wanglab/gogpt-training-data huggingface dataset:
Protein: Transport protein particle subunit trs23 (TRAPP subunit trs23) (O43041)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: TRAPP plays a key role in the late stages of endoplasmic reticulum to Golgi traffic.
Subcellular location: Golgi apparatus, cis-Golgi network {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Transport protein particle subunit bet3
- Transport protein particle subunit bet5
- Uncharacterized protein C15A10.12c
- Transport protein particle 20 kDa subunit
- Uncharacterized protein C13G6.05c
- Transport protein particle subunit trs31
- Transport protein particle subunit trs120
- Uncharacterized protein CC285.14
- GTP-binding protein ypt1
- Transport protein particle subunit trs85-2
Sequence:
MHALIIINRAGSLIFQREFGSSPTALTPNEYLVLAGTIHGVHAISTQISPLPGSSGIQLLEAGTFNMHILQTHTGMKFVLFTEKKTTNARLQLQKFYELYSDYVLKNPFYTLEMPIKCQLFDEQLKRYIDSH
Protein: GDP-fucose protein O-fucosyltransferase 2 (EC 2.4.1.221) (Peptide-O-fucosyltransferase 2) (O-FucT-2) (Q9Y2G5)
Organism: Homo sapiens (Human)
Function: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X-X-S/T-C2 of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively. O-fucosylates members of several protein families including the ADAMTS, the thrombospondin (TSP) and spondin families (Probable). Required for the proper secretion of ADAMTS family members such as ADAMTSL1 and ADAMTS13. The O-fucosylation of TSRs is also required for restricting epithelial to mesenchymal transition (EMT), maintaining the correct patterning of mesoderm and localization of the definite endoderm (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:15233996}. Golgi apparatus {ECO:0000269|PubMed:15233996}. Note=Mainly located in the endoplasmic reticulum. {ECO:0000269|PubMed:15233996}.
Interaction partners:
- GDP-fucose protein O-fucosyltransferase 1
- Beta-1,3-glucosyltransferase
- Thrombospondin-1
- Double-stranded RNA-specific editase 1
- Spondin-1
- Protein-arginine deiminase type-2
- Endoribonuclease YbeY
- ADAMTS-like protein 1
- ADAMTS-like protein 2
- Alpha-
Sequence:
MATLSFVFLLLGAVSWPPASASGQEFWPGQSAADILSGAASRRRYLLYDVNPPEGFNLRRDVYIRIASLLKTLLKTEEWVLVLPPWGRLYHWQSPDIHQVRIPWSEFFDLPSLNKNIPVIEYEQFIAESGGPFIDQVYVLQSYAEGWKEGTWEEKVDERPCIDQLLYSQDKHEYYRGWFWGYEETRGLNVSCLSVQGSASIVAPLLLRNTSARSVMLDRAENLLHDHYGGKEYWDTRRSMVFARHLREVGDEFRSRHLNSTDDADRIPFQEDWMKMKVKLGSALGGPYLGVHLRRKDFIWGHRQDVPSLEGAVRKIRSLMKTHRLDKVFVATDAVRKEYEELKKLLPEMVRFEPTWEELELYKDGGVAIIDQWICAHARFFIGTSVSTFSFRIHEEREILGLDPKTTYNRFCGDQEKACEQPTHWKITY
Protein: Twisted gastrulation protein homolog 1 (Q9GZX9)
Organism: Homo sapiens (Human)
