wanglab/gogpt-training-data huggingface dataset:
Protein: Sulfite reductase [NADPH] subunit beta (EC 1.8.1.2) (Q1K9C2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the reduction of sulfite to sulfide, one of several activities required for the biosynthesis of L-cysteine from sulfate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable phosphoadenosine phosphosulfate reductase
- Probable sulfite reductase flavoprotein component
- Cysteine synthase 1
- Adenylyl-sulfate kinase
- Cysteine synthase 2
- Sulfate adenylyltransferase
- Homocysteine synthase
- Probable cystathionine gamma-synthase
- Probable 3-mercaptopyruvate sulfurtransferase
- Probable uroporphyrinogen-III C-methyltransferase
Sequence:
MSVKASINNSQEAVSRIAFRCSDALYVVHPNNSILNGALTESLKDLKKFETLNVSGKVPHVLPLKSHADPFAHIADAILAEEEVASTQPKQITSVVASADALFFATPHLYKLAHEPLVAHVAIESTEAFDFASVRDTGFVILFSGNRPGDSSEAALEDTLETASLAHRLALKLNTGVLHFYSPVYDTTAALENIETLPSKEDAQHARVAHIPIEEKQEDSEKEGNIKEAFVPPKFDQPERDAATSEYLESLSIKPFEYSGSDDATDVLLVFGSAASELAKAAVTSSVAVAIVRVLRPWLPSKLQEVLPTSTKRLTVLEPITSLPRKWDPLYLDVLSSFVASGSSIELFAVRYGLSSSEQATEIIKAVRDNLSGALKPSLVCDFTDGVSQVFVPTPPSIEEAYHKLLHRVFKSRLNIVNDPASSATKQNIPSRLIISPQFALGSVLEYENQRRAFCDEVATLLKEKNSSVSSESLEVLSNWIVSVDNLESPVDPELVISELKKDSSAPIKSLLDRSEFFTNVSHWIIGSDAWAYDLGNSALHQVLCLEKNVNLLIVDTQPYSTREAVRSSSRKKDIGLYAMNFGNAYVASTALYSSYTQLISALLEADKFKGPSVVLAYLPYHSADDDAITVLQETKKAVDIGYWPLYRWTPALEDGEYSDFKLDSERIRRELKTFLERDNYLTQLTLRVPSLARTLTQSFGAEVRHQQNVDSRNALNKLIEGLSGPPLTILFASDGGTAENVAKRLQNRASARGSKCKIMAMDDFPIEELGNEKNVVVLVSTAGQGEFPQNGREFWEAIKGADLNLSELKYGVFGFGDYEYWPRKEDKIYYNRPGKQLDARFVELGAAPLVTLGLGNDQDPDGWETAYNLWEPELWKALGLDNVEIDIDEPKPITNEDIKQASNFLRGTIFEGLADESTGALAESDCQLTKFHGIYMQDDRDIRDERKKQGLEPAYGFMIRARMPAGVCTPEQWIAMDDISTKWGNHTLKITTRQTFQWHGVLKKNLRNTIRNIVKVFLTTLGACGDVARNVTCSSTPNNETIHDQLFAVSKQISNELLPTTSSYHEIWIEDPETVEKRKVAGEAVQDVEPLYGPTYLPRKFKVGVAAPPYNDVDVYTNDVALIAIIENDKVLGFNVGIGGGMGTTHNNKKTYPRLATVVGYVLTDKIMEVVKAILIVQRDNGDRENRKHARLKYTVDTLGVSTFVEKVEEVLGYKFEEARDHPQFIKNHDDFEGWHKTEKNKYWRSIFVENGRIENNGILQFKTGLRELAERLYTEKSEAEFRLTANQHVILFNVAENELGWINEHMAKYKLDNNAFSGLRLSSAACVALPTCGLAMAESERYLPKLITKVEEIVYEAGLQKDSIVMRMTGCPNGCSRPWVAEIACVGKAPNTYNLMLGGGFYGQRLNKLYRSSVQEKEILNLLRPLIKRYALEREDGEHFGDWVIRAGIITAVENGGANGAVHEGVSPEAF
Protein: Polyadenylation factor subunit 2 (Q9UTN4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for 3'-end cleavage and polyadenylation of pre-mRNAs. Also involved in chromosome segregation where it has a role in chromosome attachment to the mitotic spindle.
