEEEAAKEEKEESDDEAAVEEEEEEKKPKTKKVEKTVWDWELMNDIKPIWQRPSKEVEEDEYKAFYKSFSKESDDPMAYIHFTAEGEVTFKSILFVPTSAPRGLFDEYGSKKSDYIKLYVRRVFITDDFHDMMPKYLNFVKGVVDSDDLPLNVSRETLQQHKLLKVIRKKLVRKTLDMIKKIADDKYNDTFWKEFGTNIKLGVIEDHSNRTRLAKLLRFQSSHHPTDITSLDQYVERMKEKQDKIYFMAGSSRKEAESSPFVERLLKKGYEVIYLTEPVDEYCIQALPEFDGKRFQNVAKEGVKFDESEKTKESREAVEKEFEPLLNWMKDKALKDKIEKAVVSQRLTESPCALVASQYGWSGNMERIMKAQAYQTGKDISTNYYASQKKTFEINPRHPLIRDMLRRIKEDEDDKTVLDLAVVLFETATLRSGYLLPDTKAYGDRIERMLRLSLNIDPDAKVEEEPEEEPEETAEDTTEDTEQDEDEEMDVGTDEEEETAKESTAEKDEL
Protein: Claudin-14 (Q9Z0S3)
Organism: Mus musculus (Mouse)
Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Subcellular location: Cell junction, tight junction. Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Tight junction protein 1
- Occludin
- Claudin-1
- Claudin-6
- Claudin-9
- Claudin-3
- Tight junction protein ZO-3
- Claudin-16
- Claudin 34D
- Claudin-11
Sequence:
MASTAVQLLGFLLSFLGMVGTLITTILPHWRRTAHVGTNILTAVSYLKGLWMECVWHSTGIYQCQIYRSLLALPRDLQAARALMVISCLLSGMACACAVVGMKCTRCAKGTPAKTTFAVLGGALFLLAGLLCMVAVSWTTNDVVQNFYNPLLPSGMKFEIGQALYLGFISSSLSLIGGTLLCLSCQDEAPYRPYPPQSRAGATTTATAPAYRPPAAYKDNRAPSVTSAAHSGYRLNDYV
Protein: Actin-binding protein WASF1 (Protein WAVE-1) (Verprolin homology domain-containing protein 1) (Wiskott-Aldrich syndrome protein family member 1) (WASP family protein member 1) (Q92558)
Organism: Homo sapiens (Human)
Function: Downstream effector molecule involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Promotes formation of actin filaments. Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex (By similarity). As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (By similarity). Also involved in the regulation of mitochondrial dynamics.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9889097}. Synapse {ECO:0000250|UniProtKB:Q5BJU7}. Cell junction, focal adhesion {ECO:0000269|PubMed:18559503}. Note=Dot-like pattern in the cytoplasm. Concentrated in Rac-regulated membrane-ruffling areas (PubMed:9889097). Partial translocation to focal adhesion sites might be mediated by interaction with SORBS2 (PubMed:18559503). In neurons, colocalizes with activated NTRK2 after BDNF addition in endocytic sites through the association with TMEM108 (By similarity). {ECO:0000250|UniProtKB:Q8R5H6, ECO:0000269|PubMed:18559503, ECO:0000269|PubMed:9889097}.
