wanglab/gogpt-training-data huggingface dataset:
Protein: MAU2 chromatid cohesion factor homolog (MAU-2) (Cohesin loading complex subunit SCC4 homolog) (Q9D2X5)
Organism: Mus musculus (Mouse)
Function: Plays an important role in the loading of the cohesin complex on to DNA. Forms a heterodim. eric complex (also known as cohesin loading complex) with NIPBL/SCC2 which mediates the loading of the cohesin complex onto chromatin Plays a role in sister chromatid cohesion and normal progression through prometaphase.
Subcellular location: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9Y6X3}. Chromosome {ECO:0000269|PubMed:24287868}. Nucleus {ECO:0000250|UniProtKB:Q9Y6X3}. Note=Binds to chromatin from the end of mitosis until prophase. {ECO:0000250|UniProtKB:Q9Y6X3}.
Interaction partners:
- Nipped-B-like protein
- Wings apart-like protein homolog
- Structural maintenance of chromosomes protein 3
- Sister chromatid cohesion protein PDS5 homolog A
- Sister chromatid cohesion protein PDS5 homolog B
- Cohesin subunit SA-1
- Double-strand-break repair protein rad21 homolog
- Sororin
- Structural maintenance of chromosomes protein 1A
- N-acetyltransferase ESCO2
Sequence:
MAAQAAAAAQAAAAAQAAAAQAAQAEAAESWYLALLGFAEHFRTSSPPKIRLCVHCLQAVFPFKPPQRIEARTHLQLGSVLYHHTKNSEQARSHLEKAWLISQQIPQFEDVKFEAASLLSELYCQENSVDAAKPLLRKAIQISQQTPYWHCRLLFQLAQLHTLEKDLVSACDLLGVGAEYARVVGSEYTRALFLLSKGMLLLMERKLQEVHPLLTLCGQIVENWQGNPIQKESLRVFFLVLQVTHYLDAGQVKSVKPCLKQLQQCIQTISTLHDDEILPSNPADLFHWLPKEHMCVLVYLVTVMHSMQAGYLEKAQKYTDKALMQLEKLKMLDCSPILSSFQVILLEHIIMCRLVTGHKATALQEISQVCQLCQQSPRLFSNHAAQLHTLLGLYCVSVNCMDNAEAQFTTALRLTNHQELWAFIVTNLASVYIREGNRHQEVLYSLLERINPDHSFPVSSHCLRAAAFYVRGLFSFFQGRYNEAKRFLRETLKMSNAEDLNRLTACSLVLLGHIFYVLGNHRESNNMVVPAMQLASKIPDMSVQLWSSALLRDLNKACGNAMDAHEAAQMHQNFSQQLLQDHIEACSLPEHNLITWTDGPPPVQFQAQNGPNTSLASLL
Protein: Checkpoint protein (Q4QBE5)
Organism: Leishmania major
Interaction partners:
- Putative replication factor C, subunit 2
- Putative replication factor C, subunit 4
- Putative replication factor C, subunit 5
- Putative replication factor C, subunit 3
- BRCT domain-containing protein
- separase
- Serine/threonine-protein kinase ATR
- Uncharacterized protein
- Flap endonuclease 1
- non-specific serine/threonine protein kinase
Sequence:
MRFKATLKDAKGLLGVLQVCRSIQRDCIVRLQSERIRFFSNTNAADGVQVWMRCQSSFLFYEMVCDSGYDEHSITCEVLDLAQLIHIVKQAEARERSHQGTTSRVQMRLARNGRYPLWRVAMQGLSGQPDVSFDVPLRILGDREIQSLSPPPLERQHLQILVPDMLELTTFIDKLKNTAADSVTFSARVLMPPTPRRGAEDGEAEDADGGAEVRRGVKRPRDKDALPLASLLIYAEHFMARFSLKYEAVELVEQLEREDGDDDGDDDGGAVDDVRVATVMVETRKFARFFSAVKELDPMKMSMYLVDRRALVLSVFAVGNTAMVAYIPARA
Protein: CSC1-like protein 1 (Transmembrane protein 63A) (Q91YT8)
Organism: Mus musculus (Mouse)
Function: Acts as an osmosensitive calcium-permeable cation channel. Mechanosensitive ion channel that converts mechanical stimuli into a flow of ion.