Subcellular location: Nucleus {ECO:0000269|PubMed:15743824}.
Interaction partners:
- Uncharacterized RING finger protein P8B7.15c
- RNA polymerase II subunit A C-terminal domain phosphatase ssu72
- Protein cft1
- Poly
- Cleavage factor two protein 2
- Endoribonuclease ysh1
- mRNA cleavage and polyadenylation specificity factor complex subunit pta1
- Pre-mRNA polyadenylation factor fip1
- mRNA 3'-end-processing protein yth1
- Uncharacterized WD repeat-containing protein C824.04
Sequence:
MERAENARIIQKPMTRRTVDYGSGLSKYIVNRHLRSNRYHIHVPRPNPNQIINLYPPYEYKYNNTSSLCTKYIHTSANKARHVINVVRWTPDGRRLLTGSSTGEFTLWNGLTFNFELINQSHDYAVRCAEWSTDGRWLISGDGGGMVKYFEPNLNNVKIVQAHEMEVRDVAFSPNDSKFVTASDDGSLKVWNFHMSTEELKLTGHGWDVKTVDWHPSKGLLASGSKDNLVKFWDPRTGTCIATLHGHKNTIMQASFQKNFGSNYLATVSRDSTCRVFDLRAMKDVRVLRGHEKDVNCVTWHPLYPNLLTTGGSDGSVNHYSLDEPPLLSQQKYHEKHPNVTLSASSYLLYPTAEIPFAHDLGIWSMQYHPLGHLLCTGSNDKTTRFWSRSRPDDKESTMDRHHLGEEQSEAMLSQRKAAIEEDDNYEPDENPLTETLANAHNPQFSGVLNLPGLGTMPSFPSPYQHGQPQIPGMLHASLSNSYAEPSTQNSFIPGLTSKSQDGYPQNYR
Protein: Competence protein C (Q4QNA8)
Organism: Haemophilus influenzae (strain 86-028NP)
Interaction partners:
Sequence:
MKAFFNDPFTPFGKWLSQPFYVHGLTFLLLLSAVIFRPVLDYIEGSSRFHEIENELAVKRSELLHQQKILTSLQQQSESRKLSPELAAQIIPLNKQIQRLAARNGLSQHLRWEMGQKPILHLQLTGHFEKTKTFLTALLANSSQLSVSRLQFIKPEDNPLQTEIIFQLDKETK
Protein: Probable G-protein coupled receptor 75 (O95800)
Organism: Homo sapiens (Human)
Function: G protein-coupled receptor that is activated by the chemokine CCL5/RANTES. Probably coupled to heterotrimeric Gq proteins, it stimulates inositol trisphosphate production and calcium mobilization upon activation. Together with CCL5/RANTES, may play a role in neuron survival through activation of a downstream signaling pathway involving the PI3, Akt and MAP kinases. CCL5/RANTES may also regulate insulin secretion by pancreatic islet cells through activation of this receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- C-C motif chemokine 5
Sequence:
MNSTGHLQDAPNATSLHVPHSQEGNSTSLQEGLQDLIHTATLVTCTFLLAVIFCLGSYGNFIVFLSFFDPAFRKFRTNFDFMILNLSFCDLFICGVTAPMFTFVLFFSSASSIPDAFCFTFHLTSSGFIIMSLKTVAVIALHRLRMVLGKQPNRTASFPCTVLLTLLLWATSFTLATLATLKTSKSHLCLPMSSLIAGKGKAILSLYVVDFTFCVAVVSVSYIMIAQTLRKNAQVRKCPPVITVDASRPQPFMGVPVQGGGDPIQCAMPALYRNQNYNKLQHVQTRGYTKSPNQLVTPAASRLQLVSAINLSTAKDSKAVVTCVIIVLSVLVCCLPLGISLVQVVLSSNGSFILYQFELFGFTLIFFKSGLNPFIYSRNSAGLRRKVLWCLQYIGLGFFCCKQKTRLRAMGKGNLEVNRNKSSHHETNSAYMLSPKPQKKFVDQACGPSHSKESMVSPKISAGHQHCGQSSSTPINTRIEPYYSIYNSSPSQEESSPCNLQPVNSFGFANSYIAMHYHTTNDLVQEYDSTSAKQIPVPSV
Protein: I/6 autoantigen (Q26768)
Organism: Trypanosoma brucei brucei
Function: Microtubule-associated protein that may be involved in cross-linking microtubules.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
Sequence:
MLCPPDVAFEKRHFKRRDGNKVVPPSIALVAGLESGFLFKLSAVEDVARRGQFPGLLTEDGFLLMCEESEHIRDAYAMAKHLVALAPDGIFTRATLQEAAGKVGSTQDTLSVEEVDALFNALDSDNRGYVSVDEFMDALYGEEGREAMREIRREYMRRKIEVEGEPSWRMRPTPKPTRKLRQKRKREQGQKRKQGQRQKQEQGQRQKREQGQRQKQEQGQKRKRERGGAQRPPPPKQKAGCGC
Protein: Cytochrome c oxidase subunit 5A, mitochondrial (Cytochrome c oxidase polypeptide Va) (Q94514)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00427}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00427}; Matrix side {ECO:0000250|UniProtKB:P00427}.
