wanglab/gogpt-training-data huggingface dataset:
Protein: Liprin-alpha-3 (PTPRF-interacting protein alpha 3) (X1WCJ5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Mitogen-activated protein kinase kinase kinase.
- SH2 domain-containing 3Cb.
- Peripheral plasma membrane protein CASK
- Down syndrome cell adhesion molecule-like 1
- Liprin-beta-2b isoform 2
- Liprin-beta-1b
Sequence:
MMCEVMPTISEDGRGGAGGGPSSPAGGGGGMGGGAGGMGGGYGGREARGGDEGGSTGNLESLMVNMLTERERLLESLRETQESLGTAQLRLRELGHEKDSLQRQLSIALPQEFAVLTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERVAVLEEELESSTNEVLSLRDQIKRRERGLDNGKERLPNGPSSILDDGEIDRQREGEIERQRAELSQLKERLALMCRQVGEIEEQLTTARRELAKSEEANQKLQRDVKEALCQREDMEERITTLERRYLSAQREATSLHDIKDKLENELASKESLYRQSEEKNRQLQERLDDAKQKLQQTLQRAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQRERMNDEHNKRLSDTVDKLLSESNERLQLHLKERMAALEEKNALSEELANMKKIQDDLLANKDQLIAELERLQLELDQLRGRPGSSYSRSLPGSALELRYSQGGGSLPAGSTTHLEHYGNTGTGGVVRRTHRGRWSGAREDASKYGDWESGALLGSGFEGGVEDRCSDDEEDRETLFGSELLSPSGQTDVQTLAIMLQEQLEAINKEIKLIQEEKESTELRAEEIESRVSSVALDGPPIPPTSLGRDSTGRGFIPPSLTSSTLASPSPPSSGHSTPRLPHSPARETDRQNNKEDDRSLALLDSTPPPTPRALRLDRMTHTHPGALLDDSREFRSLSADGSSSNSSQDSLHKASKKKSIKSSIGRLFGKKDKVRMGQPGRESTSLASTPSDDLGTVDPLGLTKMAGPVDKDRRSKKKHELLEEACRQGLPFASWDGPTVVSWLELWVGMPAWYVAACRANVKSGAIMANLSDTEIQREIGISNPLHRLKLRLAIQEMVSLTSPSAPASTRSSTSNVWMTHAEMESLTAATKPELKEISWDQILAYGDMNHEWVGNDWLPSLGLPQYRSYFMESLVDARMLDHLTKKELRGQLKMVDSFHRVSMHYGIMCLKRLNYDRKELERRRDESQHQNKDVMVWSNERVMCWVQSIGLKEYADNLTESGVHGALLALDDTFDYTDLALLLQIPNQNTQARQLLEKEYNSLISMGTERRPDEDGTKTFTRSPSWRKMFREKDLRGVTSDSSETLPANFRASAISTPSVTLRKVQSDASPRAESGSVRTYSC
Protein: 14-3-3-like protein, putative (Q383X6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Protein DPCD
- Uncharacterized protein
- Small GTPase, putative
- Prohibitin
- SH3 domain protein, conserved
- 1-phosphatidylinositol 4-kinase
- uracil phosphoribosyltransferase
- Rab GDP dissociation inhibitor
Sequence:
MTDCIKWYNAVLLDEVVPKKNLSEFKLPDATKDLVFMAKLTEEAERYDEMVQCMRKLVKMNSELDTEERNLLSMAYKNVIGSRRNAWRIITSIENRESTKEKSDNMELIVSLRREFEAELAAVCDDLLSLLDTYLIPASQGGEAKVFYLKMKGDYHRYYAEIAPEGDQRQLALDAYAKATEVANSSLAPTHPIRLGLALNFSVFYYEIMKEHEKGFHLARQAYDEAVTELETLDDEAYRESNLIVRLLRDNLNLWTDEQPVN
Protein: Neuropeptide Y receptor type 2 (NPY2-R) (NPY-Y2 receptor) (Y2 receptor) (P97295)
Organism: Mus musculus (Mouse)
Function: Receptor for neuropeptide Y and peptide YY.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Peptide YY
- Pro-neuropeptide Y
- Pancreatic polypeptide prohormone
- Somatotropin
- Amelogenin, X isoform
- Peripherin-2
- Pro-opiomelanocortin
- Appetite-regulating hormone
- Somatostatin
- Glucagon-like peptide 1 receptor
Sequence:
MGPVGAEADENQTVEVKVEPYGPGHTTPRGELPPDPEPELIDSTKLVEVQVILILAYCSIILLGVVGNSLVIHVVIKFKSMRTVTNFFIANLAVADLLVNTLCLPFTLTYTLMGEWKMGPVLCHLVPYAQGLAVQVSTITLTVIALDRHRCIVYHLESKISKRISFLIIGLAWGISALLASPLAIFREYSLIEIIPDFEIVACTEKWPGEEKSVYGTVYSLSTLLILYVLPLGIISFSYTRIWSKLRNHVSPGAASDHYHQRRHKMTKMLVCVVVVFAVSWLPLHAFQLAVDIDSHVLDLKEYKLIFTVFHIIAMCSTFANPLLYGWMNSNYRKAFLSAFRCEQRLDAIHSEVSMTFKAKKNLEVKKNNGPTDSFSEATNV
Protein: PAN2-PAN3 deadenylation complex subunit PAN3 (PAB1P-dependent poly(A)-specific ribonuclease) (Poly(A)-nuclease deadenylation complex subunit 3) (PAN deadenylation complex subunit 3) (Q95RR8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein (PABP). PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and PABP, and to miRNA targets via its interaction with GW182 family proteins.
Subcellular location: Cytoplasm, P-body {ECO:0000255|HAMAP-Rule:MF_03181}.
Interaction partners:
- PAN2-PAN3 deadenylation complex catalytic subunit PAN2
- Polyadenylate-binding protein
- Protein Gawky
- poly
- 5'-3' exoribonuclease 1
- poly
- GH03795p
- Protein painting of fourth
- Nipped-B protein
- FI18136p1
Sequence:
MCSTYGLLSFEFSDTAAMDPIFFSPTNGIPSESKLATYMNRQNVATPSGYGLNNGFSLLNLDSPLNKKSQVTPQSPEFIPTRLGSTPNFYAPYHNAPMQLSNGLNGVNGLTAAAAAAAAAAAAAAAAVPSSTSSASSASVTISKTANGGASMLALQKTASIASVTIAQQQPQHPQKQQQHPPSVGGGAVSAASAPIAISGAPPNPAAAPFVSSMSAQTPLKGRGAMMRQESPTAAMISGAGPGEKSPPHGMTPHGASPIPSALPTSVHQENVGGTIYFYPTANAQNSQPVVNSMVVDGTHPALHGVSAVAPMSAGVPAAMMYTGHVYPGPSSNVVTMQPKTLLESAFFMPDEMRAEVLARNEISNLIMDAAEAAQHALPLEVENYHALYPLEPPAQPLHAKLTFPATTYRATHNTTGYKYCLRRIHGFRLQSTKCMTLVEMWKKLQHTNVVQLREVFTTKAFGDNSLVLVYDYHPGSQTLLAKYFTPAPETNGYTDPFQGEARPFSHKSNMQRTSNGPLLPEATIWSIIMQLTAGLKAIHHAGLACKVLDPTKIIVTGKRVRFSSCCISDITQFDPNASNPLALVNMHQQDDLTALGRLVLALACRCLQSVQRDNVQSSIDMVTRNYSTDLRNFIVYLFTTNNRRSVTDLMPMIGARFYTQLDALQSKIDMQEDELAKEMENGRLYRILVKLNSINERPDFNLDCTWSETGDRYMLKLFRDYLFHSVTEDGRPWLDHAHIVQCLNKLDAGSIERVQLMSRDEQSVLIVSYAELKNCLENAFSELMSSAAN
Protein: Transient receptor potential cation channel, subfamily C, member 7 (A0A8I6GIE6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLGSNTFKNMQRRHTTLREKGRRQAIRGPAYMFNEKGTSLTPEEERFLDSAEYGNIPVVRKMLEESKTLNFNCVDYMGQNALQLAVGNEHLEVTELLLKKENLARVGDALLLAISKGYVRIVEAILSHPAFAQGQRLTLSPLEQELRDDDFYAYDEDGTRFSHDITPIILAAHCQEYEIVHILLLKGARIERPHDYFCKCNECTEKQRKDSFSHSRSRMNAYKGLASAAYLSLSSEDPVLTALELSNELARLANIETEFKNDYRKLSMQCKDFVVGVLDLCRDTEEVEAILNGDVNLQVWSDHHRPSLSRIKLAIKYEVKKLGRTLRSPFMKFVAHAVSFTIFLGLLVVNASDRFEGVKTLPNETFTDYPKQIFRVKTTQFSWTEMLIMKWVLGMIWSECKEIWEEGPREYVLHLWNLLDFGMLSVFVASFTARFMAFLKASEAQLYVDQYVQDVTLHNVSLPPEVAYFTYARDKWWPSDPQIISEGLYAIAVVLSFSRIAYILPANESFGPLQISLGRTVKDIFKFMVIFIMVFVAFMIGMFNLYSYYRGAKYNPAFTTVEESFKTLFWSIFGLSEVISVVLKYDHKFIENIGYVLYGVYNVTMVVVLLNMLIAMINNSYQEIEEDADVEWKFARAKLWLSYFDEGRTLPAPFNLVPSPKSFYYLIMRIKMCLIKLCKSKAKRCENDLEMGMLNSKFRKTRYQAGMRNSENLTANSTFSKPTRYQKIMKRLIKRYVLKAQVDRENDEVNEGELKEIKQDISSLRYELLEEKSQATGELADLIQQLSEKFGKNLNKDHLRVNKGKDI
