wanglab/gogpt-training-data huggingface dataset:
Protein: Contactin-2 (Axonal glycoprotein TAG-1) (Axonin-1) (Transient axonal glycoprotein 1) (TAX-1) (Q02246)
Organism: Homo sapiens (Human)
Function: In conjunction with another transmembrane protein, CNTNAP2, contributes to the organization of axonal domains at nodes of Ranvier by maintaining voltage-gated potassium channels at the juxtaparanodal region. May be involved in cell adhesion.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor. Note=Attached to the neuronal membrane by a GPI-anchor and is also released from neurons.
Interaction partners:
- Contactin-associated protein-like 2
- Neuronal cell adhesion molecule
- Tax1-binding protein 1
- Neural cell adhesion molecule L1
- Potassium voltage-gated channel subfamily A member 1
- Neural cell adhesion molecule 1
- Amyloid-beta precursor protein
- Contactin-associated protein 1
- Leucine-rich glioma-inactivated protein 1
- Potassium voltage-gated channel subfamily A member 2
Sequence:
MGTATRRKPHLLLVAAVALVSSSAWSSALGSQTTFGPVFEDQPLSVLFPEESTEEQVLLACRARASPPATYRWKMNGTEMKLEPGSRHQLVGGNLVIMNPTKAQDAGVYQCLASNPVGTVVSREAILRFGFLQEFSKEERDPVKAHEGWGVMLPCNPPAHYPGLSYRWLLNEFPNFIPTDGRHFVSQTTGNLYIARTNASDLGNYSCLATSHMDFSTKSVFSKFAQLNLAAEDTRLFAPSIKARFPAETYALVGQQVTLECFAFGNPVPRIKWRKVDGSLSPQWTTAEPTLQIPSVSFEDEGTYECEAENSKGRDTVQGRIIVQAQPEWLKVISDTEADIGSNLRWGCAAAGKPRPTVRWLRNGEPLASQNRVEVLAGDLRFSKLSLEDSGMYQCVAENKHGTIYASAELAVQALAPDFRLNPVRRLIPAARGGEILIPCQPRAAPKAVVLWSKGTEILVNSSRVTVTPDGTLIIRNISRSDEGKYTCFAENFMGKANSTGILSVRDATKITLAPSSADINLGDNLTLQCHASHDPTMDLTFTWTLDDFPIDFDKPGGHYRRTNVKETIGDLTILNAQLRHGGKYTCMAQTVVDSASKEATVLVRGPPGPPGGVVVRDIGDTTIQLSWSRGFDNHSPIAKYTLQARTPPAGKWKQVRTNPANIEGNAETAQVLGLTPWMDYEFRVIASNILGTGEPSGPSSKIRTREAAPSVAPSGLSGGGGAPGELIVNWTPMSREYQNGDGFGYLLSFRRQGSTHWQTARVPGADAQYFVYSNESVRPYTPFEVKIRSYNRRGDGPESLTALVYSAEEEPRVAPTKVWAKGVSSSEMNVTWEPVQQDMNGILLGYEIRYWKAGDKEAAADRVRTAGLDTSARVSGLHPNTKYHVTVRAYNRAGTGPASPSANATTMKPPPRRPPGNISWTFSSSSLSIKWDPVVPFRNESAVTGYKMLYQNDLHLTPTLHLTGKNWIEIPVPEDIGHALVQIRTTGPGGDGIPAEVHIVRNGGTSMMVENMAVRPAPHPGTVISHSVAMLILIGSLEL
Protein: NAC domain-containing protein 77 (ONAC077) (NAC domain-containing protein 300) (ONAC300) (Q5CD17)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable transcription factor involved in stress response (By similarity). Binds to DNA-specific sequences of CLPD1 and OAT promoters in vitro.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353}.
