wanglab/gogpt-training-data huggingface dataset:
Protein: Exocyst complex component SEC6 (AtSec6) (Q94AI6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane during regulated or polarized secretion. Involved in polarized cell growth and organ morphogenesis. During cytokinesis, involved in cell plate initiation, cell plate maturation and formation of new primary cell wall.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:19895414, ECO:0000269|PubMed:23283982, ECO:0000269|PubMed:24307681}. Cell membrane {ECO:0000269|PubMed:23283982}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:20870962, ECO:0000269|PubMed:23702595}. Secreted, cell wall {ECO:0000269|PubMed:20870962}. Secreted, extracellular exosome {ECO:0000269|PubMed:24307681}. Note=During cytokinesis, localizes to the nascent cell plate and later to the cell plate insertion site and along the post-cytokinetic wall (PubMed:20870962). Shuttles from the cytoplasm to the exocyst-positive organelle (EXPO) in the presence of EXO70E2 (PubMed:24307681). {ECO:0000269|PubMed:20870962, ECO:0000269|PubMed:24307681}.
Interaction partners:
- Exocyst complex component SEC8
- Exocyst complex component SEC5A
- Exocyst complex component SEC3A
- Exocyst complex component EXO84B
- Exocyst complex component SEC10a
- Exocyst complex component SEC5B
- Exocyst complex component SEC15B
- Exocyst complex component SEC3B
- Exocyst complex component EXO84C
- Exocyst complex component EXO84A
Sequence:
MMVEDLGVEAKEAAVREVAKLLPLPELLQSISSIKADYIARQQANDAQLSTMVAEQVEQAQAGLESLSSSEKTIYELRDNFISIDKLCQECQTLIDNHDQIKLLSNARNNLNKTLKDVEGMMSISVEAAAARDSLSDDKEIVNTYERLTALDGKRRFALAAAGEEVGRLREYFEDVDRTWETFEKTLWGHVSNYYKLSKESPQTLVRALRVVEMQEILDQQLAEEAAEAEGEGAMASVANPRRPGKKSTTTSASSKGLAQQKLKVQGKGYKDKCYEQIRKAVEDRFNRLLTLVFEDLKAALEEARMIGEELGDIYDYVAPCFPPRYEIFQLMVNLYTERFIQMLRLLSDRANDLTNIEILKVTGWVVEYQENLIALGVDDSLAQVCSESGSMDPLMNAYVERMQATTKKWYMNILEADKVQPPKKTEEGKLYTPAAVDLFRILGEQVQIVRDNSTDVMLYRIALAIIQVMIDFQAAEKKRVDEPASDIGLEPLCAMINNNLRCYDLAMELSNSTLEALPQNYAEQVNFEDTCKGFLEVAKEAVHQTVRVIFEDPGVQELLVKLYQKEWCEGQVTEYLVATFGDYFTDVKMYVEERSFRRFVEACLEETVVVYVDHLLTQKNYIKEETIERMRLDEEVLMDFFREYISASKVESRIRIMSDLRELASAESLDAFTLVYSNILEHQPDCPAEVVEKLVSLREGIPRKDTKEVVQECKEIYENTLVDGNPPKTGFVFPRVKCLTASKGSMWRKLT
Protein: Propionyl-CoA carboxylase alpha chain, mitochondrial (PCCase subunit alpha) (EC 6.4.1.3) (Propanoyl-CoA:carbon dioxide ligase subunit alpha) (P05165)
Organism: Homo sapiens (Human)
Function: This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the catabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and other metabolites. Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA. Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then transfers the carboxyl group from carboxylated biotin to propionyl-CoA (By similarity). Propionyl-CoA carboxylase also significantly acts on butyryl-CoA/butanoyl-CoA, which is converted to ethylmalonyl-CoA/(2S)-ethylmalonyl-CoA at a much lower rate. Other alternative minor substrates include (2E)-butenoyl-CoA/crotonoyl-CoA (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:10101253, ECO:0000269|PubMed:16023992}.
