wanglab/gogpt-training-data huggingface dataset:
Protein: N(2)-fixation sustaining protein CowN (CO weal-nitrogenase) (Q2RNI5)
Organism: Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1)
Function: Is required to sustain N(2)-dependent growth in the presence of low levels of carbon monoxide (CO). Probably acts by protecting the N(2) fixation ability of the nitrogenase complex, which is inactivated in the presence of CO. Is not required for CO-dependent growth.
Interaction partners:
- CO-responsive transcriptional regulator RcoM
Sequence:
MTMDGPAHMPRRYVTFQGVNVEGLSQQLIARILFHVADPAKSNAFWEHFKAKLADADKTLARTADSLCLLCGAIGYIDELFEDNDDEEGLTILRRLEDELC
Protein: Polybia-mastoparan-I (Polybia-MP-I) (Polybia-MPI) (Mastoparan I) (Mastoparan-1) (MP-1) (MP1) (P0C1Q4)
Organism: Polybia paulista (Neotropical social wasp) (Swarm-founding polistine wasp)
Function: Chemotactic peptide for polymorphonucleated leukocytes (PMNL), but causing no hemolysis to rat erythrocytes and no mast cell degranulation activity at physiological concentrations. Potent antimicrobial peptide against Gram-positive bacteria B.subtilis CCT 2576 (MIC=4 ug/ml), and S.aureus ATCC 6538 (MIC=15 ug/ml) and Gram-negative bacteria E.coli ATCC 25922 (MIC=8 ug/ml) and P.aeruginosa ATCC 15422 (MIC=8 ug/ml).
Subcellular location: Secreted {ECO:0000269|PubMed:16129513}. Target cell membrane {ECO:0000269|PubMed:18328599, ECO:0000269|PubMed:28965321}. Note=Has an amphipathic alpha-helical conformation in a lipid environment (Probable). May disrupt lipid membranes by forming pore-like structure (Probable). {ECO:0000305|PubMed:18328599, ECO:0000305|PubMed:28965321}.
Interaction partners:
Sequence:
IDWKKLLDAAKQIL
Protein: Non-structural protein NS2 (P0DJZ2)
Organism: Murine minute virus (strain MVM prototype) (MVM) (Murine minute virus (strain MVM(p)))
Function: Plays an essential role in viral protein synthesis. Plays also a role in active nuclear export of mature particles before host cell lysis, by interacting with host XPO1.
Subcellular location: Host nucleus {ECO:0000269|PubMed:12021369}.
Interaction partners:
Sequence:
MAGNAYSDEVLGATNWLKEKSNQEVFSFVFKNENVQLNGKDIGWNSYKKELQEDELKSLQRGAETTWDQSEDMEWETTVDEMTKKFGTLTIHDTEKYASQPELCTNSTCIGSRGPGFRALEHTKYSCCGHCRNPEHWGSWFQSLPRWSTEPNLVRDRGGFESVLRCGTVEERLQRAAELGLRYDGASS
Protein: Pentapeptide repeat-containing protein (Q38AK5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MERCLSLGVISRLLDALNLRRKVALLSLPFETSMIRVGKNLDSHRVSSSASPSPAVPYAKLLSFPLEAEMEVQPLVRGAVLEALGESTGGQRAADGGCRRVESVRSKEIEIGSILEGRCFSSLDFACTNLSASFNRCALVSASLGGAFVSHSTFNLTDIRRSSFIGAQFHSCTFLATDAVGVDARCGRFSHCTFCRASMSGWDVRGATFYRCTFTMCDMSGWTYDSQTTVVEPVGWECCRRLNWVPFGEGAVGDCRVVREQGGERGLSLRPREHPPWVK
Protein: Ly6/PLAUR domain-containing protein 5 (Q6UWN5)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- phospholipase A2 inhibitor and Ly6/PLAUR domain-containing protein
Sequence:
MAMGVPRVILLCLFGAALCLTGSQALQCYSFEHTYFGPFDLRAMKLPSISCPHECFEAILSLDTGYRAPVTLVRKGCWTGPPAGQTQSNADALPPDYSVVRGCTTDKCNAHLMTHDALPNLSQAPDPPTLSGAECYACIGVHQDDCAIGRSRRVQCHQDQTACFQGNGRMTVGNFSVPVYIRTCHRPSCTTEGTTSPWTAIDLQGSCCEGYLCNRKSMTQPFTSASATTPPRALQVLALLLPVLLLVGLSA
Protein: GTPase IMAP family member 5 (Immunity-associated nucleotide 4 protein) (IAN-4) (Immunity-associated nucleotide 4-like 1 protein) (Q8K3L6)
Organism: Rattus norvegicus (Rat)
Function: Required for mitochondrial integrity and T-cell survival. May contribute to T-cell quiescence.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:28223986}; Single-pass type IV membrane protein {ECO:0000269|PubMed:28223986}. Endosome, multivesicular body membrane {ECO:0000269|PubMed:21487483}; Single-pass type IV membrane protein {ECO:0000305}. Endosome membrane {ECO:0000269|PubMed:28223986}; Single-pass type IV membrane protein {ECO:0000269|PubMed:28223986}.
