wanglab/gogpt-training-data huggingface dataset:
Protein: NAC domain-containing protein 13 (ANAC013) (Protein NTM1-like 1) (F4IED2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator activated by proteolytic cleavage through regulated intramembrane proteolysis (RIP). Involved in oxidative stress tolerance by mediating regulation of mitochondrial retrograde signaling during mitochondrial dysfunction. Interacts directly with the mitochondrial dysfunction DNA consensus motif 5'-CTTGNNNNNCA[AC]G-3', a cis-regulatory elements of several mitochondrial retrograde regulation-induced genes, and triggers increased oxidative stress tolerance.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24045019}; Single-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353, ECO:0000269|PubMed:24045019}. Note=Localized primarily in endoplasmic reticulum membrane as dormant form and, upon oxidative stress, is processed into a transcriptionally active and nuclear form after a proteolytic cleavage through regulated intramembrane proteolysis (RIP). {ECO:0000269|PubMed:24045019}.
Interaction partners:
- Inactive poly [ADP-ribose] polymerase RCD1
- Ubiquinol oxidase 1a, mitochondrial
- Cytosolic sulfotransferase 12
- At5g18300
Sequence:
MDLSVENGGLAPGFRFHPTDEELVVYYLKRKIRRKKLRVEAIGETDVYKFDPEELPEKALYKTRDRQWFFFSLRDRKHGSRSSRATERGYWKATGKDRVIHCDSRPVGEKKTLVFHRGRAPNGERTNWVMHEYTLHKEELKRCGGEDVKDAYVLYKIYKKSGSGPKNGEQYGAPFIEEEWAEDDDDDVDEPANQLVVSASVDNSLWGKGLNQSELDDNDIEELMSQVRDQSGPTLQQNGVSGLNSHVDTYNLENLEEDMYLEINDLMEPEPEPTSVEVMENNWNEDGSGLLNDDDFVGADSYFLDLGVTNPQLDFVSGDLKNGFAQSLQVNTSLMTYQANNNQFQQQSGKNQASNWPLRNSYTRQINNGSSWVQELNNDGLTVTRFGEAPGTGDSSEFLNPVPSGISTTNEDDPSKDESSKFASSVWTFLESIPAKPAYASENPFVKLNLVRMSTSGGRFRFTSKSTGNNVVVMDSDSAVKRNKSGGNNDKKKKKNKGFFCLSIIGALCALFWVIIGTMGGSGRPLLW
Protein: beta-ketoacyl-[acyl-carrier-protein] synthase I (EC 2.3.1.41) (F4KHF4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MQALQSSSLRASPPNPLRLPSNRQSHQLITNARPLRRQQRSFISASASTVSAPKRETDPKKRVVITGMGLVSVFGNDVDAYYEKLLSGESGISLIDRFDASKFPTRFGGQIRGFSSEGYIDGKNERRLDDCLKYCIVAGKKALESANLGGDKLNTIDKRKAGVLVGTGMGGLTVFSEGVQNLIEKGHRRISPFFIPYAITNMGSALLAIDLGLMGPNYSISTACATSNYCFYAAANHIRRGEADMMIAGGTEAAIIPIGLGGFVACRALSQRNDDPQTASRPWDKARDGFVMGEGAGVLVMESLEHAMKRGAPIVAEYLGGAVNCDAHHMTDPRADGLGVSSCIERCLEDAGVSPEEVNYINAHATSTLAGDLAEINAIKKVFKSTSGIKINATKSMIGHCLGAAGGLEAIATVKAINTGWLHPSINQFVRITGSQEKASLIPLSNPEQAVDFDTVPNEKKQHEVDVAISNSFGFGGHNSVVAFSAFKP
Protein: S-phase entry cyclin-6 (P32943)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in G1/S and or S phase progression. Interacts with CDC28.
