wanglab/gogpt-training-data huggingface dataset:
Protein: F-box/LRR-repeat protein At3g59210 (Q8GW80)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Putative RING zinc finger protein
- F-box/kelch-repeat protein At3g13680
- E3 ubiquitin-protein ligase ATL41
- F-box protein At5g07610
- E3 ubiquitin-protein ligase ORTHRUS-LIKE 1
- Putative F-box/LRR-repeat protein 21
- Putative E3 ubiquitin-protein ligase ORTHRUS 4
- At1g51400/F5D21_10
- At5g63780
- F-box protein PP2-B13
Sequence:
MDDCSKDIINCLPDNLLCQILSNLSTKEAALTSLLSKRWRYLFALVPNLDFDVLPSLHPEVAMQDQDQTSFIDFVDRVLKLRGKDHINKFSLKCGDGIEDEDVFPWILNTLRHGVSDLSLHVSPSLVYWLPSKVFASKTLVRLKIGPKDGPRVKLRNVCLPKLKTLNLDSVVFEEGKIGFAKLLSGCPVLEELSLLNLAWDRWDSCSVSSKILKRLTLYCAHSSRNPKSVSFDTPNVVYFEYSDNIANKYPKVNFDSLVEASIGIRMTKVQKANARYVSDVDEETEMVGNATDLLMGICNVKTLYLSYDTLETLNLCCQVIPVFNNLTHLTIESHPELGWESLPNLLKSCPNLGTLVFQGLLHKATDRCGDVCMCQGLENSHSCLSSSPVKCLKILKFGETNDDDDMEIEMEQIKNFLEKMPNLEQLIIYYESSIDNDLVRVSSQLQEVPTVASLKCKIQVISDNLSLSSTLPISLSMENGFHL
Protein: Diphthine--ammonia ligase (EC 6.3.1.14) (ATP-binding domain-containing protein 4) (Diphthamide synthase) (Diphthamide synthetase) (Protein DPH6 homolog) (H0YND7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MYQTVGHHAIDLYAEAMALPLYRRTIRGRSLDTRQVYTKCEGDEVEDLYELLKLVKEKEEVEGISVGAILSDYQRIRVENVCKRLNLQPLAYLWQRNQEDLLREMISSNIQAMIIKVAALGLDPDKHLGKTLDQMEPYLIELSKKYGVHVCGEGGEYETFTLDCPLFKK
Protein: Serine/threonine-protein kinase tousled-like 1 (EC 2.7.11.1) (Tousled-like kinase 1) (P34314)
Organism: Caenorhabditis elegans
Function: Essential for appropriate transcription during embryonic development. May act during transcription elongation to activate the RNA polymerase II large subunit (ama-1) by phosphorylating the Ser-2 residues of the C-terminal domain 7-residue repeats. Does not phosphorylate histone H3.
Subcellular location: Nucleus {ECO:0000269|PubMed:14614817}.
Interaction partners:
- Probable histone chaperone asf-1
- Probable histone chaperone asf-1-like protein
- Protein HIRA
Sequence:
MSMLSMDGIVAGGGSSSGGGERSFVLEQKMFNTGPQNKALPTVQSSGSSSNHAPIVGESPLGTVSSTMATGDTGRVGNVTYMSSGMLGATQFMPQNSSHPSTSVMMQQVPPQNGGATRSSPTEMQQCMQAMSEDSIEMRDYNSGVHHMHPHQMQMQQQQQHHQQQYNMSYHNHQQQMQQMHYHQQQQQYQQQQAQHHQMYAPQIQQQQQQPQQQSQQQSAQQPQQSSAALQHVNESSNLSSAGSISDREPEQHGGTPQRPTAPQSSTATDKKTRKRRKAGPTEDQATPKQERKITEFMKVGGEVASGNSVARCLLTEYHQNQGSPKRQPAVQQNGSNSYDSQQQQPQMNQHEMQNSYWGVATPSLGVNNRGTPTPTQQQHYSSDSNSNSNQSPPGQGNQSGRMVRTIDEETQTDSSLSQANPQNADEVAKMNRIIEDHRRQIEELNSKNSLERRKNEASKETIKRLLIDKNQIERKALRDKTAADSPRIGCFKTTRTGDSFRDQWVDGWAFAEMDKKTEQINAERNEIASASALLKKRKPLGIGKEPKRPQAVNSQNDSNGMQPSTSSNTNGDDAIFRRPEEPKEIQYQEYIELDEIYKLRREHLRKEETDLSMEKERLEKEKQHHVRELKRASNESASQFNDHRLLHKRYLMLNLLGKGGFSEVWKAFDIEENRYVACKIHHVNKDWKEEKKANYVKHAMREKDIHKSLDHCRIVKQYDLLTIDNHSFCTVLEYVPGNDLDFYLKQNRSISEKEARSIIMQVVSALVYLNEKSTPIIHYDLKPANILLESGNTSGAIKITDFGLSKIMEGESDDHDLGIELTSQFAGTYWYLPPETFIVPPPKITCKVDVWSIGVIFYQCIYGKKPFGNDLTQQKILEYNTIINAREVSFPSKPQVSSAAQDFIRRCLQYRKEDRADVFELAKHELFRPRGAIRASVAGSLLLVIITLCQHSNRSEDRLCVSNV
Protein: Obscurin-like protein 1 (D3ZZ80)
Organism: Rattus norvegicus (Rat)
Function: Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer (By similarity). Acts as a regulator of the Cul7-RING(FBXW8) ubiquitin-protein ligase, playing a critical role in the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain. Required to localize CUL7 to the Golgi apparatus in neurons.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O75147}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75147}. Golgi apparatus {ECO:0000250|UniProtKB:O75147}. Note=Colocalizes with CUL7 at the Golgi apparatus in neurons. {ECO:0000250|UniProtKB:O75147}.
