wanglab/gogpt-training-data huggingface dataset:
Protein: RNA-binding protein, putative (O77316)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MSIRNRDKNYMSHVNAGKHSMNKVSNNNSNSNISNNNYSLGLYIDNPQKAFLFDENDLKELFSYYKGAHDIRILADKAAAQITFNDKNMIQQVKKDINGLTINDIGTIRCIILNEGKVIEQFLPFSANDPNVTSENDNTVSNNESTVNMLKKLSSLINTNNNNNNNNNINSININNINNVNSNNGNKKWDMNNRINNINNNNINNNNNISNNNNFNQLTNNNKNEQNDNSFANKKLSRIELIDIFGFPNEFDVMNKILGKNNSNINYINEQTNNMVNIELKGKPINEAPVVERMHLSITSDNLNAYKKAIDLIMKLLNSLFQEFVDFCLENNFVLPENLSFKRHEYMYNSDGSTKYLGFKENNYGEKEIYKNDFSYNKKNKNMPKSDNDKRNNNNNNSSFNMNINGAYGNNQNVKNGRF
Protein: Platelet-derived growth factor subunit B (PDGF-2) (Platelet-derived growth factor B chain) (Platelet-derived growth factor beta polypeptide) (B1H0W5)
Organism: Bos taurus (Bovine)
Interaction partners:
- Platelet-derived growth factor receptor beta
- Platelet-derived growth factor receptor alpha
- Platelet-derived growth factor subunit A
- Platelet-derived growth factor C
- Platelet-derived growth factor D
- Vascular endothelial growth factor C
- Insulin-like growth factor 1
- Receptor protein-tyrosine kinase
- Hepatocyte growth factor
- Insulin
Sequence:
MNRCWALFLSLCCYLRLVSAEGDPIPEELYKMLSDHSIRSFDDLQRLLHGDSVDEDGAELDLNLTRSHSGGELESLSRGRRSLGSPTVAAEPAVIAECKTRTEVFEISRRLIDRTNANFLVWPPCVEVQRCSGCCNNRNVQCRPTQVQDRKVQVKKIEIVRKKKIFKKATVTLVDHLACRCETVVARAVTRTPGSSQEQRARTPQTRVTIRTVRVRRPPKGKHRKFKHTHDKTALKETLGA
Protein: Alpha-defensin 3 (Defensin-related cryptdin-3) (P28310)
Organism: Mus musculus (Mouse)
Function: Probably contributes to the antimicrobial barrier function of the small bowel mucosa.
Subcellular location: Secreted.
Interaction partners:
- Alpha-defensin 24
- Alpha-defensin 26
- Defensin, alpha, 5
- Defensin, alpha, 22
Sequence:
MKTLVLLSALVLLAFQVQADPIQNTDEETKTEEQPGEDDQAVSVSFGDPEGSSLQEESLRDLVCYCRKRGCKRRERMNGTCRKGHLMYTLCCR
Protein: Arginase (EC 3.5.3.1) (A0A1X7RC97)
Organism: Caenorhabditis elegans
Interaction partners:
- Probable ornithine aminotransferase, mitochondrial
- PABS domain-containing protein
- Histidine ammonia-lyase
- Ornithine decarboxylase
- Multifunctional protein pyr-1
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- S-adenosylmethionine decarboxylase proenzyme
- Probable fumarate hydratase, mitochondrial
- Mitochondrial glutamate carrier 1
- Proline dehydrogenase 1, mitochondrial
Sequence:
MKKSTQLARQVIRAIGCANGLAGRQLGCENAVEVIKASTYLAGVQTRLPLEWGKIIEEVNTGRHASAMSGVTQTCRQLAHETRQVIENKEELLVFGGDHSCAIGTWSGVATAMRPVGDIGLIWVDAHMDAHTPDTSDTGNIHGMPVAHLLGFGDKTLVKIGDRLPKLLPHNLCMVGIRDYESAEQELLEKLGVRIFYAHEVEKRGIQDVMQEAQYLVTRNTIGYGLSIDLDGFDVSYAPAVGTPSADGINALEFIKALLTIDLTKLIATEIVEFLPRFDDTQRTSEQLVSSLVEYIYKTKQFQINSVNEIAQRVSTSEQSQKITRAM
Protein: E3 ubiquitin-protein ligase DMA1 (EC 2.3.2.27) (Checkpoint forkhead associated with RING domains-containing protein 1) (Defective in mitotic arrest protein 1) (RING-type E3 ubiquitin transferase DMA1) (P38823)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: E3 ubiquitin-protein ligase which functions in cell cycle retarding in conjunction with the UBC4 and UBC13/MMS2 complex, 2 E2 ubiquitin conjugating enzymes. Involved in nutritional control of the cell cycle. Targets the G1 cyclin PCL1 for destruction. Required for proper spindle positioning, likely regulating septin ring deposition at the bud neck.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- E3 ubiquitin-protein ligase DMA2