Interaction partners:
Sequence:
MVESTTSLVKLEQDGGLFLPPGFRFHPTDAEVILSYLLQKLLNPSFTSLPIGEVDLNKCEPWDLPSKAKMGEKEWYFFSHKDMKYPTGMRTNRATKEGYWKATGKDREIFRQPAAVNTSSYGGSSNKKKQLVGMKKTLVFYMGRAPKGTKTNWVMHEFRLHANLHNHHPNLRLNPKDEWVVCKVFHKKQGDEAINNQQQQPQYAAVDQYSAETPNSGSSVVQAGDIDGGDDFFQLDDIIDPSIYFVSNSSNILSAPPNNNNAVYSVSASTTTTNTTAVSFQQQPNYYSLINKSSSSSSSNYSAPLQQHVSSWNITPGAGGAHGIGSSYYNLQQQQAAMVKALENVIAVPNFGTLLPSSNKLKGLSKSAMAGLTQQNPLGVPQYKIENYGDHYISRQ
Protein: Cerebellin-2 (Q8BGU2)
Organism: Mus musculus (Mouse)
Function: Acts as a synaptic organizer in specific subsets of neurons in the brain. Essential for long-term maintenance but not establishment of excitatory synapses.
Subcellular location: Secreted {ECO:0000269|PubMed:17030622, ECO:0000269|PubMed:17331201, ECO:0000269|PubMed:29782851, ECO:0000269|PubMed:34135511}.
Interaction partners:
Sequence:
MPAPGQGPRGPLLSMPGRRGALREPADFGSSLGAVLALLLLLLPACCPVRAQNDTEPIVLEGKCLVVCDSSPSGDGAVTSSLGISVRSGSAKVAFSATRSTNHEPSEMSNRTMTIYFDQVLVNIGNHFDLASSIFVAPRKGIYSFSFHVVKVYNRQTIQVSLMQNGYPVISAFAGDQDVTREAASNGVLLLMEREDKVHLKLERGNLMGGWKYSTFSGFLVFPL
Protein: Doublesex- and mab-3-related transcription factor 3 (Q80WT2)
Organism: Mus musculus (Mouse)
Function: Probable transcription factor that plays a role in configuring the spinal circuits controlling stride in vertebrates. Involved in neuronal specification within specific subdivision of spinal cord neurons and in the development of a coordinated locomotor network controlling limb movements. May regulate transcription during sexual development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00070}.
Interaction partners:
Sequence:
MNGYGSPYLYMGGPVSQPPRAPLQRTPKCARCRNHGVLSWLKGHKRYCRFKDCTCEKCILIIERQRVMAAQVALRRQQANESLESLIPDSLRALPGPPPPGDAAATAATASQSSPASQASQPPAPPRPTAELAAAAALRWVAEPQPGTLPAQLAKPDLTEERVGDSSSTDNTAEAFSDKDTDQRSSPDVVKSKNCFTPESPEIVSVDEGGYAVQKNGGNPESCPDSPKYHAEQSHLLIEGPSGTVSLPFSLKANRPPLEVLKKIFPNQKPTVLELILKGCGGDLVSAVEVLLSSRSSAAGAERTAEESLVLPSSGHIFEHTLGSYPISSSKWSVGSAFRVPDTLRFSADSSNVVPNPLAVPLQHPFPQPPRYPLMLRNTLARNQSSPFLPNDVTLWNTMTLQQQYQLRSQYVSPFPSNSTSVFRSSPVLSSRTTEDPRISIPDDGCPIVTKQSIYTEDDYDERSDSSDSRILNTSS
Protein: Potassium channel toxin alpha-KTx 15.6 (Discrepin) (P84777)
Organism: Tityus discrepans (Venezuelan scorpion)
Function: Irreversibly blocks the A-type voltage-gated potassium channels in rat cerebellum granular cells (190 nM induce 50% inhibitory effect) (IC(50)=190 nM). Also weakly inhibits Kv1.2/KCNA2 and Kv1.3/KCNA3.
Subcellular location: Secreted {ECO:0000269|PubMed:15369825}.
Interaction partners:
Sequence:
MKAFYGMLVIFILCSTCYISVDSQIDTNVKCSGSSKCVKICIDRYNTRGAKCINGRCTCYP
Protein: Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform (PP2A B subunit isoform B'-gamma) (PP2A B subunit isoform B56-gamma) (PP2A B subunit isoform PR61-gamma) (PP2A B subunit isoform R5-gamma) (Renal carcinoma antigen NY-REN-29) (Q13362)
Organism: Homo sapiens (Human)
Function: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. The PP2A-PPP2R5C holoenzyme may specifically dephosphorylate and activate TP53 and play a role in DNA damage-induced inhibition of cell proliferation. PP2A-PPP2R5C may also regulate the ERK signaling pathway through ERK dephosphorylation.