Interaction partners:
- Cullin-7
- Coiled-coil domain-containing protein 8
- Titin
- F-box/WD repeat-containing protein 8
- Cullin 7
- Cullin 9
- Cardiac-enriched FHL2-interacting protein
Sequence:
MKASSGDQGSPPCFLRFPRPVRVVSGAEAELKCVVLGEPPPTVLWEKGGQQLVASERLSFPEDGAEHGLLLSGALPTDAGVYVCRARNAAGEAYAAAAVTVLEPPAPEPEPQSSECPPPPPGTGEGAPVFLTGPQSQWVLRGAEVVLTCQVGGLPEPKLYWEKDGMALDEVWDSSHYTLEPDRGASDGGASLTLRILAARLPDSGVYVCHARNAHGHAQAGALLQVHQPHENPPQDPDEPPVRVIEPLKCAPKTFWVNEGKHAKFRCYVMGKPEPEIEWHLEGRPLLPDRRRLMYRDRDGGFVLKVLYCQAKDRGLYVCAARNSAGQTLSAVQLHVKEPRLRFTRPLQDVEGREHGIVVLECKVPNSRIPTAWFREDQRLLPCRKYEQIEEGTVRRLVIHRLKADDDGVYLCEMRGRVRTVANVTVKGPILKRLPRKLDVLEGENAVLLVETQEAGVQGCWSRDGEELPATCQSSCGHMHALVLPGVTREDAGEVTFSLGNSRTTTLLRVKCVKHSPPGPPVLVEMFKGQKNTVLLTWKPPEPPPETSFIYRLERQEVGSEDWIQCFSIEKAGAVEVPGDCVPTEGDYRFRICTVSEHGRSPHVVFNGSAHLVPTARLVSGLEDVQVYDGEDAVFSLDLSTIIQGSWFLNGELLKNDEAEGQVEPGALRYRIEQKGLQHRLILQTVKHQDNGALVGFICPGVQDSAALSIQESPVHILSPQDKVLLTFTTSERVVLTCELSRVDFPATWYKDGQKVEESESLVVKMDGRKHRLILPEAQVRDSGEFECRTEGISAFFSVTVQDPPVHIVDPQEHVFVHAITSESVMLTCEVDREDAAVHWYKDGQEVEESAVIVLEKEGPRHRLVLPAAQPSDGGEFQCVVGDERAYFTVTITDVSSWIVYPNGKVYVAAVRLERVVLTCELCRPWAEVRWTKDGEEVLESPALLLEKEDTIRRLVLPSVQLEDSGEYLCEIHDESASFTITVTEPPVRIIYPQDEVTLHAVSLECVVLTCELSRVDAPVRWYKDGLEVEETEALVLQSDGPRRRLVLPAAQPEDGGEFVCDAGDDSAFFTVTVTAPPERIVHPVARSLDLQFGAPGHVELRCEVAPAGSQVRWYKDGLEVEVSDALQLGAEGPARTLTLPHAQPEDAGEYVCETRDEAVTFNVSLAELPVQFLAPEAVPNPLCVVPGEPVMLSCELSRASAHVSWSHNGNPVKQGEGLELRAEGPRRILCIQAADLAHTGVYTCQSGTAPGAPSLSFNVQVAEPPPVKLVSELTPLTVHEGDDATFQCEVSPPDAEVTWLRNGAIVTPGPQLEMVHSGSSRTLIIRGCQLKDAGTVTARAGATDTSARLHVRETELLFLRRLQDVRAEEGQDVYLEVETGRVGAPGAVRWLRGGEPLPLDSRLTTAQDGHVHRLSIHGVLLTDQGTYGCESHHDRTLARLSVRPRQLRELRPLEDVTVHEGGSATFQLELSQEGVTGEWAQGGVRLHPGPKCHIHSEGRTHCLVLSGLGLADSGCISFTADTLRCAARLTVREVPVTIVQGPQDLEVTEGDTATFECELSQTLADVIWEKDGQALSLSPRLRLQSLGTRRLLLLRRCSSSDAGTYCCAVGTARSGPARLTVREREVSVLGELRSLSAREGDSATFECTVSESETTGRWELGGRALRPGGRVRIRQEGKKHILVLSELRTEDTGEVCFQAGPAQSLARLEVEALPLQMCRRPPREKTVLVDRRAVLEVTVSRPGGHVCWMREGVELCPGSKYEMRSHGTTHSLVIHDVRPEDQGTYSCQAGQDSADTQLLVEGDD
Protein: Proliferating cell nuclear antigen (Q6FI35)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU000641}.
