wanglab/gogpt-training-data huggingface dataset:
Protein: Alpha-2 macroglobulin receptor (Q6LBN5)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
PMDLHVFHALRQPDVPNHPCKVNNGGCSNLCLLSPGGGHKCACPTNFYLGSDGRTCVSNCTASQFVCKNDKCIPFWWKCDTEDDCGDHSDEPPDCPEFKCRPGQFQCSTGICTNPAFICDGDNDCQDNSDEANCDIHVCLPSQFKCTNTNRCIPGIFRCNGQDNCGDGEDERDCPEVTCAPNQFQCSITKRCIPRVWVCDRDNDCVDGSDEPANCTQMTCGVDEFRCKDSGRCIPARWKCDGEDDCGDGSDEPKEECDERTCEPYQFRCKNNRCVPGRWQCDYDNDCGDNSDEESCTPRPCSESEFSCANGRCIAGRWKCDGDHDCADGSDEKDCTPRCDMDQFQCKSGHCIPLRWRCDADADCMDGSDEEACGTGVRTCPLDEFQCNNTLCKPLAWKCDGEDDCGDNSDENPEECARFVCPPNRPFRCKNDRVCLWIGRQCDGTDNCGDGTDEEDCEPPTAHTTHCKDKKEFLCRNQRCLSSSLRCNMFDDCGDGSDEEDCSIDPKLTSCATNASICGDEARCVRTEKAAYCACRSGFHTVPGQPGCQDINECLRFGTCSQLCNNTKGGHLCSCARNFMKTHNTCKAEGS
Protein: UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase (EC 2.7.8.15) (GlcNAc-1-P transferase) (G1PT) (GPT) (N-acetylglucosamine-1-phosphate transferase) (P42881)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the initial step in the synthesis of dolichol-P-P-oligosaccharides.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P23338}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9H3H5}.
Interaction partners:
- UDP-N-acetylglucosamine transferase subunit alg13
- UDP-N-acetylglucosamine transferase subunit alg14
- Dolichyl-phosphate beta-glucosyltransferase
- Dolichol-phosphate mannosyltransferase
- Dolichol kinase sec59
- Dolichol-phosphate mannosyltransferase subunit 3
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Putative proline--tRNA ligase C19C7.06
- Probable proline--tRNA ligase, mitochondrial
- Probable cystathionine gamma-synthase
Sequence:
MIESCFNVGIWATGLALLMNQGQSPLLSNVGLSVLAYKATAMFIPRVGPSFIKRGFSGKDMNKVEKYVIPETMGAVSALVYFMCMIIFIPVLFYKYLVPNHNPNLPSDGSVAEVAKSQFPHDLLGAYLSALLSILSVSLLGILDDLFDIRWRHKFFLPAIAAIPLLVVYYVDYGVTYVSVPSIVRPFLKRSLINLGFLYYFYMAAVAIFCPNSINIIAGVNGVEAGQSLVLALVIACNDLFYVLSPKNKDALRAHLLSLYLVLPLIGVTAGLLKYNWWPSRVFVGDTFCYFAGMVMAVVGILGHFSKTLMLFFIPQIFNFALSVPQLFGLVECPRHRLPKLNVKTGLLENSYTEFSLNEHPLPKKTLLTISIFEKLRLIRVEYDPSTGRPLRCTNFTIINFVLYHLGPMREDHLTICIMGLQLLTGIFGLIIRHFVAPLVYPEDNI
Protein: Testicular tissue protein Li 209 (A0A140VJY2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MARELRALLLWGRRLRPLLRAPALAAVPGGKPILCPRRTTAQLGPRRNPAWSLQAGRLFSTQTAEDKEEPLHSIISSTESVQGSTSKHEFQAETKKLLDIVARSLYSEKEVFIRELISNASDALEKLRHKLVSDGQALPEMEIHLQTNAEKGTITIQDTGIGMTQEELVSNLGTIARSGSKAFLDALQNQAEASSKIIGQFGVGFYSAFMVADRVEVYSRSAAPGSLGYQWLSDGSGVFEIAEASGVRTGTKIIIHLKSDCKEFSSEARVRDVVTKYSNFVSFPLYLNGRRMNTLQAIWMMDPKDVREWQHEEFYRYVAQAHDKPRYTLHYKTDAPLNIRSIFYVPDMKPSMFDVSRELGSSVALYSRKVLIQTKATDILPKWLRFIRGVVDSEDIPLNLSRELLQESALIRKLRDVLQQRLIKFFIDQSKKDAEKYAKFFEDYGLFMREGIVTATEQEVKEDIAKLLRYESSALPSGQLTSLSEYASRMRAGTRNIYYLCAPNRHLAEHSPYYEAMKKKDTEVLFCFEQFDELTLLHLREFDKKKLISVETDIVVDHYKEEKFEDRSPAAECLSEKETEELMAWMRNVLGSRVTNVKVTLRLDTHPAMVTVLEMGAARHFLRMQQLAKTQEERAQLLQPTLEINPRHALIKKLNQLRASEPGLAQLLVDQIYENAMIAAGLVDDPRAMVGRLNELLVKALERH
Protein: RRM Nup35-type domain-containing protein (Q75JH1)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Nucleus, nuclear pore complex {ECO:0000256|ARBA:ARBA00004567}.
