wanglab/gogpt-training-data huggingface dataset:
Protein: Protein Vpr (R ORF protein) (Viral protein R) (P69726)
Organism: Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1)
Function: During virus entry, plays a role in the transport of the viral pre-integration (PIC) complex to the host nucleus. This function is crucial for viral infection of non-dividing macrophages. May act directly at the nuclear pore complex, by binding nucleoporins phenylalanine-glycine (FG)-repeat regions.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04080, ECO:0000269|PubMed:2139896, ECO:0000269|PubMed:8411357}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04080, ECO:0000269|PubMed:8411357}. Host extracellular space {ECO:0000255|HAMAP-Rule:MF_04080}. Note=Incorporation into virion is dependent on p6 GAG sequences. Lacks a canonical nuclear localization signal, thus import into nucleus may function independently of the human importin pathway. Detected in high quantity in the serum and cerebrospinal fluid of AIDS patient. {ECO:0000255|HAMAP-Rule:MF_04080, ECO:0000269|PubMed:3040055}.
Interaction partners:
Sequence:
MEQAPEDQGPQREPHNEWTLELLEELKNEAVRHFPRIWLHGLGQHIYETYGDTWAGVEAIIRILQQLLFIHFRIGCRHSRIGVTRQRRARNGASRS
Protein: Nodulin-like domain-containing protein (Q582K9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSAPVDNVVVERLSTANQKPINEPRRFALLVLGTFCCICTSFMYAFNLISGAMQARYNLTQRDLSTITTVGIAVGYFLLPYSFIFDYLGPKPIFVIAMTVFCLGALLFALTFQEVIEGSVVRLSVYNGFLTLGCMLFDLGSVVTVLSVFPSNRGAVMAIVKTFTGLGAAIVGSIQLAFFSKSVANYFFFLMSFSLVVGTLAVVFMNLPPFHLTGYQKTHLDEEEKAQRLARKGVYLKQKAPMWRFIYGFVVLLILVVFLPLEGALVAYLKLGSNFKVGFAVTVIVLTVIFPFMAFPLTTFDGKRPHDDSEGDAKEHVEADDEVSAAEDKVVETDVDYIAPQFQETFIEGLKTARLWCLLWSIFCCVGVHYVIIYNARFIYTALAGEAPDDALNALLTVLNGVGSAVGRLCMGYFEVWSQKRRAEDRVPITLSMFVPSVCIITMLTLFLTLPKAALPLPYFIAAFSNGFMAATMALVTRTIFAKDPAKHYNFCFLGSVLSAIFLNRLLYGEWYTQQADKLDQDVCTERVCVVMPLAFMLGLAFPAFATSTYLHLQYRNLCLKALEERRRIKEAEDNQTNAENVCAEPTCDDNADACLEEKAADSSK
Protein: RNA methyltransferase (A0A1D8PLX3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MLGQRMILRNTYRLTVPKSVILPICRTNYSTSSSSNNPFPLNDKERKQAKKQSQLPWYKRWTNYSNSEQFQNKTMPKVYICAFVVSLVPMYFYMRDRYHEDKQLKHINAKYAQDPSSLSEYEYLVLKSMNHSEKLRPLELKKYKIYQLMRKEFRRKNLFNQEMFNPTPQELNDWYQNQVKYESASKVVPILVDKIDSKDKINANPAIQNAEDTTAFYDSKAKEYDDAVKWEERGIFMGSKRKWLMSQAKGDVLEVSCGTGRNIPYLYLQQIKSLTFIDSARNMVEVTKEKFKKAFPEFKKVAFAVGKAEDLSNIAQDVKYDTIVEAFGLCCHEDPVKALQNMAKLLKPGGRIVLLEHGRSNWGFINNHLDFRSEKRMETWKCRWNLDIGELIDEAGLDITKEKRAHFSTTWMVVVKKPEDPINPDEKPFLDKLFGRESRKVQKS
Protein: Argininosuccinate lyase (ASAL) (EC 4.3.2.1) (Arginosuccinase) (P20673)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the reversible cleavage of L-argininosuccinate to fumarate and L-arginine, an intermediate step reaction in the urea cycle mostly providing for hepatic nitrogen detoxification into excretable urea as well as de novo L-arginine synthesis in nonhepatic tissues (By similarity). Essential regulator of intracellular and extracellular L-arginine pools. As part of citrulline-nitric oxide cycle, forms tissue-specific multiprotein complexes with argininosuccinate synthase ASS1, transport protein SLC7A1 and nitric oxide synthase NOS1, NOS2 or NOS3, allowing for cell-autonomous L-arginine synthesis while channeling extracellular L-arginine to nitric oxide synthesis pathway (By similarity).