Interaction partners:
- Cyclin-dependent kinase 1
- Sister chromatid cohesion protein 1
- G2/mitotic-specific cyclin-2
- Serine/threonine-protein kinase MEC1
- S-phase entry cyclin-5
- Protein SIC1
- Cell division control protein 6
- G1/S-specific cyclin CLN2
- APC/C activator protein CDC20
- G1/S-specific cyclin CLN1
Sequence:
MNCIPSPISERKIQINNEDCIGKENAFHTIPRESSINLTPHSTNEKKVLSEVNSNKIDSLQLPRGKLQRDSTHLEKTRKRQLSNDSTDPIEPKTVKKIKCHQWKNLDSIEMDDPFMVAEYTDSIFSHLYEKEIQMLPTHNYLMDTQSPYHLKSSMRALLIDWLVEVHEKFHCLPETLFLAINLLDRFLSQNVVKLNKLQLLCITCLFIACKFEEVKLPKITNFAYVTDGAATVEGIRKAELFVLSSLGYNISLPNPLNFIRRISKADNYCIETRNMAKFIMEYSICCNKFIHLKPSYLAAMSMYIARKIKNENSKWDETFIHYSGGIDIESDPAFKDFISELVEDIAVPDTNLDSLRLKYKKPKHGMVYFKVFDWCKQKR
Protein: Plakophilin-4 (p0071) (Q99569)
Organism: Homo sapiens (Human)
Function: Plays a role as a regulator of Rho activity during cytokinesis. May play a role in junctional plaques.
Subcellular location: Cell junction, desmosome {ECO:0000269|PubMed:17115030}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:17115030}. Midbody {ECO:0000269|PubMed:17115030}. Cell membrane {ECO:0000269|PubMed:17115030}; Peripheral membrane protein {ECO:0000269|PubMed:17115030}. Note=Associated with the pericentrosomal region in interphase and with spindle poles during mitosis. In anaphase, during chromosome segregation, is recruited to the central microtubule bundle, focussed at the spindle midzone and ultimately localizes to the midbody at cytokinesis. Constituent of the midbody cytoskeletal matrix. Colocalized with desmoplakin at desmosomal junctional plaques in cultured epithelial cells.
Interaction partners:
- PDZ domain-containing protein 2
- Desmoplakin
- Erbin
- Catenin beta-1
- Protein ECT2
- Desmocollin-3
- FERM and PDZ domain-containing protein 2
- Desmocollin-2
- Junction plakoglobin
- Desmoglein-2
Sequence:
MPAPEQASLVEEGQPQTRQEAASTGPGMEPETTATTILASVKEQELQFQRLTRELEVERQIVASQLERCRLGAESPSIASTSSTEKSFPWRSTDVPNTGVSKPRVSDAVQPNNYLIRTEPEQGTLYSPEQTSLHESEGSLGNSRSSTQMNSYSDSGYQEAGSFHNSQNVSKADNRQQHSFIGSTNNHVVRNSRAEGQTLVQPSVANRAMRRVSSVPSRAQSPSYVISTGVSPSRGSLRTSLGSGFGSPSVTDPRPLNPSAYSSTTLPAARAASPYSQRPASPTAIRRIGSVTSRQTSNPNGPTPQYQTTARVGSPLTLTDAQTRVASPSQGQVGSSSPKRSGMTAVPQHLGPSLQRTVHDMEQFGQQQYDIYERMVPPRPDSLTGLRSSYASQHSQLGQDLRSAVSPDLHITPIYEGRTYYSPVYRSPNHGTVELQGSQTALYRTGSVGIGNLQRTSSQRSTLTYQRNNYALNTTATYAEPYRPIQYRVQECNYNRLQHAVPADDGTTRSPSIDSIQKDPREFAWRDPELPEVIHMLQHQFPSVQANAAAYLQHLCFGDNKVKMEVCRLGGIKHLVDLLDHRVLEVQKNACGALRNLVFGKSTDENKIAMKNVGGIPALLRLLRKSIDAEVRELVTGVLWNLSSCDAVKMTIIRDALSTLTNTVIVPHSGWNNSSFDDDHKIKFQTSLVLRNTTGCLRNLSSAGEEARKQMRSCEGLVDSLLYVIHTCVNTSDYDSKTVENCVCTLRNLSYRLELEVPQARLLGLNELDDLLGKESPSKDSEPSCWGKKKKKKKRTPQEDQWDGVGPIPGLSKSPKGVEMLWHPSVVKPYLTLLAESSNPATLEGSAGSLQNLSAGNWKFAAYIRAAVRKEKGLPILVELLRMDNDRVVSSVATALRNMALDVRNKELIGKYAMRDLVNRLPGGNGPSVLSDETMAAICCALHEVTSKNMENAKALADSGGIEKLVNITKGRGDRSSLKVVKAAAQVLNTLWQYRDLRSIYKKDGWNQNHFITPVSTLERDRFKSHPSLSTTNQQMSPIIQSVGSTSSSPALLGIRDPRSEYDRTQPPMQYYNSQGDATHKGLYPGSSKPSPIYISSYSSPAREQNRRLQHQQLYYSQDDSNRKNFDAYRLYLQSPHSYEDPYFDDRVHFPASTDYSTQYGLKSTTNYVDFYSTKRPSYRAEQYPGSPDSWV
Protein: RUN and FYVE domain-containing protein 1 (FYVE-finger protein EIP1) (La-binding protein 1) (Rab4-interacting protein) (Zinc finger FYVE domain-containing protein 12) (Q96T51)
Organism: Homo sapiens (Human)
Function: Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate and participates in early endosomal trafficking.