Interaction partners:
- Protein BRICK1
- Nck-associated protein 1
- Abl interactor 1
- Cytoplasmic FMR1-interacting protein 1
- Cytoplasmic FMR1-interacting protein 2
- Abl interactor 2
- Nck-associated protein 1-like
- BAR/IMD domain-containing adapter protein 2
- Actin-binding protein WASF2
- Actin-related protein 2/3 complex subunit 3
Sequence:
MPLVKRNIDPRHLCHTALPRGIKNELECVTNISLANIIRQLSSLSKYAEDIFGELFNEAHSFSFRVNSLQERVDRLSVSVTQLDPKEEELSLQDITMRKAFRSSTIQDQQLFDRKTLPIPLQETYDVCEQPPPLNILTPYRDDGKEGLKFYTNPSYFFDLWKEKMLQDTEDKRKEKRKQKQKNLDRPHEPEKVPRAPHDRRREWQKLAQGPELAEDDANLLHKHIEVANGPASHFETRPQTYVDHMDGSYSLSALPFSQMSELLTRAEERVLVRPHEPPPPPPMHGAGDAKPIPTCISSATGLIENRPQSPATGRTPVFVSPTPPPPPPPLPSALSTSSLRASMTSTPPPPVPPPPPPPATALQAPAVPPPPAPLQIAPGVLHPAPPPIAPPLVQPSPPVARAAPVCETVPVHPLPQGEVQGLPPPPPPPPLPPPGIRPSSPVTVTALAHPPSGLHPTPSTAPGPHVPLMPPSPPSQVIPASEPKRHPSTLPVISDARSVLLEAIRKGIQLRKVEEQREQEAKHERIENDVATILSRRIAVEYSDSEDDSEFDEVDWLE
Protein: Acetyl-coenzyme A synthetase 1 (EC 6.2.1.1) (Acetate--CoA ligase 1) (Acyl-activating enzyme 1) (Q6FLU2)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Microsome {ECO:0000305}. Endoplasmic reticulum {ECO:0000305}.
Interaction partners:
- Malate synthase
- Citrate synthase
- Citrate synthase
- Citrate synthase
- Acyl-coenzyme A oxidase
- Candida glabrata strain CBS138 chromosome D complete sequence
- Acetyl-CoA acetyltransferase
- Aldehyde dehydrogenase
- Aldehyde dehydrogenase 5
- Candida glabrata strain CBS138 chromosome H complete sequence
Sequence:
MSPSAIAEKKQVDNIQEIKDKNQEPAHHEYEHLTNVGVVKQKPIDHRLKDNIKTHYSPHLDGLQEYKRQYQESIENPEKFFSEKARSFMNWFRDFDRVFVPDVDNPTKPSFENNAWFLNGQLNTCYNCVDRHALKTPNKTAIIYEADEPGEGYSMSYKELLEKVCQVAQILKYSMNVKKGDTVAVYMPMIPEALITLLAISRIGAIHSVVFAGFSSNSLRDRINDAGSRVVITADESNRGGKIIETKRIVDDALRETPQVEHVLVYRRTNNPQVNFQAPRDLDWETERKKYKTYFPCEPVDSEHPLFLLYTSGSTGTPKGVQHSTAGYLLGALLTMRYTFDVHQEDVFFTAGDIGWITGHTYCVYGPLLYGCTTLVFEGTPAYPNFSRYWEIIDKHQVTQFYVAPTALRLLKRAGDSFIDGFSLKSLRCLGSVGEPIAAEVWEWYSDKIGKNEIPIVDTYWQTESGSHLVTPLAGGVTPMKPGSASLPFFGIETVILDPTTGEEINDSHAEGVLAIKRPWPSFARTIWKNHDRFLDTYLNPYKGYYFTGDGAARDKDGYIWILGRVDDVVNVSGHRLSTAEIEAAIIEDRMVAECAVVGFNDDLTGQAVAAFVVLKDKSTWASASEEELQDIKKHLILTVRKDIGPFAAPKLIVLVDDLPKTRSGKIMRRILRKILAGESDQLGDVSTLSNPGVVKHLIDSVKL
Protein: Pbx1a homeodomain protein (Pre-B-cell leukemia homeobox 1a) (Pre-B-cell leukemia transcription factor 1a) (Q9I9B7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Homeobox protein Hox-B1a
Sequence:
MDDQPRLMHSSHGVGMAGHPGLAQHMQDGTGGADDEGRKQDIGNILQQIMTITDQSLDEAQARKHALNCHRMKPALFNVLCEIKEKTVLSIRGAQEEEPPDAQLMRLDNMLLAEGVSGPEKGGGSAAAAAAAAAAGGVGSDNSAEHSDYRAKLSQIRQIYHTELEKYEQACNEFTTHVMNLLREQSRTRPISPKEIERMVSIIHRKFSSIQMQLKQSTCEAVMILRSRFLDARRKRRNFNKQATEILNEYFYSHLSNPYPSEEAKEELAKKCSITVSQVSNWFGNKRIRYKKNIGKFQEEANMYAARTAANATSVSTHGSQANSPSTPNSAGSAGSFNMNSGDLFMSVQSLNGDSYQGAQVGANVQSQVDTLRHVISQTGGYSESLAASQIYSPQGINANGGWQDAPTPSSVTSPTEGPGSVHSDTSN