Interaction partners:
- Propionyl-CoA carboxylase beta chain, mitochondrial
- Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
- Biotin--protein ligase
- Methylmalonyl-CoA epimerase, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- Trifunctional enzyme subunit beta, mitochondrial
- 3-ketoacyl-CoA thiolase, peroxisomal
Sequence:
MAGFWVGTAPLVAAGRRGRWPPQQLMLSAALRTLKHVLYYSRQCLMVSRNLGSVGYDPNEKTFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPGYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLRHKQADIRINGWAVECRVYAEDPYKSFGLPSIGRLSQYQEPLHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLSDVYPDGFKGHMLTKSEKNQLLAIASSLFVAFQLRAQHFQENSRMPVIKPDIANWELSVKLHDKVHTVVASNNGSVFSVEVDGSKLNVTSTWNLASPLLSVSVDGTQRTVQCLSREAGGNMSIQFLGTVYKVNILTRLAAELNKFMLEKVTEDTSSVLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE
Protein: tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like (EC 1.3.1.88) (tRNA-dihydrouridine synthase 1-like) (Q6P1R4)
Organism: Homo sapiens (Human)
Function: Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:39354220}. Nucleus {ECO:0000269|PubMed:39354220}. Note=Predominantly cytoplasmic localization with a minor population localized to the nucleus. {ECO:0000269|PubMed:39354220}.
Interaction partners:
- tRNA
- WD repeat-containing protein 36
- Bystin
- tRNA
- Nucleolar complex protein 4 homolog
- RNA cytidine acetyltransferase
Sequence:
MPKLQGFEFWSRTLRGARHVVAPMVDQSELAWRLLSRRHGAQLCYTPMLHAQVFVRDANYRKENLYCEVCPEDRPLIVQFCANDPEVFVQAALLAQDYCDAIDLNLGCPQMIAKRGHYGAFLQDEWDLLQRMILLAHEKLSVPVTCKIRVFPEIDKTVRYAQMLEKAGCQLLTVHGRTKEQKGPLSGAASWEHIKAVRKAVAIPVFANGNIQCLQDVERCLRDTGVQGVMSAEGNLHNPALFEGRSPAVWELAEEYLDIVREHPCPLSYVRAHLFKLWHHTLQVHQELREELAKVKTLEGIAAVSQELKLRCQEEISRQEGAKPTGDLPFHWICQPYIRPGPREGSKEKAGARSKRALEEEEGGTEVLSKNKQKKQLRNPHKTFDPSLKPKYAKCDQCGNPKGNRCVFSLCRGCCKKRASKETADCPGHGLLFKTKLEKSLAWKEAQPELQEPQPAAPGTPGGFSEVMGSALA
Protein: ATP-dependent DNA helicase Q1 (EC 5.6.2.4) (DNA 3'-5' helicase Q1) (DNA helicase, RecQ-like type 1) (RecQ1) (DNA-dependent ATPase Q1) (RecQ protein-like 1) (P46063)
Organism: Homo sapiens (Human)
Function: DNA helicase that may play a role in the repair of DNA that is damaged by ultraviolet light or other mutagens. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction.
Subcellular location: Nucleus {ECO:0000269|PubMed:35025765, ECO:0000269|PubMed:7961977}.
Interaction partners:
- Exonuclease 1
- X-ray repair cross-complementing protein 6
- Flap endonuclease 1
- DNA replication ATP-dependent helicase/nuclease DNA2
- Importin subunit alpha-1
- DNA topoisomerase 3-alpha
- RecQ-mediated genome instability protein 1
- X-ray repair cross-complementing protein 5
- Importin subunit alpha-3
- RecQ-mediated genome instability protein 2
Sequence:
MASVSALTEELDSITSELHAVEIQIQELTERQQELIQKKKVLTKKIKQCLEDSDAGASNEYDSSPAAWNKEDFPWSGKVKDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISATMLNASSSKEHVKWVHAEMVNKNSELKLIYVTPEKIAKSKMFMSRLEKAYEARRFTRIAVDEVHCCSQWGHDFRPDYKALGILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFNRPNLYYEVRQKPSNTEDFIEDIVKLINGRYKGQSGIIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGRDDMKADCILYYGFGDIFRISSMVVMENVGQQKLYEMVSYCQNISKCRRVLMAQHFDEVWNSEACNKMCDNCCKDSAFERKNITEYCRDLIKILKQAEELNEKLTPLKLIDSWMGKGAAKLRVAGVVAPTLPREDLEKIIAHFLIQQYLKEDYSFTAYATISYLKIGPKANLLNNEAHAITMQVTKSTQNSFRAESSQTCHSEQGDKKMEEKNSGNFQKKAANMLQQSGSKNTGAKKRKIDDA
Protein: C2H2-type domain-containing protein (G5EB06)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSPAQDSESIKAHPRRRPFRAARPSLVPAEEQSPSLPPLRLRKGETFNPSILRSSDRDHLVPSLPRRSPTCPGALEAIAAGQQRMADILERLDLNSGTTSTSDENDDLPVPKGLLRLHLQTQARREGTVEPHSRQPSPMPKEHSRKAQRVHCHASDSGIGSSISSAQSVSSNKVKAGQLSRSNLPTSRSQSAITRSISAMDAQSTQRHKLSSEGRAEIEKHVIGPLLEDEKSKPFHPILEDVRQQIDDERISCLRDLEKTVFSLAPEVKTNDAAYVRFCQYTILCLGQTVSFLNGRDLCLPTDKQYNNGYFVDLLDQVSQFKRIRDEWKRRHEADGKVKAPQLRLEGGLSQTGRLLEMVVEQDGEAISLRTGKPYEGQPIPSMKRSLSAASTDEGVQRSMARRKKNAPPMNINKKCKDCDKVFARPCDLTKHEKSHSRPFKCPVTSCKYHIKGWATEKESERHYNDKHSDAPRLFACQFESCSYKSKRESNCKQHMEKTHGWVYMRSKNNGRSKASPQQQTTSPSSSSVQPKQAPSVWSMTPPSEAPDYRQEPNGWDLAPSPETPDLFNTYQAPMTAMPGSVTGTLDAVTPTTGTINSPSEPFDLAQENTAFSIQDIFPEMKASDGLLFPGGDMDYPDFINNHNMFNDFGYGDFTMPTQGLQYGETQQPQFEDDSAGFLLDVYNDMHTYGINPGPGGL
Protein: Low molecular weight phosphotyrosine protein phosphatase (LMW-PTP) (LMW-PTPase) (EC 3.1.3.48) (Low molecular weight cytosolic acid phosphatase) (EC 3.1.3.2) (Q9D358)
Organism: Mus musculus (Mouse)
Function: Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates with differences in substrate specificity between isoform 1 and isoform 2.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- GrpE protein homolog 1, mitochondrial
- 6-pyruvoyl tetrahydrobiopterin synthase
- Small ribosomal subunit protein mS29
- Catenin beta-1
Sequence:
MAEVGSKSVLFVCLGNICRSPIAEAVFRKLVTDEKVSDNWRIDSAATSTYEVGNPPDYRGQNCMRKHGIHMQHIARQITKEDFATFDYILCMDESNLRDLNRKSNQVKNCKAKIELLGSYDPQKQLIIEDPYYGNDSDFEVVYQQCLRCCKAFLEKTY
Protein: Cleavage and termination factor 1 (Transcription termination factor ctf1) (O43040)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the cleavage factor I (CF I) involved in pre-mRNA 3'-end processing.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Uncharacterized WD repeat-containing protein C824.04
- RNA polymerase II subunit A C-terminal domain phosphatase ssu72
- Serine/threonine-protein phosphatase PP1-1
- Protein cft1
- mRNA 3'-end-processing protein yth1
- Endoribonuclease ysh1
- Pre-mRNA polyadenylation factor fip1
- Cleavage factor two protein 2
- mRNA cleavage and polyadenylation specificity factor complex subunit pta1
- Polyadenylation factor subunit 2
Sequence:
MSMTAGNVVFVGNIPYDVSEQQMTEIFNQVGPVKTFKLVLDPETGSGKGYGFCEFFDSETTAMAVRKLNNSELGPRKIRVEFPSNDPRRNQSYEYTERTDRYMEQQNAHESSYNSRFIPPVLHSTSSLPASQGGGMPSPAIYSSSMATNLNKNINSTSVPAYNFHNSMTSDFDSASQPHTDAYNARTFQYNKSSQNKGDYTSGTSISNPTSIPLAPSVVQVLSTFSAQELLNMLSKLQTVVHIAPEEARRLLIANPALPYAAFQAMLLMNLVDANVLQQVVVAVKNKNMHQPASATSSPPSVPQKIPSSNHKSQQANGSDQGNEGKRMALIQQLLALTPEQINALPPAQRDQILSIRRQHFRQ