Interaction partners:
- Histocompatibility 2, class II antigen E alpha
Sequence:
MEDHGFEELSTRTHDLNVRRLTKGNINFLLSTGQETYSVEDSGLLRILLVGKSGCGKSATGNSILRRPAFESRLRGQSVTRTSQAEMGTWEGRSFLVVDTPPIFESKIQNQDMDKDIGNCYLMCAPGPHVLLLVTQLGRYTVEDAMAVRMVKQIFGVGVMRYMIVLFTHKEDLADESLEEFVTHTGNLDLHRLVQECGRRYCAFNNKASGEEQQGQLAELMALVRRLEQEHEGSFHSNDLFVYTQVFLRGGYSEHQEPYKFYLTKVRQEVEKQKRELEEQEGSWMAKMLCRVTSCLDWHIAVSVLLIVLGLTLLITLINMYIGRWK
Protein: Small ubiquitin-related modifier 1 (SUMO-1) (A7WLH8)
Organism: Sus scrofa (Pig)
Function: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3.
Subcellular location: Nucleus membrane {ECO:0000250|UniProtKB:P63165}. Nucleus speckle {ECO:0000250|UniProtKB:P63166}. Cytoplasm {ECO:0000250|UniProtKB:P63165}. Nucleus, PML body {ECO:0000250|UniProtKB:P63165}. Cell membrane {ECO:0000250|UniProtKB:P63165}. Nucleus {ECO:0000250|UniProtKB:P63165}. Note=Recruited by BCL11A into the nuclear body (By similarity). In the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the nucleus some of which overlap or closely associate with PML body (By similarity). {ECO:0000250|UniProtKB:P63165, ECO:0000250|UniProtKB:P63166}.
Interaction partners:
- E3 SUMO-protein ligase RanBP2
- SUMO-conjugating enzyme UBC9
- Protein inhibitor of activated STAT 1.
- Protein inhibitor of activated STAT 4.
- Cellular tumor antigen p53
- SUMO specific peptidase 1.
- protein kinase C
- Small ubiquitin-related modifier
- Small ubiquitin-related modifier 2
- SUMO specific peptidase 5
Sequence:
MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTGGHSTV
Protein: Dendrocyte expressed seven transmembrane protein (D3ZVC2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Osteoclast stimulatory transmembrane protein
- Cathepsin K
- Nuclear factor of activated T-cells 1
- Tumor necrosis factor ligand superfamily member 11
- V-type proton ATPase subunit d 2
- Matrix metalloproteinase-9
Sequence:
MGLWALGTSVFLRLWGTYVFPGSTAWTNFIQHLGVCCFVALLSVSLLSAALYWVLPSAALLSAVWMATCVFLCCSKHARCFILLAIVSCGLREGRNTLLAAGTGVVIFGHVENIFSNFRGLLDSMTCNLRAKNFSTHFPLLKRYIEAIEWIYGLTTPLNVLDDLVSWNQTLAVSLFSPSHALQAHMNDTRGEVLSVLHRMVLTTELLTSVGQKLLALAGLLLILVSTGLFLKRFLGPCGWKYENVYITRQFVLFDEEERCQQRPCVLPLNRKERKKYIIVPSLKLTPKERRNLGLFFLPVLTYLYMWMLFATVDYLLYRLISSVNKQFQSLPGLEVHLRLHGEKQGTHGVIHDSAFNISMFEPSCILKPRLSVSQTWVPLSIILLTLVILGLLSSMLMQLKILVSVSFYPKVERERIEYLHAKLLEKRSKQPLGEADRKLSLYFKKIHFWLPVLKMTRKKHMIPANEDDP
Protein: Heat shock protein 12.6 (SHSP domain-containing protein) (G5EE36)
Organism: Caenorhabditis elegans
Interaction partners:
- Heat shock protein Hsp-16.1/Hsp-16.11
- Heat shock protein Hsp-16.48/Hsp-16.49
- Stress-induced protein 1
- Heat shock protein hsp-16.2
- Heat shock transcription factor hsf-1
- Heat shock protein Hsp-16.41
- Forkhead box protein O
- Superoxide dismutase 2, mitochondrial
- Metallothionein-1
- Heat shock protein 70
Sequence:
MMSVPVMADEGTKWDWPLQKGDGVVNVLDDDDHFEVGLEAHNFLPKEIEVKNIGELLEIHMEHNVKKDSFGDVSRNITRCYKLPKNVDMKTIKSNLDSHGILHIEARKMH
Protein: NF-kappa-B essential modulator (NEMO) (IkB kinase-associated protein 1) (IKKAP1) (mFIP-3) (Inhibitor of nuclear factor kappa-B kinase subunit gamma) (I-kappa-B kinase subunit gamma) (IKK-gamma) (IKKG) (IkB kinase subunit gamma) (NF-kappa-B essential modifier) (O88522)
Organism: Mus musculus (Mouse)
Function: Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. Its binding to scaffolding polyubiquitin plays a key role in IKK activation by multiple signaling receptor pathways. Can recognize and bind both 'Lys-63'-linked and linear polyubiquitin upon cell stimulation, with a much highr affinity for linear polyubiquitin. Could be implicated in NF-kappa-B-mediated protection from cytokine toxicity. Essential for viral activation of IRF3. Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9Y6K9}. Nucleus {ECO:0000250|UniProtKB:Q9Y6K9}. Note=Sumoylated NEMO accumulates in the nucleus in response to genotoxic stress. {ECO:0000250|UniProtKB:Q9Y6K9}.
Interaction partners:
- Mitogen-activated protein kinase kinase kinase 7
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 3
- TNF receptor-associated factor 6
- Receptor-interacting serine/threonine-protein kinase 1
- TNF receptor-associated factor 2
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 2
- Toll-like receptor 4
- B-cell lymphoma/leukemia 10
Sequence:
MNKHPWKNQLSEMVQPSGGPAEDQDMLGEESSLGKPAMLHLPSEQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHESARIEDMRKRHVETPQPPLLPAPAHHSFHLALSNQRRSPPEEPPDFCCPKCQYQAPDMDTLQIHVMECIE
Protein: Histone deacetylase 11 (HD11) (EC 3.5.1.98) (Q96DB2)
Organism: Homo sapiens (Human)
Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes.
Subcellular location: Nucleus {ECO:0000269|PubMed:11948178}.
Interaction partners:
- Protein deacetylase HDAC6
- Histone acetyltransferase KAT2B
- Nuclear receptor corepressor 1
- NAD-dependent protein deacetylase sirtuin-1
- Histone acetyltransferase p300
- Nuclear receptor corepressor 2
- Histone H2A type 2-A
- Histone H2A type 2-C
- Histone H2B type 2-E
- Paired amphipathic helix protein Sin3a
Sequence:
MLHTTQLYQHVPETRWPIVYSPRYNITFMGLEKLHPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKWSFAVATITEIPPVIFLPNFLVQRKVLRPLRTQTGGTIMAGKLAVERGWAINVGGGFHHCSSDRGGGFCAYADITLAIKFLFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYNRHIYPGDRFAKQAIRRKVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVKRDELVFRMVRGRRVPILMVTSGGYQKRTARIIADSILNLFGLGLIGPESPSVSAQNSDTPLLPPAVP
Protein: Pentalenolactone synthase (EC 1.14.19.8) (Pentalenolactone biosynthesis protein M) (E3VWI3)
Organism: Streptomyces arenae
Function: Catalyzes the final step in the biosynthesis of the sesquiterpenoid antibiotic pentalenolactone by mediating the oxidative rearrangement of pentalenolactone F to pentalenolactone.