Interaction partners:
- Cytochrome b-c1 complex subunit 7
- Cytochrome b-c1 complex subunit 9
- AT02348p
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cyclope, isoform A
- Cytochrome c oxidase subunit 4
- Cytochrome c oxidase subunit 2
- Levy, isoform A
- Cytochrome c oxidase subunit
- Cytochrome c oxidase subunit 5B, isoform A
Sequence:
MLSITARNLASALRSSLVGTSSRVAAVRCLHGTEESAEEFDKRYEKYFSREGIDGWEIRKGMNDLLGMDLVPSPKIIEAGLRASRRVNDIALAIRWLEGCKDKCGDQKATLYPYLLEKITPTLQELGIPTIEELGYDKPELALKSVYDA
Protein: Protein spire homolog 1 (Spir-1) (Q08AE8)
Organism: Homo sapiens (Human)
Function: Acts as an actin nucleation factor, remains associated with the slow-growing pointed end of the new filament. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Required for asymmetric spindle positioning and asymmetric cell division during meiosis. Required for normal formation of the cleavage furrow and for polar body extrusion during female germ cell meiosis. Also acts in the nucleus: together with FMN2, promotes assembly of nuclear actin filaments in response to DNA damage in order to facilitate movement of chromatin and repair factors after DNA damage. In addition, promotes innate immune signaling downstream of dsRNA sensing. Mechanistically, contributes to IRF3 phosphorylation and activation downstream of MAVS and upstream of TBK1.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11747823}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11747823}. Cell membrane {ECO:0000269|PubMed:11747823}; Peripheral membrane protein {ECO:0000269|PubMed:11747823}; Cytoplasmic side {ECO:0000269|PubMed:11747823}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q52KF3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q52KF3}; Cytoplasmic side {ECO:0000250|UniProtKB:Q52KF3}. Note=Detected at the cleavage furrow during asymmetric oocyte division and polar body extrusion (By similarity). Punctate spots in perinuclear region and cytoplasm, colocalized with Rab11 (By similarity). {ECO:0000250|UniProtKB:Q52KF3}.