Protein: ADP/ATP translocase (ADP,ATP carrier protein) (Q59EP7)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|RuleBase:RU368008}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU368008}. Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
Sequence:
LKQHWIILACYPVTNMDNSIHLHVLSIHLISSSFFSSKKKSRKCKPFFFSCPLPFSLPCLSSVTHPPLHQVQHASKQISAEKQYKGIIDCVVRIPKEQGFLSFWRGNLANVIRYFPTQALNFAFKDKYKQLFLGGVDRHKQFWRYFAGNLASGGAAGATSLCFVYPLDFARTRLAADVGKGAAQREFHGLGDCIIKIFKSDGLRGLYQGFNVSVQGIIIYRAAYFGVYDTAKGERGASGRRRVVWKEDPMGSITHKGPDIY
Protein: Myb family transcription factor PHL8 (Protein PHR1-LIKE 8) (F4I274)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
Interaction partners:
Sequence:
MCLLMEINNNANNTNTTIDNHKAKMSLVLSTDAKPRLKWTCDLHHKFIEAVNQLGGPNKATPKGLMKVMEIPGLTLYHLKSHLQKYRLGKSMKFDDNKLEVSSASENQEVESKNDSRDLRGCSVTEENSNPAKEGLQITEALQMQMEVQKKLHEQIEVQRHLQVKIEAQGKYLQSVLMKAQQTLAGYSSSNLGMDFARTELSRLASMVNRGCPSTSFSELTQVEEEEEGFLWYKKPENRGISQLRCSVESSLTSSETSETKLDTDNNLNKSIELPLMEINSEVMKGKKRSINDVVCVEQPLMKRAFGVDDDEHLKLSLNTYKKDMEACTNIGLGFN
Protein: Mediator of RNA polymerase II transcription subunit 15 (Activator-recruited cofactor 105 kDa component) (ARC105) (CTG repeat protein 7a) (Mediator complex subunit 15) (Positive cofactor 2 glutamine/Q-rich-associated protein) (PC2 glutamine/Q-rich-associated protein) (TPA-inducible gene 1 protein) (TIG-1) (Trinucleotide repeat-containing gene 7 protein) (Q96RN5)
Organism: Homo sapiens (Human)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Required for cholesterol-dependent gene regulation. Positively regulates the Nodal signaling pathway.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 12
- Mediator of RNA polymerase II transcription subunit 19
- Mediator of RNA polymerase II transcription subunit 23
- Mediator of RNA polymerase II transcription subunit 1
- Mediator of RNA polymerase II transcription subunit 24
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 27
- Mediator of RNA polymerase II transcription subunit 16
- Mediator of RNA polymerase II transcription subunit 17
Sequence:
MDVSGQETDWRSTAFRQKLVSQIEDAMRKAGVAHSKSSKDMESHVFLKAKTRDEYLSLVARLIIHFRDIHNKKSQASVSDPMNALQSLTGGPAAGAAGIGMPPRGPGQSLGGMGSLGAMGQPMSLSGQPPPGTSGMAPHSMAVVSTATPQTQLQLQQVALQQQQQQQQFQQQQQAALQQQQQQQQQQQFQAQQSAMQQQFQAVVQQQQQLQQQQQQQQHLIKLHHQNQQQIQQQQQQLQRIAQLQLQQQQQQQQQQQQQQQQALQAQPPIQQPPMQQPQPPPSQALPQQLQQMHHTQHHQPPPQPQQPPVAQNQPSQLPPQSQTQPLVSQAQALPGQMLYTQPPLKFVRAPMVVQQPPVQPQVQQQQTAVQTAQAAQMVAPGVQMITEALAQGGMHIRARFPPTTAVSAIPSSSIPLGRQPMAQVSQSSLPMLSSPSPGQQVQTPQSMPPPPQPSPQPGQPSSQPNSNVSSGPAPSPSSFLPSPSPQPSQSPVTARTPQNFSVPSPGPLNTPVNPSSVMSPAGSSQAEEQQYLDKLKQLSKYIEPLRRMINKIDKNEDRKKDLSKMKSLLDILTDPSKRCPLKTLQKCEIALEKLKNDMAVPTPPPPPVPPTKQQYLCQPLLDAVLANIRSPVFNHSLYRTFVPAMTAIHGPPITAPVVCTRKRRLEDDERQSIPSVLQGEVARLDPKFLVNLDPSHCSNNGTVHLICKLDDKDLPSVPPLELSVPADYPAQSPLWIDRQWQYDANPFLQSVHRCMTSRLLQLPDKHSVTALLNTWAQSVHQACLSAA
Protein: Protein translocase subunit SecF (P9WGN9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01464}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01464}.
