wanglab/gogpt-training-data huggingface dataset:
Protein: Huntingtin-interacting protein 1 (C9K4U5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MDRVKSSMQQVPNPIPKVLSRRAGGANSLEVEKENFERNQAVSINKAINTQEVAVKEKHARTCILGTHHEKGAHTFWLAVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVIKDSMRHKADLNDMSRMWGHLSEGYGKLCSIYLKLLITKMEFHIKNPRFPGNLQMSNRQLDEAGENDVNNFFQLTVEMFDYLECELNLFLGVFSSLDMSRSVSVTAAGQCRLAPLIQVILDSSHLYDYTVKLLFKLHSCLPADTLQGHRDRFQEQFKKLKSLFYRSSNLQYFKRLIQIPQLPENPPNFLRASALSEHISPVVVIPAEASSPESEHVVETEDLVDTDIPPLTGTGDSKFDDLFGTSAATDPFNFNSQNGMRKDDKDRLIEQLTAELQALKEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQNSLTNERESGVKAAEALQNQLNEKESREQALESELVSLRWASLRAALEEAGKIVQDSLNQLEDPAHISCTSSADYLVSRCQVALDCVERLRSSRDGFVSDNTDVSGLVRAVTQFAHLVGDVIVQGSATSHMVPVEQADALADSVKACGAEALTLLCQLKEQESMGAADCSRLRTALDSVKALGEKLRPRGLELQQGELGDLVEQEMAATSAAVESAAARIEEMLNKSRAVDTGIKMEVNERILASCTDLMQAIRVLVLSSKDLQRDIVESGRGAASMKEFYAKNSRWTEGLISASKAVGWGATMLVDAADQVVQGKGKFEELMVCSHEIAASTAQLVAASKVKAEKGSSNLSRLQQASKGVTQATAGVVASTKSGKSQIEDTETMDFSAMTLTQIKRQEMDAQVLVLELETRLQKERERLGELRKKHYELAGVAEGWGGEEEG
Protein: Osteocalcin (Bone Gla protein) (BGP) (Gamma-carboxyglutamic acid-containing protein) (Q800Y1)
Organism: Argyrosomus regius (Meagre)
Function: Binds strongly to apatite and calcium.
Subcellular location: Secreted {ECO:0000269|PubMed:12568402}.
Interaction partners:
Sequence:
MKTLAILVLCSLAAICLTSSASAGAQPAGDSPVQGGLFMEKDQASAVVRQTRAAKELTLAQTESLREVCETNMACDEMADAQGIVAAYQAFYGPIPF
Protein: Exostosin-2 (EC 2.4.1.224) (EC 2.4.1.225) (Protein sister of tout-velu) (Q9Y169)
Organism: Drosophila melanogaster (Fruit fly)
Function: Glycosyltransferase required for the biosynthesis of heparan-sulfate and responsible for the alternating addition of beta-1-4-linked glucuronic acid (GlcA) and alpha-1-4-linked N-acetylglucosamine (GlcNAc) units to nascent heparan sulfate chains. Plays a central role in diffusion of morphogens hedgehog (hh), wingless (wg) and Decapentaplegic (dpp) via its role in heparan sulfate proteoglycans (HSPGs) biosynthesis, HSPGs being required for movement of Hh, Dpp and wg morphogens.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000269|PubMed:23720043}; Single-pass type II membrane protein {ECO:0000269|PubMed:23720043}. Note=Localization to the Golgi may be regulated by sau (PubMed:23720043).
Interaction partners:
- Exostosin-1
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase
- Dally-like, isoform A
- Adenosine 3'-phospho 5'-phosphosulfate transporter 1
- Heparin sulfate O-sulfotransferase
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase I
- 2-phosphoxylose phosphatase 1
- Extracellular sulfatase SULF-1 homolog
Sequence:
MTKIKNLLSFVTQSRAISHTNPREHILNCLTYGLLVIVALCAGFLLWDLSSSPRDGFFHGKRDSHTLILDLEHIQELAVNPEAEQRARNVNCTFWDCLNIYKCEHDRLKVYIYPLQEFVDEQSDKTATTLSSEYFQILEAVLKSRYYTSNPNEACLFLPSLDLLNQNVFDKHLAGAALASLDFWDRGANHIIFNMLPGGAPSYNTVLDVNTDNAIIFGGGFDSWSYRPGFDVAIPVWSPRLVRQHAHATAQRKFLLVVAQLNILPRFVRTLRELSLAHSEQLLLLGACENLDLTMRCPLSQHHKSLEYPRLLSRGKFCLLGRSLRMGQPDLVEIMSQHCIPVIAVDNYVLPFEDVIDWSLASVRIRENELHSVMQKLKAISSVKIVEMQKQVQWLFSKYFKDLKTVTLTALEVLESRIFPLRARSSRQWNTIDTNARSTFNPLFLPSLAPKSQGFTAVILTYDRVESLFLLIQKLAVVPSLQSILVIWNNQKKSPPHLSTFPSISKPLKIRQTKENKLSNRFYPYPEIETEAILTIDDDIIMLTTDELDFGYEVWREFPDHIVGFPSRIHVWENVTMRWHYESEWTNQISMVLTGAAFHHKYWSHMYTHAMPGDIKDWVDEHMNCEDIAMNFLVANITNNPPIKVTPRKKFKCPECTNTEMLSADLNHMRERSACIDRFSKIYGRMPLRTVEFRADPVLFRDNFPDKLKRYNDIGSL
Protein: Diphosphoinositol polyphosphate phosphohydrolase NUDT4B (DIPP-2B) (EC 3.6.1.52) (Nucleoside diphosphate-linked moiety X motif 4B) (Nudix motif 4B) (Nudix hydrolase 4B) (A0A024RBG1)
Organism: Homo sapiens (Human)
Function: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), PP-InsP4 and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphate Ap6A, but not Ap5A. The major reaction products are ADP and p4a from Ap6A. Also able to hydrolyze 5-phosphoribose 1-diphosphate. Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9NZJ9}.