Interaction partners:
- Nucleoporin 155
- Nuclear pore protein
Sequence:
MNLNASSSKLNSNSNEINRQYIPSRIFSSQDKSNEDKNNIGNLSSPPHSTNSPINQMQSPSNSQTPGTPYSSYYSRSMGPYQPPSSSSSSSPSSNHAFGYQDGNSNINMNTPNLNRRFGIGTSISGTNNSNNNNNNNNNNNSNNNSNNNNNNNNQINNQNNDLLSIPVNSIYEEPKQLKQQILSQHQQNQQQRLHQRNANIQHQQNTQNYLYNQVEQQYQQLQQQQQTSSPLSAQDLNQSIYNQQPSFYNNNNQSQTPLQNNVYNNSTVATNSPFLNIYNQQQFQQQQQQQQQQQQQQQQQQQQQQQQQQHHLQQQQQLQQLQQQQQQQQQQLQLQQQSTPYNNQQQQNNNNNNLITPTTSNIFVQSVASQQITQMFLDKYDKRWLTVFGFSHDKTDLIVDELSKYGNIIEIEYPQQPNCNWIYLKFESEYSSIDLLKKNGLILGNCMIGIVPCKEKIRNESDPIKAQPSQLGDHSLKTIEKKYHPARSDYDPQSFSNNNALGTPSRPSFFSKVSEYVFGST
Protein: MAGUK p55 scaffold protein 1 (A6NFY0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTLKASEGESGGSMHTALSDLYLEHLLQKRSRPEAVSHPLNTVTEDMYTNGSPAPGSPAQVKGQEGITLKLNEKQSCTVARILHGGMIHRQGSLHVGDEILEINGTNVTNHSVDQLQKAMKETKGMISLKV
Protein: Syntaxin 16 (A0A0G2K528)
Organism: Rattus norvegicus (Rat)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004409}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004409}.
Interaction partners:
- Vesicle transport through interaction with t-SNAREs homolog 1A
- Vesicle-associated membrane protein 4
- Syntaxin-6
- Synaptobrevin homolog YKT6
- Vesicle-associated membrane protein 3
- Vacuolar protein sorting-associated protein 45
- Vesicle transport through interaction with t-SNAREs homolog 1B
- Syntaxin-8
- Synaptosomal-associated protein 29
- Alpha-soluble NSF attachment protein
Sequence:
MATRRLTDAFLLLRNNSIQNRQLLAEQVSSHTTSSPLHSRSIAAELDELADDRMALVSGISLDPEAAIGVTKRSPPKWVDGVDEIQYDVGRIKQKMRELASLHDKHLNRPTLDDSSEEEHAIEITTQEVTQLFHRCQRAVQALPSRARRTCSEQEERLLRNVVASLAQALQELSTSFRHAQSDYLKRMKNREERSQHFFDTPVPLMDDGDDATLYGQGFTDDQLVLVEQNTLVVEEREREIRQIVQSISDLNEIFRDLGAMIVEQGTVLDRIDYNVEQSCVKTEDGLKQLHKAEQYQKKNRKMLVILILVAVIVVLIVVLIAVKSR
Protein: Misfire, isoform J (B7Z0E8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MRLLFAFGLRPAPYANRHALRFHDDLDDHELVEEREFTWWTKFYNSMYWSAAEMCHEHKHRLVIYYEELEKQAQFGYLQDWAVPVQLVHGVKFKKHGPPKEDIYATLKLQLKLTPCQCPVLEDPGGGGDMVRNMSNPIHPRHQSTLQSLGETVKLLVRVYVVQGVQMRPRDVKGDSDCYVKLFLGGKTFSDRAHFSPNHSNPVFGRLFEMEATLPGDHMLQVMVYDHDKIKDEVIGQTNIDLEDRWRTRHRATVGLANEYTKSGYNHWHDVKLPSEILIDLCQKRGIQAPYYYGNVIEVDGMLFGDETLISKDEELQERLSLAVLKNMDKLPSFGYKLVPEHVETRSLCRDDFPNVEQGKLQLWIELFEANIYVPSPIDITPVPPADFEVRVVVKNLVGIQAGDKNIFGKLMSDVYVIGWCEDEDKRQSTDIHYRSFAGDAAFNWRMVFGLKYSPNEDLMVIRRKAGLLEEIEFKKPPIIYLQVWDKDVLTKDEYLAALELNLSNMYAPYPAAQLCKPYPKKRKRINLFKRKVINGWFPLQSNAHPSQRSQAAVQNGKMQLSIEVCTDVEAVNRPAGRGQDPPMALEPPYRPDSSFNPLTHPCKSFQHILWPVIRKYVLWTLLILIVILGLVLFFSNLPAKLMTIPLE
Protein: Variant surface glycoprotein (VSG, atypical), putative (Q380U6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MTPQATALLALALTAEQARGNIPAGANEQEFGALCAIVDLSRSDITINQFPDQTAALEGAVLALNMSLADESWQKRFSKDGAKKEWIKELPAGTADPGHWKKSWPKWAAAAARLADQGTAAEIKSSGFETLNPIERAGAKASVAQIAAEAQFLTQQIAEKENVGKKHTAATVKAALNEAIYGVKQEAPPDFEPTRNYDGLNTQAREAICVGLGSEAKTTTIAGAIYCICGQDNAQAEKVCARNQADTHKWTSITNAMTKDGFEEIVKHCAGPAKTHLTSSLLMGLITKIKNLIRRVGANAYMGALKTGSSCNGDKTQGICIKYAGYDGTPTKDFAAIPWAQKLLALHDDLRQQEKAIAEATALEQQLAVAKNKAYAAALLQKTAPPTAGQTSSDNVNRKGDQGTQPTNKCNQIVTEETCNKENECSYEKESDGTKRCKYNATKATANGVPVTQPQKGPAKTTENKCKWKPEKDFKSPDCKWDGKECKNSSIIANKQFAMIVSAFVAMVF