- Translation initiation factor eIF2 assembly protein
- 2-oxoglutarate dehydrogenase, mitochondrial
- Protein BNI1
- Mitotic check point protein BUB2
- Mitosis inhibitor protein kinase SWE1
- Ubiquitin-conjugating enzyme E2 13
Sequence:
MSTNTVPSSPPNQTPPAASGIATSHDHTKFNNPIRLPISISLTINDTPNNNSNNNSVSNGLGILPSRTATSLVVANNGSANGNVGATAAAAATVETNTAPAVNTTKSIRHFIYPPNQVNQTEFSLDIHLPPNTSLPERIDQSTLKRRMDKHGLFSIRLTPFIDTSSTSVANQGLFFDPIIRTAGAGSQIIIGRYTERVREAISKIPDQYHPVVFKSKVISRTHGCFKVDDQGNWFLKDVKSSSGTFLNHQRLSSASTTSKDYLLHDGDIIQLGMDFRGGTEEIYRCVKMKIELNKSWKLKANAFNKEALSRIKNLQKLTTGLEQEDCSICLNKIKPCQAIFISPCAHSWHFHCVRRLVIMNYPQFMCPNCRTNCDLETTLESESESEFENEDEDEPDIEMDIDMEINNNLGVRLVD
Protein: E3 ubiquitin-protein ligase DZIP3 (EC 2.3.2.27) (DAZ-interacting protein 3) (RING-type E3 ubiquitin transferase DZIP3) (RNA-binding ubiquitin ligase of 138 kDa) (hRUL138) (Q86Y13)
Organism: Homo sapiens (Human)
Function: E3 Ubiquitin ligase proteins mediate ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Able to specifically bind RNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12538761}.
Interaction partners:
- Dehydrogenase/reductase SDR family member 2, mitochondrial
- RNA-binding protein MEX3B
- Ataxin-1
- Snurportin-1
- Deleted in azoospermia protein 1
Sequence:
MDSLPDEFFVRHPAVEDQRKEETENKLEKSSGQLNKQENDIPTDLVPVNLLLEVKKLLNAINTLPKGVVPHIKKFLQEDFSFQTMQREVAANSQNGEEIVPALTLRFLITQLEAALRNIQAGNYTAHQINIGYYLTLLFLYGVALTERGKKEDYTEAENKFLVMKMMIQENEICENFMSLVYFGRGLLRCAQKRYNGGLLEFHKSLQEIGDKNDHWFDIDPTEDEDLPTTFKDLLNNFIKTTESNIMKQTICSYLDCERSCEADILKNTSYKGFFQLMCSKSCCVYFHKICWKKFKNLKYPGENDQSFSGKKCLKEGCTGDMVRMLQCDVPGIVKILFEVVRKDEYITIENLGASYRKLISLKITDTDIRPKISLKFNTKDEMPIFKLDYNYFYHLLHIIIISGTDIVRQIFDEAMPPPLLKKELLIHKNVLESYYNHLWTNHPLGGSWHLLYPPNKELPQSKQFDLCLLLALIKHLNVFPAPKKGWNMEPPSSDISKSADILRLCKYRDILLSEILMNGLTESQFNSIWKKVSDILLRLGMMQEDIDKVKENPIENISLDYHQLSVYLGIPVPEIIQRMLSCYQQGIALQSITGSQRIEIEELQNEEEELSPPLMEYNINVKSHPEIQFAEINKDGTSIPSESSTESLKDLQEVKSKQRKKKKTKNKKNKDSKEDQVPYVVEKEEQLRKEQANPHSVSRLIKDDASDVQEDSAMEDKFYSLDELHILDMIEQGSAGKVTTDYGETEKERLARQRQLYKLHYQCEDFKRQLRTVTFRWQENQMQIKKKDKIIASLNQQVAFGINKVSKLQRQIHAKDNEIKNLKEQLSMKRSQWEMEKHNLESTMKTYVSKLNAETSRALTAEVYFLQCRRDFGLLHLEQTEKECLNQLARVTHMAASNLESLQLKAAVDSWNAIVADVRNKIAFLRTQYNEQINKVKQGFALSTLPPVQLPPPPPSPEILMQQFLGRPLVKESFFRPILTVPQMPAVCPGVVSATGQPRAPLMTGIAWALPAPVGDAVPPSAGLRSDPSIMNWERITDRLKTAFPQQTRKELTDFLRKLKDAYGKSLSELTFDEIVCKISQFIDPKKSQSQGKSVSNVNCVSPSHSPSQPDAAQPPKPAWRPLTSQGPATWEGASNPDEEEEEEEPCVICHENLSPENLSVLPCAHKFHAQCIRPWLMQQGTCPTCRLHVLLPEEFPGHPSRQLPKI
Protein: RAS protein activator like-3 (Q86YV0)
Organism: Homo sapiens (Human)
Function: Functions as a Ras GTPase-activating protein. Plays an important role in the expansion and functions of natural killer T (NKT) cells in the liver by negatively regulating RAS activity and the down-stream ERK signaling pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25652366}. Cytoplasm, cell cortex {ECO:0000269|PubMed:25652366}.