Protein: Tudor domain-containing protein (Q19731)
Organism: Caenorhabditis elegans
Interaction partners:
- Helicase ATP-binding domain-containing protein
- RNA-directed RNA polymerase
- Argonaute protein wago-1
- Dicer-related helicase
Sequence:
MIAVGLRLTDEVFPNPEEPIAKLPTGNENPEMLLDGVNKDGKTRIKRIVLSRSANVEFLRAESPSRIWVRLTNHITDSALTFREPFELTQKTTFKIGDYALAPTDERVYRRCRIVDVCRNNELLKVFFIDDAVIAWVQPECLGELDQHYMYYPWQAIQVSMFGATPTVDVNRSTEQLWSPIICDQLSKVLEQFFILRVEVVLSTVVFNDYAKPIPVNLFGIEADIDEKDQIRRAIEIGPILERQEPVGISFPEFFDAAYHQVFEVAERETIPNEALEIHRSFPTDWKKTSISEDQMKEEKEKALFSKNSLIPEMEHSDWDPRQNSIEMLSIDQLEEKFKFPYDSDVAPAIMLAVEGRCTKSPFEWYARPIVKTGRNANGEMVIWNDEEQLKEVDPVDWMIYGNDQLLSMAEQLDTYYSNPKNRKPLKAEEIQSMRKEKRDVFAVCAVNEEKAMYTGEWQRVLIVECDTFAEVRFLDSGGRDMVLTGSLYKIHRQHCRFPPMCLRLSMHGITSSESVVRKWTSAETSRFRTCLREDVPIFINIDDIAPLILPPDDKKDPRAHMAKHVLMVSDVSYMDESKSLLDRFTDKDEAVRAAFSQKEPIEWPN
Protein: Inner membrane protein YidI (P31446)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MGIIAQNKISSLGMLFGAIALMMGIIHFSFGPFSAPPPTFESIVADKTAEIKRGLLAGIKGEKITTVEKKEDVDVDKILNQSGIALAIAALLCAFIGGMRKENRWGIRGALVFGGGTLAFHTLLFGIGIVCSILLIFLIFSFLTGGSLV
Protein: BARP protein (Q38CW0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSITFHNLWLLLTVLCTAGVRAHHGWTNCYPAGNSPPVEEIRASCEVAHQLRGLSQTVTSAVETSAAASSKAFEAKVQAEEAVELAESKGLNVTKAKEAAVRATLAAEAAATAASNVEINAANIAAVPWLERRQNTGWEVLTKCINLDDDIKKMASKCKSAAEVVTAESISAALNDLGKTFINEKTREALRKESVEFHKELASLEEHVEEAVRAQKRAEDAAADANQTAGTNTGPVVNSVASPEGSVLLLMAGLFLGSVL
Protein: Calsequestrin-1 (Aspartactin) (Calsequestrin, skeletal muscle isoform) (Laminin-binding protein) (P07221)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, often at the interface between subunits. Can bind around 80 Ca(2+) ions. Regulates the release of lumenal Ca(2+) via the calcium release channel RYR1; this plays an important role in triggering muscle contraction. Negatively regulates store-operated Ca(2+) entry (SOCE) activity (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:P31415}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:P31415}. Sarcoplasmic reticulum lumen {ECO:0000269|PubMed:15731387, ECO:0000269|PubMed:19230141, ECO:0000269|PubMed:8227022}. Mitochondrion matrix {ECO:0000250|UniProtKB:O09165}. Sarcoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000269|PubMed:15731387}. Note=This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of fast skeletal muscle cells (PubMed:15731387). Preferentially forms linear and round aggregates in the endoplasmic reticulum (ER) of resting cells. In a minority of cells, homogeneously detected in the ER lumen. Colocalizes with STIM1 at endoplasmic reticulum in response to a depletion of intracellular calcium (By similarity). {ECO:0000250|UniProtKB:P31415, ECO:0000269|PubMed:15731387}.