Subcellular location: Nucleus. Chromosome, centromere.
Interaction partners:
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- Shugoshin 1
- Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- Protein phosphatase methylesterase 1
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit alpha
Sequence:
MLTCNKAGSRMVVDAANSNGPFQPVVLLHIRDVPPADQEKLFIQKLRQCCVLFDFVSDPLSDLKWKEVKRAALSEMVEYITHNRNVITEPIYPEVVHMFAVNMFRTLPPSSNPTGAEFDPEEDEPTLEAAWPHLQLVYEFFLRFLESPDFQPNIAKKYIDQKFVLQLLELFDSEDPRERDFLKTTLHRIYGKFLGLRAYIRKQINNIFYRFIYETEHHNGIAELLEILGSIINGFALPLKEEHKIFLLKVLLPLHKVKSLSVYHPQLAYCVVQFLEKDSTLTEPVVMALLKYWPKTHSPKEVMFLNELEEILDVIEPSEFVKIMEPLFRQLAKCVSSPHFQVAERALYYWNNEYIMSLISDNAAKILPIMFPSLYRNSKTHWNKTIHGLIYNALKLFMEMNQKLFDDCTQQFKAEKLKEKLKMKEREEAWVKIENLAKANPQYTVYSQASTMSIPVAMETDGPLFEDVQMLRKTVKDEAHQAQKDPKKDRPLARRKSELPQDPHTKKALEAHCRADELASQDGR
Protein: cysteine--tRNA ligase (EC 6.1.1.16) (Cysteinyl-tRNA synthetase) (Q8IJP3)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- N-acetylglucosaminylphosphatidylinositol deacetylase
Sequence:
MNLFLFICIALFIYLDKFHLPNSLKYNFKRSLLLKLGHQQTVLSKNSEATKSGGMFFIRNSFLYRNKNFLKIDKYIFKRLFHSKMDNANKLPKWNQPSKEGKKITNLFVNNSLTHSKVEFIPQEGNKIKWYACGPTVYDAAHLGHARTYVSFDIIRRILVNYFKYDVFMVINITDIDDKIIKRSVEEKIGFTELARKWEYEFWEDMKSLNVLLPTAITRVSEYVGDIVKYIEKIIENKYAYVSEEGSVYFDIDEFKKSEKHFYARMEPLSVKDENKILEGEGDLGVISKKKKNAYDFALWKSSKPNEPHWDSPWGKGRPGWHIECSTMASNILGDVLDIHSGGIDLRFPHHDNELAQSEAFFDHSQWVNYFLHSGHLHIEGLKMSKSLKNFITIKNMLTKYTSNQIRILFLLNKWDNFMNYSPNGESMVQCIEIDKSFTNFFAIILMKIKNFDLNSCNLYWSDADNKLNLLFRQTKNKIHEHFLDNFNTPDALLAIQKLITEINIYMDKEKIQIGLLLEIKHYINFIFDTFGLIYGDAPKGKYDKFDELLQTLGTYRRNIRINLQSNAKLIRNILKEKNKKNDLDPVAAQEKSELLHSEFINNIKANNELLLKECDLLRDQHLLNMGILIDDRPNNEFVIKIIDDNQLQQEKNKREQELSKKMAGDQKKGNQNEKRE
Protein: Putative nucleosome assembly protein C36B7.08c (Q9HGN2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Histone acetyltransferase rtt109
- Histone H2A.Z
- Histone H4
- Histone chaperone cia1
- Histone acetyltransferase type B subunit 2
- Inner kinetochore subunit cnp20
- Histone H2B-alpha
- Histone H3-like centromeric protein cnp1
Sequence:
MEAAQAFENLANLEQEFGKAEIEILKKQNELFQPLFEQRRDILKTINNFWVVVLEAAGDEISQYITPEDSVLLEKLENIYVERFNEKEPRDVRISLTFQPNEYLQDDNLTLVKEVRIKEEKAKDDEGLEKKITKYTSQPVDIHWKPGKSLFRKNKKLPPNFFDYFQWTGEEEDDDFDGATLTIFLAEDLFPNAVKYFTEAMTEEASDEDESVDLEEDEEEEDEEDEEGDEEKQEPPSKKSKKSN
Protein: O-antigen ligase (O-Ag ligase) (EC 2.4.99.26) (Q9HUG6)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Potential O-antigen polymerase, which may be involved in the synthesis of LPS.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:20824106, ECO:0000269|PubMed:30047569}; Multi-pass membrane protein {ECO:0000269|PubMed:20824106, ECO:0000269|PubMed:30047569}.