Interaction partners:
- SAM and SH3 domain-containing protein 3
- Carabin
- Ras-related protein R-Ras
- GTPase NRas
- GTPase HRas
- GTPase KRas
Sequence:
MDPPSPSRTSQTQPTATSPLTSYRWHTGGGGEKAAGGFRWGRFAGWGRALSHQEPMVSTQPAPRSIFRRVLSAPPKESRTSRLRLSKALWGRHKNPPPEPDPEPEQEAPELEPEPELEPPTPQIPEAPTPNVPVWDIGGFTLLDGKLVLLGGEEEGPRRPRVGSASSEGSIHVAMGNFRDPDRMPGKTEPETAGPNQVHNVRGLLKRLKEKKKARLEPRDGPPSALGSRESLATLSELDLGAERDVRIWPLHPSLLGEPHCFQVTWTGGSRCFSCRSAAERDRWIEDLRRQFQPTQDNVEREETWLSVWVHEAKGLPRAAAGAPGVRAELWLDGALLARTAPRAGPGQLFWAERFHFEALPPARRLSLRLRGLGPGSAVLGRVALALEELDAPRAPAAGLERWFPLLGAPAGAALRARIRARRLRVLPSERYKELAEFLTFHYARLCGALEPALPAQAKEELAAAMVRVLRATGRAQALVTDLGTAELARCGGREALLFRENTLATKAIDEYMKLVAQDYLQETLGQVVRRLCASTEDCEVDPSKCPASELPEHQARLRNSCEEVFETIIHSYDWFPAELGIVFSSWREACKERGSEVLGPRLVCASLFLRLLCPAILAPSLFGLAPDHPAPGPARTLTLIAKVIQNLANRAPFGEKEAYMGFMNSFLEEHGPAMQCFLDQVAMVDVDAAPSGYQGSGDLALQLAVLHAQLCTIFAELDQTTRDTLEPLPTILRAIEEGQPVLVSVPMRLPLPPAQVHSSLSAGEKPGFLAPRDLPKHTPLISKSQSLRSVRRSESWARPRPDEERPLRRPRPVQRTQSVPVRRPARRRQSAGPWPRPKGSLSMGPAPRARPWTRDSASLPRKPSVPWQRQMDQPQDRNQALGTHRPVNKLAELQCEVAALREEQKVLSRLVESLSTQIRALTEQQEQLRGQLQDLDSRLRAGSSEFDSEHNLTSNEGHSLKNLEHRLNEMERTQAQLRDAVQSLQLSPRTRGSWSQPQPLKAPCLNGDTT
Protein: Peptidoglycan-binding LysM domain-containing protein (Q8VYP8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MLTERGRRISGFNGSFEFSNRKFRGYGFVDRSQGFHERSPSRSCSVSKILRITPPTSSPPSSASTCAGYIEHRVSKFDTLAGIAIKYGVEVADITKLNGLVTDLQMFALESLRIPLPGRHPPSPCLSNGSLNHGEDWSEQASSSASNGNHQDVFDSFQSLRLNHSEKKISPAMNSLQGYYGLKPKNRRASEGFGMAVYKNEASQLQDNDQYLTPFPATSTPLSHHRKSRSLVDAVIAEVNQSPNPSKAGGGEVNSTDKPMRRRQKSEADFSSRAPELLLKEENRSSSGAFSAIAGKNLALRSKASSRANLSAETRHLNSIPINLMDAPVGDSFSSVRKSVSASSLQEPNCNSNGSSLWPTSKWTLKPELLTQVAMASSIFDGLPKPLTGRRNKKAVD
Protein: Transcription factor CYCLOIDEA (O49250)
Organism: Antirrhinum majus (Garden snapdragon)
Function: Involved in the dorsovental asymmetry of flowers. Retards growth rate and reduces organ number in the dorsal region of flowers. Binds specifically to the DNA sequence 5'-GGNCCCNC-3', and is able to bind to the RAD promoter sequence in vivo.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00701}.