Interaction partners:
- Triadin
- Ryanodine receptor 2
- Ryanodine receptor 3
- Aspartyl beta-hydroxylase/Triadin domain-containing protein
- Calsequestrin-2
- Ryanodine receptor 1
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
- Sarcalumenin
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
- Myozenin 1
Sequence:
MNAADRMGARVALLLLLVLGSPQSGVHGEEGLDFPEYDGVDRVINVNAKNYKNVFKKYEVLALLYHEPPEDDKASQRQFEMEELILELAAQVLEDKGVGFGLVDSEKDAAVAKKLGLTEEDSIYVFKEDEVIEYDGEFSADTLVEFLLDVLEDPVELIEGERELQAFENIEDEIKLIGYFKNKDSEHYKAFKEAAEEFHPYIPFFATFDSKVAKKLTLKLNEIDFYEAFMEEPVTIPDKPNSEEEIVNFVEEHRRSTLRKLKPESMYETWEDDMDGIHIVAFAEEADPDGYEFLEILKSVAQDNTDNPDLSIIWIDPDDFPLLVPYWEKTFDIDLSAPQIGVVNVTDADSVWMEMDDEEDLPSAEELEDWLEDVLEGEINTEDDDDEDDDDDDDD
Protein: Choline trimethylamine-lyase activating enzyme (EC 1.97.1.-) (Choline utilization protein D) (GRE activase CutD) (Glycyl-radical enzyme activating enzyme CutD) (GRE activating enzyme CutD) (Q30W71)
Organism: Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20) (Desulfovibrio alaskensis)
Function: Catalyzes activation of the choline trimethylamine-lyase CutC under anaerobic conditions by generation of an organic free radical on a glycine residue, via a homolytic cleavage of S-adenosyl-L-methionine (SAM). Is involved in the anaerobic choline utilization pathway that allows D.alaskensis to grow on choline as a source of carbon and energy.
Interaction partners:
- Choline trimethylamine-lyase
- Choline trimethylamine-lyase
- Pyruvate formate-lyase PFL
- Isethionate sulfite-lyase
- Acetaldehyde dehydrogenase
- Acetaldehyde dehydrogenase
Sequence:
MIERKALIFNIQKYNMYDGPGVRTLVFFKGCPLRCKWCSNPEGQLRQYQVLYKENLCVHCGACVPVCPAGVHTISASTLRHGFAEGAQCIGCRRCEDVCPSSALAVVGEQKTISELLEVIEEDRPFYETSGGGVTLGGGEVLMQPEAAVNLLAACKQHGINTAIETCGYAKQEVVMKAAQYVDLFLYDVKHIDSARHYELTGVRNELILSNLTWLLENKHNVKIRVPLLRGVNDSEDDLRGLVEYLRPYQDYKNFKGIDLLPYHKMGVGKYKQLGWEYPIEGNPALSDADLERVEACIRKYDFPVSVIRH
Protein: U1 small nuclear ribonucleoprotein A (U1 snRNP A) (U1-A) (U1A) (Mutant U1 die protein 1) (P32605)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in nuclear mRNA splicing. The principal role of the U1A is to help fold or maintain U1 RNA in an active configuration. It is the first snRNP to interact with pre-mRNA. This interaction is required for the subsequent binding of U2 snRNP and the U4/U6/U5 tri-snRNP.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- U1 small nuclear ribonucleoprotein 70 kDa homolog
- Pre-mRNA-processing protein PRP40
- Protein NAM8
- Pre-mRNA-splicing factor PRP9
- Small nuclear ribonucleoprotein F
- U1 small nuclear ribonucleoprotein component PRP42
- Small nuclear ribonucleoprotein E
- U2 snRNP component HSH155
- 56 kDa U1 small nuclear ribonucleoprotein component
- U1 small nuclear ribonucleoprotein C
Sequence:
MSALYFQNLPSRPANKENYTRLLLKHINPNNKYAINPSLPLPHNKLQISSQPLMLLDDQMGLLEVSISRSSKMTNQAFLTFVTQEEADRFLEKYTTTALKVQGRKVRMGKARTNSLLGLSIEMQKKKGNDETYNLDIKKVLKARKLKRKLRSDDICAKKFRLKRQIRRLKHKLRSRKVEEAEIDRIVKEFETRRLENMKSQQENLKQSQKPLKRAKVSNTMENPPNKVLLIQNLPSGTTEQLLSQILGNEALVEIRLVSVRNLAFVEYETVADATKIKNQLGSTYKLQNNDVTIGFAK
Protein: Trafficking protein particle complex subunit 12 (Tetratricopeptide repeat protein 15) (TPR repeat protein 15) (TTC-15) (Trafficking of membranes and mitosis) (Q8WVT3)
Organism: Homo sapiens (Human)
Function: Component of the TRAPP complex, which is involved in endoplasmic reticulum to Golgi apparatus trafficking at a very early stage. Also plays a role in chromosome congression, kinetochore assembly and stability and controls the recruitment of CENPE to the kinetochores.