Subcellular location: Lysosome membrane {ECO:0000250|UniProtKB:O94886}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:O94886}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:27045885, ECO:0000269|PubMed:30382938, ECO:0000269|PubMed:37543036}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MTSSPFLDPWPSKAVFVRERLGLGERPNDSYCYNSAKNSTVLQGVTFGGIPTVLLLDVSCFLFLILVFSIIRRRFWDYGRIALVSEAGSEARFQRLSSSSSGQQDFENELGCCPWLTAIFRLHDDQILEWCGEDAIHYLSFQRHIIFLLVVISFLSLCVILPVNLSGDLLGKDPYSFGRTTIANLQTDNDLLWLHTVFSVIYLFLTVGFMWHHTRSIRYKEESLVRQTLFITGLPREARKETVESHFRDAYPTCEVVDVQLCYSVAKLIYLCKERKKTEKSLTYYTNLQAKTGRRTLINPKPCGQFCCCEVQGCEREDAISYYTRMNDSLLERITAEESRVQDQPLGMAFVTFREKSMATYILKDFNACKCQGLRCKGEPQPSSYSRELCVSKWTVTFASYPEDICWKNLSIQGVRWWLQWLGINFSLFVVLFFLTTPSIIMSTMDKFNVTKPIHALNNPVISQFFPTLLLWSFSALLPSIVYYSTLLESHWTRSGENRIMVSKVYIFLIFMVLILPSLGLTSLDFFFRWLFDKTSSETSIRLECVFLPDQGAFFVNYVIASAFIGSGMELLRLPGLILYTFRMIMAKTAADRRNVKQNQAFEYEFGAMYAWMLCVFTVIMAYSITCPIIVPFGLIYILLKHMVDRHNLYFAYLPAKLEKRIHFAAVNQALAAPILCLFWLFFFSFLRLGLTAPATLFTFLVVLLTILACLLYTCFGCFKHLSPWNYKTEESASDKGSEAEAHVPPPFTPYVPRILNGLASERTALSPQQQQTYGAIRNISGTLPGQPVAQDPSGTAAYAYQES
Protein: 2-carboxy-D-arabinitol-1-phosphatase (EC 3.1.3.63) (W5EP13)
Organism: Triticum aestivum (Wheat)
Function: Phosphoglycerate mutase-like protein lacking PGM activity, but having 2-carboxy-D-arabinitol 1-phosphate (CA1P) phosphatase activity. Can dephosphorylate the closely related compounds 2-carboxy-D-arabinitol 1,5-bisphosphate (CABP) and 2-carboxy-D-ribitol-1,5-bisphosphate(CRBP), and 2,3-diphosphoglycerate. Prevents the accumulation of D-glycero-2,3-pentodiulose-1,5-bisphosphate (PDBP) a potent inhibitor of ribulose-1,5-bisphosphate carboxylase (RuBisCO). PDBP is produced during the oxidation of ribulose-1,5-bisphosphate, the substrate of RuBisCO.
Subcellular location: Plastid, chloroplast stroma {ECO:0000250|UniProtKB:Q9FNJ9}.
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Triosephosphate isomerase
- Triose-phosphate isomerase
- Triosephosphate isomerase
- Triosephosphate isomerase, cytosolic
- Triosephosphate isomerase, cytosolic
- Triosephosphate isomerase, cytosolic
- Triosephosphate isomerase
Sequence:
MLLFAPTPPPSPATAHRRPGGSAASCIRCSSVRELDRSPSRPPLPPLAEAKRVVLVRHGQSTWNADGRIQGSSDFSVLTPKGESQAETSRLMLLADSFDACFTSPLARSRRTAEIIWDTRDKDLIPDYDLREIDLYSFQGLLKHEGKEKYGALFQQWQKNPSDCSIDGHYPVRELWDRAQGCWERILTHEGKSVLVVAHNAVNQALVATSLGLGTEYFRTLLQSNCGASVLDFTPQPGGRPPSVCLNRLNQTPSSPISAESSAGRKSSKRIILVCQGATQSSSEGSLGGVGYAPLNMLGVIQAQKTAELLLDLKVNSIICSPQVAAVDTATAICEVQEAAGCLGADCVPRYVEMKNLLGLEIDDAFLTKQKSLEQIVQSGWMGGMEHQKLKTLWAQSEDAWQALVNELPEDDGAESDRVVVAIGHPAIHLGLLCRCLNLTMDYMPSFHLDDGSISVIDFPDGPKGGGIVRCTNYTAHLGRWSVPITKSTENNDEF
Protein: Protein DETOXIFICATION 31 (AtDTX31) (Multidrug and toxic compound extrusion protein 31) (MATE protein 31) (Protein ROOT HAIR SPECIFIC 2) (Q9LPV4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Positively mediates root hair elongation.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Serine/threonine-protein kinase RHS3