Interaction partners:
Sequence:
MFGKNTYLHLPQVSSSLHSRAATSVVDLNGNEIQLHDMLSGHYLTTANAPVLESTALFNNNNNFNHDVVNGLNRDPSPTFPTKQAVKKDRHSKIYTSQGPRDRRVRLSIGIARKFFDLQEMLGFDKPSKTLDWLLTKSKTAIKELVQSKSTKSNSSSPCDDCEEVVSVDSENVTDHSKGKSLKANNKCKEAMDSHQAAAKESRAKARARARERTKEKMCIKQLNEAIVLRNHQFEVSGTREAFVHPVFGFHQQNYGNASHENWDQSNLSSQSNQLCAILNQHKFIN
Protein: Pcbp2 protein (Poly(rC)-binding protein 2) (Q7ZVK5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Polypyrimidine tract-binding protein 1
- Transformer 2 beta homolog.
Sequence:
MDSGVIEGGLNVTLTIRLLMHGKEVGSIIGKKGESVKKMREESGARINISEGNCPERIITLAGPTTAIFKAFSMIIEKLEEDISSSMSNSTATSKPPVTLRIVVPASQCGSLIGKGGCKIKEIRESTGAQVQVAGDMLPNSTERAITIAGTPLSIIECVKQICVVMLESPPKGVTIPYRPKPSGSPVIFAGGQAYAVQGQHAIPQPDLTKLHQLAMQQSPFPLAPSSQGFTAGMDASAQTGSHELTIPNDLIGCIIGRQGAKINEIRQMSGAQIKIANPVEGSSDRQVTITGSPASISLAEYLINARLSSEATGMAAN
Protein: Small GTP-binding protein RAB6, putative (Q586J5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Vacuolar protein sorting 33, putative
- Rab GDP dissociation inhibitor
- Ribosome control protein 1 domain-containing protein
- ADP-ribosylation factor-like protein, putative
- Vps53 N-terminal domain-containing protein
- Conserved oligomeric Golgi complex subunit 6
- Conserved oligomeric Golgi complex subunit 8
- Uncharacterized protein
- RanBD1 domain-containing protein
- Ran-binding protein 1, putative
Sequence:
METNSAPVASTKKGGDGVTAETAPVVKHKIVLLGDQAVGKTSLITRFMYDTFDQQYQATIGIDFFSKTLHINNRATRLHVWDTAGQERFRSLIPSYIRNSAATVVVYDITSRSSFLSTFKWIDEVRAARGDDVIIALVGNKCDVQEKREVSADEAQKRADENRLIFVEVSAKTGTNVKSLFRKVAEAIPVVEICEKGTVPLGKRRDPFLLTPSQQQKDGEGAGWREGGCC
Protein: Phosphoprotein (Protein P) (P12579)
Organism: Human respiratory syncytial virus
Function: Plays critical roles in regulating RNA replication and transcription through its interactions with multiple proteins. Tethers the RNA-directed RNA polymerase L to the nucleoprotein-RNA complex. Recruits the M2-1 protein, a processivity factor that is required for efficient transcription of viral RNA. Acts as a chaperone for neo-synthesized nucleoprotein by forming an N-P complex that preserves N in a monomeric and RNA-free state and prevents the association of nascent N with host cell RNAs. Recruits the host phosphatase PP1 to inclusion bodies to regulate viral transcription. Together with the nucleoprotein, sequesters host NF-kappa-B in inclusion bodies (IBs) thereby inhibiting this host defense pathway.
Subcellular location: Virion {ECO:0000250|UniProtKB:P03421}. Host cytoplasm {ECO:0000250|UniProtKB:P03421}. Note=Localizes in cytoplasmic inclusion bodies. {ECO:0000250|UniProtKB:P03421}.