Interaction partners:
- Argininosuccinate synthase
- N-acetylglutamate synthase, mitochondrial
- Ornithine aminotransferase, mitochondrial
- Arginase-2, mitochondrial
- Arginase-1
- Nitric oxide synthase 1
- Nitric oxide synthase, inducible
- Nitric oxide synthase 3
- Ornithine transcarbamylase, mitochondrial
- Adenylosuccinate lyase
Sequence:
MASESGKLWGGRFAGSVDPTMDKFNSSIAYDRHLWNVDLQGSKAYSRGLEKAGLLTKAEMQQILQGLDKVAEEWAQGIFKLYPNDEDIHTANERRLKELIGEAAGKLHTGRSRNDQVVTDLRLWMRQTYSKLSTFLKVLIEAMVDRAEAECEVLFPGYTHLQRAQPIRWSHWILSHAVALTRDLERLKEVQKRINVLPLGSGAIAGNPLGVDREFLCAELNFGAITLNSMDATSERDFVAEFLFWASLCMTHLSRMAEDLILYGTKEFNFVQLSDAYSTGSSLMPQKKNPDSLELIRSKARRVFGRCAGLLMTLKGLPSTYNKDLQEDKEAVFEVSDTMTAVLQVATGVISTLQIHRENMAQALSPDMLATDLAYYLVRKGMPFRQAHEASGKAVVVAEMKGVALNQLSLQELQTVSPLFSSDVNLVWDYSHSVEQYTALGGTAQSSVEWQISQVRALLQM
Protein: Oxalate--CoA ligase (EC 6.2.1.8) (Oxalyl-CoA synthetase) (Peroxisomal-coenzyme A synthetase) (O74976)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the first step in a degradation pathway of oxalate to CO(2) to protect the cell against the harmful effects of oxalate derived from endogenous processes or an environmental sources.
Subcellular location: Peroxisome matrix {ECO:0000250|UniProtKB:P38137}. Peroxisome membrane {ECO:0000250|UniProtKB:P38137}; Peripheral membrane protein {ECO:0000250|UniProtKB:P38137}.
Interaction partners:
- L-2-aminoadipate reductase
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 10
- Putative acyl carrier protein, mitochondrial
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 7
- RQC trigger complex subunit RQT4 homolog
- Mediator of RNA polymerase II transcription subunit 31
- Probable acetyl-coenzyme A synthetase
Sequence:
MSFTTLYSAIQGDASARALVAPSLNAELSFSELRIAIMDLQRQIASLGIKVGDPVNIAIPNGLEFVVAFYAVSWQRAICGPLNSNYKQSEFEFYIDDLKSKLVIVPEGSVAANTPAVRAAKKLSVAVAELAWCPKSRLVRIVHFEGAKINAPQPLGLPQPDDVMLVLHTSGTTGRPKVVPLTHKNLCRSIHNITTSYRLDPRDTSYVVMPLFHVHGLLCGLLSTLASGGCAVVPPKFSAHSFWKEFIQYGATWYTAVPTIHQILLRTPPPKPLPRIRFIRSCSSPLAPPVLSKLEATFRAPVLEAYAMTEASHQMTTNPLPPLVHKPHSVGKPFGVELKILDQKGNEMPQGKEGEICVRGINVTKGYLNNPAANKSSFTKDRFFRTGDEGKLDKDGYVFITGRIKELVNRGGEKISPAEIDAVLMQHPDVSEAVCFAVPDEKYGQDIQAAINPVAGKTVTPKQLHDYLEQKVAAFKIPKKFYFTDRIPKTATGKVQRRLVCDAFFNHSKAKL
Protein: Eukaryotic translation initiation factor 5A (eIF-5A) (Q9GU68)
Organism: Drosophila melanogaster (Fruit fly)
Function: mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Critical for the efficient synthesis of peptide bonds between consecutive proline residues. Can resolve ribosomal stalling caused by consecutive prolines during translation (By similarity). Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Functions as a regulator of apoptosis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P23301}.