Interaction partners:
Sequence:
MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSMDSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMDLDVEQLGIPEQEYSCVVKMPSGEFACICRDLSHIGDAVVISCAKDGVKFSASGELGNGNIKLSQTSNVDKEEEAVTIEMNEPVQLTFALRYLNFFTKATPLSSTVTLSMSADVPLVVEYKIADMGHLKYYLAPKIEDEEGS
Protein: SLP adapter and CSK-interacting membrane protein (Q3UU41)
Organism: Mus musculus (Mouse)
Function: Lipid tetraspanin-associated transmembrane adapter/mediator that acts as a scaffold for Src-family kinases and other signaling proteins in immune cells. It is involved in major histocompatibility complex class II (MHC-II) signaling transduction in B cells, where it is required in generating the calcium response and enhancing ERK activity upon MHC-II stimulation (By similarity). In dendritic cells, it is involved in sustaining CLEC7A/DECTIN1 signaling after CLEC7A activation by fungal beta-glucans. It also acts as an agonist-inducible signaling adapter for TLR1, TLR2, TLR3, TLR4, and TLR7 by selectively enabling the expression of pro-inflammatory cytokines IL6 and IL12B in macrophages and acting as a scaffold for phosphorylation of Toll-like receptors by Src-family kinases.
Subcellular location: Cell membrane {ECO:0000269|PubMed:28098138}; Single-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q6UWF3}; Lipid-anchor {ECO:0000250|UniProtKB:Q6UWF3}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:27288407}. Cell projection, ruffle {ECO:0000269|PubMed:28098138}. Cell projection, filopodium {ECO:0000269|PubMed:28098138}. Note=Together with MHC-II, associates with lipid-enriched microdomains called tetraspanin-enriched microdomains (TEMs) (By similarity). Rapidly translocates into immunological synapse (IS) at cell-cell contacts between antigen-presenting cells (APCs) and T-cells (By similarity). Colocalized with tetraspanins CD37, CD53, and CD81 at the uropod (By similarity). Present at regions of cell-cell contacts but also at the leading edge of migrating cells (By similarity). Localizes to phagosomes in dendritic cells after exposure to particulate beta-glucan (PubMed:27288407). {ECO:0000250|UniProtKB:Q6UWF3, ECO:0000269|PubMed:27288407}.
Interaction partners:
Sequence:
MSWWRDNFWIILAMSIIFISLVLGLILYCVCRWQLRQGRNWEIAKPSKQDGRDEEKMYENVLNSSPGQLPALPPRGSPFPGDLAPQEAPRQPSAWYSSVKKVRNKKVFAISGSTEPENDYDDVEIPATTETQHSKTTPFWQAEVGLHSSF
Protein: tRNA (guanine(9)-N1)-methyltransferase (EC 2.1.1.221) (tRNA methyltransferase 10) (tRNA(m1G9)-methyltransferase) (tRNA(m1G9)MTase) (Q12400)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNAs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- tRNA
- tRNA
- tRNA
- tRNA pseudouridine
- tRNA
- tRNA pseudouridine synthase 1
- tRNA
- tRNA
- tRNA
- tRNA wybutosine-synthesizing protein 2
Sequence:
MSNDEINQNEEKVKRTPPLPPVPEGMSKKQWKKMCKRQRWEENKAKYNAERRVKKKRLRHERSAKIQEYIDRGEEVPQELIREPRINVNQTDSGIEIILDCSFDELMNDKEIVSLSNQVTRAYSANRRANHFAEIKVAPFDKRLKQRFETTLKNTNYENWNHFKFLPDDKIMFGDEHISKDKIVYLTADTEEKLEKLEPGMRYIVGGIVDKNRYKELCLKKAQKMGIPTRRLPIDEYINLEGRRVLTTTHVVQLMLKYFDDHNWKNAFESVLPPRKLDAEAKSASSSPAPKDT
Protein: Ras association (RalGDS/AF-6) and pleckstrin homology domains 1 (G5E867)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MEQLSDEEIDHGAEEDSDKEDQDLDKMFGAWLGELDRLTQSLDSDKPKEPVKRSPLRQETNMANFSYRFSIYNLNEALNQGETVDLDALMADLCSIEQELSSIGSGNSKRQVTEPKVPQKLPAGRHTSKHGTLRGPSSSSNRTTKPSHANYSLDDITAQLEQASLSMDEAAQQSLVEDPKPLVTNQHRRTASAGTVSDAEARSISNSSRSSITSAASSMDSLDIDKVTRPQELDLTTHQGQPITEHAISLSCPSKQAKHHSDFTEEQAELTPHSYLDRETSLLLRNIAGKPSHLLTKEEQAAKLKAEKIRVALEKIKEAQVKKLVIRVHMSDDSSKTMMVDERQTVRQVLDNLMDKSHCGYSLDWSLVETISELQMERIFEDHENLVENLLNWTRDSQNKLIFMERIEKYALFKNPQNYLLGKKETAEMADRNKEVLLEECFCGSSVTVPEIEGVLWLKDDGKKSWKKRYFLLRASGIYYVPKGKAKVSRDLVCFLQLDHVNVYYGQDYRNKYKAPTDCCLALKHPQIQKKSQYIKYLCCDDARTLHQWVNGIRIAKYGKQLYTNYQEALKRTESAYDWTSLSSSSIKSGSSSSSIPESQSNHSNQSDSGVSDTLPTGHIRSQSTVSSIFSEAWKRGTQLEESSKRTRVQFPAPSSGNSKPPITPAPKDPMSSSGLQGT
Protein: Elongation of very long chain fatty acids protein 5 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL5) (ELOVL fatty acid elongase 5) (ELOVL FA elongase 5) (Very long chain 3-ketoacyl-CoA synthase 5) (Very long chain 3-oxoacyl-CoA synthase 5) (B6V6V0)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|HAMAP-Rule:MF_03205}; Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_03205}. Cell projection, dendrite {ECO:0000256|HAMAP-Rule:MF_03205}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Note=In Purkinje cells, the protein localizes to the soma and proximal portion of the dendritic tree. {ECO:0000256|HAMAP-Rule:MF_03205}.
Interaction partners:
- Elongation of very long chain fatty acids protein 2
- Elongation of very long chain fatty acids protein 5
- Delta-6 fatty acyl desaturase
- Delta-6 fatty acyl desaturase
- Estradiol 17-beta-dehydrogenase 12-B
- Very-long-chain 3-oxoacyl-CoA reductase-like isoform X1
- 3-ketoacyl-CoA reductase
- hydroxymethylglutaryl-CoA lyase
Sequence:
MEAFNHKLNTYIDSWMGPRDERVQGWLLLDNYPPTFALTLMYLLIVWLGPKYMRHRQPVSCQGLLVLYNLALTLLSFYMFYEMVSAVWQGGYNFYCQDTHSAGETDTKIINVLWWYYFSKVIEFMDTFFFILRKNNHQITFLHIYHHASMLNIWWFVMNWVPCGHSYFGASLNSFVHVLMYSYYGLSAVPAIRPYLWWKKYITQGQLIQFFLTMSQTICAVIWPCGFPRGWLFFQIFYMASLIAFFSNFYIQTYKKHRVSQKEYHQNGSVDSLNGHANGVTPTETITHRKVRVD
Protein: Metalloendopeptidase (EC 3.4.24.-) (Q05AP0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MYLLVVVISLLLSSGPVQSRPVEDLIEKMSKKTGGNFTKKGNLLVSSVIETSKHAGENTDGPVILFGDIAFPRGLQNADQCTARGCKWDRSRDGLVYVPYQISRAYSPREVAVIEQGLQSFSAVSCIRFVPHTGERNYLNIKSESGCYSYLGRIGGGQVVSLQRQGCVYFSTVQHELLHALGFHHEQNRSDRDNHIRILYQNIIPAQQYNFNKQNTNNLGTPYDYNSVMQYSRYAFSMNNQPTMVPVPNANVVLGEAQSMSPNDILRINRLYCN
Protein: 3,2-trans-enoyl-CoA isomerase, mitochondrial, putative (EC 5.3.3.8) (Q580R2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Probable enoyl-CoA hydratase, mitochondrial