Interaction partners:
Sequence:
MEKFAPEFHGEDANNRATKFLESIKGKFTSPKDPKKKDSIISVNSIDIEVTKESPITSNSTIINPTNETDDNAGNKPNYQRKPLVSFKEDPIPSDNPFSKLYKETIETFDNNEEESSYSYEEINDQTNDNITARLDRIDEKLSEILGMLHTLVVASAGPTSARDGIRDAMVGLREEMIEKIRTEALMTNDRLEAMARLRNEESEKMAKDTSDEVSLNPTSEKLNNLLEGNDSDNDLSLEDF
Protein: Protein phosphatase 1 regulatory subunit 14A (17 kDa PKC-potentiated inhibitory protein of PP1) (Protein kinase C-potentiated inhibitor protein of 17 kDa) (CPI-17) (Q96A00)
Organism: Homo sapiens (Human)
Function: Inhibitor of PPP1CA. Has over 1000-fold higher inhibitory activity when phosphorylated, creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Protein phosphatase 1 regulatory subunit 12A
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Protein phosphatase 1 regulatory subunit 12C
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Protein phosphatase 1 regulatory subunit 14D
- Transforming protein RhoA
- Serine/threonine-protein kinase N1
- Immortalization up-regulated protein
- Protein phosphatase 1 regulatory subunit 12B
Sequence:
MAAQRLGKRVLSKLQSPSRARGPGGSPGGLQKRHARVTVKYDRRELQRRLDVEKWIDGRLEELYRGMEADMPDEINIDELLELESEEERSRKIQGLLKSCGKPVEDFIQELLAKLQGLHRQPGLRQPSPSHDGSLSPLQDRARTAHP
Protein: 3-ketoacyl-CoA synthase 16 (KCS-16) (EC 2.3.1.199) (Very long-chain fatty acid condensing enzyme 16) (VLCFA condensing enzyme 16) (Q9SYZ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Very-long-chain 3-oxoacyl-CoA reductase-like protein At1g24470
- Very-long-chain 3-oxoacyl-CoA reductase 1
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- Oleosin family protein
- At5g38020
- Protein ECERIFERUM 26
- Methylsterol monooxygenase 1-3
- Protein ECERIFERUM 26-like
- Lecithin-cholesterol acyltransferase-like 1
- ARM repeat superfamily protein
Sequence:
MDYPMKKVKIFFNYLMAHRFKLCFLPLMVAIAVEASRLSTQDLQNFYLYLQNNHTSLTMFFLYLALGSTLYLMTRPKPVYLVDFSCYLPPSHLKASTQRIMQHVRLVREAGAWKQESDYLMDFCEKILERSGLGQETYVPEGLQTLPLQQNLAVSRIETEEVIIGAVDNLFRNTGISPSDIGILVVNSSTFNPTPSLSSILVNKFKLRDNIKSLNLGGMGCSAGVIAIDAAKSLLQVHRNTYALVVSTENITQNLYMGNNKSMLVTNCLFRIGGAAILLSNRSIDRKRAKYELVHTVRVHTGADDRSYECATQEEDEDGIVGVSLSKNLPMVAARTLKINIATLGPLVLPISEKFHFFVRFVKKKFLNPKLKHYIPDFKLAFEHFCIHAGGRALIDEMEKNLHLTPLDVEASRMTLHRFGNTSSSSIWYELAYTEAKGRMTKGDRIWQIALGSGFKCNSSVWVALRNVKPSTNNPWEQCLHKYPVEIDIDLKE
Protein: Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS2 (AtMANIa) (EC 3.2.1.113) (Alpha-mannosidase IA) (Q8H116)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Class I alpha-mannosidase essential for early N-glycan processing. Progressively trims alpha-1,2-linked mannose residues. Produces Man(5)GlcNAc(2) from Man(8)GlcNAc(2), but only Man(6)GlcNAc(2) from Man(9)GlcNAc(2). Has difficulty acting on the terminal mannose of the b-branch. Involved in root development and cell wall biosynthesis.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:19914916, ECO:0000269|PubMed:20023195}; Single-pass type II membrane protein {ECO:0000269|PubMed:19914916, ECO:0000269|PubMed:20023195}.