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1B (Ribophorin IB) (RPN-IB) (Ribophorin-1B) (Q9ZUA0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
- Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3B
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD2
- Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3A
- Dol-P-Glc:Glc
- SecY protein transport family protein
Sequence:
MAARIGIFSVFVAVLLSISAFSSAQDLQIVNAERRIDLSSHIVKAFLTLKVENIGKDPAAEMLLAFPPTQIKNLAMVQALATTGKKKKKTYLPLDVKPTEQPDAPNDTGYYRVTFISPLGPGETVSLEVLYILTHSLEPFPVEITQSESQLVYYHDSAVILSPYHVKQQTTFIKTPSTRVESFTSIEPANRAGKEIKYGPYENRASYSYTPVIIHFENNSPFAVVEELVREIEISHWGSLQITENYRLTHGGARHKGVFSRVDYQSKRSVSGASSFNALLAVLPPRVNSVYYRDEIGNISTSHLRTGFRKSELEFEPRYPLFGGWSATFIIGYRVPLEDYLFEASDGRRYLNFTFGCPLVETIVNKLTIKVVLPEGSKDPSAVLPFTVNQELQVKYSYLDIVGRTVVVLQKDNVVPTHNVPFQVYYTFKPIYMLAEPFMLVSAFFLVFVASLAYVHIDLNIVRK
Protein: Evasin P1104 (A0A090XA85)
Organism: Ixodes ricinus (Common tick) (Acarus ricinus)
Function: Salivary chemokine-binding protein which binds to host chemokines CXCL1, CXCL2, CXCL3, CXCL5, CXCL6, CXCL12 and CXCL13.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MASNLFTIFQLAGFVAIVFIVNLHSVSAESKEASASQGPGKSFKVEFCETNCTENNGVWSGCTGDCICVSVGDSKEGRCMDLGDKVIDTPVAQG
Protein: Golgi SNAP receptor complex member 1 (28 kDa Golgi SNARE protein) (28 kDa cis-Golgi SNARE p28) (GOS-28) (O95249)
Organism: Homo sapiens (Human)
Function: Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor. May play a protective role against hydrogen peroxide induced cytotoxicity under glutathione depleted conditions in neuronal cells by regulating the intracellular ROS levels via inhibition of p38 MAPK (MAPK11, MAPK12, MAPK13 and MAPK14). Participates in docking and fusion stage of ER to cis-Golgi transport. Plays an important physiological role in VLDL-transport vesicle-Golgi fusion and thus in VLDL delivery to the hepatic cis-Golgi.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:15215310, ECO:0000269|PubMed:15728195, ECO:0000269|PubMed:17274796, ECO:0000269|PubMed:17337506, ECO:0000269|PubMed:21669198}; Single-pass type IV membrane protein {ECO:0000269|PubMed:15215310, ECO:0000269|PubMed:15728195, ECO:0000269|PubMed:17274796, ECO:0000269|PubMed:17337506, ECO:0000269|PubMed:21669198}. Note=Localizes throughout the Golgi apparatus, with lowest levels in the trans-Golgi network (By similarity). Enriched on vesicular components at the terminal rims of the Golgi. Found in Golgi microtubules at low temperature (15 degrees Celsius). {ECO:0000250}.