- Probable pectate lyase 16
- Putative methylesterase 15, chloroplastic
- Expansin-A7
- Proline-rich receptor-like protein kinase PERK13
- Putative pectinesterase/pectinesterase inhibitor 24
- Probable LRR receptor-like serine/threonine-protein kinase At4g29180
- Uncharacterized protein
- Phosphatidylinositol/phosphatidylcholine transfer protein SFH1
- Extensin-like protein
Sequence:
MEKDNDFKDPFLASTEEEELDPATQKALMEYLGVGSRASSLVSFSSTAVDIPPISGVGDFVREFRIESRKLWKLAGPAIFTTMSQYSLGAVTQVFAGHISTLALAAVSIENSVIAGFSFGIMLGMGSALETLCGQAFGAGKVSMLGVYLQRSWVILSVTALFLSLIYIFAAPILTFIGQTAAISAMAGIFSIYMIPQIFAYAINFPTAKFLQSQSKIMVMAGISGVVLVIHSFFTWLVMSRLHWGLPGLALVLNTSWWVIVVAQLVYIFNCTCGEAWSGFTWEAFHNLWGFVKLSLASAAMLCLEIWYFMALVLFAGYLKNAEVSVAALSICMNILGWAAMVAFGTNAAVSVRVSNELGASHPRTAKFSLVVAVILSTAIGMFIAAGLLFFRNEYPVLFVEDEEVRNVVRELTPMLAFCIVINNVQPVLSGVAVGAGWQAVVAYVNIACYYLFGVPFGLLLGFKLEYGVMGIWWGMVTGTFVQSIVLTWMICKTNWEKEASMAEERIKEWGGVPAEKETLLN
Protein: cAMP-dependent protein kinase regulatory subunit (cAPK regulatory subunit) (Bypass of cyclase mutations protein 1) (Protein kinase A regulatory subunit) (PKA regulatory subunit) (P07278)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Regulatory subunit of the cyclic AMP-dependent protein kinase (PKA), an effector of the Ras/cAMP pathway. Inhibits PKA activity in the absence of cAMP. cAMP activates PKA and promotes growth and proliferation in response to good nutrient conditions. Together with ZDS1, provides a negative feedback control on the cell wall integrity-signaling pathway by acting as a negative regulator of MAP kinase SLT2/MPK1.
Subcellular location: Cytoplasm. Nucleus. Note=Cytoplasmic when phosphorylated. Nuclear when not phosphorylated.
Interaction partners:
- cAMP-dependent protein kinase type 3
- cAMP-dependent protein kinase type 1
- cAMP-dependent protein kinase type 2
- Thiamine pyrophosphokinase
- Adenylate cyclase
- Ras-like protein 2
- Inhibitory regulator protein IRA2
- Ras-like protein 1
- 3',5'-cyclic-nucleotide phosphodiesterase 2
- Serine/threonine-protein kinase SCH9
Sequence:
MVSSLPKESQAELQLFQNEINAANPSDFLQFSANYFNKRLEQQRAFLKAREPEFKAKNIVLFPEPEESFSRPQSAQSQSRSRSSVMFKSPFVNEDPHSNVFKSGFNLDPHEQDTHQQAQEEQQHTREKTSTPPLPMHFNAQRRTSVSGETLQPNNFDDWTPDHYKEKSEQQLQRLEKSIRNNFLFNKLDSDSKRLVINCLEEKSVPKGATIIKQGDQGDYFYVVEKGTVDFYVNDNKVNSSGPGSSFGELALMYNSPRAATVVATSDCLLWALDRLTFRKILLGSSFKKRLMYDDLLKSMPVLKSLTTYDRAKLADALDTKIYQPGETIIREGDQGENFYLIEYGAVDVSKKGQGVINKLKDHDYFGEVALLNDLPRQATVTATKRTKVATLGKSGFQRLLGPAVDVLKLNDPTRH
Protein: Mannan endo-1,4-beta-mannosidase C (EC 3.2.1.78) (Endo-beta-1,4-mannanase C) (Q5AZ53)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Endo-1,4-mannanase that catalyzes the random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans and heteromannans. It is a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Active against locust bean gum and gum guar. Also has transglycosylation activity. Produces mainly mannopentaose and mannohexaose out of mannotetraose.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q99036}.