Subcellular location: Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:21525244}. Nucleus {ECO:0000269|PubMed:25918224}. Note=Mainly localizes to structures resembling the Golgi and a small amount is found in the nucleus. {ECO:0000269|PubMed:25918224}.
Interaction partners:
- Trafficking protein particle complex subunit 8
- Trafficking protein particle complex subunit 11
- Trafficking protein particle complex subunit 13
- Trafficking protein particle complex subunit 2-like protein
- Trafficking protein particle complex subunit 3
- Trafficking protein particle complex subunit 2
- Trafficking protein particle complex subunit 4
- Trafficking protein particle complex subunit 5
- Trafficking protein particle complex subunit 6B
- Trafficking protein particle complex subunit 1
Sequence:
MEDAGGGEETPAPEAPHPPQLAPPEEQGLLFQEETIDLGGDEFGSEENETASEGSSPLADKLNEHMMESVLISDSPNSEGDAGDLGRVRDEAEPGGEGDPGPEPAGTPSPSGEADGDCAPEDAAPSSGGAPRQDAAREVPGSEAARPEQEPPVAEPVPVCTIFSQRAPPASGDGFEPQMVKSPSFGGASEASARTPPQVVQPSPSLSTFFGDTAASHSLASDFFDSFTTSAFISVSNPGAGSPAPASPPPLAVPGTEGRPEPVAMRGPQAAAPPASPEPFAHIQAVFAGSDDPFATALSMSEMDRRNDAWLPGEATRGVLRAVATQQRGAVFVDKENLTMPGLRFDNIQGDAVKDLMLRFLGEKAAAKRQVLNADSVEQSFVGLKQLISCRNWRAAVDLCGRLLTAHGQGYGKSGLLTSHTTDSLQLWFVRLALLVKLGLFQNAEMEFEPFGNLDQPDLYYEYYPHVYPGRRGSMVPFSMRILHAELQQYLGNPQESLDRLHKVKTVCSKILANLEQGLAEDGGMSSVTQEGRQASIRLWRSRLGRVMYSMANCLLLMKDYVLAVEAYHSVIKYYPEQEPQLLSGIGRISLQIGDIKTAEKYFQDVEKVTQKLDGLQGKIMVLMNSAFLHLGQNNFAEAHRFFTEILRMDPRNAVANNNAAVCLLYLGKLKDSLRQLEAMVQQDPRHYLHESVLFNLTTMYELESSRSMQKKQALLEAVAGKEGDSFNTQCLKLA
Protein: 3-ketoacyl CoA thiolase 1, peroxisomal (PhKAT1) (EC 2.3.1.16) (C8YNG6)
Organism: Petunia hybrida (Petunia)
Function: Component of the floral volatile benzenoid/phenylpropanoid (FVBP) biosynthetic pathway. Thiolase that catalyzes the conversion of 3-oxo-3-phenylpropionyl-CoA (benzoylacetyl-CoA) to benzoyl-CoA.
Subcellular location: Peroxisome {ECO:0000269|PubMed:19659733}.