- propanoyl-CoA C-acyltransferase
- Nonspecific lipid-transfer protein, putative
Sequence:
MAATPYRFRLSSQCSHIRRHVCRRLITPQLSVRTCATGTESSNGARLIEVMESPIENIKILSMNNAPANVLSSAMIKEMLSSISEVCNPEKGCCKGIVLTSSLPNVFCNGLDLQLLIDKLPYDSFSSYWKQLQMLYITLNTLPVPVVAAINGDATGFGCIMALSTDYRVMAEKAEEGGGKQLKIGVDTVRCGLAVPPCFGAVVAHTVGYRACEMFLQRGVILCAAEAENAGLVDETVERADEVLVRALDMAENLSGGPPWSFWLVKDASRKAFMAPLCTQALRDADCANFYEFISNTEVRRDMRAYIAGSA
Protein: Zinc finger protein 662 (Q6ZS27)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MLENYGAVASLAAFPFPKPALISQLERGETPWCSVPRGALDGEAPRGISSGYPFLKPAGISHPEQVEEPLNLKLQGEGPSLICPEGVLKRKKEDFILKEEIIEEAQDLMVLSSGPQWCGSQELWFGKTCEEKSRLGRWPGYLNGGRMESSTNDIIEVIVKDEMISVEESSGNTDVNNLLGIHHKILNEQIFYICEECGKCFDQNEDFDQHQKTHNGEKVYGCKECGKAFSFRSHCIAHQRIHSGVKPYECQECAKAFVWKSNLIRHQRIHTGEKPFECKECGKGFSQNTSLTQHQRIHTGEKPYTCKECGKSFTRNPALLRHQRMHTGEKPYECKDCGKGFMWNSDLSQHQRVHTGDKPHECTDCGKSFFCKAHLIRHQRIHTGERPYKCNDCGKAFSQNSVLIKHQRRHARDKPYNCQISHLLEH
Protein: Muscleblind like splicing regulator 1 (A0A0A0MQX8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAVSVTPIRDTKWLTLEVCREFQRGTCSRPDTECKFAHPSKSCQVENGRVIACFDSLKGRCSRENCKYLHPPPHLKTQLEINGRNNLIQQKNMAMLAQQMQLANAMMPGAPLQPVPMFSVAPSLATNASAAAFNPYLGPVSPSLVPAEILPTAPMLVTGNPGVPVPAAAAAAAQKLMRTDRLEVCREYQRGNCNRGENDCRFAHPADSTMIDTNDNTVTVCMDYIKGRCSREKCKYFHPPAHLQAKIKAAQYQVNQAAAAQAAATAAAMTQSAVKSLKRPLEATFDLGIPQAVLPPLPKRPALEKTNGATAVFNTGIFQYQQALANMQLQQHTAFLPPGSILCMTPATSVVPMVHGATPATVSAATTSATSVPFAATATANQIPIISAEHLTSHKYVTQM
Protein: Probable alpha-tubulin polyglutamylase Ttll1 (EC 6.-.-.-) (Tubulin-tyrosine ligase family protein 1) (Q23SI8)
Organism: Tetrahymena thermophila (strain SB210)
Function: Probable tubulin polyglutamylase with a strong preference for alpha-tubulin. Modifies alpha-tubulin, generating side chains of glutamate on the gamma-carboxyl groups of specific glutamate residues within the C-terminal tail of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15890843}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:15890843}. Contractile vacuole {ECO:0000269|PubMed:15890843}. Note=Associated with microtubules from basal bodies, contractile vacuole pore and oral deep fiber.
Interaction partners:
Sequence:
MASKKLKYKTDFDKCVLTDNFAARGWTRCGDKDDDDWNIYWATVWNVRNIFNPKSGIRLNDMQIINHFPNHYELTRKDLMVKNFKRYKKELEKENSPYCQKDENGNYLYLDFIPQTFTLPGEYSLFVEEFHRNPNATWIVKPASRSQGKGIFLLRKIQQLKKIGGGTNSNPLQAFSLKEAYVVSRYIDNPLLVGGRKFDLRIYALVTSYRPLKVYLYAMGFGRFCNEQYTQDIAEMDNMFIHLTNVAIQKFSDKYSEKHGGKWSLQSLRYYLEMVYGTDMANKCFDDINNIIIMSLKSVQSIIINDKHCFEMYGYDILIDENCKPWLIEINASPSLTVTGKIDKELKTELIKNVYQIVIPDDWNDDSSKTGANTSTQTKVGDFNILYDEAQEKKISQQQQQQKKNINSKTIWK
Protein: Nitric oxide synthase 1 (EC 1.14.13.39) (Constitutive NOS) (NC-NOS) (NOS type I) (Neuronal NOS) (N-NOS) (nNOS) (Nitric oxide synthase, brain) (bNOS) (Peptidyl-cysteine S-nitrosylase NOS1) (P29475)
Organism: Homo sapiens (Human)
Function: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR.