Function: May be involved in dorsoventral axis formation. Seems to antagonize BMP signaling by forming ternary complexes with CHRD and BMPs, thereby preventing BMPs from binding to their receptors. In addition to the anti-BMP function, also has pro-BMP activity, partly mediated by cleavage and degradation of CHRD, which releases BMPs from ternary complexes. May be an important modulator of BMP-regulated cartilage development and chondrocyte differentiation. May play a role in thymocyte development (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Chordin
- Bone morphogenetic protein 4
- Chordin-like protein 2
- BMP-binding endothelial regulator protein
- von Willebrand factor C and EGF domain-containing protein
- Bone morphogenetic protein 5
Sequence:
MKLHYVAVLTLAILMFLTWLPESLSCNKALCASDVSKCLIQELCQCRPGEGNCSCCKECMLCLGALWDECCDCVGMCNPRNYSDTPPTSKSTVEELHEPIPSLFRALTEGDTQLNWNIVSFPVAEELSHHENLVSFLETVNQPHHQNVSVPSNNVHAPYSSDKEHMCTVVYFDDCMSIHQCKISCESMGASKYRWFHNACCECIGPECIDYGSKTVKCMNCMF
Protein: Oxidation resistance protein 1 (A0A0B4K6S8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MSRENSPRHGSFRRTLNSRDPSAGAPGSGSGSGPGSPHHQQSNHQHYQHHHHHHHHHQPPIMEHAGAPISTSASNIATVLEDGENQQLPPLTGSGPSRQRSLRDRLKDGITGSFSWQSKSRSVDHGLAAPFDLDSLRSKVEQRFESVDKLSRQKSSLPTIPTISYTVGNRDTLTSVAARFDTTPSELTHLNRLNSSFIYPGQQLLVPDKSAKDDASSSSTHDADGASLSGKSSPVERKLSGDESREKDILEGLRPGSPKPGHIERVGGSSQQQQAEEEANKSDDPVITQRFLKINVRHITDGQGVVGGVLLVTPNAVMFDPNVSDPLVIEHGPESYGVIAPMELVVNAAIFHDIAHMRVAGGAGQGLNSASGDAEKPEIYYPKPVLVEEDSKELPEQQSLLGEDGNKRLDAEIGSLEIADDQESLCSSTGRDGDAFPKAFDRERVEDSSMEAKDSAKTDALDDEDKKAGLGLSSTRSTLEERRKSLLDHHWAIPSKDRSSEDEGDNESNVTVDSGARVQDPHSANSSVSGVPLSQPPVAAAAAAAAVAPASAVVPLPPSGIDLEHLEQLSKQSCYDSGIDIREPVPNVQPIPKKTVYSDADIVLSSDWVPPKTIVPTHFSESPPRSTILGQSLDAGTGGAGGVRKKTSSVSFSVDDEAAQQAQAQSAALAVTDKQADKKNKMLKRLSYPLTWVEGLTGEGGAVPPGGVGSGSLNKSGDTDSAPNTGDSNQSVFSKVFSSSPITLVSELGGNLFSKTPSEDSGGSPVPPLTPHSTHSEGHMTYGRSSIGTFIRPHSSEGTSSSTKLKEAKQAPKLDYRSMVSMDDKPELFISVDKLIPRPARACLDPPLYLRLRMGKPIGKAIPLPTSVMSYGKNKLRAEYWFSVPKNRVDELYRFINTWVKHLYGELDEEQIKARGFELIQEDTEWTKSGTTKAGMGGGSQDGEEISDLTRESWELIKAPFAKTYKIIKTASHAASHDLEMLGGEVLSMSTDEYRKTSLFATGSFDLDFPIPDLIGKTEILTEEHREKLCSHLPARAEGYSWSLIFSTSQHGFALNSLYRKMARLESPVLIVIEDTEHNVFGALTSCSLHVSDHFYGTGESLLYKFNPSFKVFHWTGENMYFIKGNMESLSIGAGDGRFGLWLDGDLNQGRSQQCSTYGNEPLAPQEDFVIKTLECWAFV
Protein: Bifunctional monodehydroascorbate reductase and carbonic anhydrase nectarin-3 (EC 1.6.5.4) (EC 4.2.1.1) (Nectarin-III) [Cleaved into: Nectarin-2] (Q84UV8)
Organism: Nicotiana langsdorffii x Nicotiana sanderae (Ornamental tobacco)
Function: Bifunctional enzyme which has both carbonate dehydratase and monodehydroascorbate reductase activities. May be involved in regulation of nectar pH. May also regulate nectar ascorbate concentration, protecting floral tissues from free radical damage.
Subcellular location: Secreted {ECO:0000269|PubMed:15284496}. Note=Found in the nectar.