Protein: Nuclear cap-binding protein subunit 2 (20 kDa nuclear cap-binding protein) (NCBP 20 kDa subunit) (CBP20) (Q9V3L6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the cap-binding complex (CBC), which binds co-transcriptionally to the 5' cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing and RNA-mediated gene silencing (RNAi). The CBC complex is involved in miRNA-mediated RNA interference via its interaction with Ars2 and is required for primary microRNAs (miRNAs) processing. Also involved in innate immunity via the short interfering RNAs (siRNAs) processing machinery by restricting the viral RNA production. In the CBC complex, Cbp20 recognizes and binds capped RNAs (m7GpppG-capped RNA) but requires Cbp80 to stabilize the movement of its N-terminal loop and lock the CBC into a high affinity cap-binding state with the cap structure.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Nuclear cap-binding protein subunit 1
- Serrate RNA effector molecule homolog
- U1 small nuclear ribonucleoprotein 70 kDa
- Probable small nuclear ribonucleoprotein G
- LD21442p
- Small nuclear ribonucleoprotein F
- Probable small nuclear ribonucleoprotein Sm D2
- Phosphorylated adapter RNA export protein
- U1 small nuclear ribonucleoprotein C
- THO complex subunit 2
Sequence:
MFASVELSSYRDQHFKGSRSEQERSLRDSCTLYVGNLSFYTTEEQIHELFSRCGDVRVIVMGLDKYKKTPCGFCFVEYYVRSEAEAAMRFVNGTRLDDRLIRVDWDAGFVEGRQYGRGKTGGQVRDEYRTDYDAGRGGYGKLLSQKIAPNTDNR
Protein: Calcium/calmodulin-dependent protein kinase type 1 (EC 2.7.11.17) (CaM kinase I) (CaM-KI) (CaM kinase I alpha) (CaMKI-alpha) (Q91YS8)
Organism: Mus musculus (Mouse)
Function: Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK1 signaling cascade and, upon calcium influx, regulates transcription activators activity, cell cycle, hormone production, cell differentiation, actin filament organization and neurite outgrowth. Recognizes the substrate consensus sequence [MVLIF]-x-R-x(2)-[ST]-x(3)-[MVLIF]. Regulates axonal extension and growth cone motility in hippocampal and cerebellar nerve cells. Upon NMDA receptor-mediated Ca(2+) elevation, promotes dendritic growth in hippocampal neurons and is essential in synapses for full long-term potentiation (LTP) and ERK2-dependent translational activation. Downstream of NMDA receptors, promotes the formation of spines and synapses in hippocampal neurons by phosphorylating ARHGEF7/BETAPIX on 'Ser-673', which results in the enhancement of ARHGEF7 activity and activation of RAC1. Promotes neuronal differentiation and neurite outgrowth by activation and phosphorylation of MARK2 on 'Ser-91', 'Ser-92', 'Ser-93' and 