Subcellular location: Early endosome membrane {ECO:0000269|PubMed:20534812, ECO:0000269|PubMed:36282215}; Peripheral membrane protein {ECO:0000269|PubMed:20534812}. Note=In oocytes, localizes in non-membrane-bound compartments called endo-lysosomal vesicular assemblies (ELVAs). {ECO:0000250|UniProtKB:Q8BIJ7}.
Interaction partners:
- Ras-related protein Rab-4A
- Cytoplasmic tyrosine-protein kinase BMX
- Ras-related protein Rab-5A
- Ras-related protein Rab-14
- Ephrin type-A receptor 3
- RUN and FYVE domain-containing protein 2
- Podocalyxin
Sequence:
MADREGGCAAGRGRELEPELEPGPGPGSALEPGEEFEIVDRSQLPGPGDLRSATRPRAAEGWSAPILTLARRATGNLSASCGSALRAAAGLGGGDSGDGTARAASKCQMMEERANLMHMMKLSIKVLLQSALSLGRSLDADHAPLQQFFVVMEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIATSVRNLPELKTAVGRGRAWLYLALMQKKLADYLKVLIDNKHLLSEFYEPEALMMEEEGMVIVGLLVGLNVLDANLCLKGEDLDSQVGVIDFSLYLKDVQDLDGGKEHERITDVLDQKNYVEELNRHLSCTVGDLQTKIDGLEKTNSKLQEELSAATDRICSLQEEQQQLREQNELIRERSEKSVEITKQDTKVELETYKQTRQGLDEMYSDVWKQLKEEKKVRLELEKELELQIGMKTEMEIAMKLLEKDTHEKQDTLVALRQQLEEVKAINLQMFHKAQNAESSLQQKNEAITSFEGKTNQVMSSMKQMEERLQHSERARQGAEERSHKLQQELGGRIGALQLQLSQLHEQCSSLEKELKSEKEQRQALQRELQHEKDTSSLLRMELQQVEGLKKELRELQDEKAELQKICEEQEQALQEMGLHLSQSKLKMEDIKEVNQALKGHAWLKDDEATHCRQCEKEFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLLLQRCSSTAS
Protein: NADH dehydrogenase (ubiquinone) complex I, assembly factor 6 (A2AIL4)
Organism: Mus musculus (Mouse)
Function: Involved in the assembly of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I) at early stages. May play a role in the biogenesis of complex I subunit MT-ND1.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:18614015}. Note=Peripherally localized on the matrix face of the mitochondrial inner membrane. {ECO:0000250}.