Interaction partners:
Sequence:
MRMAAITKMLFISFLFLSSVFLARSGEVDDESEFSYDEKSENGPANWGNIRPDWKECSGKLQSPIDIFDLRAEVVSNLRILQKDYKPSNATLLNRGHDIMLRLDDGGYLKINETQYQLKQLHWHTPSEHTINGERFNLEAHLVHESNNGKFVVIGIVYEIGLWPDPFLSMIENDLKVPANKKGIERGIGIIDPNQIKLDGKKYFRYIGSLTTPPCTEGVVWIIDRKVKTVTRRQIKLLQEAVHDGFETNARPTQPENERYINSTYHSFGIEKQQ
Protein: ABC transporter G family member STR (EC 7.6.2.-) (Protein STUNTED ARBUSCULE) (D3GE74)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Function: Together with STR2, required for arbuscule development in arbuscular mycorrhizal (AM) symbiosis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20453115}; Multi-pass membrane protein {ECO:0000255}. Note=Located in the peri-arbuscular membrane of arbuscular mycorrhiza (AM). {ECO:0000269|PubMed:20453115}.
Interaction partners:
Sequence:
MARLERDGTNKSLESLMDSHKPGGTTTNLNQLRTQKSIPGYGLEFTNLSYSIIKKQKKDGVWINKETYLLHDISGQAIKGEIMAIMGPSGAGKSTFLDALAGRIAKGSLQGSVRIDGKPVTTSYMKMVSSYVMQDDQLFPMLTVFETFMFAAEVRLPPSISRDEKKKRVHELLNKLGLQSATHTYIGDEGRRGVSGGERRRVSIGIEIIHKPSLLFLDEPTSGLDSTSAYSVVEKIKDIAQGGSIVLMTIHQPSFRIQMLLDKITILARGRLIYMGRPDALHTHLSGFGRPVPDGENNIEYLLDVITEYDQATVGLDPLVQYQHDGHKPDPAAMTPVPKPPRTPYRRNTPASKHMISLRSQGFTAGTPQPDSSQFGLDDDDNDDDENFDNSLERRSVQTSRNIVTSGVYPRLASQFYQDFSAKDFSVWLYNGVVGTPRRPPSWTPARTPGWTPGKTPLSGPRSFVSNQHSASYQDPYYIQKTNTVVGQSMDYSATSYAPSYEEFEIEEVLDEPDLGPKYANPWLREVAVLSWRTVLNVIRTPELFASREIVLTVMALVLSTIFKNLGDTTFIDINRLLNFYIFAVCLVFFSSNDAVPSFIMERFIFIRETSHNAYRASSYVISSLIVYLPFFAVQGLTFAVITKLMLHLKSNLFNFWMILFASLITTNAYVMLVSALVPSYITGYAVVIATTALFFLTCGFFLKRTQIPAYWKWLHYISAIKYPFEGLLINEFKNNRGCYSGNKADLSPGPLGDVKPSKHHNASLPLNCLLGEDVLSTMDITMESLWYDILILLAWGVLYRFFFYLVLRFYSKNERK
Protein: Large ribosomal subunit protein uL22c (50S ribosomal protein L22, chloroplastic) (Q8LDU0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At1g43860
- Large ribosomal subunit protein eL42z/eL42y
- Large ribosomal subunit protein eL38z/eL38y
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- 50S ribosomal protein L33
- Large ribosomal subunit protein uL24c
- Large ribosomal subunit protein uL5c
- Large ribosomal subunit protein bL28c
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL4m
Sequence:
MVGWKRNLQTVIRQVGRRVKNSHISTANYSSSTRNLESPFSQGYLQSLLRPSYSSRPLYHHLQQLGISTSRQLQASEEPVSSPLSSPALLGSGKEEEQKIIPKRQKVQAVLKSIKQSPKKVNLVAALVRGMRVEDALIQLQVTVKRAAQTVYRVIHAARANATHNHGLDPDRLLVAEAFVGKGLFGKKVAYHAKGRSGIISIPRCRLTVIVRETTPEEEAEIARLKVHNFKKKSKRERQLVPHKLIETSPIWNRRGTKANHRSSELVRSSH
Protein: Sphingosine 1-phosphate receptor 2 (S1P receptor 2) (S1P2) (Endothelial differentiation G-protein coupled receptor 5) (Lysophospholipid receptor B2) (Sphingosine 1-phosphate receptor Edg-5) (S1P receptor Edg-5) (P52592)
Organism: Mus musculus (Mouse)