Interaction partners:
Sequence:
MTDLPRLPFDNPDIMGIAPQMLALQKEGPIARVGTAGEDAWLVTRYDEVRTLLADRRLRLSNPNPQPSAKSAARAFMVALMAGDDHETEPARHAQMRSLLIPRFSTRRLRLMKTRIEHHVDELLDQLAASAPPVDLHRVLSFRLPTMVVCDLLGVPLADRERFGQWARGTFDQSDNEHSANTFQQVVDYMLELVARKRVEPGDDILSELIAEKDGALSDADIAHLGNAVLLFGYETTIVRIDLGTLLLLRNPVQRAQLAEDPGLAPAAVEEILRLGVGGKGSNALIPRYAHGDITVGETVIRTGDAVMLAIGAANYDDRAFPDGGLFDLTRVRPRSHLAFGHGARHCIGRTLARIELTAVFERLFRRLPDLRLAVPEESLRWQEHRITGGFDEIPVTF
Protein: Vigilin (High density lipoprotein-binding protein) (HDL-binding protein) (Q00341)
Organism: Homo sapiens (Human)
Function: Appears to play a role in cell sterol metabolism. It may function to protect cells from over-accumulation of cholesterol.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8605996}. Nucleus {ECO:0000269|PubMed:8605996}.
Interaction partners:
- Lipoprotein lipase
- Apolipoprotein A-I
- Cholesteryl ester transfer protein
- Apolipoprotein A-II
- Apolipoprotein A-IV
- Apolipoprotein C-III
- Apolipoprotein A-V
- Apolipoprotein B-100
- Small ribosomal subunit protein RACK1
- Apolipoprotein C-II
Sequence:
MSSVAVLTQESFAEHRSGLVPQQIKVATLNSEEESDPPTYKDAFPPLPEKAACLESAQEPAGAWGNKIRPIKASVITQVFHVPLEERKYKDMNQFGEGEQAKICLEIMQRTGAHLELSLAKDQGLSIMVSGKLDAVMKARKDIVARLQTQASATVAIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPDDPSNQIKITGTKEGIEKARHEVLLISAEQDKRAVERLEVEKAFHPFIAGPYNRLVGEIMQETGTRINIPPPSVNRTEIVFTGEKEQLAQAVARIKKIYEEKKKKTTTIAVEVKKSQHKYVIGPKGNSLQEILERTGVSVEIPPSDSISETVILRGEPEKLGQALTEVYAKANSFTVSSVAAPSWLHRFIIGKKGQNLAKITQQMPKVHIEFTEGEDKITLEGPTEDVNVAQEQIEGMVKDLINRMDYVEINIDHKFHRHLIGKSGANINRIKDQYKVSVRIPPDSEKSNLIRIEGDPQGVQQAKRELLELASRMENERTKDLIIEQRFHRTIIGQKGERIREIRDKFPEVIINFPDPAQKSDIVQLRGPKNEVEKCTKYMQKMVADLVENSYSISVPIFKQFHKNIIGKGGANIKKIREESNTKIDLPAENSNSETIIITGKRANCEAARSRILSIQKDLANIAEVEVSIPAKLHNSLIGTKGRLIRSIMEECGGVHIHFPVEGSGSDTVVIRGPSSDVEKAKKQLLHLAEEKQTKSFTVDIRAKPEYHKFLIGKGGGKIRKVRDSTGARVIFPAAEDKDQDLITIIGKEDAVREAQKELEALIQNLDNVVEDSMLVDPKHHRHFVIRRGQVLREIAEEYGGVMVSFPRSGTQSDKVTLKGAKDCVEAAKKRIQEIIEDLEAQVTLECAIPQKFHRSVMGPKGSRIQQITRDFSVQIKFPDREENAVHSTEPVVQENGDEAGEGREAKDCDPGSPRRCDIIIISGRKEKCEAAKEALEALVPVTIEVEVPFDLHRYVIGQKGSGIRKMMDEFEVNIHVPAPELQSDIIAITGLAANLDRAKAGLLERVKELQAEQEDRALRSFKLSVTVDPKYHPKIIGRKGAVITQIRLEHDVNIQFPDKDDGNQPQDQITITGYEKNTEAARDAILRIVGELEQMVSEDVPLDHRVHARIIGARGKAIRKIMDEFKVDIRFPQSGAPDPNCVTVTGLPENVEEAIDHILNLEEEYLADVVDSEALQVYMKPPAHEEAKAPSRGFVVRDAPWTASSSEKAPDMSSSEEFPSFGAQVAPKTLPWGPKR
Protein: Enhancer of polycomb-like protein 1 (Q9UU94)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. Involved in gene silencing by neighboring heterochromatin, blockage of the silencing spreading along the chromosome, and required for cell cycle progression through G2/M (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- SWR1-complex protein 4