Interaction partners:
- Protein translocase subunit SecD
- Protein translocase subunit SecY
- Protein translocase subunit SecE
- Sec translocon accessory complex subunit YajC
- Membrane protein insertase YidC
- Probable protein-export membrane protein SecG
- Uncharacterized lipoprotein Rv2585c
- Adenine phosphoribosyltransferase
- Protein translocase subunit SecA 1
- Bifunctional
Sequence:
MASKAKTGRDDEATSAVELTEATESAVARTDGDSTTDTASKLGHHSFLSRLYTGTGAFEVVGRRRLWFGVSGAIVAVAIASIVFRGFTFGIDFKGGTTVSFPRGSTQVAQVEDVYYRALGSEPQSVVIVGAGASATVQIRSETLTSDQTAKLRDALFEAFGPKGTDGQPSKQAISDSAVSETWGGQITKKAVIALVVFLVLVALYITVRYERYMTISAITAMLFDLTVTAGVYSLVGFEVTPATVIGLLTILGFSLYDTVIVFDKVEENTHGFQHTTRRTFAEQANLAINQTFMRSINTSLIGVLPVLALMVVAVWLLGVGTLKDLALVQLIGIIIGTYSSIFFATPLLVTLRERTELVRNHTRRVLKRRNSGSPAGSEDASTDGGEQPAAADEQSLVGITQASSQSAPRAAQGSSKPAPGARPVRPVGTRRPTGKRNAGRR
Protein: Receptor-interacting serine/threonine-protein kinase 4 (EC 2.7.11.1) (Ankyrin repeat domain-containing protein 3) (PKC-delta-interacting protein kinase) (P57078)
Organism: Homo sapiens (Human)
Function: Involved in stratified epithelial development. It is a direct transcriptional target of TP63. Plays a role in NF-kappa-B activation.
Subcellular location: Cytoplasm. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Protein kinase C delta type
- WD repeat-containing protein 90
- Interferon regulatory factor 6
Sequence:
MEGDGGTPWALALLRTFDAGEFTGWEKVGSGGFGQVYKVRHVHWKTWLAIKCSPSLHVDDRERMELLEEAKKMEMAKFRYILPVYGICREPVGLVMEYMETGSLEKLLASEPLPWDLRFRIIHETAVGMNFLHCMAPPLLHLDLKPANILLDAHYHVKISDFGLAKCNGLSHSHDLSMDGLFGTIAYLPPERIREKSRLFDTKHDVYSFAIVIWGVLTQKKPFADEKNILHIMVKVVKGHRPELPPVCRARPRACSHLIRLMQRCWQGDPRVRPTFQGNGLNGELIRQVLAALLPVTGRWRSPGEGFRLESEVIIRVTCPLSSPQEITSETEDLCEKPDDEVKETAHDLDVKSPPEPRSEVVPARLKRASAPTFDNDYSLSELLSQLDSGVSQAVEGPEELSRSSSESKLPSSGSGKRLSGVSSVDSAFSSRGSLSLSFEREPSTSDLGTTDVQKKKLVDAIVSGDTSKLMKILQPQDVDLALDSGASLLHLAVEAGQEECAKWLLLNNANPNLSNRRGSTPLHMAVERRVRGVVELLLARKISVNAKDEDQWTALHFAAQNGDESSTRLLLEKNASVNEVDFEGRTPMHVACQHGQENIVRILLRRGVDVSLQGKDAWLPLHYAAWQGHLPIVKLLAKQPGVSVNAQTLDGRTPLHLAAQRGHYRVARILIDLCSDVNVCSLLAQTPLHVAAETGHTSTARLLLHRGAGKEAMTSDGYTALHLAARNGHLATVKLLVEEKADVLARGPLNQTALHLAAAHGHSEVVEELVSADVIDLFDEQGLSALHLAAQGRHAQTVETLLRHGAHINLQSLKFQGGHGPAATLLRRSKT
Protein: Galactoside 2-alpha-L-fucosyltransferase (EC 2.4.1.-) (Xyloglucan alpha-(1,2)-fucosyltransferase) (AtFUT1) (Q9SWH5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in cell wall biosynthesis. Is both necessary and sufficient for the addition of the terminal fucosyl residue on xyloglucan side chains, but is not involved in the fucosylation of other cell wall components. Associates with other xyloglucan-synthesizing enzymes to form multiprotein complexes for xyloglucan synthesis in the Golgi.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:21143678}; Single-pass type II membrane protein {ECO:0000269|PubMed:21143678}. Golgi apparatus membrane {ECO:0000269|PubMed:25392066}; Single-pass type II membrane protein {ECO:0000305|PubMed:25392066}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000269|PubMed:21143678}.