'Ser-294'. Promotes nuclear export of HDAC5 and binding to 14-3-3 by phosphorylation of 'Ser-259' and 'Ser-498' in the regulation of muscle cell differentiation. Regulates NUMB-mediated endocytosis by phosphorylation of NUMB on 'Ser-276' and 'Ser-295'. Involved in the regulation of basal and estrogen-stimulated migration of medulloblastoma cells through ARHGEF7/BETAPIX phosphorylation. Is required for proper activation of cyclin-D1/CDK4 complex during G1 progression in diploid fibroblasts. Plays a role in K(+) and ANG2-mediated regulation of the aldosterone synthase (CYP11B2) to produce aldosterone in the adrenal cortex. Phosphorylates EIF4G3/eIF4GII. In vitro phosphorylates CREB1, ATF1, CFTR, MYL9 and SYN1/synapsin I (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly cytoplasmic. {ECO:0000250}.
Interaction partners:
- Calmodulin-1
- Calmodulin-like protein 3
- Calmodulin 5
- Calmodulin-4
- Calmodulin-like protein 4
- Neuronal migration protein doublecortin
- Nitric oxide synthase 3
- Cyclic AMP-responsive element-binding protein 1
- Cyclic AMP-dependent transcription factor ATF-2
- Cyclic AMP-dependent transcription factor ATF-1
Sequence:
MPGAVEGPRWKQAEDIRDIYDFRDVLGTGAFSEVILAEDKRTQKLVAIKCIAKKALEGKEGSMENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQLVSGGELFDRIVEKGFYTERDASRLIFQVLDAVKYLHDLGIVHRDLKPENLLYYSLDEDSKIMISDFGLSKMEDPGSVLSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSPYWDDISDSAKDFIRHLMEKDPEKRFTCEQALQHPWIAGDTALDKNIHQSVSEQIKKNFAKSKWKQAFNATAVVRHMRKLQLGTSQEGQGQTGSHGELLTPTAGGPAAGCCCRDCCVEPGSELPPAPPPSSRAMD
Protein: Sodium/proline symporter (Proline carrier) (Proline permease) (Propionate transporter) (P07117)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the sodium-dependent uptake of extracellular L-proline. This protein is also capable of using lithium as the transport cation. Also catalyzes the uptake of propionate.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:3007935, ECO:0000269|PubMed:3512540, ECO:0000269|PubMed:3902503, ECO:0000269|PubMed:9756872}; Multi-pass membrane protein {ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:9756872}.
Interaction partners:
- Bifunctional protein PutA
- Tryptophan synthase alpha chain
- Tryptophan synthase beta chain
- Aminodeoxychorismate synthase component 1
- DNA polymerase IV
- Isocitrate dehydrogenase
- Proline/betaine transporter
- Uncharacterized transporter YaaJ
- DNA polymerase II
- Beta-glucuronidase
Sequence:
MAISTPMLVTFCVYIFGMILIGFIAWRSTKNFDDYILGGRSLGPFVTALSAGASDMSGWLLMGLPGAVFLSGISESWIAIGLTLGAWINWKLVAGRLRVHTEYNNNALTLPDYFTGRFEDKSRILRIISALVILLFFTIYCASGIVAGARLFESTFGMSYETALWAGAAATILYTFIGGFLAVSWTDTVQASLMIFALILTPVIVIISVGGFGDSLEVIKQKSIENVDMLKGLNFVAIISLMGWGLGYFGQPHILARFMAADSHHSIVHARRISMTWMILCLAGAVAVGFFGIAYFNDHPALAGAVNQNAERVFIELAQILFNPWIAGILLSAILAAVMSTLSCQLLVCSSAITEDLYKAFLRKHASQKELVWVGRVMVLVVALVAIALAANPENRVLGLVSYAWAGFGAAFGPVVLFSVMWSRMTRNGALAGMIIGALTVIVWKQFGWLGLYEIIPGFIFGSIGIVVFSLLGKAPSAAMQKRFAEADAHYHSAPPSRLQES