- Protein AF-9 homolog
- Probable chromatin modification-related protein eaf7
- Chromatin modification-related protein png1
- Histone acetyltransferase mst1
- Chromatin modification-related protein eaf6
- Chromatin modification-related protein eaf3
- NuA4 acetyltransferase complex subunit Tra2
- Chromatin modification-related protein vid21
- Actin
Sequence:
MSSVSKNARAYRQRKVGIKTVMPIYFERDIPDFDEEASLQRTVPLVESGVEKEEEEEKHLQQVINEAHEAIVRGSEKKLIIPTREAKNIGIIDKYYKKNFILPKTLIRFSLTVEECTNPEYCMDEHDTEYFLKLKQAQPSLSKFSELDFEIVMQTFEEEINQNQPFLSMDTSQILPLSELITSFELKDVLYLKPLASQVYPYWRERRISKGGLPIMAKAQVGDDKDDDDPYVCFRRREIRQARKTRRSDAQSYDRLRRLRQSMETSLQLLEQVYKREQKKLQALEDDYAIFQKRCLVKKLKRTLNIKDSDELLINPKRRPIEVKPAAPVPTPAPPVKTSPHPASYRPQPTRNVEVRPLLMLDDVQSAQITQFQIRLQQRLTKKEQLDRNWVDLLETPSTVIHTNYPDSFYRNIIPYYSGKETKQSHNQLSIPSSTPSTPLSDNGPTYSTPHSSLSNFNTCDSLSFSSNNSLYGYSTLLHPRNPICVRQRIGRGGRLMLDRTRALPVHRLSKPKSRVEDRWLFDIPFDADDTIILDDESDASIMFRASLLNDDMGTQS
Protein: BHLH domain-containing protein (Q75H21)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MQGDPGYGYGGYGYGYGYGYGGAGYDMAGYGGGGGGYYTSDPYNAAPAAYEDPLAVAGRRQHDFPAPLTGVEFQPSDTCPKNYVIFDQTYDRSRVMFHPSLANNLGNSGGGYDHHHHCGYGGFEQDYASKSAYYGVEDDGGGGCSIRQKEDTDEIDALMSTEDGEEEDDVLSTGRTPGCRAGGSPDSTCSSGASRSDCGGGRKPEAGGGERKKERMKKMMRTLKGIIPGGDRMDTPAVLDEAVRYLKSLKVEVKKLGPVRRRRRRNSSRAPPPLWSSSSLGMVAVGFAKLLPSSSRPPFPPKIAGAPLSPSTRTSPPPRPRRRHCRLSSIVVRALGEFAASPSTRRCCPFAPPRRHSPASTRCRAAIGNDVIVDVSATSAVDPW
Protein: Melanocortin-2 receptor accessory protein 2 (MC2R accessory protein 2) (Q96G30)
Organism: Homo sapiens (Human)
Function: Modulator of melanocortin receptor 4 (MC4R), a receptor involved in energy homeostasis. Plays a central role in the control of energy homeostasis and body weight regulation by increasing ligand-sensitivity of MC4R and MC4R-mediated generation of cAMP (By similarity). May also act as a negative regulator of MC2R: competes with MRAP for binding to MC2R and impairs the binding of corticotropin (ACTH) to MC2R. May also regulate activity of other melanocortin receptors (MC1R, MC3R and MC5R); however, additional evidence is required in vivo.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19329486}; Single-pass membrane protein {ECO:0000269|PubMed:19329486}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:19329486}; Single-pass membrane protein {ECO:0000269|PubMed:19329486}. Note=The formation of antiparallel homo- and heterodimers suggest that N- and C-terminus can both localize in the cytoplasmic and extracellular parts, depending on the context. {ECO:0000269|PubMed:20371771}.