Interaction partners:
- Arginine-hydroxylase NDUFAF5, mitochondrial
- Protein arginine methyltransferase NDUFAF7, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex assembly factor 4
- NADH-ubiquinone oxidoreductase chain 1
- NADH dehydrogenase 1 alpha subcomplex assembly factor 2
- NADH dehydrogenase 1 alpha subcomplex assembly factor 3
- NADH dehydrogenase 1 alpha subcomplex subunit 10, mitochondrial
- Iron-sulfur cluster transfer protein NUBPL
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- FAD-dependent oxidoreductase domain-containing protein 1
Sequence:
MATSMLGSVRGPRPFGLANLFHRQPPRDAWERVRRLPGPSAVRRSVAAASGPGIPGSHLYCLELLRKRDYESYLCSLLFPAECQRSASALRAFNVELAQVKDSVSEKTIGLMRMQFWKKAVEDMYCDNPPHQPVAIELWKAVKKHNLTKRWLMRIIDEREKNLDDKAYRSMQELENYAENTQGSLLYLTLEVLGVKDLHADHAASHIGKAQGIVTCLRATPYHSSRRQVFLPMDVCVQHGVSQEDFLRRNQDKNVRDVVYDIASQAHLHLKHARSFHRSVPAEAFPAFLQTVSLEDYLKKIQRVDFDIFHPSLQQKNMLLPLSLYIQSWRKRY
Protein: FAS receptor variant 9 (Fas cell surface death receptor) (K9J972)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLGIWTLLPLVLTSVARLSSKSVNAQVTDINSKGLELRKTVTTVETQNLEGLHHDGQFCHKPCPPGERKARDCTVNGDEPDCVPCQEGKEYTDKAHFSSKCRRCRLCDEGHGLEVEINCTRTQNTKCRCKPNFFCNSTVCEHCDPCTKCEHGIIKECTLTSNTKCKEEGSRSNLGWLCLLLLPIPLIVWGNSGNKFI
Protein: Lysine-specific demethylase 5D (EC 1.14.11.67) (Histocompatibility Y antigen) (H-Y) (Histone demethylase JARID1D) (Jumonji/ARID domain-containing protein 1D) (Protein SmcY) ([histone H3]-trimethyl-L-lysine(4) demethylase 5D) (Q62240)
Organism: Mus musculus (Mouse)
Function: Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. May play a role in spermatogenesis. Involved in transcriptional repression of diverse metastasis-associated genes; in this function seems to cooperate with ZMYND8. Suppresses prostate cancer cell invasion. Regulates androgen receptor (AR) transcriptional activity by demethylating H3K4me3 active transcription marks (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9BY66, ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000255|PROSITE-ProRule:PRU00537}.
Interaction partners:
- Histone demethylase UTY demethylase UTY)
- ATP-dependent RNA helicase DDX3Y
- Eukaryotic translation initiation factor 2 subunit 3, Y-linked
- Ubiquitin carboxyl-terminal hydrolase 9Y
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
- ATP synthase F
- Predicted gene, 20826
Sequence:
MKPGSDDFLPPPECPVFEPSWAEFRDPLGYIAKIRPIAEKSGICKIRPPADWQPPFAVEVDNFRFTPRIQRLNELEAQTRVKLNYLDQIAKFWEIQGSSLKIPNVERKILDLYSLNKIVMEEGGYEAICKDRRWARVAQRLNYPSGKNIGSLLRSHYERIIYPYEIFQSGANLVQCNTDPFDSEERDKEYKPHSIPLRQSVQPSKFSCYSRRGKRLQPEPEPTEEDIEKNPELKKLQIYGAGPKMIGLGLKAKEKTLRKKDSKQPDKEEVTCPATIVVKGEASEFGKVTSAFSDKNLNHSFEPCMKMTMQLRNNHSSTQFMNSYVCRICSRGDEVDKFLLCDGCSDNYHIFCLLPPLSEVPKGVWRCPKCILAECKSPPEAFGFEQATQEYTLQSFGEMADSFKADYFNMPVHMVPTEVVEKEFWRLVSSIEEDVTVEYGADIHSKEFGSGFPVNNSKWDLSPEEKEYAACGWNLNVMPVLDQSVLCHINADISGMKVPWLYVGMVFSAFCWHIEDHWSYSINYLHWGEPKTWYGVPSLAAEHLEDVMKRLTPELFDSQPDLLHQLVTLMNPNTLMSHGVPVVRTNQCAGEFVITFPRAYHSGFNQGYNFAEAVNFCTADWLPVGRQCIEHYRRLRRYCVFSHEELICKMAAFPEKLDLNLAVAVHKEMFIMVQEERRLRKTLLEKGITEAEREAFELLPDDERQCIKCKTTCFLSALACYDCPDSLVCLSHINDLCKCSRNRQYLRYRYTLDELPAMLQKLKIRAESFDNWANKVQAALEVEDGRKRSFEELRALESEARDRRFPNSELLQRLKKCLTEAEACISQVLGLISNSEDRLQTPQITLTELQLLLKQMGTLPCTMHQIDEVKDVLQQVESYQIETREALTSLPYSLEILQSLMEKGQQLRVEVPEAHQLEELLEQAQWLDQVKQALAPSGQRHSLVIMKKLLVMGTKVASSPSVNKARAELQELLTIAECWEEKAHFCLKASQKHSPATLEVIIREAENIPVYLPNIQSLKEALTKAQAWIADVNEIQNGDHYPCLDDLEGLVAVGRDLPVELEELRQLENQVLTAHSWKEKASKTFLKKNSCYTLLEVLCPCADAGSVSTKRSRWIEKEMGLYKYDTELLGLSAQDLRDPGSVIMAFKEGEEKEKEGILHLRHINSAKPSPMSSSMNASATSICICGQVCAGVESLQCDLCHDWFHGQCVTVPHLLSSVRASHTSSQLLAWWEWDTKFLCPLCMRSRRPRLETILSLLVGLQRLSVRLPEGEALQCLTERAIGWQGRARQALASEDVTALLKQLEKSRQQLQDELRHKKPPTLPSGFAFDCLTENSGKDILKEEEELVLNEERIKSSEKIVPKESSCKGDKELLPSLLSQLTGPVLELPEATRAPLEELMMEGDLLEVTLDENYSIWQLLQAGQNPNLERIHTLLELEKPENPGNWSEEQTPERRRQRRQKVVLSRKGEDFTQKELESKRVKSSRIKPKEEKFQKPILGDNVLYTHHTEHTNILKEHINSVQGKDPSPSSSFPSLTPLLHLSYFHQQKL