Interaction partners:
- Synaptobrevin homolog YKT6
- Golgi SNAP receptor complex member 2
- Syntaxin-5
- BET1-like protein
- BET1 homolog
- Sec1 family domain-containing protein 1
- Vesicle-trafficking protein SEC22b
- General vesicular transport factor p115
- Golgin subfamily B member 1
- Vesicle-associated membrane protein 8
Sequence:
MAAGTSSYWEDLRKQARQLENELDLKLVSFSKLCTSYSHSSTRDGRRDRYSSDTTPLLNGSSQDRMFETMAIEIEQLLARLTGVNDKMAEYTNSAGVPSLNAALMHTLQRHRDILQDYTHEFHKTKANFMAIRERENLMGSVRKDIESYKSGSGVNNRRTELFLKEHDHLRNSDRLIEETISIAMATKENMTSQRGMLKSIHSKMNTLANRFPAVNSLIQRINLRKRRDSLILGGVIGICTILLLLYAFH
Protein: Respiratory burst oxidase homolog protein B (EC 1.11.1.-) (EC 1.6.3.-) (NADPH oxidase RBOHB) (StRBOHB) (Q948T9)
Organism: Solanum tuberosum (Potato)
Function: Calcium-dependent NADPH oxidase that generates superoxide. Involved in the massive phase II oxidative burst induced by pathogen infection.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16551687}; Multi-pass membrane protein {ECO:0000269|PubMed:16551687}.
Interaction partners:
- Calcium-dependent protein kinase 5
- Calcium-dependent protein kinase 4
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
Sequence:
MEIENTRDSDSMRGSRVGFSGSLVSGKKSARFKDDESYVEITLDVRDDSVSVQNIKGADHEAALLASRLEKRPNNTLGSQLSFHLRQVSKELKRMTSSNKFQKIDRSKSGAARALRGLQFMNKNVGTEGWSEVESRFDQLAVNGMLTKSLFGQCIGMKESSEFAEELFDALARKRCITSPAVTKDELREFWEQITDTSFDARLQTFFDMVDKDADGRITQEEVKEIISLSASANKLSKIQDNSDEYAALIMEELDPGNVGYIELYNLETLLLQAPSHSMNLSTNSRVLSRMLSQKLKPTKERNPFKRCKRRLDYFIEDNWKRIWVMALWLSICAGLFTWKFIQYKRRAVFDVMGYCVSVAKGGAETTKFNMALVLLPVCRNTITWLRSRTKLGKIIPFDDNINFHKVIAFGIAVGVGLHAISHLTCDFPRLLHATDEEYEPMKPFFGDERPNNYWWFVKGTEGWTGVVMVVLMIIAYVLAQPWFRRNRLNLPSTIKKLTGFNAFWYSHHLFVIVYVLFIIHGYFLYLSKKWYKKTTWMYIAVPMILYACERLLRAFRSGYKAVKILKVAVYPGNVMAVHMSKPQGFKYTSGQYIFVNCSDVSSFQWHPFTISSAPGDDYLSMHIRTLGDWTSQLKTLFSKVCEPPTGDQSGLLRADVAKADYKPRLPKLLIDGPYGAPAQDYKKYDVVLLVGLGIGATPLISIVKDVLNNIKQQKNIEDGTKGSKRSPFATKRAYFYWVTREQGSFEWFKGVMDEVSENDQEGLIELHNYCTSVYEEGDARSALITMLQSIQQAKSGVDIVSGTRVKTHFARPNWRQVFKRVTINHPDQRIGVFYCGPQGLVGELRHLSQDFSHKTGTKFEFHKENF
Protein: PDZ and LIM domain protein 3 (Alpha-actinin-associated LIM protein) (Q9PU47)
Organism: Gallus gallus (Chicken)
Function: May play a role in the organization of actin filament arrays within muscle cells.