Interaction partners:
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein eS6
- Small ribosomal subunit protein uS17
- Probable deoxyhypusine synthase
- FI01658p
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL5
- 40S ribosomal protein S15
Sequence:
MAELDDQFETTDSGASTTYPMQCSALRKNGFVMLKSRPCKIVEMSTSKTGKHGHAKVHMVGIDIFSNKKYEDICPSTHNMDVPNVKREDLQLIAISDDSFLTLMTESGDLREDLKVPEGELGEQLRLDFDSGKDLLCTVLKACGEECVIAIKTNTALDK
Protein: Peregrin (Bromodomain and PHD finger-containing protein 1) (B2RRD7)
Organism: Mus musculus (Mouse)
Function: Scaffold subunit of various histone acetyltransferase (HAT) complexes, such as the MOZ/MORF and HBO1 complexes, which have a histone H3 acetyltransferase activity (By similarity). Plays a key role in HBO1 complex by directing KAT7/HBO1 specificity towards histone H3 'Lys-14' acetylation (H3K14ac) (By similarity). Some HAT complexes preferentially mediate histone H3 'Lys-23' (H3K23ac) acetylation. Positively regulates the transcription of RUNX1 and RUNX2 (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P55201}. Chromosome {ECO:0000250|UniProtKB:P55201}. Cytoplasm {ECO:0000250|UniProtKB:P55201}. Note=Localization to the nucleus depends on KAT6A, ING5 and MEAF6. Localizes to transcription start sites. {ECO:0000250|UniProtKB:P55201}.
Interaction partners:
- Histone acetyltransferase KAT6A
- Histone acetyltransferase KAT6B
- Inhibitor of growth protein 5
- Histone acetyltransferase KAT7
- Chromatin modification-related protein MEAF6
- Histone H4
- Histone H2A type 2-A
- Histone H2A type 3
- Histone H2A type 2-C
- Histone H2A type 1-B
Sequence:
MGVDFDVKTFCHNLRATKPPYECPVETCRKVYKSYSGIEYHLYHYDHDSPPPPQQTPLRKHKKKGRQSRPANKQSPSPSEVSQSPGREVMSYAQAQRMVEVDLHGRVHRISIFDNLDVVSEDEEAPEEAPENGSNKENTETPAATPKSGKHKNKEKRKDSNHHHHSAPASAAPKLPEVVYRELEQDTPDAPPRPTSYYRYIEKSAEELDEEVEYDMDEEDYIWLDIMNERRKTEGVSPIPQEIFEYLMDRLEKESYFESHNKGDPNALVDEDAVCCICNDGECQNSNVILFCDMCNLAVHQECYGVPYIPEGQWLCRRCLQSPSRAVDCALCPNKGGAFKQTDDGRWAHVVCALWIPEVCFANTVFLEPIDSIEHIPPARWKLTCYICKQRGSGACIQCHKANCYTAFHVTCAQQAGLYMKMEPVRETGANGTSFSVRKTAYCDIHTPPGSARRLPALSHSEGEEEEDEEEDEGKSWSSEKVKKAKAKSRIKMKKARKILAEKRAAAPVVSVPCIPPHRLSKITNRLTIQRKSQFMQRLHSYWTLKRQSRNGVPLLRRLQTHLQSQRNCEQVGRDSDDKNWALKEQLKSWQRLRHDLERARLLVELIRKREKLKRETIKIQQIAMEMQLTPFLILLRKTLEQLQEKDTGNIFSEPVPLSEVPDYLDHIKKPMDFFTMKQNLEAYRYLNFDDFEEDFNLIVSNCLKYNAKDTIFYRAAVRLREQGGAVLRQARRQAEKMGIDFETGMHIPHNLAGDEVSHHTEDVEEERLVLLENQKHLPVEEQLKLLLERLDEVNASKQSVGRSRRAKMIKKEMTALRRKLAHQRETGRDGPERHGPSGRGNLTPHPAACDKDGQTDSAAEESSSQETSKGLGPNMSSTPAHEVGRRTSVLFSKKNPKTAGPPKRPGRPPKNRESQMTPSHGGSPVGPPQLPIMGSLRQRKRGRSPRPSSSSDSDSDKSTEDPPMDLPANGFSSGNQPVKKSFLVYRNDCNLPRSSSDSESSSSSSSSAASDRTSTTPSKQGRGKPSFSRGTFPEDSSEDTSGTENEAYSVGTGRGVGHSMVRKSLGRGAGWLSEDEDSPLDALDLVWAKCRGYPSYPALIIDPKMPREGMFHHGVPIPVPPLEVLKLGEQMTQEAREHLYLVLFFDNKRTWQWLPRTKLVPLGVNQDLDKEKMLEGRKSNIRKSVQIAYHRALQHRSKVQGEQSSETSDSD