Subcellular location: Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q9Z0J4}; Peripheral membrane protein {ECO:0000255}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P29476}. Note=In skeletal muscle, it is localized beneath the sarcolemma of fast-twitch muscle fiber by associating with the dystrophin glycoprotein complex (By similarity). In neurons, enriched in dendritic spines (By similarity). {ECO:0000250|UniProtKB:P29476, ECO:0000250|UniProtKB:Q9Z0J4}.
Interaction partners:
- Calmodulin-like protein 4
- Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein
- Calmodulin-1
- Calmodulin-like protein 3
- Calmodulin-like protein 6
- Calmodulin-like protein 5
- Disks large homolog 4
- Dexamethasone-induced Ras-related protein 1
- Glutamate receptor ionotropic, NMDA 2B
- Alpha-1-syntrophin
Sequence:
MEDHMFGVQQIQPNVISVRLFKRKVGGLGFLVKERVSKPPVIISDLIRGGAAEQSGLIQAGDIILAVNGRPLVDLSYDSALEVLRGIASETHVVLILRGPEGFTTHLETTFTGDGTPKTIRVTQPLGPPTKAVDLSHQPPAGKEQPLAVDGASGPGNGPQHAYDDGQEAGSLPHANGLAPRPPGQDPAKKATRVSLQGRGENNELLKEIEPVLSLLTSGSRGVKGGAPAKAEMKDMGIQVDRDLDGKSHKPLPLGVENDRVFNDLWGKGNVPVVLNNPYSEKEQPPTSGKQSPTKNGSPSKCPRFLKVKNWETEVVLTDTLHLKSTLETGCTEYICMGSIMHPSQHARRPEDVRTKGQLFPLAKEFIDQYYSSIKRFGSKAHMERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKPPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMNLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPDPWNTHVWKGTNGTPTKRRAIGFKKLAEAVKFSAKLMGQAMAKRVKATILYATETGKSQAYAKTLCEIFKHAFDAKVMSMEEYDIVHLEHETLVLVVTSTFGNGDPPENGEKFGCALMEMRHPNSVQEERKSYKVRFNSVSSYSDSQKSSGDGPDLRDNFESAGPLANVRFSVFGLGSRAYPHFCAFGHAVDTLLEELGGERILKMREGDELCGQEEAFRTWAKKVFKAACDVFCVGDDVNIEKANNSLISNDRSWKRNKFRLTFVAEAPELTQGLSNVHKKRVSAARLLSRQNLQSPKSSRSTIFVRLHTNGSQELQYQPGDHLGVFPGNHEDLVNALIERLEDAPPVNQMVKVELLEERNTALGVISNWTDELRLPPCTIFQAFKYYLDITTPPTPLQLQQFASLATSEKEKQRLLVLSKGLQEYEEWKWGKNPTIVEVLEEFPSIQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIVSYRTRDGEGPIHHGVCSSWLNRIQADELVPCFVRGAPSFHLPRNPQVPCILVGPGTGIAPFRSFWQQRQFDIQHKGMNPCPMVLVFGCRQSKIDHIYREETLQAKNKGVFRELYTAYSREPDKPKKYVQDILQEQLAESVYRALKEQGGHIYVCGDVTMAADVLKAIQRIMTQQGKLSAEDAGVFISRMRDDNRYHEDIFGVTLRTYEVTNRLRSESIAFIEESKKDTDEVFSS
Protein: RNA-binding (RRM/RBD/RNP motifs) family protein (F4I321)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAGGIGLGDTTYTKVFVGGLAWETHKETMKKHFEQFGEILEAVVITDKASGRSKGYGFVTFREAEAARSACVDATPVIDGRRANCNLASLGLQRSKPSTPNHGGGGRINNMRVMMSTMQTGFGPPPPPQPPTFTHYPHLPLNLFGYSPYSPDYSSFPTNLYGMYGCTSGGQYGVYGNRNSGGGGLTAAAASATPFYPCGGGHGGVQFSQPQPFYHHLSSYNPHHYSPPTFSMQQGSRNRLSASTTSYSLPLKKLRVFGSYQASYHHLLLLRSRAILWFKGCSWLISALSFSPSALKATPFYGIWRWLFKQIPMGSPVSDGDHVVFVISHLLAIASSRENGFLFERYC
Protein: Ubiquitin carboxyl-terminal hydrolase (EC 3.4.19.12) (E9QFQ5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Receptor
- Transcription factor GATA-3
- Polyubiquitin-C
- Polyubiquitin-B
- Si:ch211-202a12.4.