Protein: Immunoglobulin superfamily member 8 (IgSF8) (CD81 partner 3) (Glu-Trp-Ile EWI motif-containing protein 2) (EWI-2) (Keratinocyte-associated transmembrane protein 4) (KCT-4) (Prostaglandin regulatory-like protein) (PGRL) (CD antigen CD316) (Q8R366)
Organism: Mus musculus (Mouse)
Function: May play a key role in diverse functions ascribed to CD81 and CD9 such as oocytes fertilization or hepatitis C virus function. May regulate proliferation and differentiation of keratinocytes. May be a negative regulator of cell motility: suppresses T-cell mobility coordinately with CD81, associates with CD82 to suppress prostate cancer cell migration, regulates epidermoid cell reaggregation and motility on laminin-5 with CD9 and CD81 as key linkers. May also play a role on integrin-dependent morphology and motility functions. May participate in the regulation of neurite outgrowth and maintenance of the neural network in the adult brain.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21609323}; Single-pass membrane protein {ECO:0000269|PubMed:21609323}.
Interaction partners:
- CD9 antigen
- CD81 antigen
- Tetraspanin-3
- CD82 antigen
Sequence:
MGVPSPTPLSSLLLLLLILGTRCYARQVHVPRGPLYRVAGTAVSISCNVSDYEGPAQQDFEWFMYRPEAPATSLGIVSTKDSQFSYAVFGPRVASGDLQVQRLKGDSVVLKIARLQAQDSGFYECYTPSTDTQYLGNYSAKVELRVLPDELQVSAAPPGPRGRQAATSPSRLTVHEGQELALGCLAQTKTKKHTHLSVSFGRAIPEAPVGRATLQEVVGLRSDMAVEAGAPYAERLASGELRLSKEGTDRYRMVVGGAQAGDSGTYHCTAAEWIQDPDGSWVQVAEKRAVLAHVDVQTLSSQLAVTVGPGERRIGPGEPLELLCNVSGALPPPGRHAAYSVGWEMAPAGAPGPGRLVAQLDTEGIGSLGPGYEDRHIAMEKVASRTYRLRLEAARPADAGTYRCLAKAYVRGSGTRLREAASARSRPLPVHVREEGVVLEAVAWLAGGTVYRGETASLLCNISVRGGPPGLRLAASWWVERPEEGELSSGPAQLVGGVGQDGVAELGVRPGGGPVSVELVGPRSHRLRLHGLGPEDEGIYHCAPSAWVQHADYSWYQAGSARSGPVTVYPYTHAVDTLFVPLLVGTGVALVTGASVLATITCCFMKRMRKR
Protein: POU domain protein (Q2VUE0)
Organism: Coturnix japonica (Japanese quail) (Coturnix coturnix japonica)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MASLYSQPGGFTVNGMLSPAGGGQSLVHPGLVRGGETAELGEHPGHHHHHHHPHPGHHAPHHGAVNSHEAHSDEDTPTSDDLEQFAKQFKQRRIKLGFTQADVGLALGTLYGNVFSQTTICRFEALQLSFKNMCKLKPLLNKWLEEADSSTGSPTSIDKIAAQGRKRKKRTSIEVSVKGALESHFLKCPKPSAQEITNLADSLQLEKEVVRVWFCNRRQKEKRMTPPGIQQQTPDDVYSQVGAVSSDTPPPHHGLQSGVQ
Protein: Pinin (P79149)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Transcriptional activator binding to the E-box 1 core sequence of the E-cadherin promoter gene; the core-binding sequence is 5'CAGGTG-3'. Capable of reversing CTBP1-mediated transcription repression. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Participates in the regulation of alternative pre-mRNA splicing. Associates to spliced mRNA within 60 nt upstream of the 5'-splice sites. Component of the PSAP complex which binds RNA in a sequence-independent manner and is proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. Involved in the establishment and maintenance of epithelia cell-cell adhesion (By similarity).