Interaction partners:
- Formin-2
- Formin-1
Sequence:
MAQAAGPAGGGEPRTEAVGGEGPREPGAAGGAAGGSRDALSLEEILRLYNQPINEEQAWAVCYQCCGSLRAAARRRQPRHRVRSAAQIRVWRDGAVTLAPAADDAGEPPPVAGKLGYSQCMETEVIESLGIIIYKALDYGLKENEERELSPPLEQLIDHMANTVEADGSNDEGYEAAEEGLGDEDEKRKISAIRSYRDVMKLCAAHLPTESDAPNHYQAVCRALFAETMELHTFLTKIKSAKENLKKIQEMEKSDESSTDLEELKNADWARFWVQVMRDLRNGVKLKKVQERQYNPLPIEYQLTPYEMLMDDIRCKRYTLRKVMVNGDIPPRLKKSAHEIILDFIRSRPPLNPVSARKLKPTPPRPRSLHERILEEIKAERKLRPVSPEEIRRSRLAMRPLSMSYSFDLSDVTTPESTKNLVESSMVNGGLTSQTKENGLSTSQQVPAQRKKLLRAPTLAELDSSESEEETLHKSTSSSSVSPSFPEEPVLEAVSTRKKPPKFLPISSTPQPERRQPPQRRHSIEKETPTNVRQFLPPSRQSSRSLEEFCYPVECLALTVEEVMHIRQVLVKAELEKYQQYKDIYTALKKGKLCFCCRTRRFSFFTWSYTCQFCKRPVCSQCCKKMRLPSKPYSTLPIFSLGPSALQRGESSMRSEKPSTAHHRPLRSIARFSSKSKSMDKSDEELQFPKELMEDWSTMEVCVDCKKFISEIISSSRRSLVLANKRARLKRKTQSFYMSSPGPSEYCPSERTISEI
Protein: Aspartokinase (EC 2.7.2.4) (Aspartate kinase) (P10869)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Aspartate-semialdehyde dehydrogenase
- Homoserine dehydrogenase
- Homoserine kinase
- Threonine synthase
- Aspartate aminotransferase, mitochondrial
- Argininosuccinate synthase
- Aspartate aminotransferase, cytoplasmic
- Asparagine synthetase 1
- Histidine biosynthesis trifunctional protein
- Histidinol-phosphate aminotransferase
Sequence:
MPMDFQPTSSHSNWVVQKFGGTSVGKFPVQIVDDIVKHYSKPDGPNNNVAVVCSARSSYTKAEGTTSRLLKCCDLASQESEFQDIIEVIRQDHIDNADRFILNPALQAKLVDDTNKELELVKKYLNASKVLGEVSSRTVDLVMSCGEKLSCLFMTALCNDRGCKAKYVDLSHIVPSDFSASALDNSFYTFLVQALKEKLAPFVSAKERIVPVFTGFFGLVPTGLLNGVGRGYTDLCAALIAVAVNADELQVWKEVDGIFTADPRKVPEARLLDSVTPEEASELTYYGSEVIHPFTMEQVIRAKIPIRIKNVQNPLGNGTIIYPDNVAKKGESTPPHPPENLSSSFYEKRKRGATAITTKNDIFVINIHSNKKTLSHGFLAQIFTILDKYKLVVDLISTSEVHVSMALPIPDADSLKSLRQAEEKLRILGSVDITKKLSIVSLVGKHMKQYIGIAGTMFTTLAEEGINIEMISQGANEINISCVINESDSIKALQCIHAKLLSERTNTSNQFEHAIDERLEQLKRLGI
Protein: Bifunctional riboflavin kinase/FMN phosphatase [Includes: FMN phosphatase (EC 3.1.3.102) (FMN phosphohydrolase); Riboflavin kinase (EC 2.7.1.26) (Flavokinase)] (Q84MD8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Bifunctional enzyme that catalyzes the hydrolysis of flavin-mononucleotide (FMN) to riboflavin (vitamin B2) and the phosphorylation of riboflavin to form (FMN) coenzyme.
Interaction partners:
- FAD synthetase 2, chloroplastic
- Nudix hydrolase 23, chloroplastic
- FAD synthetase 1, chloroplastic
- Riboflavin synthase
- 6,7-dimethyl-8-ribityllumazine synthase, chloroplastic
- Purple acid phosphatase 8
- Purple acid phosphatase 4
- Purple acid phosphatase 3
- Purple acid phosphatase 7
- Purple acid phosphatase 17
Sequence:
MSMSNSLKKLSSCVLIDLDGTLINTDGVVGDILRKYLCKYGKQWDGRESLKIVGKTPVEAATTIVEDYELPCKVDEFNSEFYPLFSAQMDKIKSLPGANRLIRHLKCHGVPVALASNSSRANIESKISYHEGWKECFSVIVGSDEVSKGKPSPDIFLEAAKRLKKDPADCLVIEDSVPGVMAGKAAGTKVIAVPSLPKQTHLYTSADEVINSLLDIRLEKWGLPPFQDWIENTLPIDPWHIGGPVIKGFGRGSKVLGIPTANLSTKDYADELVEHPSGVYFGWAGLAKRGVFKMVMSIGWNPYFNNKEKTIEPWLLHDFTEDFYGEELRLIIVGYIRPEANFSSLESLIAKIHEDREVAEKALDLPSYAKFKGDPYLTK
Protein: Uncharacterized protein Rv2307c (P9WLC7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein Rv2305
- Uncharacterized protein Rv2304c
Sequence:
MSLKRCRALPVVAIVALVASGVIMFIWSQQRRLIYFPSAGPVPSASSVLPAGRDVVVETQDGMRLGGWYFPHTSGGSGPAVLVCNGNAGDRSMRAELAVALHGLGLSVLLFDYRGYGGNPGRPSEQGLAADARAAQEWLSGQSDVDPARIAYFGESLGAAVAVGLAVQRPPAALVLRSPFTSLAEVGAVHYPWLPLRRLLLDHYPSIERIASVHAPVLVIAGGSDDIVPATLSERLVAAAAEPKRYVVVPGVGHNDPELLDGRVMLDAIRRFLTETAVLGQ
Protein: Nodulation protein D 1 (P03031)
Organism: Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Function: NodD regulates the expression of the nodABCFE genes which encode other nodulation proteins. NodD is also a negative regulator of its own expression. Binds flavonoids as inducers.