Interaction partners:
- O-antigen translocase
- ABC subunit of A-band LPS efflux transporter
- Transport permease protein
- Lipopolysaccharide heptosyltransferase 1
- Alpha-1,3-rhamnosyltransferase WapR
- Toluene tolerance protein
- Bifunctional protein HldE
- Lipopolysaccharide core heptose
- O-antigen chain length regulator
- dTDP-4-dehydrorhamnose 3,5-epimerase
Sequence:
MFAATRLSRLRHDTSRILSHWILPLGWLALLTGMFWVGDRSDYHRLFYILLAAPTLLYVILQPRLLRPLTGSPLFIAFLAFSSYMMLSLSWSTPENSTGSLLKRPLYIALLFFCAAILALEAPLRLKTATWLAALGAVISAAATLLRYYWDANPLRLTGYGALYNPLLSAHVYGAFTALWLAYWMQSRPILAPLPLISLALLGGLLIATGSRTPLVGLTAALMWLVLAGDRKKALIALALALAGALLGYILYPEVITQRGASFRPEIWADALRQISEHPWLGHGYDHPMRIVLSNGMLLADPHNIELGVLFAGGIIGLLLWVAIYALAFGFSWKNRKSPAVLLASTWLVFGLAAGLTEGNAFLPRPKEHWFLIWIPMALLYALWIQQRFAASRRGEDIAAP
Protein: Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC 3.1.3.16) (EC 3.1.3.48) (EC 3.1.3.67) (Phosphatase and tensin homolog) (B8XSI6)
Organism: Sus scrofa (Pig)
Subcellular location: Cell projection, dendritic spine {ECO:0000256|ARBA:ARBA00004552}. Cytoplasm {ECO:0000256|PIRNR:PIRNR038025}. Nucleus {ECO:0000256|PIRNR:PIRNR038025}. Nucleus, PML body {ECO:0000256|PIRNR:PIRNR038025}. Postsynaptic density {ECO:0000256|ARBA:ARBA00034105}.
Interaction partners:
Sequence:
MTAIIKEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNHLDYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMYFEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGGLCDQEIDSICSIERADNDKEYLVLTLTKNDLDKANKDKANRYFSPNFKVKLYFTKTVEEPSNPEASSSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHTQITKV
Protein: AP2-like ethylene-responsive transcription factor ANT (Complementing a protein kinase C mutant protein 1) (Protein AINTEGUMENTA) (Protein DRAGON) (Protein OVULE MUTANT) (Q38914)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator that recognizes and binds to the DNA consensus sequence 5'-CAC[AG]N[AT]TNCCNANG-3'. Required for the initiation and growth of ovules integumenta, and for the development of female gametophyte. Plays a critical role in the development of gynoecium marginal tissues (e.g. stigma, style and septa), and in the fusion of carpels and of medial ridges leading to ovule primordia. Also involved in organs initiation and development, including floral organs. Maintains the meristematic competence of cells and consequently sustains expression of cell cycle regulators during organogenesis, thus controlling the final size of each organ by controlling their cell number. Regulates INO autoinduction and expression pattern. As ANT promotes petal cell identity and mediates down-regulation of AG in flower whorl 2, it functions as a class A homeotic gene.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transmembrane protein