Protein: RE36938p (Uncharacterized protein, isoform A (EC 3.4.14.1, EC 3.4.14.2, EC 3.4.14.4, EC 3.4.14.5)) (Uncharacterized protein, isoform B) (Q8SXS7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- FI02848p
- Serine protease K12H4.7
- trypsin
- Aminopeptidase
- V-type proton ATPase subunit a
- Aminopeptidase
- Aminopeptidase
- Maltase A2
- Metalloendopeptidase
- Trypsin eta
Sequence:
MKLWLGISLALLALGQTHGSIFERTFKRIHEEPPLPTTQNRADVVQTLWIEQKLDHFDPEETRTWQMRYMLNDALYQSGAPLFIYLGGEWEISSGRITGGHLYDMAKEHNALLAYTEHRYYGQSKPLPDLSNENIKYLNVNQSLADLAYFINTIKQNHEGLSDSKVIIVGGSYSATMVTWFKKLYPDLVAGGWASSAPLLAKVNFVEYKEITGQSIEQMGGSACYKRIENGIAEMETMIATKRGAEVKALLKLCEPFDVYSDLDVWTLFSEISDIFAGVVQTHNAGQIEGVCEKIMAGSNDLIGVAGYLLDVFEESGGKCYDLSYDAITALLLDTNYNGNIMRQWIFQTCNEYGWYQTSGSSAQPFGTKFPVTYYTTMCADLYGSEYSNEFISNQVSITNQFFGGLFPNVENVYLTHGQLDPWRAMGIQDETQATIIPEHAHCKDFNSISSSDTAEMRASKERIAELVREWVK
Protein: Protein VACUOLELESS GAMETOPHYTES (Q6NQN8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential for development of both female (megagametogenesis) and male (microgametogenesis) gametophytes by promoting the formation of large vacuoles early in development, maybe via the regulation of vesicular fusion.
Subcellular location: Endomembrane system {ECO:0000269|PubMed:28107777}. Prevacuolar compartment {ECO:0000269|PubMed:28107777}. Endosome, multivesicular body {ECO:0000269|PubMed:28107777}. Note=Localized to multivesicular bodies in gametophytes during mega- and microgametogenesis. {ECO:0000269|PubMed:28107777}.
Interaction partners:
- Senescence-induced receptor-like serine/threonine-protein kinase
- Probable LRR receptor-like protein kinase At1g51890
- pEARLI1-like lipid transfer protein 3
- Transmembrane protein
- Probable WRKY transcription factor 29
- Similarity to disease resistance protein domain family protein)
- Reticulon-like protein B4
- Dirigent protein 11
- Uncharacterized protein At3g61930
- Cytochrome P450 81F2
Sequence:
MASRPSVRHPSHNHPLRGHKAQVEDEIICSGCDLDLLGAYFKCTKSECDYFLHKSCFDLPREIRHKSHPDHPLILLYSPQNNNSTYTCDACGEYGSGFTYNCSICQYDVHVGCVSVPETMKHDEHVHPLALIYKAPCPKDHIFTCDVCDETMPHNLWLYYCQKCDYGAHLHSCVAEEEEKSKKGGRGRGGEGGSGGNGVNRGRSSANSELAAMLKAQREMEQMQIALHLEMQRAKIDKKSRKHMLKMI
Protein: Ufm1-specific protease 2 (UfSP2) (EC 3.4.22.-) (Q99K23)
Organism: Mus musculus (Mouse)
Function: Thiol-dependent isopeptidase that recognizes and hydrolyzes the peptide bond at the C-terminal Gly of UFM1, a ubiquitin-like modifier protein bound to a number of target proteins. Does not hydrolyze SUMO1 or ISG15 ubiquitin-like proteins. Through TRIP4 deufmylation may regulate intracellular nuclear receptors transactivation and thereby regulate cell proliferation and differentiation (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:21228277}. Cytoplasm {ECO:0000269|PubMed:21228277}. Nucleus {ECO:0000269|PubMed:21228277}.