Protein: Cytosolic sulfotransferase 10 (AtSOT10) (EC 2.8.2.-) (Sulfotransferase 4a) (AtST4a) (O82330)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to specifically catalyze the sulfate conjugation of brassinosteroids, including castasterone (CS), brassinolide (BL), related 24-epimers, and the naturally occurring (22R, 23R)-28-homobrassinosteroids. No activity on phenolic acids, desulfo-glucosinolates, flavonoids, steroids, gibberellic acids, cytokinins, phenylpropanoids, hydroxyjasmonates and coumarins.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- BAHD acyltransferase BIA1
- Cytochrome P450 72C1
- UDP-glycosyltransferase 73C5
- Brassinosteroid-related acyltransferase 1
- UDP-glycosyltransferase 73C6
- BAHD acyltransferase DCR
- At2g15730
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
- 3-epi-6-deoxocathasterone 23-monooxygenase CYP90C1
Sequence:
MDEKDRPKNLREEEEKPSEETKILISSLPWEIDYLGNKLFNYEGYWYSEDILQSIPNIHTGFQPQETDIILASFYKSGTTWLKALTFALVQRSKHSLEDHQHPLLHHNPHEIVPNLELDLYLKSSKPDLTKFLSSSSSSPRLFSTHMSLDPLQVPLKENLCKIVYVCRNVKDVMVSVWYFRQSKKITRAEDYSLEAIFESFCNGVTLHGPFWDHALSYWRGSLEDPKHFLFMRYEDLKAEPRTQVKRLAEFLDCPFTKEEEDSGSVDKILELCSLSNLRSVEINKTRTSSRVDFKSYFRKGQVGDWKSYMTPEMVDKIDMIIEEKLKGSGLKF
Protein: Phosphate transporter PHO1-2 (Protein PHO1-2) (OsPHO1;2) (Q6K991)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in the transfer of inorganic phosphate (Pi) from roots to shoots.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MVKFSREYEASIIPEWKAAFVDYKRLKKLIKRIKVTRRDDSFAAANAAAAADHLLPPPPAEKEAGGYGFSILDPVRAIAARFSAGQQPSASEDEECPDRGELVRSTDKHEREFMERADEELEKVNAFYTGQEAELLARGDALLEQLRILADVKRILADHAAARRARGLARSRSMPPPPPSSSPPSSVHGSSGRYLLSGLSSPQSMSDGSLELQQAQVSEGAAVADEVMAALERNGVSFVGLAGKKDGKTKDGSGKGRGGGGGGGGGVLQLPATVRIDIPATSPGRAALKVWEELVNVLRKDGADPAAAFVHRKKIQHAEKNIRDAFMALYRGLELLKKFSSLNVKAFTKILKKFVKVSEQQRATDLFSEKVKRSPFSSSDKVLQLADEVECIFMKHFTGNDRKVAMKYLKPQQPRNTHMITFLVGLFTGTFVSLFIIYAILAHVSGIFTSTGNSAYMEIVYHVFSMFALISLHIFLYGCNLFMWKNTRINHNFIFDFSSNTALTHRDAFLMSASIMCTVVAALVINLFLKNAGVAYANALPGALLLLSTGVLFCPFDIFYRSTRYCFMRVMRNIIFSPFYKVLMADFFMADQLTSQIPLLRHMEFTACYFMAGSFRTHPYETCTSGQQYKHLAYVISFLPYFWRALQCLRRYLEEGHDINQLANAGKYVSAMVAAAVRFKYAATPTPFWVWMVIISSSGATIYQLYWDFVKDWGFLNPKSKNRWLRNELILKNKSIYYVSMMLNLALRLAWTESVMKIHIGKVESRLLDFSLASLEIIRRGHWNFYRLENEHLNNVGKFRAVKTVPLPFRELETD