Function: Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P) (By similarity). S1P is a bioactive lysophospholipid that elicits diverse physiological effects on most types of cells and tissues (By similarity). Receptor for the chemokine-like protein FAM19A5 (By similarity). Mediates the inhibitory effect of FAM19A5 on vascular smooth muscle cell proliferation and migration (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O95136}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-13
- Guanine nucleotide-binding protein subunit alpha-12
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Reticulon-4
- Apolipoprotein M
- Sphingosine kinase 1
- Sphingosine kinase 2
Sequence:
MGGLYSEYLNPEKVLEHYNYTKETLDMQETTSRKVASAFIIILCCAIVVENLLVLIAVARNSKFHSAMYLFLGNLAASDLLAGVAFVANTLLSGHVTLSLTPVQWFAREGSAFITLSASVFSLLAIAIERQVALAKVKLYGSDKSCRMLMLIGASWLISLILGGLPILGWNCLNQLEACSTVLPLYAKHYVLCVVTIFSVILLAIVALYVRIYFVVRSSHADVAGPQTLALLKTVTIVLGVFIICWLPAFSILLLDSTCPVRACPVLYKAHYFFAFATLNSLLNPVIYTWRSRDLRREVLRPLQCWRRGKGVTGRRGGNPGHRLLPLRSSSSLERGMHMPTSPTFLEGNTVV
Protein: Transcriptional repressor p66 alpha (GATA zinc finger domain-containing protein 2A) (Q8CHY6)
Organism: Mus musculus (Mouse)
Function: Transcriptional repressor. Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin. Enhances MBD2-mediated repression. Efficient repression requires the presence of GATAD2B.
Subcellular location: Nucleus speckle {ECO:0000250|UniProtKB:Q86YP4}. Nucleus {ECO:0000250|UniProtKB:Q86YP4}. Chromosome {ECO:0000250|UniProtKB:Q86YP4}. Note=Speckled nuclear localization requires both CR1 and CR2 regions. Localizes to sites of DNA damage in a manner partially dependent on ZMYND8. {ECO:0000250|UniProtKB:Q86YP4}.
Interaction partners:
- DNA helicase
- Histone deacetylase 1
- Histone-binding protein RBBP4
- Chromodomain-helicase-DNA-binding protein 4
- Histone deacetylase 2
- Histone-binding protein RBBP7
- Metastasis-associated protein MTA2
- Cyclin-dependent kinase 2-associated protein 1
- Transcriptional repressor p66-beta
- Metastasis-associated protein MTA3
Sequence:
MSEEACRTRSQKRTLEPDLTEDDVENKKMKMEKGSSELTVDGDSRVMPEPSAGSAQGLLRTTEAMGTGSGEGLLGDGPVDMRTSHSDMKSEKRPPSPDVIVLSDSEQPSSPRVNGLTTVALKDTSTEALLKSSPEERERMIKQLKEELRLEEAKLVLLKKLRQSQIQKEATAQKPTASSGSTVTTPPPLVRGTQNIPAGKTSLQTSSTRIPGSIIPPPLVRGGQQVSAKLGPQASSQVVMPPLVRGAQIHNIRQHSSTGPPPLLLAPRASVPSMQIQGQRIIQQGLIRVANVPNTSLLVNIPQPTAASMKGTAVASAQANSTPTSVASVVASAESPASRQAAAKLALRKQLEKTLLEIPPPKPPAPEMNFLPSAANNEFIYLVGLEEVVQNLLETQAGRISATAAAAVLSREPYMCVQCKTDFTCRWREKGGAVMCENCMTSNQKKALKVEHTSRLKAAFVKALQQEQEMEQRLLQQGVGTASIKAEPAAPHPTLKQVIKPRRKLAFRSGEARVWNNGSSLQASSQLSRGSATAPRGVLHTFSQSPKLQNAASATALVSRTGRHSERVVGTGKGTASNWKKTPLSTGGTLAFVSPSLAVHKTSSAVDRQREYLLDMIPPRSIPQSATWK
Protein: Dimethylsulfoniopropionate lyase (DMSP lyase) (EC 4.4.1.3) (Symbiodinium-A1) (P0DN22)
Organism: Durusdinium sp. clade D (Symbiodinium sp. clade D)
Function: Mediates cleavage of dimethylsulfonioproprionate (DMSP) into dimethyl sulfide (DMS) and acrylate. DMS is the principal form by which sulfur is transported from oceans to the atmosphere and is a key component of the ocean sulfur cycle.