Interaction partners:
- Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS3
- Alpha-mannosidase 2
- Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS1
- Alpha-1,2-mannosyltransferase ALG9
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dol-P-Man:Man
- Calnexin homolog 2
- Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Calnexin homolog 1
Sequence:
MARNKLVSGSHGIWKYFNPAFYLRRPRRLALLIILFVSVSMVVWDRQSLSRDYQFEVSKLNEEVLRLQQMLEEIKSVTEDVSVNSLKDVQEDPVDAQRMQRVKEAMVHAWSSYEKYAWGQDELQPQTKDGVDSFGGLGATMIDALDTLYIMGLDEQFQKAREWVASSLDFDKDYAASMFETTIRVVGGLLSAYDLSGDKIFLEKAMDIADRLLPAWDTQSGIPYNIINLKHGNAHNPTWAGGDSILADSGTEQLEFIALSQRTGDPKYQQKVEKVISVLNKNFPADGLLPIYINPDTANPSQSTITFGAMGDSFYEYLLKVWVFGNKTSAVKHYRDMWEKSMNGLLSLVKKSTPLSFTYICEKSGNSLIDKMDELACFAPGMLALGASGYSDPAEGKKFLTLAEELAWTCYNFYQSTPTKLAGENYFFNSGSDMSVGTSWNILRPETVESLFYLWRLTGNKTYQEWGWNIFEAFEKNSRIESGYVGLKDVNTGVKDNKMQSFFLAETLKYLYLLFSPTTVIPLDEWVFNTEAHPLKIKSRNDQVNLKQSNKVLLRKPAFRIRQRHYGRITKK
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q3LS18)
Organism: Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MDHNNREKDERPRPAKALPVRTGHSSRPSSSTTSSGVLMVGPNFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPIKSRAPQLHLEYRFYKQLGNTAEGLPQVFYFGPCGKYNAMVLELLGPSLEDLFDLCDRTFTLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRQGNKKEHIIHIIDFGLAKEYIDPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRNTPVEVLCENFPEEMATYLRYVRRLDFFEKPDYDYLRTLFSELFERKGYSFDYVYDWVGRPIPTPGGSVHVDSGTSAITRESHGHRERPSQTQPLRNQTGVPDRRGAWDLQVGRQAHPAYLVPHLASDRHGGSVQVMSSTNGQLNADDQTGGHSNAPITAQAEVEVVEEAKCCCFFKRKRKNHSQRHHK
Protein: Receptor-like protein 54 (AtRLP54) (F4KHA2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Duplicated homeodomain-like superfamily protein
- Kelch repeat-containing protein At3g27220
- F25A4.19 protein
- Protein REVEILLE 8
- Telomere repeat-binding factor 3
- ADP,ATP carrier protein 1, mitochondrial
Sequence:
MKSNLAVFFITCFFCCVFVTSDSVYTLPFPFPRDQVEILLELKNEFPSFNCDLTWKLDYFGRMDTRANISSWTKDSDSFSGVSFDSETGVVKELSLGRQCLTSLKANSSLFRFQHLRYLDLSENHFDSSPIPSGFGRLTYLESLDLSKNGFIGEVPSSISNLSRLTNLDLSYNKLTGGIPNLHSLTLLENIDLSYNKFSGAIPSYLFTMPFLVSLNLRQNHLSDPLENINYSATSKLLILDMAYNLMSHRILEPISKLANLIQIDLSFQKTPYTFNFDFLLFKSLVRLDLSGNSVSVVGTGSENLTHLDLSSCNITEFPMFIKDLQRLWWLDISNNRIKGKVPELLWTLPSMLHVNLSRNSFDSLEGTPKIILNSSISELDLSSNAFKGSFPIIPPYVNIMAASNNYFTGGIPLIFCKRYRLSLLDLSNNNFSGTIPRCLTNVSLGLEALKLSNNSLTGRLPDIEDRLVLLDVGHNQISGKLPRSLVNCTTLKFLNVEGNHINDTFPFWLKALTRLEIIVLRSNRFHGPISSPEVSLSFTALRIIDISRNSFNGSLPQNYFANWSAPLVNTPQGYRWPEYTGDEHSKYETPLWSYPSIHLRIKGRSIELGKIPDTYTSIDFSGNSFEGQIPESIGDLKSLIVLDLSNNSFTGRIPSSLAKLKQLESLDLSQNRISGNIPQELRELTFLGYVNMSHNRLTGQIPQSTQVGGQPKSSFEGNINLCGLPLQESCLRGNGVPSTPHTQEQELPKQEHALNWKAAAIGYGPGVLFGLAIGQAFARYKPVLFYKLFRL
Protein: SPX domain-containing protein 3 (Protein SPX DOMAIN GENE 3) (OsSPX3) (Q7XEY9)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Functional repressor of PHR2. Involved in maintaining cellular Pi homeostasis when plants are exposed to an external change in Pi. Negatively regulates root-to-shoot Pi translocation redundantly with SPX3. Down-regulates the non-coding RNA IPS1 (At3g09922) and suppresses the responses of miR399 and PHO2 to Pi-starvation.