Interaction partners:
Sequence:
MRFRGLDLNLLVALDALMTERKLTAAARRINLSQPAMSAAIARLRTYFGDELFSMQGRELIPTPRAEALAPAVRDALLHIQLSVIAWDPLNPAQSDRRFRIILSDFMILVFFARIVERVAREAPGVSFELLPLDDDPHELLRRGDVDFLIFPDVFMSSAHPKAKLFDEALVCVGCPTNKKLLGNISFETYMSMGHVAAQFGREMKPSVEQWLLLEHGFNRRIELVVPGFTLIPRLLSGTNRIATLPLRLVKYFEQTIPLRIVTSPLPPLFFTEAIQWPALHNTDPGNIWLREILLQEASRIDPQSDTC
Protein: Leucine-rich repeat flightless-interacting protein 1 (LRR FLII-interacting protein 1) (GC-binding factor 2) (TAR RNA-interacting protein) (Q32MZ4)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'-AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. May control smooth muscle cells proliferation following artery injury through PDGFA repression. May also bind double-stranded RNA. Positively regulates Toll-like receptor (TLR) signaling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding.
Subcellular location: Nucleus. Cytoplasm.
Interaction partners:
- Protein flightless-1 homolog
- Catenin beta-1
- Intron Large complex component GCFC2
- Gamma-interferon-inducible protein 16
- Tropomodulin-1
- Myeloid differentiation primary response protein MyD88
- Probable ATP-dependent RNA helicase DDX41
- ATP-dependent DNA/RNA helicase DHX36
Sequence:
MTSPAAAQSREIDCLSPEAQKLAEARLAAKRAARAEAREIRMKELERQQKEEDSERYSRRSRRNTSASDEDERMSVGSRGSLRVEERPEKDFTEKGSRNMPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEKHGIILNSEIATNGETSDTLNNVGYQGPTKMTKEELNALKSTGDGTLGRASEVEVKNEIVANVGKREILHNTEKEQHTEDTVKDCVDIEVFPAGENTEDQKSSEDTAPFLGTLAGATYEEQVQSQILESSSLPENTVQVESNEVMGAPDDRTRTPLEPSNCWSDLDGGNHTENVGEAAVTQVEEQAGTVASCPLGHSDDTVYHDDKCMVEVPQELETSTGHSLEKEFTNQEAAEPKEVPAHSTEVGRDHNEEEGEETGLRDEKPIKTEVPGSPAGTEGNCQEATGPSTVDTQNEPLDMKEPDEEKSDQQGEALDSSQKKTKNKKKKNKKKKSPVPVETLKDVKKELTYQNTDLSEIKEEEQVKSTDRKSAVEAQNEVTENPKQKIAAESSENVDCPENPKIKLDGKLDQEGDDVQTAAEEVLADGDTLDFEDDTVQSSGPRAGGEELDEGVAKDNAKIDGATQSSPAEPKSEDADRCTLPEHESPSQDISDACEAESTERCEMSEHPSQTVRKALDSNSLENDDLSAPGREPGHFNPESREDTRGGNEKGKSKEDCTMS
Protein: Nuclear pore complex protein 15 (Nucleoporin npp-15) (P34343)
Organism: Caenorhabditis elegans
Function: Important for early nematode development.