- Stomatal closure-related actin-binding protein 2
- B3 domain-containing protein At5g57720
- Protein TIME FOR COFFEE
- TIC-like protein
- B3 domain-containing protein At3g17010
Sequence:
MKSFCDNDDNNHSNTTNLLGFSLSSNMMKMGGRGGREAIYSSSTSSAATSSSSVPPQLVVGDNTSNFGVCYGSNPNGGIYSHMSVMPLRSDGSLCLMEALNRSSHSNHHQDSSPKVEDFFGTHHNNTSHKEAMDLSLDSLFYNTTHEPNTTTNFQEFFSFPQTRNHEEETRNYGNDPSLTHGGSFNVGVYGEFQQSLSLSMSPGSQSSCITGSHHHQQNQNQNHQSQNHQQISEALVETSVGFETTTMAAAKKKRGQEDVVVVGQKQIVHRKSIDTFGQRTSQYRGVTRHRWTGRYEAHLWDNSFKKEGHSRKGRQVYLGGYDMEEKAARAYDLAALKYWGPSTHTNFSAENYQKEIEDMKNMTRQEYVAHLRRKSSGFSRGASIYRGVTRHHQHGRWQARIGRVAGNKDLYLGTFGTQEEAAEAYDVAAIKFRGTNAVTNFDITRYDVDRIMSSNTLLSGELARRNNNSIVVRNTEDQTALNAVVEGGSNKEVSTPERLLSFPAIFALPQVNQKMFGSNMGGNMSPWTSNPNAELKTVALTLPQMPVFAAWADS
Protein: High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8 (EC 3.1.4.53) (Phosphodiesterase 8) (Q6NNF2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes (By similarity). Involved in the positive regulation of MAP kinase signaling and in inhibiting oxidative stress-induced cell death.
Interaction partners:
- 3',5'-cyclic-AMP phosphodiesterase, isoform I
- AMP deaminase
- Adenosine kinase
- Adenylosuccinate lyase
- 5'-Nucleotidase C-terminal domain-containing protein
- Uncharacterized protein, isoform C
- Adenylate kinase 2
- Adenine phosphoribosyltransferase
- GTP:AMP phosphotransferase, mitochondrial
- Adenosine kinase
Sequence:
MGCSPSTLPPAPSAGQTGERGSLPLDASEKDESRLFCIKLRRSRLRRCSCGGVTLQPPSDGNGSTAGDNLCGQVLLNPLQTKSEADYEKLSTGKKDSIVTVAALGNFTHSVVRRATGSTGTSGTSSSGGNSRPGHRKSSLALALTPEDEPMDVYQRNLMDLKYPTVLPPNPPLKALLVFHKSDSICEAITAACQRHQLDVTLVKSKEEALDTLQKSYATAQCYHLIIIDARSSKNLDAEHIARTIRHTHGHHLTTIIAVCKKSFFEKDDVLIALLDAGVNRCVAETTNLAMCSVELKQILHSIIRPHNVMSTQQALYTALHRLKEVVLITDDLLRIQYANRATERLLNMRLDEIISKQLEDIFVSDLSTISEQCKNIKEFDGILTVRRKSQEGIPMHVRVVPVACIGSAPTHLIFNFDVPGGQMDFIATLPQPKEAPRGSLHSVRRCSFDVRSIASDGLRRTSLAKLTSLPLEAPITKIINLLSQVQENCSADEARLIDKVLEFLKREGLYSPQMKEIRTDDPIATDLIGALLTGPSVYSSRRSSNDSIIRTGSSTRTAAIVPAKMKSNPIIMELLDESLSWDFDIFKLEEITDYHPLLYLGMEMFRRFDVFATLNIDENVCKAWLAVIEAHYRKSNTYHNSTHAADVMQATGAFITQLTNKDMLVMDRMEEATALIAAAAHDVDHPGRSSAFLCNSNDALAVLYNDLTVLENHHAAITFKLTLGDDKINIFKNLDKETYKSARSTIIDMILATEMTRHFEHLAKFVSVFGGEEPRDHNPQTDEETSILMRRMLIKVADVSNPARPMQFCIEWARRIAEEYFMQTDEEKQRHLPIVMPMFDRATCSIPKSQIGFIEYIIQDMMHAWESFIDMPQLITYMQINYSQWKKYDEQGVNTLAEIMAKQPPVGKMANSK
Protein: Imidazole glycerol phosphate synthase hisHF (IGP synthase) (IGPS) (ImGP synthase) (EC 4.3.2.10) [Includes: Glutaminase (EC 3.5.1.2); Cyclase] (O94303)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The glutaminase domain produces the ammonia necessary for the cyclase domain to produce IGP and AICAR from PRFAR. The ammonia is channeled to the active site of the cyclase domain.