Protein: Proton-coupled amino acid transporter 1 (Proton/amino acid transporter 1) (Lysosomal amino acid transporter 1) (LYAAT-1) (Neutral amino acid/proton symporter) (Solute carrier family 36 member 1) (Q924A5)
Organism: Rattus norvegicus (Rat)
Function: Electrogenic proton/amino acid symporter with selectivity for small apolar L-amino acids, their D-enantiomers and selected amino acid derivatives such as 4-aminobutanoate/GABA. May be involved in the efflux from the lysosomal compartment of neutral amino acids resulting from proteolysis. May play a role in specifying sites for exocytosis in neurons.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12598615}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q7Z2H8}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:11390972, ECO:0000269|PubMed:12598615}; Multi-pass membrane protein {ECO:0000255}. Note=In neurons, colocalizes with the exocyst complex in the axonal processes. {ECO:0000269|PubMed:12598615}.
Interaction partners:
- Neutral amino acid transporter B
- Amino acid transporter
Sequence:
MSTQRLRNEDYHDYSSTDVSPEESPSEGLGSFSPGSYQRLGENSSMTWFQTLIHLLKGNIGTGLLGLPLAVKNAGLLLGPLSLLVIGIVAVHCMGILVKCAHHLCRRLNKPFLDYGDTVMYGLECSPSTWIRNHSHWGRRIVDFFLVVTQLGFCCVYFVFLADNFKQVIEAANGTTTNCNNNETVILTPTMDSRLYMLTFLPFLVLLSFIRNLRILSIFSLLANISMFVSLIMIYQFIVQRIPDPSHLPLVAPWKTYPLFFGTAIFAFEGIGVVLPLENKMKDSQKFPLILYLGMAIITVLYISLGSLGYLQFGADIKGSITLNLPNCWLYQSVKLLYSIGIFFTYALQFYVAAEIIIPAIVSRVPERFELVVDLSARTAMVCVTCVLAVLIPRLDLVISLVGSVSSSALALIIPPLLEVTTYYGEGISPLTITKDALISILGFVGFVVGTYESLWELIQPSHSDSSTNSTSAFI
Protein: Lipid-binding serum glycoprotein family protein (F4JDK0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MNRSKEENVAPTMKDDSPFGKLTEDLLIEIFIRIPITNWEQVSCVRKQWANLFRGECLWLAALNRAYPLASKTKSWIGPIRQGLSKRRYVALYISRNILGVDDTDIDEMLGHIYVFLNDQLQLSTMPASGILHGTLIDQLIVCGQSKEEAGELATKIWLALLDNLEDTKHTFTVLKSIAQEYDGFLPYPYSRPIKVQWKVFEKLFVDFRDLLDHSEYCDLIGIAKNKFQTIPYFSYPSTLFFFLEMALMKVMTILVLFVSVSSTLAQSNNGGHISIIVSETGLEFAKDYLIKKVITTTLPLQLPDIENKVKIPLIGKVRMGLSNIQIDAVHVQSSKMETRKDGIILSVLGATANLSMDWSYTYRASFFEISDHGDASVEVKGMNVRITATLVNDNGSLKIASRENDCTVKNIDIHINGGASWLYQGVVDAFQKMIISTVEKTVSTKIVEKMKKLDSFLQSLPKQRKIDDSAAVNLTFTGNPVLGNSSVEVDINGLFMPKGDDIKVAGSRSSSFFGGVNKRMVTISVEEGVFNSATLVYFNAKVMHLVMEETKNGSILSTSDWKLILPELYKHYPDNKMVLNMSVTSPPAVKITENGIDATIQLDIAFDVQDSGENLSVARLSTILSVACSTEIVKNNLIGSLRLNDFNATMKWSKIGEFQTNYVQAATSRILEALFLPYVNTRLKRGFPLPIPGDFTIKNIKIVYVNSGILVCTDIGTSTNQ