Interaction partners:
Sequence:
MPLILGGLAGAAAGYGAAAWLERRKPPPGKDPNIKHASLGVVRLDWHYHPLPGDVGSPDSFEYPVYYRAVPGLTFEICQSGKMSPEIQQNFKDAIEFLDKERGVSVITSDCGFFMWFQKEARLYTSKPVVMSSLALLPSLHAAIGTDGKIAIFSANSTSLGPMHDTVAKECGVDWDEACYVLVGCQDVEGFEAVASGEPLDLEKVTPGIVRKAKQVIAEHPDIHAILMECTQLPPFSDDVRAATGLPVYDAIVSADFFIRGFVDNPRFGLNDWHRPWDGHQEKYKLGDNVQDKEKLLHYKP
Protein: Serine-threonine kinase receptor-associated protein (Q9XI22)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- La-related protein 6C
- Serine-threonine kinase receptor-associated protein
- Serine-threonine kinase receptor-associated protein
- La-related protein 6A
- La-related protein 6B
- La-related protein 1A
Sequence:
MGAPLVCHGHSRPVVDVAYSPVTPDGFFLISASKDSNPMLRNGETGDWIGTFEGHKGAVWSCSLDKNAIRAASASADFTAKIWNALTGDELHSFEHKHIVRACAFSEDTHRLLTGGMEKILRIFDLNRPDAPPKEVGNSPGSIRTVEWLHSDNTILSSCTDTGDIRLWDIRSDKIVHTLETKSPVTSAEVSQDGRYITTADGSSVKFWDAKNFGLLKSYDMPCNVESASLEPKHGNTFIAGGEDMWVHRFDFQTGEEIGCNKGHHGPVHCVRYAPGGESYTSGSEDGTVRIWVVGSVNHPEESNLSGHVKLVAEEVVRKAESLRISEKAAEAK
Protein: 1,4-beta-D-glucan cellobiohydrolase B (EC 3.2.1.91) (Beta-glucancellobiohydrolase B) (Exocellobiohydrolase B) (Exoglucanase B) (Q8NK02)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- 1,4-beta-D-glucan cellobiohydrolase C
- Endo-beta-1,4-glucanase A
- Glucanase
- Endo-beta-1,4-glucanase B
- Probable beta-glucosidase A
- Endo-beta-1,4-glucanase celB
- Probable 1,4-beta-D-glucan cellobiohydrolase A
- Extracellular endoglucanase, putative
- beta-glucosidase
- Xylanolytic transcriptional activator xlnR
Sequence:
MASSFQLYKALLFFSSLLSAVQAQKVGTQQAEVHPGLTWQTCTSSGSCTTVNGEVTIDANWRWLHTVNGYTNCYTGNEWDTSICTSNEVCAEQCAVDGANYASTYGITTSGSSLRLNFVTQSQQKNIGSRVYLMDDEDTYTMFYLLNKEFTFDVDVSELPCGLNGAVYFVSMDADGGKSRYATNEAGAKYGTGYCDSQCPRDLKFINGVANVEGWESSDTNPNGGVGNHGSCCAEMDIWEANSISTAFTPHPCDTPGQTLCTGDSCGGTYSNDRYGGTCDPDGCDFNSYRQGNKTFYGPGLTVDTNSPVTVVTQFLTDDNTDTGTLSEIKRFYVQNGVVIPNSESTYPANPGNSITTEFCESQKELFGDVDVFSAHGGMAGMGAALEQGMVLVLSLWDDNYSNMLWLDSNYPTDADPTQPGIARGTCPTDSGVPSEVEAQYPNAYVVYSNIKFGPIGSTFGNGGGSGPTTTVTTSTATSTTSSATSTATGQAQHWEQCGGNGWTGPTVCASPWACTVVNSWYSQCL