Interaction partners:
- Imidazoleglycerol-phosphate dehydratase
- 1-
- Histidine biosynthesis bifunctional protein his7
- Histidinol-phosphate aminotransferase
- ATP phosphoribosyltransferase
- Histidinol dehydrogenase
- Bifunctional purine biosynthesis protein ade10
- Bifunctional polynucleotide phosphatase/kinase
- ATP-dependent helicase rhp16
- Probable phosphoserine phosphatase
Sequence:
MIVSIVDYGSGNVRSLINAVRYLGFETQWIRNPHDIEKAECLIFPGVGNFGFVCDSLAKQGFLEPLRRYALSGKPFMAVCVGIQALFEGSVEAPHSKGLGVFPGLVQRFDNDDKTVPHIGWNSCAVRSDTSKEFFGMRPHDKFYFVHSYMIPEKGLILPPEFKIATTKYGNETFVGAIVKNNFLATQFHPEKSGSAGLRCLKAFLTGNYEQPISGEASKLIENSFGGLTKRIIACLDVRSNDAGDLVVTKGDQYDVREKSSGSEVRNLGKPVELCQRYFQEGADEVVFLNITSFRNCPMADAPMLQVLEKAAQTVFVPLTVGGGIRDVSDPDGTFHPAVEVAGIYFRSGADKVSIGSDAVYAAEKYYENGKKLSGKTAIETISKAYGNQAVVISVDPKRQYVKVPEDTKHHVVKTSRLGPNGEAYCWYQCTVKGGREYRDIDVVELTRACEAMGAGEVLLNCMDQDGSNAGYDIELVRLVKNSVNIPVIASSGAGIPQHFEEVFKETDCDAALAAGIFHRQTCRIEDVKEYLAIHDVLVRT
Protein: COMPASS component SHG1 (Complex proteins associated with SET1 protein SHG1) (Set1C component SHG1) (P38337)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- COMPASS component SWD2
- COMPASS component SDC1
- COMPASS component BRE2
- COMPASS component SPP1
- COMPASS component SWD1
- COMPASS component SWD3
- Histone-lysine N-methyltransferase, H3 lysine-4 specific
- Uncharacterized protein YBR259W
- Protein SLM6
- Histone-lysine N-methyltransferase, H3 lysine-36 specific
Sequence:
MAYNQEDSKRLSDKYKKEGHFDKLKREILSNPWNNTEENSESFEQALRKRVASTVKEMVNEDEELIFKNRGLTSALIESQLVKDNYLKLGSKMEGDNGDGEKKFDLDVYVRSKLQDPKLLEMIKGQLQETLNSYEEEANGST
Protein: Actin-binding protein WASF2 (Protein WAVE-2) (Verprolin homology domain-containing protein 2) (Wiskott-Aldrich syndrome protein family member 2) (WASP family protein member 2) (Q9Y6W5)
Organism: Homo sapiens (Human)
Function: Downstream effector molecule involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Promotes formation of actin filaments. Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Basolateral cell membrane {ECO:0000269|PubMed:30250061}. Note=At the interface between the lamellipodial actin meshwork and the membrane. {ECO:0000250}.