Interaction partners:
Sequence:
MEKAIQRQRVLLEHLQPIRHHTHDHSSSLTTSICAAGDSAAYQRTAAFGDDVVIVAAYRTAICKSKRGGFKDTLSDDLLAPVLKAVIEKTNLDPKEVGDIVVGTVLAPGSIRAMECRMAAFYAGFPETVPIRTVNRQCSSGLQAVADVAASIKAGFYDIGIGAGLELMTVDNIGRVQQRNTKVDTFAQARDCLLPMGITSENVAQRFGVTRLEQDQAAVNSHQRAAAATASGKFKDEIIPVLTKIVDPQTGKEKPVVISVDDGIRPNTNLTSLGKLKPAFKNDGTTTAGNASQVSDGAAAVLLMKRSVAMKKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPPAVKSAGLDLDDIDLYEINEAFASQFVYCQKKLNLDPEKVNVNGGAMALGHPLGATGARCVATLLHEMKRRGKDCRFGVISMCIGSGMGAAAVFERGDAVDDLCNARVSNNNSFLSKDAK
Protein: Protein pxr1 (PinX1-related protein 1) (Q9URX9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in rRNA-processing at A0, A1 and A2 sites and regulates negatively telomerase.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable pre-mRNA-splicing factor ATP-dependent RNA helicase prp43
- Probable U3 small nucleolar RNA-associated protein 7
- Uncharacterized protein C13G1.09
- rRNA 2'-O-methyltransferase fibrillarin
- Suppressor of glycerol defect protein 1
- Protein gar2
- ATP-dependent RNA helicase fal1
- 13 kDa ribonucleoprotein-associated protein
- Probable ATP-dependent RNA helicase prh1
- Protein mak16
Sequence:
MGLAGVKKKQQIGVDPRNSKWAKDTNRLGFKLLSSYGWVNGNGLGEKQHGRIHNIKVSLKDDTLGIGAKATNDLEWSGLGEFNAIFGRLNGDESAYGVYAEKAKVQQLTYERQSANEKGLKSLELSRRFVLGGTFTSEFSEWMQKAEEDEDRVCEDASSSDEAKREKRKKHSSKKKSKKKTSTGSALDPKKLEKITKKKKKEHKKKDKESSSKKRKSGSSDKEEKKKKKIKLKDKPESTSSVEKVKEGNRPASIHFHTRRKFLAQKRAAVSDPVALREILGIKG
Protein: Protein IscX (P0C0M0)
Organism: Escherichia coli O157:H7
Function: May function as iron donor in the assembly of iron-sulfur clusters.
Interaction partners:
- 2Fe-2S ferredoxin
- 2Fe-2S ferredoxin
- Co-chaperone protein HscB
- Co-chaperone protein HscB
- Chaperone protein HscA
- Chaperone protein HscA
- Iron-sulfur cluster assembly scaffold protein IscU
- Iron-sulfur cluster assembly scaffold protein IscU
- Cysteine desulfurase IscS
- Iron-sulfur cluster assembly protein CyaY
Sequence:
MGLKWTDSREIGEALYDAYPDLDPKTVRFTDMHQWICDLEDFDDDPQASNEKILEAILLVWLDEAE
Protein: Serine protease 3 (Trypsinogen 11) (Q792Z0)
Organism: Mus musculus (Mouse)
Interaction partners:
- Chymotrypsinogen B
- Serine protease inhibitor Kazal-type 1
- Proteinase-activated receptor 2
- Carboxypeptidase A1
- Amyloid-beta precursor protein
- Thyroglobulin
- Reg III delta
- Anionic trypsin-2
- Trypsin-5
- Proteinase-activated receptor 1
Sequence:
MNALLILALVGAAVAFPVDDDDKIVGGYTCQENSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKTRIQVRLGEHNINVLEGNEQFVNAAKIIKHPNFNRKTLNNDIMLLKLSSPVTLNARVATVALPSSCAPAGTQCLISGWGNTLSFGVSEPDLLQCLDAPLLPQADCEASYPGKITGNMVCAGFLEGGKDSCQGDSGGPVVCNRELQGIVSWGYGCALPDNPGVYTKVCNYVDWIQDTIAAN
Protein: UDP-arabinopyranose mutase 3 (OsUAM3) (EC 5.4.99.30) (Reversibly glycosylated polypeptide 3) (UDP-L-arabinose mutase 3) (Q6Z4G3)
Organism: Oryza sativa subsp. japonica (Rice)
Function: UDP-L-arabinose mutase involved in the biosynthesis of cell wall non-cellulosic polysaccharides. Catalyzes the interconvertion of UDP-L-arabinopyranose (UDP-Arap) and UDP-L-arabinofuranose (UDP-Araf). Preferentially catalyzes the formation of UDP-Arap from UDP-Araf. At thermodynamic equilibrium in vitro the ratio of the pyranose form over the furanose form is 90:10. Is probably active as heteromer in vivo.