Protein: [histone H3]-lysine(27) N-trimethyltransferase (EC 2.1.1.356) (A0A8I6A7B9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDIASPPTSKCITYWKRKVKSEYMRLRQLKRLQANMGAKALYVANFAKVQEKTQLLNEEWKKLRVQPVQPMKPVSGHPFLKKCTIESIFPGFDSQDMLMRSLNTVALVPIMYSWSPLQQNFMVEDETVLCNIPYMGDEVKEEDETFIEELINNYDGKVHGEEEMIPGSVLISDAVFLELVDALNQYSDEEEEGHNDTSDGKQDDSKEDLPVTRKRKRHAIEGNKKSSKKQFPNDMIFSAIASMFPENGVPDDMKERYRELTEMSDPNALPPQCTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNVYKRKNREIKIEPEPCGADCFLWLEGAKEYAMLHNPRSKCSGRRRRRHPVVSASCSNTSASAMAETKEGDSDRDTGNDWASSSSEANSRCQTPTKQKASPAPPQLCVVEAPSEPVEWTGAEESLFRVFHGTYFNNFCSIARLLGTKTCKQVFQFAVKESLILKLPTDELMNPSQKKKRKHRLWAAHCRKIQLKKDNNSTQVYNYQPCDHPDRPCDSTCPCIMTQNFCEKFCQCSPDCQNRFPGCRCKTQCNTKQCPCYLAVRECDPDLCLTCGASEHWDCKVVSCKNCSIQRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYDKYMSSFLFNLNNGMAWPSVPG
Protein: Ferritin light chain (Ferritin L subunit) (P02792)
Organism: Homo sapiens (Human)
Function: Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity).
Subcellular location: Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:24695223}. Cytoplasm {ECO:0000250|UniProtKB:P29391}. Autolysosome {ECO:0000250|UniProtKB:P29391}.
Interaction partners:
- Ferritin heavy chain
- Nuclear receptor coactivator 4
- Ferroportin
- Scavenger receptor class A member 5
- Transferrin receptor protein 1
- Pantothenate kinase 2, mitochondrial
- 85/88 kDa calcium-independent phospholipase A2
- Natural resistance-associated macrophage protein 2
- Iron-responsive element-binding protein 2
- Cytoplasmic aconitate hydratase
Sequence:
MSSQIRQNYSTDVEAAVNSLVNLYLQASYTYLSLGFYFDRDDVALEGVSHFFRELAEEKREGYERLLKMQNQRGGRALFQDIKKPAEDEWGKTPDAMKAAMALEKKLNQALLDLHALGSARTDPHLCDFLETHFLDEEVKLIKKMGDHLTNLHRLGGPEAGLGEYLFERLTLKHD
Protein: Sorting nexin-30 (Q5VWJ9)
Organism: Homo sapiens (Human)
Function: Involved in the regulation of endocytosis and in several stages of intracellular trafficking. Together with SNX4, involved in autophagosome assembly.
Subcellular location: Early endosome membrane {ECO:0000269|PubMed:32513819}; Peripheral membrane protein {ECO:0000250|UniProtKB:O95219}; Cytoplasmic side {ECO:0000250|UniProtKB:O95219}.