Interaction partners:
- BAR/IMD domain-containing adapter protein 2
- Abl interactor 1
- Nck-associated protein 1-like
- Nck-associated protein 1
- Protein BRICK1
- Cytoplasmic FMR1-interacting protein 2
- Cytoplasmic FMR1-interacting protein 1
- Abl interactor 2
- Actin-binding protein WASF1
- Actin-related protein 2
Sequence:
MPLVTRNIEPRHLCRQTLPSVRSELECVTNITLANVIRQLGSLSKYAEDIFGELFTQANTFASRVSSLAERVDRLQVKVTQLDPKEEEVSLQGINTRKAFRSSTIQDQKLFDRNSLPVPVLETYNTCDTPPPLNNLTPYRDDGKEALKFYTDPSYFFDLWKEKMLQDTKDIMKEKRKHRKEKKDNPNRGNVNPRKIKTRKEEWEKMKMGQEFVESKEKLGTSGYPPTLVYQNGSIGCVENVDASSYPPPPQSDSASSPSPSFSEDNLPPPPAEFSYPVDNQRGSGLAGPKRSSVVSPSHPPPAPPLGSPPGPKPGFAPPPAPPPPPPPMIGIPPPPPPVGFGSPGTPPPPSPPSFPPHPDFAAPPPPPPPPAADYPTLPPPPLSQPTGGAPPPPPPPPPPGPPPPPFTGADGQPAIPPPLSDTTKPKSSLPAVSDARSDLLSAIRQGFQLRRVEEQREQEKRDVVGNDVATILSRRIAVEYSDSEDDSSEFDEDDWSD
Protein: Chlorophyll a-b binding protein CP29.2, chloroplastic (LHCB4.2) (LHCII protein 4.2) (Q9XF88)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
Subcellular location: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein.
Interaction partners:
- Chlorophyll a-b binding protein CP26, chloroplastic
- Photosystem II CP43 reaction center protein
- Photosystem I reaction center subunit V, chloroplastic
- Photosystem II D2 protein
- Photosystem II CP47 reaction center protein
- Photosystem II protein D1
- Oxygen-evolving enhancer protein 2-1, chloroplastic
- Oxygen-evolving enhancer protein 1-1, chloroplastic
- Photosystem II reaction center protein H
- Photosystem I reaction center subunit XI, chloroplastic
Sequence:
MAATSTAAAASSIMGTRVVSDISSNSSRFTARFGFGTKKASPKKAKTVISDRPLWFPGAKSPEYLDGSLVGDYGFDPFGLGKPAEYLQFDLDSLDQNLAKNLYGEVIGTRTEAVDPKSTPFQPYSEVFGLQRFRECELIHGRWAMLATLGAITVEWLTGVTWQDAGKVELVDGSSYLGQPLPFSISTLIWIEVLVIGYIEFQRNAELDSEKRLYPGGKFFDPLGLASDPVKKAQLQLAEIKHARLAMVGFLGFAVQAAATGKGPLNNWATHLSDPLHTTIIDTFSSS
Protein: Protein SINE3 (Q9C900)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus membrane {ECO:0000269|PubMed:24891605}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein SINE2
- Protein SINE4
- Protein SINE1
- Hypthetical protein
Sequence:
MKEIQIPRKSFARSSELGAKRLKDPEMKNRKVTTEKRQIATFSDVSFESTKDPMDFSPISQISGAISDSEAESVIQGSSLDLMSTPEICLPADDSPVSTITSVEARIDTSSTDRIQSIVDLPASVQSLRGEINELKKLICSVDNSAEINWVDRVVTVKFRIVLLSFILWAILAAIVVFFSSGEERAYRGPLPT
Protein: tRNA mitochondrial 2-thiouridylase (A0A2R8YDK3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQALRHVVCALSGGVDSAVAALLLRRRGADAIATGHYARTSLEDEEVFEQKHVKKPEGLFRNRFEVRNAVKLLQAADSFKDQTFFLSQVSQDALRRTIFPLG
Protein: Tritrans,polycis-undecaprenyl-diphosphate synthase (geranylgeranyl-diphosphate specific) (EC 2.5.1.89) (Undecaprenyl diphosphate synthase) (UDS) (Undecaprenyl pyrophosphate synthase) (UPP synthase) (Q8TJQ7)
Organism: Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Function: Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with geranylgeranyl diphosphate (GGPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30E,34E,38E)-undecaprenyl diphosphate (tritrans,heptacis-UPP). It is probably the precursor of glycosyl carrier lipids.