Subcellular location: Nucleus {ECO:0000269|PubMed:24368504}. Cytoplasm {ECO:0000269|PubMed:19566645, ECO:0000269|PubMed:24368504}.
Interaction partners:
Sequence:
MKFGKRLKKQVEESLPEWRDKFLAYKRLKKLVRLVSSSSGDVGGGGGGEAEFVRLLDGEVDRINAFFLEQEEEFVIRQRELQETVEKVAGGGGGGRRPAAAEMRRVRKEIVDLHGEMVLLLNYSAVNYTGLAKILKKYDKRTGRLLRLPFIEKVLRQPFFTTELISRLVRDCEATMEAIFTSSVATTAMAGDRRTWKGCSGDAGMAPMADQQGIFRNTVAALATMKELRSGSSTYGRFSLPPMAAPASPESDVLQSIRSDPHLKENGRIPSLQFFYA
Protein: Plasma membrane ascorbate-dependent reductase CYBRD1 (EC 7.2.1.3) (Cytochrome b reductase 1) (Duodenal cytochrome b) (Q925G2)
Organism: Mus musculus (Mouse)
Function: Plasma membrane reductase that uses cytoplasmic ascorbate as an electron donor to reduce extracellular Fe(3+) into Fe(2+). Probably functions in dietary iron absorption at the brush border of duodenal enterocytes by producing Fe(2+), the divalent form of iron that can be transported into enterocytes. It is also able to reduce extracellular monodehydro-L-ascorbate and may be involved in extracellular ascorbate regeneration by erythrocytes in blood. May also act as a ferrireductase in airway epithelial cells (By similarity). May also function as a cupric transmembrane reductase.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q53TN4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53TN4}. Apical cell membrane {ECO:0000305|PubMed:11230685, ECO:0000305|PubMed:12547225}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53TN4}. Note=Localized at the brush border of duodenal cells. {ECO:0000269|PubMed:11230685, ECO:0000269|PubMed:12547225}.
Interaction partners:
- Natural resistance-associated macrophage protein 2
- Ferroportin
- Hepcidin
- Hephaestin
- Hepcidin-2
- Metalloreductase STEAP3
- Hereditary hemochromatosis protein homolog
- Transferrin receptor protein 1
- Transferrin receptor protein 2
- Proton-coupled folate transporter
Sequence:
MAMEGYRGFLGLLVSALLVGFLSVIFVLIWVLHFREGLGWNGSGLEFNWHPVLAVTGFVFIQGIAIIVYRLPWTWKCSKLLMKSIHAGLNAVAAILAIISVVAVFEYHNVQKVPHMYSLHSWVGLTALILYIQQLVVGFFVFLLPWAPPSLRAIVMPIHVYSGLLLFGTVIATVLMGVTEKLFFVLKHPSYHSFPPEGVFTNTLGLLILVFGALIFWIVTRPQWKRPREPGSVPLQLNGGNAECRMEGAIAISSAHSMDAADPADAESSSEGAARKRTLGLADSGQRSTM
Protein: Copper binding protein 4 (Lamin-like protein) (F4YAW3)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MERSKAMMMAVAAVGLALVLMVPQADATRYIVGGGGIGWTTNVNYTVWARGKHFYNGDWLYFVYDRNQMNVLEVNKTDYESCNADHPLHNWTTGAGRDVVPLNVTRHYYFISGKGFCYGGMKLAVRVENPPPPPKAAPLNEKSGSSPSSIVYRGQLVLPAAFAIAALWDTFVRIW
Protein: Dystroglycan 1 (Dystroglycan) (Dystrophin-associated glycoprotein 1) [Cleaved into: Alpha-dystroglycan (Alpha-DG); Beta-dystroglycan (Beta-DG)] (O18738)
Organism: Bos taurus (Bovine)
Function: The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization.