Interaction partners:
- Mannan endo-1,4-beta-mannosidase A
- Mannan endo-1,4-beta-mannosidase D
- Phosphotransferase
- Hexokinase
- Phosphotransferase
- GH26 domain-containing protein
- Uncharacterized protein
- Probable mannan endo-1,4-beta-mannosidase E
Sequence:
MIFSTLLSLALLATTATARKGFVTTKGDKFQLDGKDFYFAGSNAYYFPFNNNQTDVELGLSAAKKAGLLVFRTWGFNDKNVTYIEDGLPQYGGEGAGTTEVVFQWWQNGTSTIDLEPFDKVVNAAAKTGIKLIVTLVNNWADYGGMDVYTVNLGGQYHDDFYRLPQIKKAYKRYVKEMVTRYRNSPAIMAWELANEPRCGADGVRNLPASDECTPELLTSWIDEMSTYVKRLDPHHLVTWGGEGGFNYDSDDWAYNGSDGGDFEAELKLKNIDFGVFHSYPDWWSKTVEWTNKWIVDHARAARRVGKPVVHEEYGWLTPQGRLDNLGTVSNITRLEAVGGWQSISLREKMSDMFWQFGYSGYSYGRNHDDGFTIYLDDAEAQELVYKHAKEVNKLNRRR
Protein: FACT complex subunit POB3 (Facilitates chromatin transcription complex subunit POB3) (Q04636)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. Transcription elongation is promoted by the repression of transcription initiation from cryptic sites. Also acts in establishing transcription initiation complexes and promotes SPT15/TBP-binding to a TATA box. Together with replication factor-A protein (RPA), FACT may play a role in nucleosome deposition during DNA replication.
Subcellular location: Nucleus {ECO:0000269|PubMed:10413469}. Chromosome {ECO:0000269|PubMed:10413469, ECO:0000269|PubMed:14585989}. Note=Colocalizes with RNA polymerase II on chromatin (PubMed:10413469, PubMed:14585989, PubMed:14739930). Recruited to actively transcribed loci (PubMed:14585989). Associates with the coding region of HTA1 (PubMed:19683497). {ECO:0000269|PubMed:10413469, ECO:0000269|PubMed:14585989, ECO:0000269|PubMed:14739930, ECO:0000269|PubMed:19683497}.
Interaction partners:
- Transcription elongation factor SPT6
- RNA polymerase-associated protein RTF1
- Histone H3
- Transcription elongation factor SPT5
- RNA polymerase II-associated protein 1
- Cell division control protein 73
- Histone H4
- RNA polymerase-associated protein LEO1
- RNA polymerase-associated protein CTR9
- FACT complex subunit SPT16
Sequence:
MSTDFDRIYLNQSKFSGRFRIADSGLGWKISTSGGSAANQARKPFLLPATELSTVQWSRGCRGYDLKINTKNQGVIQLDGFSQDDYNLIKNDFHRRFNIQVEQREHSLRGWNWGKTDLARNEMVFALNGKPTFEIPYARINNTNLTSKNEVGIEFNIQDEEYQPAGDELVEMRFYIPGVIQTNVDENMTKKEESSNEVVPKKEDGAEGEDVQMAVEEKSMAEAFYEELKEKADIGEVAGDAIVSFQDVFFTTPRGRYDIDIYKNSIRLRGKTYEYKLQHRQIQRIVSLPKADDIHHLLVLAIEPPLRQGQTTYPFLVLQFQKDEETEVQLNLEDEDYEENYKDKLKKQYDAKTHIVLSHVLKGLTDRRVIVPGEYKSKYDQCAVSCSFKANEGYLYPLDNAFFFLTKPTLYIPFSDVSMVNISRAGQTSTSSRTFDLEVVLRSNRGSTTFANISKEEQQLLEQFLKSKNLRVKNEDREVQERLQTALGSDSDEEDINMGSAGEDDESVDEDFQVSSDNDADEVAEEFDSDAALSDAEGGSDEERPSKKPKVE