Interaction partners:
- Sorting nexin-4
Sequence:
MAGGPPKALPSTGPHSLRDMPHPLAGSSSEEAVGGDSTPSPDLLMARSFGDKDLILPNGGTPAGTSSPASSSSLLNRLQLDDDIDGETRDLFVIVDDPKKHVCTMETYITYRITTKSTRVEFDLPEYSVRRRYQDFDWLRSKLEESQPTHLIPPLPEKFVVKGVVDRFSEEFVETRRKALDKFLKRITDHPVLSFNEHFNIFLTAKDLNAYKKQGIALLTRMGESVKHVTGGYKLRTRPLEFAAIGDYLDTFALKLGTIDRIAQRIIKEEIEYLVELREYGPVYSTWSALEGELAEPLEGVSACIGNCSTALEELTDDMTEDFLPVLREYILYSDSMKSVLKKRDQVQAEYEAKLEAVALRKEDRPKVPADVEKCQDRMECFNADLKADMERWQNNKRQDFRQLLMGMADKNIQYYEKCLMAWESIIPLLQEKQEAK
Protein: bZIP transcription factor 60 (AtbZIP60) (Q9C7S0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor involved in the unfolded protein response (UPR). Acts during endoplasmic reticulum stress (ER) by activating unfolded protein response (UPR) target genes via direct binding to the UPR element (UPRE). Plays a role in plant immunity and abiotic stress responses.
Subcellular location: [Isoform 1]: Endoplasmic reticulum membrane; Single-pass membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus. Note=The bZIP domain is translocated into the nucleus in response to ER stress.
Interaction partners:
- Serine/threonine-protein kinase/endoribonuclease IRE1b
- NAC domain-containing protein 62
- Serine/threonine-protein kinase/endoribonuclease IRE1a
- Heat shock 70 kDa protein BIP3
- NAC domain-containing protein 89
- Subtilisin-like protease SBT6.1
- Basic leucine zipper 8
- Membrane-bound transcription factor site-2 protease homolog
- NAC domain containing protein 103
- Heat shock 70 kDa protein BIP1
Sequence:
MAEEFGSIDLLGDEDFFFDFDPSIVIDSLPAEDFLQSSPDSWIGEIENQLMNDENHQEESFVELDQQSVSDFIADLLVDYPTSDSGSVDLAADKVLTVDSPAAADDSGKENSDLVVEKKSNDSGSEIHDDDDEEGDDDAVAKKRRRRVRNRDAAVRSRERKKEYVQDLEKKSKYLERECLRLGRMLECFVAENQSLRYCLQKGNGNNTTMMSKQESAVLLLESLLLGSLLWLLGVNFICLFPYMSHTKCCLLRPEPEKLVLNGLGSSSKPSYTGVSRRCKGSRPRMKYQILTLAA
Protein: Vacuolar protein sorting-associated protein atg6 (Autophagy-related protein 6) (P87117)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for cytoplasm to vacuole transport (Cvt), autophagy, nucleophagy, and mitophagy, as a part of the autophagy-specific vps34 PI3-kinase complex I. This complex is essential to recruit the atg8-phosphatidylinositol conjugate and the atg12-atg5 conjugate to the preautophagosomal structure. Also involved in endosome-to-Golgi retrograde transport as part of the vps34 PI3-kinase complex II (By similarity). Plays a role in meiosis and sporulation.
Subcellular location: Endosome membrane; Peripheral membrane protein. Vacuole membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q02948}; Peripheral membrane protein. Cytoplasm.
Interaction partners:
- Serine/threonine-protein kinase atg1
- Phosphatidylinositol 3-kinase pik3
- Serine/threonine-protein kinase vps15
- Vacuolar protein sorting-associated protein 38
- Autophagy-related protein 14
- Putative lipase atg15
- Autophagy-related protein 9
- PtdIns3K complex I subunit atg38
- Autophagy-related protein 8
- Autophagy-related protein 3
Sequence:
MQYLCQRCHSLINFKDVYDDDLLKLKNLPKSRFVQASSLTEMNESGESDDQMNSSSEDYPAQRLQLYKKTISEGDYNFDNVPPPELRTPTLDSFVVLPAAKDGYEEEKNSPEEVNDLFSWKIEIYNRIFDLLSSKTKVDHPLCVECAELLTEEMSKTLRALKEEKKMYFNYDNFLSSQTVHEENTAALDSEIDELMKQINEKEEKIEEISDETDKLQKLLRELDEEKEKVYAEEQEFYNNLNQFQIKKLSLERQYDCANLEFEHNSRKLEKLQKMNVFSDIFYISHYSEPNGEGSIATINGLRLGRLPSQKVNWAEINAAWGMTVLLLDVLTEKLDFHSSSYQLKPFGSQSFIIRFDRDPNGNQVKPTKLDLFSSGELKIFMNRRFDQGMVAFLDYLHQFGDFCAAKTPSAVLPYAIENDRIGGKCIRLAFNQDENWTRALKFVLTDIKFLEAYVSSQDKQSNF
Protein: Isoamyl acetate-hydrolyzing esterase (EC 3.1.1.112) (P41734)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Plays a crucial role in the hydrolysis of isoamyl acetate in sake mash (Ref.2). Hydrolyzes short chain esters from acetate (C2) to hexanoate (C6), showing more specificity for shorter chain exters. No activity for decanoate (C10) esters.