Subcellular location: [Alpha-dystroglycan]: Secreted, extracellular space {ECO:0000250}.; SUBCELLULAR LOCATION: [Beta-dystroglycan]: Cell membrane {ECO:0000250}; Single-pass type I membrane protein. Cytoplasm, cytoskeleton. Nucleus, nucleoplasm. Cell membrane, sarcolemma {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}. Note=The monomeric form translocates to the nucleus via the action of importins and depends on RAN. Nuclear transport is inhibited by Tyr-892 phosphorylation. In skeletal muscle, this phosphorylated form locates to a vesicular internal membrane compartment. In muscle cells, sarcolemma localization requires the presence of ANK2, while localization to costameres requires the presence of ANK3. Localizes to neuromuscular junctions (NMJs) in the presence of ANK2 (By similarity). Colocalizes with ERM proteins in Schwann-cell microvilli (By similarity). In peripheral nerves, localizes to the Schwann cell membrane. {ECO:0000250}.
Interaction partners:
- Agrin
- Dystrophin
- Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2
- Neurexin-3-beta
- Pikachurin
- Neurexin 2.
- Neurexin-1
- Uncharacterized protein.
- Dolichyl-phosphate-mannose--protein mannosyltransferase
- Dolichyl-phosphate-mannose--protein mannosyltransferase
Sequence:
MRMSVGSAVPLPLWGRTFLLLLSVAVTQSHWPSEPSEAVRDWENQLEASMHSALSDLHETVPTVVGIPDGTAVVGRSFRVTIPTDLIASNGEVIKVSAAGKEALPSWLHWDPQSHTLEGLPLDTDKGVHYISVSAARLGANGSHVPQTSSVFSIEVYPEDHSEPQSLRAASPDPGEVVSLVCAADEPVTVLTVILDADLTKMTPKQRIDLLRRMRGFSEVEPHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCCLNQNSVPDIRGVEVPAREGAMSAQLGYPVVGWHIANKKPSLPKRIRRQIHATPTPVTAIGPPTTAIQEPPSRIVPTPTSPAIAPPTETMAPPVRDPVPGKPTVTIRTRGAIIQTPTLGPIQPTRVSEAGTTVPSQIRPTMTIPGYMEPSTVTTPPTTTTKKPRVSTPRPATPSTDSSTTTTRRPTKKPRTSRPVPRVTTKAPITRLETASPATRMRTTTSGVPHGGEPNQRPELKNHIDRVDAWVGTYFEVKIPSDTFYDNEDTTTDKLKLTLKLREQQLVGEKSWVQFNSNSQLMYGLPDSSHVGKHEYFMHATDKGGLSAVDAFEIHVHRRPQGDKAPARFKAKLTGDPAAVTNDIHKKIALVKKLAFAFGDRNCSTITLQNITRGSIVVEWTNNTLPLEPCPKEQITALSRRIAEDDGKPRGAFVNALEPDFQAMSITVTGSGSCRHLQFVPVAPPMRVPSEAPATEVPDRDPEKSSEDDVYLHTVIPAVVVAAILLIAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKAPLPPPEYPNQSMPETTPLNQDTVGEYAPLRDEDPSAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP
Protein: Candida glabrata strain CBS138 chromosome G complete sequence (Q6FSQ5)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Secreted, cell wall {ECO:0000256|ARBA:ARBA00004191}.
Interaction partners:
Sequence:
MRLPTAKSCALGFTLATSLVEALPQFDRYKEHSKKDVSHQHQRKRAVTVEYVYATVTVAHDAEQQNNAANDLLKEDEVQGNVAAAGSPAQEAVQPTTTDYAQGQTSTLQPETPPSSSSQYNANQEQQQQQNQPNDQQAAAQPAGNDQQSNAYSSEVPAAPQSAQVPTSPSSTPSNAATSNSGSSSNTNSGSSSAGTGSIYGDLASFSGPNQPFQDGTIPCSQFPSGQGVIALDWLNQGGWSGIENSDTSTGGPCQEGSYCSYACQPGMSKTQWPSNQPADGRSVGGLLCKNGFLYKSNPSANYLCEWGVNAAYVESHISQGVAICRTDYPGTENMVIPTFVEAGSTLPLTVVDQDTYYQWQGKKTSAQYYVNNAGVSVDQGCIWGTPGSGVGNWAPLNFGAGSTNGITYLSLIPNPNNRSPLNFNVKIVASDDSSVVNGQCSYENGVYSGGADGCTVAVTSGSAKFVLY