Interaction partners:
- Ubiquitin-fold modifier 1
- Ubiquitin-like modifier-activating enzyme 5
- E3 UFM1-protein ligase 1
- Ubiquitin-fold modifier-conjugating enzyme 1
- DDRGK domain-containing protein 1
- CDK5 regulatory subunit-associated protein 3
Sequence:
MDILFRIRGGFDLAFQLAPPKEMFIKNALRQVLSDLTTKLSSDALVLRVCNSSVYLWPNSDANTGELTDSSACKNVVRFIQFDQEEDTKRKFIKKKDKKLTDTQQIVNIDLMLEISTPLGAVTPILERENEEHHYINMSLPIDAVVSVAPEESWGKVRKLLVDAILRQLVDVEKCILRYMKGTSIVVPEPLHFQLPGKKNLVTVLYPSGIPDDQLQAYRKELHDLFNLPHDRPYFKRINAYHFPDELYKDGYIRNPHTYLSPPNIEGSMICVVQGTYAYHHYMQDRIDDNGWGCAYRSLQTICSWFRHQGYTERSIPTHREIQQALVDAGDKPATFVGSRQWIGSIEVQMVLNQLIGVTSKILFVNQGSEMASQGRELANHFQNVGTPVMVGGGVLAHTILGVAWNETTGQIKFLILDPHYTGAEDLQVMLEKGWCGWKSPDFWNKDAYYNLCLPQRPNAL
Protein: H/ACA ribonucleoprotein complex subunit 3 (Nucleolar protein 10) (Nucleolar protein family A member 3) (snoRNP protein NOP10) (Q9NPE3)
Organism: Homo sapiens (Human)
Function: Required for ribosome biogenesis and telomere maintenance. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ('psi') residues, which may serve to stabilize the conformation of rRNAs. May also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:11074001}. Nucleus, Cajal body {ECO:0000269|PubMed:11074001}. Note=Also localized to Cajal bodies (coiled bodies).
Interaction partners:
- H/ACA ribonucleoprotein complex subunit DKC1
- H/ACA ribonucleoprotein complex subunit 1
- Telomerase Cajal body protein 1
- H/ACA ribonucleoprotein complex subunit 2
- Telomerase reverse transcriptase
- Protein SHQ1 homolog
- NHP2-like protein 1
- H/ACA ribonucleoprotein complex non-core subunit NAF1
- Nucleolar protein 58
- RuvB-like 2
Sequence:
MFLQYYLNEQGDRVYTLKKFDPMGQQTCSAHPARFSPDDKYSRHRITIKKRFKVLMTQQPRPVL
Protein: Dual specificity protein phosphatase (EC 3.1.3.16) (EC 3.1.3.48) (G3V9L3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAMGCGTTQCLYALCYDDPIKGPAAAMSGSFELSVQDLNDLLSDGSGCYSLPSQPCNEVIPRVYVGNASVAQDITQLQKLGITHVLNAAEGRSFMHVNTSASFYKDTGITYMGIKANDTQEFNLSAYFERAADFIDQALAHKNGRVLVHCREGYSRSPTLVIAYLMLRQKMDVRSALSTVRQNREIGPNDGFLAQLCQLNDRLAEEGKVKL
Protein: Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH5 (EC 2.1.1.-) (EC 2.1.1.367) (Histone H3-K9 methyltransferase 5) (H3-K9-HMTase 5) (Protein SET DOMAIN GROUP 9) (Suppressor of variegation 3-9 homolog protein 5) (Su(var)3-9 homolog protein 5) (O82175)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Histone methyltransferase. Methylates 'Lys-9' of histone H3. H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00358}. Chromosome, centromere {ECO:0000250}. Note=Associates with centromeric constitutive heterochromatin. {ECO:0000250}.