Protein: SCP domain-containing protein (H2L058)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MNYLLTALIALLAPISVAYNVPHGFLTGEAVTSHSGPNDLDGELPATDEVKREKRGYFFPSHFQSDSGLLSRSEHPNEYLKKWITHEHNRYRRMVPASDMNMLYWSDELAASAQRHADTCDFRHSRGRINVGENIWAAPYSNYSDAISIWFNEVHNPRCGCNHAYKHCCGHYVQVVWAKTNLVGCGFSRCRDVQGVWGRGHRNVFVCHYNPQGNTMPAFTWASGDNGKCSNCPANAPACYQGLCYMPKNYEAPTTTTESTTTSTTTEEPTTTCEPDEPEAEGADNNQEEEEENNDGFRMRV
Protein: Uncharacterized protein (G8BEL8)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
Sequence:
MHLTQLSLSICLVAVAFAQVVLSQESHTLPKFKSSSKYFDQSDTNVPTSNVNYTHNFGLKNDYSWNDVLEQLDENNKLFFIIRHAAGVHQCNTPSTDWTCYWQTLDGYGGQVWADALLTQEGVDQCRELSQQINNTKEFPYPNRYYSSPLRRTLQTWHYVWRDLVSDAPTIKEFARETYGIQTESKRHPKSYIQANWEYVNFEDGFTEKDELWSNSSRETSQHRKYRAASVLTDIFEASKSDKVVSLVSHSELIGSILDVVGHRDYPVENAKLIPVLIHKKKHKTKTYKLDDPDKTFEDICSDKPSQITQGPELTCSAAPFDERA
Protein: Protein bunched, class 1/class 3/D/E isoforms (Protein shortsighted) (Q24522)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable transcription factor required for peripheral nervous system morphogenesis, eye development and oogenesis. May be required for the transmission of the dpp signal and for a morphogenetic movement of the medulla in the brain that reorients the second optic lobe relative to the first. Plays a role in determining proper dorsal cell fates leading to the formation of the dorsal appendages.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:7555710}. Nucleus {ECO:0000269|PubMed:7555710}.
Interaction partners:
Sequence:
MKTETGSNNNNTTVVNMDFDMYPSISGKQQDPVREVVMKYIDYFLPDASGTSAVAIDNKIEQAMDLVKSHLMIAVREEVEVLKERISELMDKINKLELENSILKSNIPQETLQQLQLQLQLAAPPATPAIQAAPAVQSVVAPAAAGQAVQQQAAGAVAVTGVATSPASAVVPTSIPNGSAENGSSAVESAAVSVEQQVQQVTSAAAAAASVVTANGPMS
Protein: Neuronal vesicle trafficking-associated protein 2 (Neuron-specific protein family member 2) (Protein p19) (Hmp19) (Q9Y328)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q3KR51}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q3KR51}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q3KR51}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q3KR51}. Endosome membrane {ECO:0000250|UniProtKB:Q3KR51}. Early endosome membrane {ECO:0000250|UniProtKB:Q3KR51}. Late endosome membrane {ECO:0000250|UniProtKB:Q3KR51}. Lysosome lumen {ECO:0000250|UniProtKB:Q3KR51}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P47759}. Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:P47759}. Endosome, multivesicular body membrane {ECO:0000250|UniProtKB:P47759}. Note=Endocytosed from the cell surface, thus entered into early endosomes, trafficks to late endosomes and degradates in lysosomes (By similarity). Mainly Golgi stack, but also found in small vacuolar organelles and multivesicular bodies. Found in both stationary and motile endosomes (By similarity). {ECO:0000250|UniProtKB:P47759, ECO:0000250|UniProtKB:Q3KR51}.