Protein: Purkinje cell protein 2 homolog (Q8IVA1)
Organism: Homo sapiens (Human)
Function: May function as a cell-type specific modulator for G protein-mediated cell signaling.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MMDQEEKTEEGSGPCAEAGSPDQEGFFNLLSHVQGDRMEGQRCSLQAGPGQTTKSQSDPTPEMDSLMDMLASTQGRRMDDQRVTVSSLPGFQPVGSKDGAQKRAGTLSPQPLLTPQDPTALGFRRNSSPQPPTQAP
Protein: STAG3 cohesin complex component (C9JTG4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSPLQRAVGDTKRALSASSSSSASLPFDDRDSNHTSEGNGDSLLADEDTDFEDSLNRNVKKRAAKRPPKTTPVAKHPKKGSRVVHRHSRKQSEPPANDLFNAVKAAKSDMQSLVDEWLDSYKQDQDAGFLELVNFFIQSCGCK
Protein: Zinc finger protein ZIC 1 (Zinc finger protein of the cerebellum 1) (Q8JJC0)
Organism: Gallus gallus (Chicken)
Function: Acts as a transcriptional activator. Involved in neurogenesis. Plays important roles in the early stage of organogenesis of the CNS, as well as during dorsal spinal cord development and maturation of the cerebellum. Binds to the minimal GLI-consensus sequence 5'-TGGGTGGTC-3' (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
- Forkhead box protein D3
- Paired box 3
- Homeobox protein GHOX-7
- Transcription factor SOX-10
- TF_AP-2 domain-containing protein.
- Paired box protein Pax-6
- Transcription factor SOX-9
- PAX7 protein
- Homeobox protein GBX-2
Sequence:
MLLDAGPQYPAIGVTTFGSSRHHSAADVTDREVGLGINPFADGMGAFKLNPGGHELASAGQTAFTSQAPGYAAALGHHHHPPHVGSYSSAAFNSTRDFLFRNRGFGEAAAASAQHSLFASAAGGFGGPHGHGDAAGHILFPGLHEQAAGHASPNVVNGQMRLGFSGDMYGRAEQYGQVTSPRSEHYASSQLHGYGHMNMNMAAHHGAGAFFRYMRQPIKQELICKWIEPEQLANPKKSCNKTFSTMHELVTHVTVEHVGGPEQSNHICFWEECPREGKPFKAKYKLVNHIRVHTGEKPFPCPFPGCGKVFARSENLKIHKRTHTGEKPFKCEFEGCDRRFANSSDRKKHMHVHTSDKPYLCKMCDKSYTHPSSLRKHMKVHESSSQGSQPSPAASSGYESSTPPTIVSPSTENQTASSLSPSSSAGHHTASHSTLTSNFNEWYV
Protein: Replication protein A, subunit RPA32 (F4IYI1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MYGGDFDGNAAFAGGGFMPSQATTQAHESSSSLKNRDVRTLLPLTLKQLSSASTTGESNFSIDGVDIKTVVIVGRISRMENRITQVDFVVDDGTGWVDCVRWCHARQETEEMEAVKLGMYVRLHGHLKIFQGKRSVNVFSVRPVTDFNEIVHHFTECMYVHMYNTKLRGGSITQDTATPRPQMPYSTMPTPAKPYQTGPSNQFPNQFNDSMHGVKQTVLNYLNQPMHM
Protein: High-affinity nitrate transporter 2.2 (OsNRT2.2) (P0DKH0)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in nitrate transport, but does not seem to be able to mediate transport by its own. Acts as a dual component transporter with NAR2.1. Imports nitrate with high affinity when expressed with NAR2.1 in a heterologous system (Xenopus oocytes).