Subcellular location: Nucleus speckle {ECO:0000250}. Cell junction, desmosome {ECO:0000250}. Note=Cell-cell contact area, predominantly desmosome of intercellular adherens junction. Not a nucleocytoplasmic shuttling protein (By similarity). {ECO:0000250}.
Interaction partners:
- RNA binding protein with serine rich domain 1.
- Sin3A associated protein 18.
- Apoptotic chromatin condensation inducer 1.
- PNN interacting serine and arginine rich protein.
- Eukaryotic translation initiation factor 4A3
- Pre-mRNA processing factor 4B.
- Trafficking protein particle complex 6B.
- Leucine rich repeat and fibronectin type III domain containing 5.
- LUC7 like 3 pre-mRNA splicing factor.
- RNA binding motif protein 39.
Sequence:
MAVAVRTLQEQLEKAKESLKNVDENIRKLTGRDPNDVRPIQARLLALSGPGGGRGRGSLLLRRGFSDSGGGPPAKQRDLEGAVSRLGGERRTRRESRQESDPEDDDVKKPALQSSVVATSKERTRRDLIQDQNMDEKGKQRNRRIFGLLMGTLQKFKQESTVATERQKRRQEIEQKLEVQAEEERKQVENERRELFEERRAKQTELRLLEQKVELAQLQEEWNEHNAKIIKYIRTKTKPHLFYILGRMCPATQKLIEESQRKMNALFEGRRIEFAEQINKMEARPRRQSMKEKEHQVVRNEEQKAEQEEGKVAQREEELEETGNQHNDVEIEEAGEEEEKEIGIVHSDAEKEQEEEEQKQEMEVKIEEETEVRESEKQQDSQPEEVMDVLEMLLHVAVKNVIAEQEVMETNQVESVEPSENETSKELEPEMEFEVEPDKECKSLSPVRENASALEMENEPEEKEERESEPQPEPVRHLQPLPQPEPEPELQPEPQPQLQPEPQLQPQLQLQLQPQPQSQSQPQPQLQLPLPLPLQPQPQVQAQSQPQAVLQPQPVSQPETLPLAVLQAPVQVIQEQGHLLPERKEFPVESVKLTEVTVEPVLIVHSDSKTKTKTRSRSRGRARNKTSKSRSRSSSSSSSSSSSTSSSSGGSSSSGSSSSRSSSSSSSSTSGSSRRDSSSSTTSSSESRSRSRGRGHNRDRKHRRSVDRKRRDTSGLERSHKSSKGGSSRDTKGSKDKNSRSDRKRSISESSRSGKRSSRSERDRKSDRKDKRR
Protein: Rolling pebbles, isoform I (M9PC91)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Postsynapse {ECO:0000256|ARBA:ARBA00034110}.