Interaction partners:
- Adrenocorticotropic hormone receptor
- Melanocortin receptor 4
- Melanocortin receptor 5
- Melanocortin receptor 3
- Prokineticin receptor 1
- Melanocyte-stimulating hormone receptor
Sequence:
MSAQRLISNRTSQQSASNSDYTWEYEYYEIGPVSFEGLKAHKYSIVIGFWVGLAVFVIFMFFVLTLLTKTGAPHQDNAESSEKRFRMNSFVSDFGRPLEPDKVFSRQGNEESRSLFHCYINEVERLDRAKACHQTTALDSDVQLQEAIRSSGQPEEELNRLMKFDIPNFVNTDQNYFGEDDLLISEPPIVLETKPLSQTSHKDLD
Protein: Zinc finger protein 4 (Q39263)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as negative regulator of abscisic acid (ABA) signaling during germination and early seedling development.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q39261}.
Interaction partners:
- C2H2-type zinc finger family protein
Sequence:
MRPILDLEIEASSGSSSSQVASNLSPVGEDYKPISLNLSLSFNNNNNNNLDLESSSLTLPLSSTSESSNPEQQQQQQPSVSKRVFSCNYCQRKFYSSQALGGHQNAHKRERTLAKRAMRMGLAGVFPGRGSSSNYAAAATAAALSCLPLHGSGNGNMTSFRTLGIRAHSSAHDVSMTRQTPETLIRNIARFNQGYFGNCIPFYVEDDEAEMLWPGSFRQATNAVAVEAGNDNLGERKMDFLDVKQAMDMESSLPDLTLKL
Protein: Ephrin-A3 (EFL-2) (EHK1 ligand) (EHK1-L) (EPH-related receptor tyrosine kinase ligand 3) (LERK-3) (P52797)
Organism: Homo sapiens (Human)
Function: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling (By similarity).
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Ephrin type-A receptor 1
- Ephrin type-A receptor 4
- Ephrin type-A receptor 2
- Ephrin type-A receptor 3
- Ephrin type-A receptor 5
- Ephrin type-A receptor 10
- Ephrin type-A receptor 7
- Ephrin type-A receptor 8
- Ras GTPase-activating protein 1
- Tyrosine-protein kinase Fyn
Sequence:
MAAAPLLLLLLLVPVPLLPLLAQGPGGALGNRHAVYWNSSNQHLRREGYTVQVNVNDYLDIYCPHYNSSGVGPGAGPGPGGGAEQYVLYMVSRNGYRTCNASQGFKRWECNRPHAPHSPIKFSEKFQRYSAFSLGYEFHAGHEYYYISTPTHNLHWKCLRMKVFVCCASTSHSGEKPVPTLPQFTMGPNVKINVLEDFEGENPQVPKLEKSISGTSPKREHLPLAVGIAFFLMTFLAS
Protein: Uncharacterized protein (Q57YZ2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTDTTKGALKRSNTLFLSDAEQFVFDFGGSAGGRAVSPGSSHGSGGQPGEGDGEKGIEETDLANGRTGVVTPFSERERTAPVAPLDAEEVQRYFDKALKGGRRILLENVPLDEAIEKFQLGLRRYEEWLCNQANSRNRGDSSKSRGDPLNEGYRGKPGDVARDAKDRKRPRL
Protein: Myocyte enhancer factor 2C (A0A0D9SFD0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSTNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVEALNKKENKGCESPDPDSSYALTPRTEEKYKKINEEFDNMIKSHKIPAVPPPNFEMPVSIPVSSHNSLVYSNPVSSLGNPNLLPLAHPSLQRNSMSPGVTHRPPSAGNTGGLMGGDLTSGAGTSAGNGYGNPRNSPGLLVSPGNLNKNMQAKSPPPMNLGMNNRKPDLRVLIPPGSKNTMPSVNQRINNSQSAQSLATPVVSVATPTLPGQGMGGYPSAISTTYGTEYSLSSADLSSLSGFNTASALHLGSVTGWQQQHLHNMPPSALSQLGDRTTTPSRYPQHTRHEAGRSPVDSLSSCSSSYDGSDREDHRNEFHSPIGLTRPSPDERESPSVKRMRLSEGWAT
Protein: CYP enzymes assisting alcohol dehydrogenase (CrCYPADH) (EC 1.1.1.-) (Alcohol dehydrogenase 2) (A0A0C5DM37)
Organism: Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)
Function: May be a positive catalyzer of strictosidine production by assisting secologanin biosynthesis, thus being involved in monoterpene indole alkaloids accumulation.