Subcellular location: Nucleus envelope {ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:35852146}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:12937276}. Note=Recruited early during nuclear envelope assembly after mitosis. {ECO:0000269|PubMed:16950114}.
Interaction partners:
- Nuclear pore complex protein Nup85
- Nuclear pore complex protein 5
- WD_REPEATS_REGION domain-containing protein
- Nucleoporin SEH1
- Protein SEC13 homolog
- Nuclear Pore complex Protein
- Nsp1_C domain-containing protein
- Nuclear pore complex protein Nup98-Nup96
- Nuclear Pore complex Protein
- Protein mel-28
Sequence:
MSGRDLELTLDRVSSIEYPALVKEAFLNNWHASAHRSEVTSNCASLNDRYCWVLSRNQIFIWERAKSSHRAIIPTQLPLPTSGLPRSVKCVVVYDGVHRGANKTPCPGILVVSPEGVLRHWTSIESQTYIEEVLDINNEVALRVELTDEPIDGKSASFLLTTTSGTVYFLNGKGQDSAKTGALECNKVAGREAHGFRRRLSSIMFGGESKESTSLITNSFQHQSKDLLVVTVSPDVLTVYNMYTPCELWSLKTKEFFQPKIASFFEADLKRTPLKVRARLIDAAVFRDGLMILIGGTHEESQSVHMFMVWMSANWQTEQPTGVVWSARVPMNEHRALFSKIDDSIYSNLTLCIPKNTAESKKADRTDGIIIINPYFAVSLYLPFDLAKPKKPESLYRHVSIPPRDQLLGYAICSQYVYIMMLESGVSTIRLLPRGFADSSIYTHEQVVVPSLSVGTDDWPILSELLSEMVASGLPKTPLYQSLHRAFELFAEKHMAESEEELKAIIKMPDQEIARIVSQFLYAIIDYSDAANKTDTELHAKRVLTSRIMLFLKHMGVYERIISSPLGISRGGILSLRVGGTMLGEVSERVAASTAIWTWKTSNETNSAVFDAIIEKVLRIPEVQDLGLKDKDALFGRCGLVHHIPVVAAQQLEKNVIGKTKSHRFEVFHAVCELLSGIKETIISWRNCRTKVAIPKFPIWWTLETFASCYRDVAEKIIEELKNGSSTDSERARLLMYILSIYDFYLSESDSQPDNDKVLQEMIALGKPADAMELAEKHKDFGTLVKNYLTTDVGTRQKTFERYKKMFEKDDFEMYLCDYLKEHGRNDVLLQQGGSRVDAYLDNFKELRYSREIANKQFGKAALTLMSLADAETKSFSKFVEFLTRAYYCACSSIDGTDVSEVLDFYKRRYPEMKHRKRIPTEILKICFGNDLDAMMSVEDMLEWNMAVQPNDEASVEGFARAFHLLADLLAVHPDSDELKKKIDKTWKALVDYDEWNRVRSKEDVEKKTIFGKFCNYLINSYPADKGDSFPIWMPISRRLIFPTDIDTVLDECIANTTGNHLSWIKGHLKWIGEQLCKQALLPKSAFFRPDMKQVGSISQAALEAFGPILQRREQRFIDQLNRDSMMET
Protein: Plant thionin family protein (A7REF0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Plant thionin family protein
- Transmembrane protein
- S-protein homolog 2
- Uncharacterized protein
- Uncharacterized protein
- Plant thionin family protein
- Transmembrane protein
- Uncharacterized protein AT4g31280
- Gag-Pol polyprotein/retrotransposon
- Secreted protein
Sequence:
MGIQTRSVLIIVAILTMMFSAHIAQSNSITMCVKHCAQNECLKAAKKPTPKICDEACKKICNNQLFGDEKWFVPAPKGSSRICRWAPKYCQF
Protein: Peroxisomal membrane protein PEX13 (Peroxin-13) (P80667)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 or PEX21 receptors. The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm. Mechanistically, PEX5 (or PEX21) receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:8858167}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Peroxisomal membrane protein PEX17
- Peroxisomal membrane protein import receptor PEX19
- Peroxisomal biogenesis factor 2