Interaction partners:
Sequence:
MPSLQQIALAMEGDQSELQTPPLPINPPPKVMANGIVYGFRTRHLSCIEENDSDSLHGSSIPHAYDMMQQADETFQKLNANEEQDESGSEDGGLENLDDTIAMIDESRLLEADYLDELVAEEQLQEQDEDEEESSDLVDSGNVEEDFWQPSFNRNDIMMTSVYGALNGSLTSEVSSTAAPGYSECATPRKEAEPVYATPEKRRASNRSFDSTCASLTSSLYGGSMNSSLDLKYSSLGGGDSVSGGISGTSTLRGTSVPPMDLSMISSDGVSALDWGSASVSCVLDSGDGNPAEELNEEMAAKCLSAAESDLQSIRRLLEHDASGSVCPSCRISFDKGKRRKLIDTCGHERCYSCMFRNDQCPMCMNSSLKDVDGANAQGYDTGIGGSTSTIVSPLGSPQPQLRSHAQRNAALARYMQHRQESQSPDYHHRYASNGKLPRAAALSTNGNGFTTGTTQTVTVDVHHQLGGGGGGAAAAAKQLMANGISGHSRSSSMSHNIHAAAYSELSAAPPAFATPPTRRRFFNHKNLRSALTGGSGGGSGVGGGVGGAGGVGGGHRRTASNGGCPIDTASILSGGSDAIDHHSSFLNEKLQKDQLHARLGLLLNDPGSNGNSSSSGSGCEPISAHSTTSTTSSSGVGAASTTTSGSSQNVSPEQTLASGAGMLSGSQLSVATSHGVKEDALSLCGKFKAGCSMLHVYEALPSKSRKGNVRRSTRGQQGSSSSASAASAVGSRVTASSLAAVQLALKPLFFEVPLQEPDPPYVGRQWLVQQLSNILLGTETRVVLINGQPGTGKTAFCLQLVEYSCFGRRQMQDDPDGIYSQLQLGAHCERMRGLASHMVGYHFCQADANLTCQVPDFVHSLAAQLCQAPQLTAYRDYLLSEPHLQDILSVRECIADAERVMKLAILEPLAHLHRAGKIPAKVAVIVVDALCEAEYHRPDHGHTIASFLAQLTPHFPAWLKLVATVRTQMLELVKAPSYTQLTLDSWASSQALQQDMLDYIGARLADSPEIRMNIGGGGGQNSQSGSQPQTKFVSHLQSLSRGSMLYAKLILDLIARGQLVIKSSSYKVLPVSLAQIFLLHFNLRFPTARSFEQAAPILNICLAALYPLTLDEIYYSMEALSHGREALSWPDFMQRFKLLDGFLIKRLDNTYMFFHSSLREWLMRRDEGESNKFLCDARLGHAGIAFRLSRLQAPLSPQLTLELGHHMLKAHLYGGTSLTLLSPRDLQSYWLAGAADNISSSLGALRNVYSPNLKVSRLVLLAGASPNHRTDYMGGAPILCIAAHEGILPMVSLLLEFGADVGLTNSQGCTPLILAAMRGHCDVVRPLVAAGSSLGQLDITQRCALVHAARMGHLSVVKYLLACDWSPRPHSQDVTRSVALQQALIGAAAQAHCKILEDLLDLNETEFDLDVNGMEPSSGELALTAAARHGCIDVVGILLSRGAQIDARNRQGYSALWLAVKEGHWSVVEHLLQRGALLDEPLGQTRKTPLMIAAEEGHLELVDLLLARGAQREAQDHEGFTALSWACLRGHLAAAKTLIEHGCNRHHEDHNGRTALDLAAYQGAASLVIYILEQGGNLEHIDVHGMRPLDRAIACRNIQAVQVFLRKGAKLGPTTWSMAMGKPEILVILLNKLLEDGNVLYRKNRFQEAAHRYQYALRKISGLEQLLERNAIFAQLRTNLLLNLSRCKRKLNELDASIDLATQAIAQKPHSYEGYYARAKARMELGALNEALVDANEAMQQAAQSGVLCEVVEVLKRIQTELLTRISISSEDQTGRMSNIGGGASVAYESHHEITDL
Protein: UPF0494 membrane protein C212.04c (Q9HGP8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Endoplasmic reticulum {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Uncharacterized transporter C757.13
- ATP-dependent DNA helicase tlh1
- ATP-dependent DNA helicase tlh2
- WW domain-containing protein C11B10.08
- Uncharacterized cox1 intron-2 37.2 kDa protein
- Uncharacterized transcriptional regulatory protein C11D3.11c
Sequence:
MSNPESLKKQVEPPGYNELFMVEDVCNVDLEQGLDLCKPEKVNKQSQRSRQSRQSLFTNTIKPQKDKMNIKTNKIKEFLNDLFTEFSKFHNSYYPNGRISTQDKSRWVLLIIWSIITILTIDKKFKIKESYLEWIGENQSHSEIWGPIVIYVGLFILLLSAFNYCSKLIIKALPLISMVIAWVGVVIAAFSVIITATIAGVIAAFSVIITATIAGVIAAMVGILYFGHWLVYKILILAFGFKIVTSGDVCVSNTLPTHNGETALHSDATVGSDIEQIELQNMPTPVKK
Protein: tRNA (Uracil-5-)-methyltransferase (Q4GYR8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- tRNA
- Ribosome biogenesis protein BOP1 homolog
- tRNA