Interaction partners:
- DNA
- Histone H3.1
- Histone H3.3
- Histone H3-like 2
- Histone H3-like 4
- DNA
- Histone H3-like 3
- Histone H3-like 5
- Histone H3-like 1
- Histone H3-like centromeric protein CENH3
Sequence:
MVHSESSILSSLRGGDGGGIPCSKDELAINGSYTDPMGRRKSKRFKVAAESEFSPDFGSITRQLRSRRMQKEFTVETYETRNVSDVCVLSSQADVELIPGEIVAERDSFKSVDCNDMSVGLTEGAESLGVNMQEPMKDRNMPENTSEQNMVEVHPPSISLPEEDMMGSVCRKSITGTKELHGRTISVGRDLSPNMGSKFSKNGKTAKRSISVEEENLVLEKSDSGDHLGPSPEVLELEKSEVWIITDKGVVMPSPVKPSEKRNGDYGEGSMRKNSERVALDKKRLASKFRLSNGGLPSCSSSGDSARYKVKETMRLFHETCKKIMQEEEARPRKRDGGNFKVVCEASKILKSKGKNLYSGTQIIGTVPGVEVGDEFQYRMELNLLGIHRPSQSGIDYMKDDGGELVATSIVSSGGYNDVLDNSDVLIYTGQGGNVGKKKNNEPPKDQQLVTGNLALKNSINKKNPVRVIRGIKNTTLQSSVVAKNYVYDGLYLVEEYWEETGSHGKLVFKFKLRRIPGQPELPWKEVAKSKKSEFRDGLCNVDITEGKETLPICAVNNLDDEKPPPFIYTAKMIYPDWCRPIPPKSCGCTNGCSKSKNCACIVKNGGKIPYYDGAIVEIKPLVYECGPHCKCPPSCNMRVSQHGIKIKLEIFKTESRGWGVRSLESIPIGSFICEYAGELLEDKQAESLTGKDEYLFDLGDEDDPFTINAAQKGNIGRFINHSCSPNLYAQDVLYDHEEIRIPHIMFFALDNIPPLQELSYDYNYKIDQVYDSNGNIKKKFCYCGSAECSGRLY
Protein: Sarcoglycan, alpha (D3ZDQ9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane, sarcolemma {ECO:0000256|ARBA:ARBA00004513}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004513}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Gamma-sarcoglycan
- Dystrophin
- Sarcoglycan, delta
- Dystroglycan 1
- Sarcospan
- Utrophin
- Beta-sarcoglycan
- Caveolin-3
- Sarcoglycan zeta
- Alpha-1-syntrophin
Sequence:
MVAAATWIPLLAGLLAGLRDSKAQQTTLHPLVGRVFVHPLEHATFLRLPEHIAVPPTVRLTYHAHLQGHPDLPRWLHYTQRSPYNPGFLYGTPTPEDRGHQVIEVTAYNRDSFDTTRQRLLLLIGDPEGPRLPYQAEFLVRSHDVEEVLPSTPANRFLTALGGLWEPGELQLLNITSALDRGGRVPLPIEGRKEGVYIKVGSATPFSTCLKMVASPDSYARCAQGQPPLLSCYDTLAPHFRVDWCNVSLVDKSVPEPLDEVPTPGDGILEHDPFFCPPTEATGRDFLTDALVTLLVPVLVALLLTLLLVYIMCCRREGRLKRDMATSDIQMFHHCSIHGNTEELRQMAASREVPRPLSTLPMFNVRTGERLPPRVDSAQMPLILDQH
Protein: U3 small nucleolar RNA-associated protein 25 (U3 snoRNA-associated protein 25) (U three protein 25) (O74974)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: DEAD-box RNA helicase-like protein required for pre-18S rRNA processing, specifically at sites A0, A1, and A2.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized protein C3B8.09
- U3 small nucleolar ribonucleoprotein protein mpp10
- U3 small nucleolar RNA-associated protein 22
- U3 small nucleolar RNA-associated protein 21 homolog
- Uncharacterized protein C18B11.06
- U3 small nucleolar ribonucleoprotein protein imp4
- rRNA biogenesis protein rrp36
- Probable ATP-dependent RNA helicase prh1
- Pre-rRNA-processing protein esf2
- rRNA-processing protein fcf1
Sequence:
MAIESDLDGASMDELAGKSYEALLYLMNKNKKRKPEKKDDKEKSSKKVQKKNKVIESLNEMEVEMEDENENENDEQEAIQYYINVESQDADETLHQEAQDSSEDPFHQHFDYDDSEVIKNSIAAYDEGKLCKSIEESKLGVSQSFFPDVTKRLPCSCLSEIKNIDDLGLKQRILDSYKKQKPSGQLTSMQIELAKAMFNYQDVFFTNMSMKSHKLGTSLLALHALNHVFKTRDRVLKNSARISQNPELEFRDQGYTRPKVLILLPTRNSAFEFINLLISYSGTNQVENRKRFDNEFSIEKEVISEKKPEDFRYLFSGNTDDMFRLGVKFTRKTVKLFSQFYNSDIIVASPLGLRLAIGNKGDKKRDLDYLSSIEIAMVDQAHALVMQNWEHIECIFDELNGLPKEAHGCDFSRVRPWYLDQQARYMRQTILFSQYNNLDINSFFSHYMSNIAGKVKFRSLLHGVLNRLGYKVTQTFVRISVDSIIKVPDARFSYFTGSILVQLKKYSQSGILVYIPSYFDFVRVRNYMDEEGINYSAISEYSSVSDMTRARNLFYQGRTNIMLYTERAHHFRRFDFRGVKAVVMYGPPTNPQFYVELVRMPMRTISEGNLDSDAAKCRIMYTKFDSICLEGIVGYQRVSNMCHGKHEVFEFL
Protein: Calmodulin-binding transcription activator 1 (A2A891)
Organism: Mus musculus (Mouse)
Function: Transcriptional activator.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9Y6Y1, ECO:0000255|PROSITE-ProRule:PRU00767}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y6Y1}.