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Nitrate reductase 1
- High-affinity nitrate transporter-activating protein 2.1
- Nitrate reductase
- Nitrate reductase
- Ferredoxin--nitrite reductase, chloroplastic
- Os02g0765900 protein
- Os11g0242400 protein
- Probable high-affinity nitrate transporter 2.4
- High-affinity nitrate transporter 2.3
- Plastocyanin
Sequence:
MDSSTVGAPGSSLHGVTGREPAFAFSTEVGGEDAAAASKFDLPVDSEHKAKTIRLLSFANPHMRTFHLSWISFFSCFVSTFAAAPLVPIIRDNLNLTKADIGNAGVASVSGSIFSRLAMGAICDMLGPRYGCAFLIMLAAPTVFCMSLIDSAAGYIAVRFLIGFSLATFVSCQYWMSTMFNSKIIGLVNGLAAGWGNMGGGATQLIMPLVYDVIRKCGATPFTAWRLAYFVPGTLHVVMGVLVLTLGQDLPDGNLRSLQKKGDVNRDSFSRVLWYAVTNYRTWIFVLLYGYSMGVELTTDNVIAEYFYDRFDLDLRVAGIIAASFGMANIVARPTGGLLSDLGARYFGMRARLWNIWILQTAGGAFCLLLGRASTLPTSVVCMVLFSFCAQAACGAIFGVIPFVSRRSLGIISGMTGAGGNFGAGLTQLLFFTSSRYSTGTGLEYMGIMIMACTLPVVLVHFPQWGSMFLPPNAGAEEEHYYGSEWSEQEKSKGLHGASLKFAENSRSERGRRNVINAAAAAATPPNNSPEHA
Protein: Glucagon receptor (GL-R) (P30082)
Organism: Rattus norvegicus (Rat)
Function: G-protein coupled receptor for glucagon that plays a central role in the regulation of blood glucose levels and glucose homeostasis. Regulates the rate of hepatic glucose production by promoting glycogen hydrolysis and gluconeogenesis. Plays an important role in mediating the responses to fasting. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Promotes activation of adenylate cyclase. Besides, plays a role in signaling via a phosphatidylinositol-calcium second messenger system.
Subcellular location: Cell membrane {ECO:0000269|PubMed:8384375}; Multi-pass membrane protein {ECO:0000269|PubMed:8384375}. Note=Is rapidly internalized after ligand-binding. {ECO:0000250|UniProtKB:P47871}.
Interaction partners:
- Pro-glucagon
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Neuroendocrine secretory protein 55
- Gastric inhibitory polypeptide
- Insulin-1
- Insulin-2
- Dipeptidyl peptidase 4
Sequence:
MLLTQLHCPYLLLLLVVLSCLPKAPSAQVMDFLFEKWKLYSDQCHHNLSLLPPPTELVCNRTFDKYSCWPDTPPNTTANISCPWYLPWYHKVQHRLVFKRCGPDGQWVRGPRGQSWRDASQCQMDDDEIEVQKGVAKMYSSYQVMYTVGYSLSLGALLLALVILLGLRKLHCTRNYIHGNLFASFVLKAGSVLVIDWLLKTRYSQKIGDDLSVSVWLSDGAVAGCRVATVIMQYGIIANYCWLLVEGVYLYSLLSITTFSEKSFFSLYLCIGWGSPLLFVIPWVVVKCLFENVQCWTSNDNMGFWWILRIPVLLAILINFFIFVRIIHLLVAKLRAHQMHYADYKFRLARSTLTLIPLLGVHEVVFAFVTDEHAQGTLRSTKLFFDLFFSSFQGLLVAVLYCFLNKEVQAELLRRWRRWQEGKALQEERMASSHGSHMAPAGTCHGDPCEKLQLMSAGSSSGTGCEPSAKTSLASSLPRLADSPT
Protein: WASH complex subunit 2A (Q641Q2)
Organism: Homo sapiens (Human)
Function: Acts at least in part as component of the WASH core complex whose assembly at the surface of endosomes inhibits WASH nucleation-promoting factor (NPF) activity in recruiting and activating the Arp2/3 complex to induce actin polymerization and is involved in the fission of tubules that serve as transport intermediates during endosome sorting. Mediates the recruitment of the WASH core complex to endosome membranes via binding to phospholipids and VPS35 of the retromer CSC. Mediates the recruitment of the F-actin-capping protein dimer to the WASH core complex probably promoting localized F-actin polymerization needed for vesicle scission. Via its C-terminus binds various phospholipids, most strongly phosphatidylinositol 4-phosphate (PtdIns-(4)P), phosphatidylinositol 5-phosphate (PtdIns-(5)P) and phosphatidylinositol 3,5-bisphosphate (PtdIns-(3,5)P2). Involved in the endosome-to-plasma membrane trafficking and recycling of SNX27-retromer-dependent cargo proteins, such as GLUT1. Required for the association of DNAJC13, ENTR1, ANKRD50 with retromer CSC subunit VPS35. Required for the endosomal recruitment of CCC complex subunits COMMD1 and CCDC93 as well as the retriever complex subunit VPS35L.