- Peroxisomal targeting signal 2 receptor
- Peroxisomal membrane protein PEX14
- Peroxisomal targeting signal receptor
- Peroxisomal biogenesis factor 8
- Peroxisome assembly protein 12
- Peroxisome biogenesis factor 10
- Peroxisomal membrane protein PMP27
Sequence:
MSSTAVPRPKPWETSASLEEPQRNAQSLSAMMTSNQQDSRPTEESNNSNSASESAPEVLPRPAALNSSGTYGESNTIPGIYGNSNYGIPYDNNPYSMNSIYGNSIGRYGYGGSYYGNNYGSFYGGGYGAGAGYGMNNGSGLGESTKATFQLIESLIGAVTGFAQMLESTYMATHNSFFTMISVAEQFGNLKEMLGSFFGIFAIMKFLKKILYRATKGRLGIPPKNFAESEGSKNKLIEDFQKFNDSGTINSNEKATRRKISWKPLLFFLMAVFGFPYLLNKFITKLQTSGTIRASQGNGSEPIDPSKLEFARALYDFVPENPEMEVALKKGDLMAILSKKDPLGRDSDWWKVRTKNGNIGYIPYNYIEIIKRRKKIEHVDDETRTH
Protein: Hyaluronan synthase 3 (EC 2.4.1.212) (Hyaluronate synthase 3) (Hyaluronic acid synthase 3) (HA synthase 3) (O08650)
Organism: Mus musculus (Mouse)
Function: Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation. This is one of three isoenzymes responsible for cellular hyaluronan synthesis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10455188, ECO:0000269|PubMed:16014622}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:16014622}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:16014622}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle {ECO:0000269|PubMed:16014622}. Note=Travels through endoplasmic reticulum (ER), Golgi, plasma membrane, and endocytic vesicles (PubMed:16014622). Actives only when present in plasma membrane (PubMed:16014622). O-GlcNAcylation controls its membrane localization (By similarity). A rapid recycling of HAS3 between plasma membrane and endosomes is controlled by the cytosolic levels of UDP-GlcUA and UDP-GlcNAc (By similarity). {ECO:0000250|UniProtKB:O00219, ECO:0000269|PubMed:16014622}.
Interaction partners:
- CD44 antigen
- UDP-glucose 6-dehydrogenase
- Hyaluronan and proteoglycan link protein 1
- Hyaluronidase-2
- Hyaluronidase-1
- Hyaluronan mediated motility receptor
Sequence:
MPVQLTTALRVVGTSLFALVVLGGILAAYVTGYQFIHTEKHYLSFGLYGAILGLHLLIQSLFAFLEHRRMRRAGRPLKLHCSQRPRSVALCIAAYQEDPEYLRKCLRSAQRIAFPNLKVVMVVDGNRQEDTYMLDIFHEVLGGTEQAGFFVWRSNFHEAGEGETEASLQEGMERVRAVVWASTFSCIMQKWGGKREVMYTAFKALGNSVDYIQVCDSDTVLDPACTIEMLRVLEEDPQVGGVGGDVQILNKYDSWISFLSSVRYWMAFNVERACQSYFGCVQCISGPLGMYRNSLLQQFLEDWYHQKFLGSKCSFGDDRHLTNRVLSLGYRTKYTARSKCLTETPTRYLRWLNQQTRWSKSYFREWLYNSLWFHKHHLWMTYESVVTGFFPFFLIATVIQLFYRGRIWNILLFLLTVQLVGIIKATYACFLRGNAEMIFMSLYSLLYMSSLLPAKIFAIATINKSGWGTSGRKTIVVNFIGLIPVSIWVAVLLGGLAYTAYCQDLFSETELAFLVSGAILYGCYWVALLMLYLAIIARRCGKKPEQYSLAFAEV
Protein: Nardilysin-like (EC 3.4.24.61) (N-arginine dibasic convertase-like) (NRD convertase-like) (NRD-C) (F4HNU6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cleaves peptide substrates on the N-terminus of arginine residues in dibasic pairs.