- Ubiquitin-ribosomal protein eS31 fusion protein
Sequence:
MPRAESTSMDNSCQALYRTLVTQNGLQPENVDISQSVLYTSIMGLLLVTDKERELQLGNGQVGLRNVGNTCFLNAIVQCLSHTRSLRDYCLMRAYVQDKHSNQEPVLMDEFSKVLAGLWECDAGETTVNPGKFYRVFKESVPYFSGYSQQDAQEFLRFLLDRLHTEINRRPSKRPAVIERKEPAYTRFRISEEAFAMWQRHLDRDDSKIVDLFSGQLRSSLHCSVCSHYSNTFDVFCDLSLPIPKKSDYGRAVTLRECLDLFSQEEKLDKENSPMCERCNRRTESTKRLTIQRFPRVLVIHLNRFAMSRFSISKSTVPVSFPLTALDLGLFGPVDCGPVLYDLYAVCNHSGTVNMGHYTAACREEEGWCFYNDSCVDAISEEKLQSNQAYVLFYELKSCNISRK
Protein: Cleavage and polyadenylation specificity factor subunit 4 (CPSF 30 kDa subunit) (Cleavage and polyadenylation specificity factor 30 kDa subunit) (Q98881)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU369008}.
Interaction partners:
Sequence:
MQELIATVDHIKFDLEIAVEQQLGAQPLPFPGMDKSGAAVCEYFMRAACMKGGMCPFRHISGEKTVVCKHWLRGLCKKGDQCEFLHEYDMTKMPECYFYSKFGECSNKECPFLHIDPESKIKDCPWYDRGFCKHGPDCRHRHTRRVICVNYLVGFCPEGKSCKFMHPRFELPMGATEQPPLPQQVQTQQKQQNMQPINRSSQSLIQLTNPNISNNNHQRIPNAVGIVHSNSHMGGARGPRPLDQVTCYKCGEKGHYANKCTKGHLAFLSGQ
Protein: Olfactomedin 1a (A2AWU1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MSVPLLKIGVVLSTMAMITNWMSQTLPSLVGLNSTKLSVAPPGVPDRSTGVLPANPEESWQVYSSAQDSEGRCVCTVVAPQQTMCSRDARTKQLRQLLEKVQNMTQSIQNLDQRTQKDLQYVQRMEVQLRGLETKFKQVEESHKQNIAKQYKAIKAKMEELRPMIPVLEEYKADAKLVMQFKEEVKNLTSVLSELQEEIGAFDYEELHNRVSNLEERLRACMQKLACGKLTGISDAITIKTSGSRYGSWMTDPLAPDGDTRVWYMDGYHNNRFVREYKSMADFMYSDNFTSHRLPHPWSGTGQVVYNGSIYFNKFQSNTIIKFDFKTATISKSGQLDYAGFNNRYHYSWGGHSDIDLMVDEGGLWAIYATNQNAGNIVISKLNPATLQIVKSYTTNHPKRSAGEAFMICGTLYVTNGYSGGTKVYYAFHTNSSTYEYIDIPLQNKYSHISMLDYNPRDRALYAWNNGHQVLYNVTLFHVIRSEEL
Protein: Protein rotatin homolog (Anastral spindle 3) (A1Z8X3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Participes in the structural integrity of both centrioles and basal bodies and in centriole cohesion. Participates in the later stages of centriole assembly through the interaction with Rcd4 leading to the centriole to centrosome conversion.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:19948479, ECO:0000269|PubMed:32543652}. Note=Associated with the daughter centriole on mitotic entry (PubMed:32543652). Ana3 recruitment to the procentriole in interphase precedes the Rcd4 one (PubMed:32543652). Localizes to the basal bodies (PubMed:19948479). {ECO:0000269|PubMed:19948479, ECO:0000269|PubMed:32543652}.