Interaction partners:
- Bifunctional short chain isoprenyl diphosphate synthase
- Polyprenyl synthetase
- dTDP-4-dehydrorhamnose 3,5-epimerase
Sequence:
MKNRTFSMFYQEYEQLLEKEILSSEIPDHIAVIMDGNRRYAGQRGRTRSFGHAMGAEVTEQVIEWCYEIGVKELTLYAFSTENFQRSEEEVDGLFNLINEKFLKLYNDKRTYEKETQIRVIGDRTKLPAFLNKSIEKIEKATETHRKFNLNVAIAYGGRQDIMQAVRDIAACVSSGKLSLEDVDENLISKHLYPAPGVSVPNVDLIVRTGGDERVSNFLPWQANGSECATYFCAPFWPEFRKIDLLRSIRVYQARKDEKKQENSYRVSKVINFLGVGKYGEKSEELGQLLPLKKQGVA
Protein: Cysteine/Histidine-rich C1 domain family protein (T23K8.9 protein) (Q9S9J8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEPEMVRLPIHEHWLTPARDNRWGKCCGLQFKTISDGYNCRKCRYFFHKSCSNCPKEINHPSHKCDKNLSLITNFASWSVRCRTCKETIQPYIQNYECQRCEFNIHLDCFKYPPPKVIDFPQNHDHKLKLEMVRSSFTCFTCGKGGSGYPYKCHECDLAFHVDCEKYGAEVNHPSHSLHTLKLITGKPPAYTDGNCSLCGKKIFDEMFYHCSACNFTLDLRCVSLPPPLNLHDQNTHNHELTLMPKLISFTCTTCGLHGDRSPYVCLQCNFTSHNNCSGFPWVININRHDHRVSRTSLLGIIDSVCGVCRKKMDWSCGGYSCKRCSESTFHTKCATREDVWDGIEMKDEPEEDEPMEPFEVISEGIIRHFSHIEHNLRLDKSGTFVEERSCKACAYPIYHDPFYSCMSCDFLLHENCAKHPTRKRHVLSNKPYILHASQRNYSKCKACGVFFNCFIYGTFPFGLDVRCASFSGSLVHPSHQHPLFYTSPKGVCSACNKETSHVLRCVEDKCGYALDFKCALLPHEVKHRVDDHFLSLCYGERDASGKYWCDICEKETDPTKWFYTCKDCGVTLHTNCVLGDFRGLEPETNIVLDDDRMQMTLYETVRNNSMSRPVCYKCKYHCIFPIILKVTDEDKYFCSISCCDIKTLPFYN
Protein: SD09407p (Q95TG0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MISVQAPPEFTEKLRNQTARRGEPAVLQCEAKGEKPIGILWNMNNMRLDPKNDNRYTIREEILSTGVMSSLSIKRTERSDSALFTCVATNAFGSDDASINMIVQEVPEMPYALKVLDKSGRSVQLSWAQPYDGNSPLDRYIIEFKRSRASWSEIDRVIVPGHTTEAQVQKLSPATTYNIRIVAENAIGTSQSSEAVTIITAEEAPSGKPQNIKVEPVNQTTMRVTWKPPPRTEWNGEILGYYVGYKLSNTNSSYVFETINFITEEGKEHNLELQNLRVYTQYSVVIQAFNKIGAGPLSEEEKQFTAEGTPSQPPSDTACTTLTSQTIRVGWVSPPLESANGVIKTYKVVYAPSDEWYDETKRHYKKTASSDTVLHGLKKYTNYTMQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPSRDLPELSAEDTIRIILSNLNLVVPVVAALLVIIIAIIVICILRSKGNHHKDDVVYNQTMGPGATLDKRRPDLRDELGYIAPPNRKLPPVPGSNYNTCDRIKRGRGGLRSNHSTWDPRRNPNLYEELKAPPVPMHGNHYGHAHGNAECHYRHPGMEDEICPYATFHLLGFREEMDPTKAMNFQTFPHQNGHAGPVPGHAGTMLPPGHPGHVHSRSGSQSMPRANRYQRKNSQGGQSSIYTPAPEYDDPANCAEEDQYRRYTRVNSQGGSLYSGPGPEYDDPANCAPEEDQYGSQYGGPYGQPYDHYGSRGSMGRRSIGSARNPGNGSPEPPPPPPRNHDMSNSSFNDSKESNEISEAECDRDHGPRGNYGAVKRSPQPKDQRTTEEMRKLIERNETGPKQLQLQQANGAGFTAYDTMAV