- U3 small nucleolar RNA-associated protein 13 C-terminal domain-containing protein
Sequence:
MEGTECGTEQAKSSVPLRTHSNENLLKFDTHDKYSTVASVKKAIMRSLPPPKTNVPPQPLFTGLLRMAKSPNTPLLFLAFETPEHRAAAAEMLSTMSFRGRKPWHEVPVTPRDLQLTYKGAGRKRERTEDAEGQSKVTQWGGCPMEEQLQRKKKHCLQVMRAITLGGGSEYEKLFTGIHPSPHQTGYRNHVQFTFGFTEAGEATIGFLKGSVIDGIYAIESVLEKDIETVNPLAKLVADAVMTVYHLFKPLEKGGLEVYDKIKEEGFWRRLQVRHNVLGEVMVDAEMDTESVAEDIVASVKAQLVAALQGETLRKKLCAAHGKDTANIVSVQYHHGTGMNPAPPEAPRHVLFGSATLTEHLLGLQFELSPTSFFQVNTAGMELLLRETVAVAELTPETTLLDLCCGTGTIGIALAKHVKRVIGIELVESAVRDARLNAERNGVRNATFNCGRVEHLLPSVISQLSPEDRKDIVAILDPPRAGVTPTVLKWIRGTATIRRLVYISCEQKALQRDCPPLTKPATKAYRESPFNVVAGFAIDMFPHTPHVEMVAVLSRSNSS
Protein: Endoplasmic reticulum membrane protein complex subunit 10 (Q12025)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q5UCC4}.
Interaction partners:
- Protein SOP4
- ER membrane protein complex subunit 1
- ER membrane protein complex subunit 3
- ER membrane protein complex subunit 6
- ER membrane protein complex subunit 4
- ER membrane protein complex subunit 2
- ER membrane protein complex subunit 5
- Actin-like protein ARP10
- Nuclear migration protein JNM1
- F-actin-capping protein subunit beta
Sequence:
MLVRLLRVILLASMVFCADILQLSYSDDAKDAIPLGTFEIDSTSDGNVTVTTVNIQDVEVSGEYCLNAQIEGKLDMPCFSYMKLRTPLKYDLIVDVDEDNEVKQVSLSYDETNDAITATVRYPEAGPTAPVTKLKKKTKTYADKKASKNKDGSTAQFEEDEEVKEVSWFQKNWKMLLLGLLIYNFVAGSAKKQQQGGAGADQKTE
Protein: Sperm acrosome membrane-associated protein 3 (Lysozyme-like protein 3) (Sperm lysozyme-like protein 1) (mSLLP1) [Cleaved into: Sperm acrosome membrane-associated protein 3, membrane form; Sperm acrosome membrane-associated protein 3, processed form] (Q9D9X8)
Organism: Mus musculus (Mouse)
Function: Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization. It could be a potential receptor for the egg oligosaccharide residue N-acetylglucosamine, which is present in the extracellular matrix over the egg plasma membrane. The processed form has no detectable bacteriolytic activity in vitro (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000305|PubMed:15982649}; Single-pass type II membrane protein {ECO:0000305|PubMed:15982649}. Note=Anterior acrosome in non-capacitated spermatozoa and retained in the equatorial segment and in the luminal face of both the inner and outer acrosomal membranes following capacitation and the acrosome reaction.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
Interaction partners:
- Transmembrane protein 190
- Sperm acrosome membrane-associated protein 1
Sequence:
MGICMSMYTQVLVPVDADGDHHILWSRFYERWGSCFNPCAGLVNCLPPHSSALYLCHRMEARSRAPRRQLCPPGITWLALAYLLSCLLASSKAKVFSRCELAKEMHDFGLDGYRGYNLADWVCLAYYTSGFNTNAVDHEADGSTNNGIFQISSRRWCRTLASNGPNLCRIYCTDLLNNDLKDSIVCAMKIVQEPLGLGYWEAWRHHCQGRDLSDWVDGCDF