Interaction partners:
- Anastral spindle 1, isoform A
- Protein PPP1R35 homolog
- Centrosomal protein 135kDa, isoform B
- Spindle assembly abnormal protein 6 homolog
- Anastral spindle 2, isoform A
- Spindle assembly abnormal 4
- BcDNA.LD24702
Sequence:
MSTKQSPALQLAEGQLTKLTSESEEIRMRALDQIETRFIRCLQLGEPIQFKPVLLLKQLIRWFGYTPPLVPDRVLAMIMELLRSEYAEAVIRKIPYERFKAELQKVRRVLHKQESKRVSELLDDMNLLLLEKYNIDRVTPSVSSLSSNDIPSQATESADSSSNQIYDNLKPEDYEPSWSHPCLDDVATMKSMIDLPRNSVELQLQLTELIIRMGDYPTEYFLQPPFVFLHLVQLQTMTDGSLIHVNRALIACLRLLQQRILLRRNTLSYADRFDPPSRPKQVKVVSALVILLENCMKLIRPLLFSCTNDNWHIMELIVEIVRTHDVLSSKIPLVSITLIADAVKSLLAYCNSVEGSCMTQLMDSLRIPRLQSLILNGVLHDMVALNINYDKRMDRRQAKALIQPIVLDSAYLSGMPERMKSLNTLISSLDSGPSPDEELIKLKRAYSVALNQLHPNTELTGSLLIQKYRQVCLVLVQLGSETLVKQLFGAVVKCIPFYAGNLKLRKDADELLYTLVDLPALKLRSLIYRLMIKSTVAHFHSFMNKTVYMTGCSNVDLIRQHILGVPLTPLLLRRMIIQSSEANTSERMQQWCLDYPIMIMKLNAILAPQDFSVVFPLLLPVLPLLISRSVTHKILHNVIWNVLEPDSSRLDPQLMLRGYVYFMFHPDGEVRSEATTTIAYVLQCQEQTNRYLPTASNVPVEHIANDLCIIQPPFCYRSIFIKCSDERFQGQRSLDALFRLLQAKDIKSNIRKSTMTQLNVLLRNWRACEEFSTKEDGYRLIMESLHNALKKGNDTDILLPTVSILMKLLFNDDEFRLEVANTFGVYTLLLRALFLFPHLEQLRQDVSICLFQMLFQNCITSTEDKLVLNANMEPLILPVTYEIEHKVIPTAVTEGLELQQNVEATHFGRDRAKAAQHWRLYMAYRVCQVPSSITLESVSALDIRESLKIKMADLALVRSSDLNEQLSCQFIAAENCSKHEDLQKTVSAIQLFLVVLRNSLSDTVAENLWKLIHKYIRLAPGNEADDKVYKSMLDLCVTCIRFSQPHAINGLSYALETDHHHSFQLLLHDSQISLDKLFLICQCMMQLLSNELSDDSMNWYGKFFMQLSAVAKTHFELRQLQHVRCILCMLRFVSERNLKFSNAQLMSYSQHFIQLSSNLRTSTQTGSEWQRDCLYIICQLQIHLIYQEPKASSKASIPNDVGASYKVLRYFLTLCGHGDSEVRALSWVSLANWITICGSQVAEILPRLDFLPGGLPACCLTTLTDAHEMMLIRELAGRVFILLMPLIGAESSLELLRKHDLLKTAYNSLKAIHDTPWMFKKIVGERHSCEVISCYVAICTKMVAMKPEWCAALCGHSLMSGLSDVMKKLKSQASCSIPLVELCASQICELYSMCYTNNFEFLKMTICRDSVFLQNYLTLINDVLSLECPEYMVIPLLKMFLIFCTDSNSNSFLIEQIKNKPSLFMDFFLFGLHVKLINSPFQRFTLSALSLVFTKAQLAAYDISMLSELEKFELAFSDPDIAKDGKQEFESKKKQSVSQCIYDESSDNSDDNKQRPNHAIQATNAAIIIFHRLDQLFDRYYLSKALNFLELPAVGQVQVCEALGELLKASTWAVKAAGESKLLGKVVHILDDFLNDEKIGNAAVYVKRVGPHKAQSIISNLLVLINMLSQWHSSPNSEIIQTSMAANIAKILIRIWPWLSHSYHLKKVTVQLIMFLTEHSFEMCKQISLLQSGHAQSLLHLMARVADFETTKKEIPNKEPSLNMVPALRVMVNCCCCTEGRLSLSKMNLLDMFDTILPANPCSTHLKVRPPVLIAWLGFWEVFSRYDVGGKACHLQSLINTIRRSPPLSHKRILCLRILRNMCFFNGNRPRLVELADFINLLRDILEQRVQKAPTSEKNGLNSFEEHRLAVLMLWKLFGFGAKYKGMLRGTKLFKLLIGLRVEMSVVFSEEENKYAGVPYANDLAKLLEKLMESMRQ
Protein: Regulator of ribonuclease activity B (P0AF90)
Organism: Escherichia coli (strain K12)
Function: Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01888}.
Interaction partners:
- Regulator of ribonuclease activity A
- Ribonuclease E
- ATP-dependent RNA helicase RhlB
- Lipoprotein NlpI
- RNA chaperone ProQ
- UPF0352 protein YejL
- Met repressor
- Negative modulator of initiation of replication
- Polyribonucleotide nucleotidyltransferase
- Der GTPase-activating protein YihI
Sequence:
MANPEQLEEQREETRLIIEELLEDGSDPDALYTIEHHLSADDLETLEKAAVEAFKLGYEVTDPEELEVEDGDIVICCDILSECALNADLIDAQVEQLMTLAEKFDVEYDGWGTYFEDPNGEDGDDEDFVDEDDDGVRH