Interaction partners:
- Xyloglucan 6-xylosyltransferase 2
- Xyloglucan galactosyltransferase MUR3
- Xyloglucan glycosyltransferase 4
- GDP-mannose 4,6 dehydratase 2
- B3 domain-containing transcription factor VRN1
- Xyloglucan 6-xylosyltransferase 1
- Probable xyloglucan 6-xylosyltransferase 5
- Polycomb group protein VERNALIZATION 2
- Xyloglucan galactosyltransferase XLT2
- Protein TERMINAL FLOWER 1
Sequence:
MDQNSYRRRSSPIRTTTGGSKSVNFSELLQMKYLSSGTMKLTRTFTTCLIVFSVLVAFSMIFHQHPSDSNRIMGFAEARVLDAGVFPNVTNINSDKLLGGLLASGFDEDSCLSRYQSVHYRKPSPYKPSSYLISKLRNYEKLHKRCGPGTESYKKALKQLDQEHIDGDGECKYVVWISFSGLGNRILSLASVFLYALLTDRVLLVDRGKDMDDLFCEPFLGMSWLLPLDFPMTDQFDGLNQESSRCYGYMVKNQVIDTEGTLSHLYLHLVHDYGDHDKMFFCEGDQTFIGKVPWLIVKTDNYFVPSLWLIPGFDDELNKLFPQKATVFHHLGRYLFHPTNQVWGLVTRYYEAYLSHADEKIGIQVRVFDEDPGPFQHVMDQISSCTQKEKLLPEVDTLVERSRHVNTPKHKAVLVTSLNAGYAENLKSMYWEYPTSTGEIIGVHQPSQEGYQQTEKKMHNGKALAEMYLLSLTDNLVTSAWSTFGYVAQGLGGLKPWILYRPENRTTPDPSCGRAMSMEPCFHSPPFYDCKAKTGIDTGTLVPHVRHCEDISWGLKLV
Protein: Aldehyde-alcohol dehydrogenase (Q6Q3H8)
Organism: Listeria welshimeri
Interaction partners:
Sequence:
MAIKENAAQEVLEVQKVINRLADNGQQALKAFENYDQEQVDNIVHAMALAGLDQHMPLAKLAVEETGRGLYEDKCIKNIFATEYIWNNIKNNKTVGVIHEDVQTGVIEIAEPVGVVAGVTPVTNPTSTTLFKAIIAIKTRNPIIFAFHPSAQRCSAAAAKVVYDAAVAAGAPEHCIQWVEKPSLEATKQLMNHDKVALVLATGGAGMVKSAYSTGKPALGVGPGNVPAYIDKTAKIKRSVNDIILSKSFGQGMICASEQAVIVDKEVAKEVKAEMEANKCYFVKGAEFKKLESYVINPEKGTLNPDVVGKSPAWIANQAGFKVPEDTKILVAEIKGVGDKYPLSHEKLSPVLAFIEAANQAEAFDRCEEMLVYGGLGHSAVIHSTDKEVQKAFGIRMKACRIIVNAPSAQSGIGDIYNGFIPSLTLGCGSYGKNSVSQNVSATNLLNVKRIADRRNNMQWFKLPPKIFFEKYSTQYLQKMEGVERVFIVTDPGMVQFKYVDVVIEHLKKRGNDVAYQVFADVEPDPSDVTVYKGAELMKDFKPDTIIALGGGSAMDAAKGMWLFYEHPEASFFGLKQKFLDIRKRTFKYPKLGGKAKFVAIPTTSGTGSEVTPFAVITDKENNIKYPLADYELTPDVAIVDAQYVTTVPAHITADTGMDVLTHAIESYVSVMASDYTRGLSIRAIELVFENLRESVLTGDPDAREKMHNASALAGMAFANAFLGINHSLAHKIGPEFHIPHGRANAILMPHVIRYNALKPKKHALFPRYESFRADEDYARISRIIGLPAATTEEGVKSLVDAIIKLGKDVGIDMSLKGQNVAKKDLDAVVDTLADRAFMDQCTTANPKQPLVSELKEIYLEAYKGV
Protein: Espin-like protein (Q6ZVH7)
Organism: Homo sapiens (Human)
Function: Binds to but does not cross-link actin. Required for the formation and maintenance of inner ear hair cell stereocilia and staircase formation. Essential for normal hearing.