Subcellular location: Golgi apparatus {ECO:0000250|UniProtKB:Q9SRT9}.
Interaction partners:
- Probable inactive UDP-arabinopyranose mutase 2
- UDP-sugar pyrophosphorylase
- Probable UDP-arabinose 4-epimerase 3
- Probable UDP-arabinose 4-epimerase 1
- Probable UDP-arabinose 4-epimerase 2
- UDP-arabinopyranose mutase 1
- Actin-related protein 4
- Os06g0255200 protein
- Actin-related protein 2/3 complex subunit
- ARID transcription factor
Sequence:
MASSDAAAAQAATPLLKDELDIVIPTIRNLDFLEMWRPFFQPYHLIIVQDGDPKKTIRVPEGFDYELYNRDDINRILGPRASCISFKDSACRCFGYMVSKKKYIYTIDDDCFVAKDPSGKDINALEQHIKNLLNPSTPFFFNTLYDPYRDGADFVRGYPFSLREGAPTAVSHGLWLNIPDYDAPTQLVKPLERNSRYVDAVMTIPKGTLFPMCGMNLAFDRDLIGPAMYFGLMGDGQPIGRYDDMWAGWCTKVITDHLGLGVKTGLPYIWHSKASNPFVNLKKEYNGIFWQEELIPFFQSASLPKEADTVQKCYLELAKQVRAKLGKVDGYFNKLADSMVTWIEAWDQLNPPKGAVATANGTAKSK
Protein: Zinc finger CCCH domain-containing protein 28 (AtC3H28) (Q5PP65)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Putative zinc finger CCCH domain-containing protein 10
- Putative zinc finger CCCH domain-containing protein 9
- Zinc finger CCCH domain-containing protein 46
- Zinc finger CCCH domain-containing protein 51
- Zinc finger CCCH domain-containing protein 55
- Zinc finger CCCH domain-containing protein 62
- Zinc finger CCCH domain-containing protein 53
- Zinc finger CCCH domain-containing protein 56
- Zinc finger CCCH domain-containing protein 59
- Zinc finger CCCH domain-containing protein 1
Sequence:
MSHRRDYGSDAVHVRITHDPPPENCFPNSGDSSVWATEDDYSRVWAINSDGAESPSKKTRSSSSSEIGKSFFKTKLCFKFRAGTCPYSASSCHFAHSAEELRLPPPPPPNWQETVTEASRNRESFAVSLGPRGNVAQTLKSPNWKTRICNKWQTTGYCPFGSHCHFAHGPSELHTFGGGLVEGECKIGTSATLDTKQRGQVDTVTSLVSPGVSSQRTSSAVTQKPNGVRTQRKWKGPDKISRVYGDWIDDIE
Protein: Ca3427-like PBP 2 domain-containing protein (Q59X88)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
Interaction partners:
- 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase
Sequence:
MPTLKVAYIPEHFSTPLFFAQQQGYYKAHDLSIEFVKVPEGSGRLINLLNSNEVDIAIGLTEAFIADIAKGNENIHVLDTYVKSPLLWAVSTGSNRDDVTDAKQLKRIGVSRIGSGSYVMSFVLAHQLGVPSFDQFQVLSNFKNLRDSVNLKDGVEGSDAFMWEYFTSKKYYDNHEIKQIDQIYTPWSSWVVATSSDSLQAKSDVIKNFIDAVNQGIQYYNEHVDEAIEYISSNLDYSAEDAKEWTKTVEFNSRIGKTPLDWDTIVVKTKDTLKLAGVLAESDDVILKRLNSNVKKTNL