Interaction partners:
- Probable mitochondrial-processing peptidase subunit alpha-1, mitochondrial
- Probable mitochondrial-processing peptidase subunit alpha-2, chloroplastic/mitochondrial
Sequence:
MSSMKSVSALDNVVVKSPNDRRLYRVIELENGLCALLIHDPDIYPEGSVPDQIDEDDEDGEEEDSDGSSEDDDDDEDDEEDGEGDEEDEDEDEDEVKGKGDHQTKKAAAAMCVSMGSFLDPPEAQGLAHFLEHMLFMGSTEFPDENEYDSYLSKHGGSSNAYTEMEHTCYHFEVKREFLQGALKRFSQFFVAPLMKTEAMEREVLAVDSEFNQALQNDACRLQQLQCYTSAKGHPFNRFAWGNKKSLSGAMENGVDLRECIVKLYKEYYHGGLMKLVVIGGESLDMLESWVVELFGDVKNGSKIRPTLEAEGPIWKGGKLYRLEAVKDVHILDLTWTLPPLRSAYVKKPEDYLAHLLGHEGRGSLHSFLKAKGWATSLSAGVGDDGINRSSLAYVFGMSIHLTDSGLEKIYDIIGYIYQYLKLLRDVSPQEWIFKELQDIGNMDFRFAEEQPADDYAAELSENMLAYPVEHVIYGDYVYQTWDPKLIEDLMGFFTPQNMRIDVVSKSIKSEEFQQEPWFGSSYIEEDVPLSLMESWSNPSEVDNSLHLPSKNQFIPCDFSIRAINSDVDPKSQSPPRCIIDEPFMKFWYKLDETFKVPRANTYFRINLKGAYASVKNCLLTELYINLLKDELNEIIYQASIAKLETSLSMYGDKLELKVYGFNEKIPALLSKILAIAKSFMPNLERFKVIKENMERGFRNTNMKPLNHSTYLRLQLLCKRIYDSDEKLSVLNDLSLDDLNSFIPELRSQIFIEALCHGNLSEDEAVNISNIFKDSLTVEPLPSKCRHGEQITCFPMGAKLVRDVNVKNKSETNSVVELYYQIEPEEAQSTRTKAVLDLFHEIIEEPLFNQLRTKEQLGYVVECGPRLTYRVHGFCFCVQSSKYGPVHLLGRVDNFIKDIEGLLEQLDDESYEDYRSGMIARLLEKDPSLLSETNDLWSQIVDKRYMFDFSHKEAEELRSIQKKDVISWYKTYFRESSPKCRRLAVRVWGCDTNMKETQTDQKAVQVIADAVAFKSTSKFYPSLC
Protein: Fimbrin (O59945)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Plays a role in cytokinesis. Plays important roles in mating and in spore formation.
Subcellular location: Cytoplasm, cytoskeleton, actin patch {ECO:0000269|PubMed:11294907}. Note=Localizes both to the cortical actin patches and to the medial ring in an F-actin-dependent manner.
Interaction partners:
- Actin
- Tropomyosin
- Cofilin
- F-actin-capping protein subunit beta
- Transgelin
- Myosin-1
- Profilin
- Coronin-like protein crn1
- Protein app1
- Actin-related protein 2
Sequence:
MLALKLQKKYPELTNEEILTLTDQFNKLDVDGKGYLDQPTTIKAFEDSKKGSYDEVREAIREVNVDSSGRVEPEDFVGIFNVLKKGVEGTEVKKGRITIKGSSSSVSHTINEEERREFIKHINSVLAGDPDVGSRVPINTETFEFFDQCKDGLILSKLINDSVPDTIDERVLNKQRNNKPLDNFKCIENNNVVINSAKAMGGISITNIGAGDILEGREHLILGLVWQIIRRGLLGKIDITLHPELYRLLEEDETLDQFLRLPPEKILLRWFNYHLKAANWPRTVSNFSKDVSDGENYTVLLNQLAPELCSRAPLQTTDVLQRAEQVLQNAEKLDCRKYLTPTAMVAGNPKLNLAFVAHLFNTHPGLEPLNEEEKPEIEPFDAEGEREARVFTLWLNSLDVTPSIHDFFNNLRDGLILLQAYDKITPNTVNWKKVNKAPASGDEMMRFKAVENCNYAVDLGKNQGFSLVGIQGADITDGSRTLTLALVWQMMRMNITKTLHSLSRGGKTLSDSDMVAWANSMAAKGGKGSQIRSFRDPSISTGVFVLDVLHGIKSEYVDYNLVTDGSTEELAIQNARLAISIARKLGAVIFILPEDIVAVRPRLVLHFIGSLMAV