Interaction partners:
Sequence:
MWRAEGKWLPKTSRKSVSQSVFCGTSTYCVLNTVPPIEDDHGNSNSSHVKIFLPKKLLECLPKCSSLPKERHRWNTNEEIAAYLITFEKHEEWLTTSPKTRPQNGSMILYNRKKVKYRKDGYCWKKRKDGKTTREDHMKLKVQGVECLYGCYVHSSIIPTFHRRCYWLLQNPDIVLVHYLNVPAIEDCGKPCGPILCSINTDKKEWAKWTKEELIGQLKPMFHGIKWTCSNGNSSSGFSVEQLVQQILDSHQTKPQPRTHNCLCTGSLGAGSSVHHKCNSAKHRIISPKVEPRAGGYGGHSEVQHNDVSEGKHEPSHGRSTSREKRNGKVAKPALLHQNSTEVSSTNQVEVPDTTQSSPVSISSGLNSDPDMVDSPVVTGVSSMAVASVMGGLSQSATVFMSEVTNEAVYTMSPTAGPNHHLLSPDASQGLVLAVSSDGHKFAFPTTGSSDSLSMLPANVSEELVLSTTLDGGRKIPETAMNFDPDCFLNNPKQGQTYGGGGLKAEMVSTNIRHSPPAERSFGFTSVLTKEIKTEDTSFEQQMAKEAAYSSSAAAAASSSLTLTAAGSSLLPSGGGLSPSTTLEQMDFSAIDSNKDYASSFSQTGHSPHIHQTPSPSFFLQDASKPLPLEQNTHSSLSESGAAFVMPTVKTEASSQTSSCSGHVETRIESTSSLHLMQFQANFQAMAAEGEVTMETSQAAEGNEVLLKSGELQACGSEHYLQPETNGVIRSAGGVPLLPSNVVQGLYPVAQPSLGNSSNMELSLDHFDISFSNQFSDLINDFISVEGGSGTIYGHQLVSGDSAALSQSEDGARAPFTQAEMCIPCCSPQQGSLQLSSAEGGPSTMAYMHVAEVVSAASAQGALGMLQQSGRVFMVTDYSPEWSYPEGGVKVLITGPWQEASNNYSCLFDQISVPASLIQPGVLRCYCPAHDTGLVTLQVAFNNQIISNSVVFEYKARALPTLPSSQHDWLSLDDNQFRMSILERLEQMERRMAEMTGSQQHKQASGGGGSGSGSGSGAGGGQAQCASGAGTLGSCFESRVVVVCEKMMSRACWAKSKHLIHSKTFRGMTLLHLAAAQGYATLIQTLIKWRTKHADSIDLELEVDPLNVDHFSCTPLMWACALGHLEAAVVLYKWDRRAISIPDSLGRLPLGIARSRGHVKLAECLEHLQRDEQAQLGQASRIHCAPSEEPTTDSWMAQWQREAMSPPEIPKGVTVIASTNPELRRPRSEPSNYYSTEGHKDYPAPKKHKLNPESFQARQEKLLCTALSLEQPNIRKQSPRSKQPSPETISPSEGVREYSREAAPPTPETAASQASASQPVVKWSAKDLYIGVSTVQVTGNPKGTSVVKDAAPSQVRPREPMSVLMLANREVVNTEMGAYRDRTEHEDCPQPMDDIQVNMMTLAEHIIEATPDRIKQENFVPMESSALERTDPATISSTMSWLASYLADADRLPSAAHIRSAYTEPLTPSSNASLSPAGSPVSEVAFEKPSLPSAADWSEFLSASTSEKVESELAQLTLSDHEQRELYEAARLVQTAFRKYKGRPLREQQEVAAAVIQRCYRKYKQLTWIALKYALYKKMTQAAILIQSKFRSYYEQKRFQQSRRAAVLIQNFYRSYKKCGRRRPARRTAVIVQQKLRSSLLTKKQDQAARKIMRFLRRCRHSPLVDHRLYKRSERIEKGQGT