Subcellular location: Note=Isoform 1 colocalizes with alpha-actinin along actin stress fibers and lammellipodia of spreading fibroblasts. Isoform 2 colocalizes with alpha-actinin at the Z-lines of myotubes. {ECO:0000269|PubMed:10506181}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton. Cell projection, lamellipodium. Note=Isoform 1 colocalizes with alpha-actinin along actin stress fibers and lammellipodia of spreading fibroblasts.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere, Z line. Note=Isoform 2 colocalizes with alpha-actinin at the Z-lines of myotubes.
Interaction partners:
Sequence:
MPQNVILPGPAPWGFRLSGGIDFNQPLIITRITPGSKASTANLCPGDIIVAINGLSTENMTHNDAQERIKAAAHQLSLRIERAETKLWSPQVSEDGKANPYKINLEAEPQEFKPIGTAHNRRAQPFVAAANIDDKRQVVSSSYNSPIGLYSSGNIQDALHGQLRSLIPNASQNDPAPAAVPQSDVYRMLHSNQEEPSQPRQSGSFKVLQNLVSEEDGRPVGTRSVKAPVTKIPTGLPGAQKVPQCDKCGSGILGTVVKARDKYRHPECFVCSDCNLNLKQKGYFFVEGQLYCEAHARARMRPPEGYEAVTVYPKC
Protein: Cell wall synthesis protein KRE9 (Killer toxin resistant protein 9) (P39005)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in cell wall beta(1->6) glucan synthesis.
Subcellular location: Secreted, cell wall {ECO:0000305}.
Interaction partners:
- Beta-glucan synthesis-associated protein KRE6
- Protein KRE1
- Killer toxin-resistance protein 5
- Beta-glucan synthesis-associated protein SKN1
- Protein ROT1
- Trafficking protein particle complex II-specific subunit 65
- Protein BIG1
- Transcription factor SKN7
- Ras modification protein ERF4
Sequence:
MRLQRNSIICALVFLVSFVLGDVNIVSPSSKATFSPSGGTVSVPVEWMDNGAYPSLSKISTFTFSLCTGPNNNIDCVAVLASKITPSELTQDDKVYSYTAEFASTLTGNGQYYIQVFAQVDGQGYTIHYTPRFQLTSMGGVTAYTYSATTEPTPQTSIQTTTTNNAQATTIDSRSFTVPYTKQTGTSRFAPMQMQPNTKVTATTWTRKFATSAVTYYSTFGSLPEQATTITPGWSYTISSGVNYATPASMPSDNGGWYKPSKRLSLSARKINMRKV
Protein: Proenkephalin-B (Beta-neoendorphin-dynorphin) (Preprodynorphin) [Cleaved into: Alpha-neoendorphin; Beta-neoendorphin; Big dynorphin (Big Dyn); Dynorphin A(1-17) (Dyn-A17) (Dynorphin A); Dynorphin A(1-13); Dynorphin A(1-8); Leu-enkephalin; Rimorphin (Dynorphin B) (Dyn-B) (Dynorphin B(1-13)); Leumorphin (Dynorphin B-29)] (P06300)
Organism: Rattus norvegicus (Rat)