Interaction partners:
Sequence:
MVKLNSNPSEKGTKPPSVEDGFQTVPLITPLEVNHLQLPAPEKVIVKTRTEYQPEQKNKGKFRVPKIAEFTVTILVSLALAFLACIVFLVVYKAFTYDHSCPEGFVYKHKRCIPASLDAYYSSQDPNSRSRFYTVISHYSVAKQSTARAIGPWLSAAAVIHEPKPPKTQGH
Protein: CREB homolog crh-1 (Cyclic AMP responsive element binding protein crh-1) (Q9U2I0)
Organism: Caenorhabditis elegans
Function: Transcription factor. Transcriptional activity probably positively regulated by phosphorylation. Modulates expression of target genes, acting by binding to regulatory cAMP response elements (CRE). Acts downstream of the calcium-triggered CaMKK-CaMK1 signaling cascade, consisting of the protein kinase kinase ckk-1 and the protein kinase cmk-1. Plays a role in learning and memory, feeding behavior, stress response, entry into the dauer stage and modulation of lifespan. Involved in commitment to the developmentally arrested larval state known as dauer, acting by positively regulating the expression of dauer-inhibiting TGF-beta-like daf-7 in the ASI neurons. Plays a role in both associative and non-associative long-term memory (LTM). Involved in modulating feeding behavior, acting by regulating transcription of tryptophan hydroxylase tph-1 in serotonergic ADF neurons. Regulates transcription of genes involved in endoplasmic reticulum (ER) stress. Involved in modulation of lifespan, in response to raised temperature, but independently of the heat-shock response pathway, acting by regulating transcription of FMRFamide-like neuropeptides flp-6 in the AFD neuron.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00312, ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
Sequence:
MATMASTSNCSPVATSPLMMLLFKALQEGGDSEDEARRRREQLNRRPSYRMILKDLETADKVMKKEPEETPPSSVDASPLQFQSVMRPPPTAPPTSAATPNRILPSSNAASPYGSPLGSSILSNQPLVLPFAPINGDFDFSAAIAAASQPKVFPGGPQQNGLGGGGGGGGVPGPSSGIAGMSVQPPTSSTPSQQQSVQSLEGTSGLIGSAMKPMLGIDAVSFPEFGTTDWQSPMLSGGYSSSPSPTMTGGSMRMGGGPLHGEDESNRKRQVRLLKNREAAKECRRKKKEYVKCLENRVSVLENQNKALIEELKTLKELYCRKEKDGM
Protein: Aquaporin PIP2-6 (Plasma membrane intrinsic protein 2-6) (ZmPIP2-6) (ZmPIP2;6) (Q9ATM5)
Organism: Zea mays (Maize)
Function: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MGKEVDVSTLEAGGVRDRDYADPPPAPLIDIDELGKWSLYRAVIAEFVATLLFLYITVATVIGYKHQTDASASGPDAACSGVGILGIAWAFGGMIFILVYCTAGISGGHINPAVTFGLFLARKVSLVRALLYMAAQSLGAICGVALVKGFQSGFYARYGGGANEVSAGYSTGTGLAAEIIGTFVLVYTVFSATDPKRNARDSHVPVLAPLPIGFAVFMVHLATIPITGTGINPARSLGAAVVYNNSKAWSDQWIFWVGPFIGAAIAALYHQIVLRASARGYGSFRSNA
Protein: RAB23, member RAS oncogene family (Rab23 protein) (Ras-related protein Rab-23 (EC 3.6.5.2)) (Q503R5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MLEEDMEVAIKVVVVGNGAVGKSSMIQRYCKGIFTKDYKKTIGVDFLERQIIVNGEDVRLMLWDTAGQEEFDAITKAYYRGAQACVLVFSTTDRESFEAISSWKEKVEMEVGDIPTVLVQNKIDLLDDTVIKNEEAEGLAKRLKLRFYRTSVKEDLNVNEVFKYLADKYLQRLKQQSAEETDIIHTSSNKIGVFNTTGSGHPNQNSSDLNGREIVNLRPNKQRTKKTKNPFGSCRLL
Protein: Molybdate-binding protein ModA (Molybdate/tungstate-binding protein ModA) (Q8PHA1)
Organism: Xanthomonas axonopodis pv. citri (strain 306)
Function: Part of the ABC transporter complex ModABC involved in the transport of molybdenum into the cell (Probable). Binds molybdate and tungstate with high affinity in vitro.
Interaction partners:
Sequence:
MRMIGFWQRALCVLMLTLPVLASAQTAPVTVFAAASLKESMDEAATAYEKATGTPVRVSYAASSALARQIEQGAPADVFFSADLEWMDYLQQHGLVLPAQRHNLLGNTLVLVAPASSKLRVDPRAPGAIAKALGENGRLAVGQTASVPAGKYAAAALRKLGQWDSVSNRLAESESVRAALMLVSRGEAPLGIVYGSDARADAKVRVVATFPDDSHDAIVYPVAALKNSNNPATAAFVSWLGSKPAKAIFARRGFSLKD
Protein: RNA polymerase sigma factor SigO (O34843)
Organism: Bacillus subtilis (strain 168)
Function: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Together with its coactivator RsoA, positively regulates the expression of at least three operons, including oxdC-yvrL, sigO-rsoA and yvrJ. Required for the acid stress-dependent induction of the oxalate decarboxylase oxdC.