Interaction partners:
Sequence:
MQIITCKAVVCWAAGEPPVVEEILVEPPRSGEVRIKILFASLCHTDVLACKGFPTPMFPRVLGHEGVGVVECVGEGVSELREGDVVIPTYLGECGECENCESGRTNLCRTYPLQAFTGLMPDGSSRMSSAKGGEMLYQFLSCSTWSEYTVIDANYAVKIDSRIPLPHASFLSCGFTTGFGATWKEAKLQEGSSTVAVLGLGAVGLGAVEGARVQGVTQIIGIDINDNKREKGEAFGMTHFINPKKDNNKSISELVKELTKGQGVDVCFECTGVPDLVNEALESTKIGTGNMIMLGAGTQKSMTINFVSLLGCRTFKYSVFGGVKVQSDLPLIIQKCLNKEIQKIEQLLTHQVQLEDINRAFELLKEPDCVKVLITL
Protein: RNA-binding protein 8A (RNA-binding motif protein 8A) (Ribonucleoprotein RBM8A) (Q9CWZ3)
Organism: Mus musculus (Mouse)
Function: Required for pre-mRNA splicing as component of the spliceosome (By similarity). Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Its removal from cytoplasmic mRNAs requires translation initiation from EJC-bearing spliced mRNAs. Associates preferentially with mRNAs produced by splicing. Does not interact with pre-mRNAs, introns, or mRNAs produced from intronless cDNAs. Associates with both nuclear mRNAs and newly exported cytoplasmic mRNAs (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9Y5S9}. Nucleus speckle {ECO:0000250|UniProtKB:Q9Y5S9}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y5S9}. Note=Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles. {ECO:0000250|UniProtKB:Q9Y5S9}.
Interaction partners:
- Protein CASC3
- Protein mago nashi homolog 2
- Eukaryotic initiation factor 4A-III
- Protein mago nashi homolog
- Partner of Y14 and mago
- Regulator of nonsense transcripts 2
- Regulator of nonsense transcripts 1
- UPF3 regulator of nonsense transcripts homolog B
- Eukaryotic initiation factor 4A-III
- Serine/arginine-rich splicing factor 1
Sequence:
MADVLDLHEAGGEDFAMDEDGDESIHKLKEKAKKRKGRGFGSEEGSRARMREDYDSVEQDGDEPGPQRSVEGWILFVTGVHEEATEEDIHDKFAEYGEIKNIHLNLDRRTGYLKGYTLVEYETYKEAQAAMEGLNGQDLMGQPISVDWCFVRGPPKGKRRGGRRRSRSPDRRRR
Protein: Protein tyrosine phosphatase Ptpmeg (Q9NHZ3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
AGAGTILTITKTSRPHDNKVTSKEADSMPRKAWEQQSDEYDIQLDVGFIEQCTRRFESASPSPMPPAYSSGQHSPILLPTTIADAVGHQQPESGSDLITIRLQADEQGRYGFNVKGGVDLSLPVQVSKVVPHTPADRCTPRVCEGDEVLMINGRDVHGLRHEQVVAMIRDCRHQASGELLLTVRPQRSAPLLLEEEPLYQYVPESDEIGSHSNLLDGDALFTQSLLLLSDGLASGALLAQYELMYRKNPDLAITEARKPANAPKNRYRDISPYDCTRVSLVNSLTGDYINANYVNMEIPGGAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGEELQLAEGFSVRCLSEKPDETGSFVFREFVLKDKHEQRHIHHMQYLAWPDHCVPSDPNLFLEFTERVRAARNRTLLQEIEESLKQVRLMDADADADENGGLMRERKCAASNGATPEDETPVSTSVHQCISAANPPVIVHCSAGIGRTGVLILMDTALALMEAR