Function: Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Pro-opiomelanocortin
- Kappa-type opioid receptor
- Mu-type opioid receptor
- Delta-type opioid receptor
- Nociceptin receptor
- Glutamate receptor ionotropic, NMDA 2B
- Proenkephalin-A
- Glutamate receptor ionotropic, NMDA 2A
- Glutamate receptor ionotropic, NMDA 3A
- Glutamate receptor ionotropic, NMDA 2D
Sequence:
MAWSRLMLAACLLVIPSEVAADCLSLCSLCAVRTQDGPHPINPLICSLECQDLVPPSEEWETCRGFWSFLTLTASGLHGKDDLENEVALEEGYTALTKLLEPLLKELEKGQLLTSVSEEKLRGLSSRFGNGRESELLGTDLMNDEAAQAGTLHFNEEDLRKQAKRYGGFLRKYPKRSSEMTGDEDRGQDGDQVGHEDLYKRYGGFLRRIRPKLKWDNQKRYGGFLRRQFKVVTRSQENPNTYSEDLDV
Protein: Coproporphyrinogen-III oxidase 1, chloroplastic (AtCPO-I) (Coprogen oxidase) (Coproporphyrinogenase) (EC 1.3.3.3) (Protein LESION INITIATION 2) (Q9LR75)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Key enzyme in heme biosynthesis. Catalyzes the oxidative decarboxylation of propionic acid side chains of rings A and B of coproporphyrinogen III.
Subcellular location: Plastid, chloroplast {ECO:0000269|Ref.2}. Plastid {ECO:0000269|Ref.2}.
Interaction partners:
- Uroporphyrinogen decarboxylase 1, chloroplastic
- Uroporphyrinogen decarboxylase 2, chloroplastic
- Protoporphyrinogen oxidase 2, chloroplastic/mitochondrial
- Protoporphyrinogen oxidase 1, chloroplastic
- Porphobilinogen deaminase, chloroplastic
- Magnesium protoporphyrin IX methyltransferase, chloroplastic
- Uroporphyrinogen-III synthase, chloroplastic
- Glutamate-1-semialdehyde 2,1-aminomutase 2, chloroplastic
- Glutamyl-tRNA reductase 1, chloroplastic
- Glutamate-1-semialdehyde 2,1-aminomutase 1, chloroplastic
Sequence:
MASHSSTLLSSPTFAPFSSHRLHYSPNPSTLRFSRPIRNKPNLALRCSVSIEKEVPETERPFTFLRDSDDVTPSSSSSSVRARFETMIRAAQDSVCDAIEAIEGGPKFKEDVWSRPGGGGGISRVLQDGNVFEKAGVNVSVVYGVMPPEAYRAAKGSASDQKPGPVPFFAAGVSSVLHPKNPFAPTLHFNYRYFETDAPKDVPGAPRQWWFGGGTDFTPAYIFEEDVKHFHSIQKQACDKFDPSFYPRFKKWCDDYFYIKHRDERRGLGGIFFDDLNDYDQEMLLSFATECANSVVPAYIPIVEKRKDMEFTEQHKAWQQLRRGRYVEFNLVYDRGTTFGLKTGGRIESILVSLPLSARWEYDHKPEEGTEEWKLLDACINPKEWI
Protein: Probable coatomer subunit beta' (Beta'-coat protein) (Beta'-COP) (Q20168)
Organism: Caenorhabditis elegans
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}.