Subcellular location: Cell projection, stereocilium {ECO:0000250|UniProtKB:Q3UYR4}.
Interaction partners:
- Myosin-IIIb
- Myosin-IIIa
- Epidermal growth factor receptor kinase substrate 8-like protein 2
- Unconventional myosin-XV
- Whirlin
- Twinfilin-2
- Epidermal growth factor receptor kinase substrate 8
- Espin
- Gelsolin
- 55 kDa erythrocyte membrane protein
Sequence:
MEKQRALVAAKDGDVATLERLLEAGALGPGITDALGAGLVHHATRAGHLDCVKFLVQRAQLPGNQRAHNGATPAHDAAATGSLAELCWLVREGGCGLQDQDASGVSPLHLAARFGHPVLVEWLLHEGHSATLETREGARPLHHAAVSGDLTCLKLLTAAHGSSVNRRTRSGASPLYLACQEGHLHLAQFLVKDCGADVHLRALDGMSALHAAAARGHYSLVVWLVTFTDIGLTARDNEGATALHFAARGGHTPILDRLLLMGTPILRDSWGGTPLHDAAENGQMECCQTLVSHHVDPSLRDEDGYTAADLAEYHGHRDCAQYLREVAQPVPLLMTPPPPPFPPPPLLATRRSLEDGRRGGPGPGNPSPMSLSPAWPGHPDQPLPREQMTSPAPPRIITSATADPEGTETALAGDTSDGLAALQLDGLPSGDIDGLVPTRDERGQPIPEWKRQVMVRKLQARLGAESSAEAQDNGGSSGPTEQAAWRYSQTHQAILGPFGELLTEDDLVYLEKQIADLQLRRRCQEYESELGRLAAELQALLPEPLVSITVNSHFLPRAPGLEVEEASIPAAEPAGSAEASEVAPGVQPLPFWCSHISRLVRSLSLLLKGVHGLVQGDEKPSTRPLQDTCREASASPPRSEAQRQIQEWGVSVRTLRGNFESASGPLCGFNPGPCEPGAQHRQCLSGCWPALPKPRSGLASGEPRPGDTEEASDSGISCEEVPSEAGAAAGPDLASLRKERIIMLFLSHWRRSAYTPALKTVACRTLGARHAGLRGQEAARSPGPPSPPSEGPRLGHLWQQRSTITHLLGNWKAIMAHVPARQLRRLSRQPRGALSPEQFLPHVDGAPVPYSSLSLDLFMLGYFQLLECDLPAEERKLRHLLCFEVFEHLGTHGWEAVRAFHKAVTDEVAAGRRAWTDGFEDIKARFFGSSQRPAWDTEPGRKSGLTLLGPLPHAAVPCSGPEPTAQRLGSRSQQGSFNGEDICGYINRSFAFWKEKEAEMFNFGE
Protein: Small ribosomal subunit protein mS25 (28S ribosomal protein S25, mitochondrial) (MRP-S25) (S25mt) (Q9VY28)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P82669}.
Interaction partners:
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS15m
- Mitochondrial ribosomal protein S21, isoform A
- Small ribosomal subunit protein uS12m
- LD06441p
- Mitochondrial ribosomal protein S11
- 28S ribosomal protein S14
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein uS7m
Sequence:
MPFMKGREPIRRTLKYLNAGKLVLKDKVRIFSVNYNTYGAHHAGARDFVFWNIPQIQFKNPEVQVLTLKNMTPSPFVRCYFDDGRDMLIDLDSRNRNDIIDHLVKVVGKTREQLDAEERLKESKDNPANFGYGCGRHCICEIPGQVPCPGTVPLPDHMRGKILFAPK