Interaction partners:
- Sigma-O factor regulatory protein RsoA
- Membrane-bound negative regulator YvrL
- Oxalate decarboxylase OxdC
- Negative regulator of flagellin synthesis
- DNA-directed RNA polymerase subunit beta'
- DNA-directed RNA polymerase subunit beta
- Chemotaxis protein CheV
- Flagellar motor switch phosphatase FliY
- Flagellar basal body rod protein FlgB
- Flagellar basal-body rod protein FlgC
Sequence:
MKHPIVKHFLSNPQHYRLFKNVMESPNEKDARSLDELFKQFYKEIRIVKYMNSMIRIFSIDFDKRVRKNQKRYPLTVDHPEAGDRLSSETGSDAFEEFLDRQDDLSQHVQDYQLYQAIQKLTDKQKSVLTKVYLHGATMQEIADSLGESRQNISNIHKKGLENIRKQLAAQKKGEK
Protein: Serine/threonine-protein phosphatase 2B catalytic subunit 3 (EC 3.1.3.16) (Calmodulin-dependent calcineurin A3 subunit) (Q9VXF1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.
Interaction partners:
- Calcineurin subunit B type 1
- Calcineurin subunit B type 2
- Serine/threonine-protein phosphatase 2B catalytic subunit 1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
- Serine/threonine-protein phosphatase 2B catalytic subunit 2
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase classes I and II
- Protein sarah
- Peptidyl-prolyl cis-trans isomerase Fkbp12
- Serine/threonine-protein phosphatase PP2A 65 kDa regulatory subunit
- Serine/threonine-protein phosphatase 4 regulatory subunit 2
Sequence:
MSSPAAQSNSSSSQSQSAAQQQQQQNQKANVNNTHDNKNAAATTGTAAGSGSGGAAGSAGTQQQGQGGTGTSSGPSSPTKRSTISTKERVIDSVAFPPSRKLTCADVFDARTGKPQHDVLKQHFILEGRIEESAALRIIQEGATLLRTEKTMIDIEAPVTVCGDIHGQFYDLMKLFEIGGSPATTKYLFLGDYVDRGYFSIECVLYLWSLKITYPQTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEIHELEDIRRLDRFKEPPAFGPMCDLLWSDPLEDFGNEKNSDFYTHNSVRGCSYFYSYAACCDFLQNNNLLSIIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLNICSDDELMTEESEEPLSDDEAALRKEVIRNKIRAIGKMARVFSVLREESESVLQLKGLTPTGALPLGALSGGKQSLKNAMQGFSPNHKITSFAEAKGLDAVNERMPPRRDATPSPAEEGQKSLSAAAAAAANANANSING
Protein: Uncharacterized protein DKFZp434B061 (Q9UF83)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRRPSTASLTRTPSRASPTRMPSRASLKMTPFRASLTKMESTALLRTLPRASLMRTPTRASLMRTPPRASPTRKPPRASPRTPSRASPTRRLPRASPMGSPHRASPMRTPPRASPTGTPSTASPTGTPSSASPTGTPPRASPTGTPPRAWATRSPSTASLTRTPSRASLTRWPPRASPTRTPPRESPRMSHRASPTRTPPRASPTRRPPRASPTRTPPRESLRTSHRASPTRMPPRASPTRRPPRASPTGSPPRASPMTPPRASPRTPPRASPTTTPSRASLTRTPSWASPTTTPSRASLMKMESTVSITRTPPRASPTGTPSRASPTGTPSRASLTGSPSRASLTGTPSRASLIGTPSRASLIGTPSRASLTGTPPRASLTGTSSTASLTRTPSRASLTRTQSSSSLTRTPSMASLTRTPPRASLTRTPPRASLTRTPPRASLTRTPPRASLTRTPSMVSLKRSPSRASLTRTPSRASLTMTPSRASLTRTPSTASLTGTPPTASLTRTPPTASLTRSPPTASLTRTPSTASLTRMPSTASLTRKSNVNQQCPASTPSSEVIS