Subcellular location: Early endosome membrane {ECO:0000269|PubMed:28892079}. Cell membrane {ECO:0000250|UniProtKB:Q9Y4E1}.
Interaction partners:
- WASH complex subunit 1
- WASH complex subunit 5
- WASH complex subunit 4
- WASH complex subunit 3
- WASH complex subunit 2C
- F-actin-capping protein subunit beta
- F-actin-capping protein subunit alpha-1
- Vacuolar protein sorting-associated protein 35
- Coiled-coil domain-containing protein 93
- VPS35 endosomal protein-sorting factor-like
Sequence:
MMNRTTPDQELAPASEPVWERPWSVEEIRRSSQSWSLAADAGLLQFLQEFSQQTISRTHEIKKQVDGLIRETKATDCRLHNVFNDFLMLSNTQFIENRVYDEEVEEPVLKAEAEKTEQEKTREQKEVDLIPKVQEAVNYGLQVLDSAFEQLDIKAGNSDSEEDDANGRVELILEPKDLYIDRPLPYLIGSKLFMEQEDVGLGELSSEEGSVGSDRGSIVDTEEEKEEEESDEDFAHHSDNEQNRHTTQMSDEEEDDDGCDLFADSEKEEEDIEDIEENTRPKRSRPTSFADELAARIKGDAVGRVDEEPTTLPSGEAKPRKTLKEKKERRTPSDDEEDNLFAPPKLTDEDFSPFGSGGGLFSGGKGLFDDEDEESDLFTEAPQDRQAGASVKEESSSSKPGKKIPAGAVSVFLGDTDVFGAASVPSMKEPQKPEQPTPRKSPYGPPPTGLFDDDDGDDDDDFFSAPHSKPSKTGKVQSTADIFGDEEGDLFKEKAVASPEATVSQTDENKARAEKKVTLSSSKNLKPSSETKTQKGLFSDEEDSEDLFSSQSASKLKGASLLPGKLPTLVSLFDDEDEEDNLFGGTAAKKQTLCLQAQREEKAKASELSKKKASALLFSSDEEDQWNIPASQTHLASDSRSKGEPRDSGTLQSQEAKAVKKTSLFEEDEEDDLFAIAKDSQKKTQRVSLLFEDDVDSGGSLFGSPPTSVPPATKKKETVSEAPPLLFSDEEEKEAQLGVKSVDKKVESAKESLKFGRTDVAESEKEGLLTRSAQETVKHSDLFSSSSPWDKGTKPRTKTVLSLFDEEEDKMEDQNIIQAPQKEVGKGRDPDAHPKSTGVFQDEELLFSHKLQKDNDPDVDLFAGTKKTKLLEPSVGSLFGDDEDDDLFSSAKSQPLVQEKKRVVKKDHSVDSFKNQKHPESIQGSKEKGIWKPETPQDSSGLAPFKTKEPSTRIGKIQANLAINPAALLPTAASQISEVKPVLPELAFPSSEHRRSHGLESVPVLPGSGEAGVSFDLPAQADTLHSANKSRVKMRGKRRPQTRAARRLAAQESSETEDMSVPRGPIAQWADGAISPNGHRPQLRAASGEDSTEEALAAAAAPWEGGPVPGVDRSPFAKSLGHSRGEADLFDSGDIFSTGTGSQSVERTKPKAKIAENPANPPVGGKAKSPMFPALGEASSDDDLFQSAKPKPAKKTNPFPLLEDEDDLFTDQKVKKNETKSNSQQDVILTTQDIFEDDIFATEAIKPSQKTREKEKTLESNLFDDNIDIFADLTVKPKEKSKKKVEAKSIFDDDMDDIFSSGIQAKTTKPKSRSAQAAPEPRFEHKVSNIFDDPLNAFGGQ