Interaction partners:
- Probable coatomer subunit delta
- Coatomer subunit epsilon
- Probable coatomer subunit gamma
- Coatomer subunit alpha
- Coatomer subunit beta
- Probable coatomer subunit zeta
- Uncharacterized protein F07F6.4
- ADP-ribosylation factor 1-like 2
- WD_REPEATS_REGION domain-containing protein
- Nuclear envelope integral membrane protein
Sequence:
MPLRLDVKRKLLARSDRVKCVDLHPVETWLLAALYNGNVHIWNYETQTLVKSFEVCDVPVRAAKFVPRKSWVVTGSDDMHIRVFNYNTLERVHQFEAHSDYLRSLVVHPTLPYVISSSDDMLVKMWDWDNKWAMKQSFEGHTHYVMQIAINPKDNNTFATASLDKTVKVWQFGSNVPNFTLEGHEKGVNCVDYYHGGEKPYIISGADDHLVKIWDYQNKTCVQTLDGHAQNVSSVCFHPELPLIITGSEDSTVRLWHANTYRLETTLNYGLERVWCIQAQKGANTIAIGYDEGSVTLKLGREEPAVSMDSSGKILWAKHSEIQQANLKTISTEESEAIQDGERLPLSVKDLGSSEIYPQTLAHSSNGRFVVACGDGEYIVYTAMALRNKDFGQGLEFVWAVDPNMFAVRESATNVKIKKNFKDHKSIRSDMVLEGISGGPLLALRSNNSLCFFDWESAVLVRRIEITSKSIYWSDNGEMVAICGDDSFYVLKYSAEAVANATEVTEDGIEDAFEVIGEQAEAVKTGFWIGDCFIFTTALNRINYYVGGEIVTIAHVDRPLYLLGYMAKESRVYAVDKDLNVISYKLLLSVLEYQTAVMRRDFDTADKVLTTIPKEQRTRVAHFLEKQGFKKQALAVSQDPDHKFDLSVALGDLKTAYDLALQSDSEEKWKALSNAATLKSELLLAGECLGRARDFGGLMLLATCAGSAPLLQKLADDSAAAESHNISFLSSLLLGDIDACLDKLISTGRLPEAAFLARTHAPSRVSSILELWKAKASGHSEKSSRKIGESLADPVKYENLFPGFTQSLKAESFVREISKIPVPASVRVPSAATRNIQEELDEAVASGAVSFTDDGQAVLKNAPRQTETQLKAPPPPSVARQPSPVRQPSPIREPSPIREPEPEEEEEQEEFDDDQQEVHVPANQESADAHGTSKTPDVVLETSRPDIVPPRGSAAPDLVSASSQQSAQDFQDDTQWSDEDFGDAENGDLNMDDLNLDEED
Protein: Run domain Beclin-1-interacting and cysteine-rich domain-containing protein (Rubicon) (Beclin-1 associated RUN domain containing protein) (Baron) (Q92622)
Organism: Homo sapiens (Human)
Function: Inhibits PIK3C3 activity; under basal conditions negatively regulates PI3K complex II (PI3KC3-C2) function in autophagy. Negatively regulates endosome maturation and degradative endocytic trafficking and impairs autophagosome maturation process. Can sequester UVRAG from association with a class C Vps complex (possibly the HOPS complex) and negatively regulates Rab7 activation.
Subcellular location: Late endosome {ECO:0000269|PubMed:19270696}. Lysosome {ECO:0000269|PubMed:19270696}. Early endosome {ECO:0000269|PubMed:19270696, ECO:0000269|PubMed:20974968}. Note=Predominantly located in late endosomes/lysosomes, only partially detected in early endosome and not at all in the Golgi apparatus.