Interaction partners:
- Medium-chain fatty acid ethyl ester synthase/esterase 2
- Medium-chain fatty acid ethyl ester synthase/esterase 1
- Alcohol O-acetyltransferase 1
- Pyridoxal 5'-phosphate synthase subunit SNO1
- Probable pyridoxal 5'-phosphate synthase subunit SNO3
- Probable pyridoxal 5'-phosphate synthase subunit SNO2
- Ethanol acetyltransferase 1
- Branched-chain-amino-acid aminotransferase, cytosolic
Sequence:
MDYEKFLLFGDSITEFAFNTRPIEDGKDQYALGAALVNEYTRKMDILQRGFKGYTSRWALKILPEILKHESNIVMATIFLGANDACSAGPQSVPLPEFIDNIRQMVSLMKSYHIRPIIIGPGLVDREKWEKEKSEEIALGYFRTNENFAIYSDALAKLANEEKVPFVALNKAFQQEGGDAWQQLLTDGLHFSGKGYKIFHDELLKVIETFYPQYHPKNMQYKLKDWRDVLDDGSNIMS
Protein: Ras-related protein Rab-35 (EC 3.6.5.2) (Q5U316)
Organism: Rattus norvegicus (Rat)
Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in the process of endocytosis and is an essential rate-limiting regulator of the fast recycling pathway back to the plasma membrane. During cytokinesis, required for the postfurrowing terminal steps, namely for intercellular bridge stability and abscission, possibly by controlling phosphatidylinositol 4,5-bis phosphate (PIP2) and SEPT2 localization at the intercellular bridge. May indirectly regulate neurite outgrowth. Together with TBC1D13 may be involved in regulation of insulin-induced glucose transporter SLC2A4/GLUT4 translocation to the plasma membrane in adipocytes (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q15286}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q15286}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q15286}. Endosome {ECO:0000269|PubMed:23572513}. Melanosome {ECO:0000250|UniProtKB:Q15286}. Note=Present on sorting endosomes and recycling endosome tubules. Tends to be enriched in PIP2-positive cell membrane domains. During mitosis, associated with the plasma membrane and present at the ingressing furrow during early cytokinesis as well as at the intercellular bridge later during cytokinesis. Identified in stage I to stage IV melanosomes. {ECO:0000250|UniProtKB:Q15286}.
Interaction partners:
- Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2
- DENN domain containing 1B
- DENN domain containing 1A
- TBC1 domain family, member 10a
- DENN domain containing 1C
- Inositol polyphosphate 5-phosphatase OCRL
- TBC1 domain family member 24
- TBC1 domain family, member 10b
- AP-4 complex accessory subunit RUSC2
- Tumor susceptibility gene 101 protein
Sequence:
MARDYDHLFKLLIIGDSGVGKSSLLLRFADNTFSGSYITTIGVDFKIRTVEINGEKVKLQIWDTAGQERFRTITSTYYRGTHGVIVVYDVTSAESFVNVKRWLHEINQNCDDVCRILVGNKNDDPERKVVETEDAYKFAGQMGIQLFETSAKENVNVEEMFNCITELVLRAKKDNLAKQQQQQQNDVVKLTKNSKRKKRCC