Interaction partners:
- Beclin-1
- UV radiation resistance-associated gene protein
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Phosphoinositide 3-kinase regulatory subunit 4
- Beclin 1-associated autophagy-related key regulator
- Ras-related protein Rab-7a
- Activating molecule in BECN1-regulated autophagy protein 1
- Ubiquitin-like modifier-activating enzyme ATG7
- Endophilin-B1
Sequence:
MRPEGAGMELGGGEERLPEESRREHWQLLGNLKTTVEGLVSTNSPNVWSKYGGLERLCRDMQSILYHGLIRDQACRRQTDYWQFVKDIRWLSPHSALHVEKFISVHENDQSSADGASERAVAELWLQHSLQYHCLSAQLRPLLGDRQYIRKFYTDAAFLLSDAHVTAMLQCLEAVEQNNPRLLAQIDASMFARKHESPLLVTKSQSLTALPSSTYTPPNSYAQHSYFGSFSSLHQSVPNNGSERRSTSFPLSGPPRKPQESRGHVSPAEDQTIQAPPVSVSALARDSPLTPNEMSSSTLTSPIEASWVSSQNDSPGDASEGPEYLAIGNLDPRGRTASCQSHSSNAESSSSNLFSSSSSQKPDSAASSLGDQEGGGESQLSSVLRRSSFSEGQTLTVTSGAKKSHIRSHSDTSIASRGAPESCNDKAKLRGPLPYSGQSSEVSTPSSLYMEYEGGRYLCSGEGMFRRPSEGQSLISYLSEQDFGSCADLEKENAHFSISESLIAAIELMKCNMMSQCLEEEEVEEEDSDREIQELKQKIRLRRQQIRTKNLLPMYQEAEHGSFRVTSSSSQFSSRDSAQLSDSGSADEVDEFEIQDADIRRNTASSSKSFVSSQSFSHCFLHSTSAEAVAMGLLKQFEGMQLPAASELEWLVPEHDAPQKLLPIPDSLPISPDDGQHADIYKLRIRVRGNLEWAPPRPQIIFNVHPAPTRKIAVAKQNYRCAGCGIRTDPDYIKRLRYCEYLGKYFCQCCHENAQMAIPSRVLRKWDFSKYYVSNFSKDLLIKIWNDPLFNVQDINSALYRKVKLLNQVRLLRVQLCHMKNMFKTCRLAKELLDSFDTVPGHLTEDLHLYSLNDLTATRKGELGPRLAELTRAGATHVERCMLCQAKGFICEFCQNEDDIIFPFELHKCRTCEECKACYHKACFKSGSCPRCERLQARREALARQSLESYLSDYEEEPAEALALEAAVLEAT
Protein: Alpha-hemoglobin-stabilizing protein (Erythroid differentiation-related factor) (Erythroid-associated factor) (Q9NZD4)
Organism: Homo sapiens (Human)
Function: Acts as a chaperone to prevent the harmful aggregation of alpha-hemoglobin during normal erythroid cell development. Specifically protects free alpha-hemoglobin from precipitation. It is predicted to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12066189}.
Interaction partners:
- Protein 4.2
- Hemoglobin subunit alpha
- Hemoglobin subunit delta
- Hemoglobin subunit beta
- Hemoglobin subunit epsilon
- Hemoglobin subunit theta-1
- 5-aminolevulinate synthase, erythroid-specific, mitochondrial
- Hemoglobin subunit gamma 1
- Krueppel-like factor 1
- Hemoglobin subunit gamma-2
Sequence:
MALLKANKDLISAGLKEFSVLLNQQVFNDPLVSEEDMVTVVEDWMNFYINYYRQQVTGEPQERDKALQELRQELNTLANPFLAKYRDFLKSHELPSHPPPSS
Protein: Annexin D2 (AnnAt2) (Q9XEE2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May mediate regulated, targeted secretion of Golgi-derived vesicles during seedling development.
Subcellular location: Cytoplasm, cytosol. Membrane. Note=translocate from cytosol to membrane in a calcium-dependent manner.
Interaction partners:
- DEAD-box ATP-dependent RNA helicase 37
- DEAD-box ATP-dependent RNA helicase 11
- DEAD-box ATP-dependent RNA helicase 52
Sequence:
MASLKVPSNVPLPEDDAEQLHKAFSGWGTNEKLIISILAHRNAAQRSLIRSVYAATYNEDLLKALDKELSSDFERAVMLWTLDPPERDAYLAKESTKMFTKNNWVLVEIACTRPALELIKVKQAYQARYKKSIEEDVAQHTSGDLRKLLLPLVSTFRYEGDDVNMMLARSEAKILHEKVSEKSYSDDDFIRILTTRSKAQLGATLNHYNNEYGNAINKNLKEESDDNDYMKLLRAVITCLTYPEKHFEKVLRLSINKMGTDEWGLTRVVTTRTEVDMERIKEEYQRRNSIPLDRAIAKDTSGDYEDMLVALLGHGDA