Interaction partners:
Sequence:
MMKFKPNQTRTYDREGFKKRAACLCFRSEQEDEVLLVSSSRYPDQWIVPGGGMEPEEEPGGAAVREVYEEAGVKGKLGRLLGIFEQNQDRKHRTYVYVLTVTEILEDWEDSVNIGRKREWFKVEDAIKVLQCHKPVHAEYLEKLKLGCSPANGNSTVPSLPDNNALFVTAAQTSGLPSSVR
Protein: DNA repair protein RAD5A (EC 3.6.4.-) (Putative SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3-like 2) (SMARCA3-like protein 2) (RAD5 homolog A) (AtRAD5a) (Q9FNI6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions in error-free postreplication DNA repair or DNA-damage tolerance (DTT) pathway. Required for homologous recombination (HR) induced by DNA double-strand break (DSB) in somatic cells. Required for damage-induced DNA repair, independently of MUS81 and RECQL4A. Plays a role in synthesis-dependent strand annealing (SDSA) but not in single-strand annealing (SSA). Possesses double-stranded DNA-dependent ATPase activity. Is able to regress replication forks with preference for forks with a leading strand gap. Is able to catalyze branch migration of Holliday junctions and is unaffected by protein blockades.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA polymerase zeta catalytic subunit
- Ubiquitin-conjugating enzyme E2 13
- Fanconi-associated nuclease 1 homolog
- ATP-dependent DNA helicase Q-like 4A
- DNA repair protein REV1
- Proliferating cell nuclear antigen 2
- Crossover junction endonuclease MUS81
- DNA repair endonuclease UVH1
- DEAD-box ATP-dependent RNA helicase FANCM
- DNA 5'-3' helicase FANCJ
Sequence:
MGTKVSDDLVSTVRSVVGSDYSDMDIIRALHMANHDPTAAINIIFDTPSFAKPDVATPTPSGSNGGKRVDSGLKGCTFGDSGSVGANHRVEEENESVNGGGEESVSGNEWWFVGCSELAGLSTCKGRKLKSGDELVFTFPHSKGLKPETTPGKRGFGRGRPALRGASDIVRFSTKDSGEIGRIPNEWARCLLPLVRDKKIRIEGSCKSAPEALSIMDTILLSVSVYINSSMFQKHSATSFKTASNTAEESMFHPLPNLFRLLGLIPFKKAEFTPEDFYSKKRPLSSKDGSAIPTSLLQLNKVKNMNQDANGDENEQCISDGDLDNIVGVGDSSGLKEMETPHTLLCELRPYQKQALHWMTQLEKGNCTDEAATMLHPCWEAYCLADKRELVVYLNSFTGDATIHFPSTLQMARGGILADAMGLGKTVMTISLLLAHSWKAASTGFLCPNYEGDKVISSSVDDLTSPPVKATKFLGFDKRLLEQKSVLQNGGNLIVCPMTLLGQWKTEIEMHAKPGSLSVYVHYGQSRPKDAKLLSQSDVVITTYGVLTSEFSQENSADHEGIYAVRWFRIVLDEAHTIKNSKSQISLAAAALVADRRWCLTGTPIQNNLEDLYSLLRFLRIEPWGTWAWWNKLVQKPFEEGDERGLKLVQSILKPIMLRRTKSSTDREGRPILVLPPADARVIYCELSESERDFYDALFKRSKVKFDQFVEQGKVLHNYASILELLLRLRQCCDHPFLVMSRGDTAEYSDLNKLSKRFLSGKSSGLEREGKDVPSEAFVQEVVEELRKGEQGECPICLEALEDAVLTPCAHRLCRECLLASWRNSTSGLCPVCRNTVSKQELITAPTESRFQVDVEKNWVESSKITALLEELEGLRSSGSKSILFSQWTAFLDLLQIPLSRNNFSFVRLDGTLSQQQREKVLKEFSEDGSILVLLMSLKAGGVGINLTAASNAFVMDPWWNPAVEEQAVMRIHRIGQTKEVKIRRFIVKGTVEERMEAVQARKQRMISGALTDQEVRSARIEELKMLFT
Protein: DNA primase small subunit (EC 2.7.7.-) (DNA polymerase alpha:primase complex p48 subunit) (DNA polymerase-primase complex p48 subunit) (Pol alpha-primase complex p48 subunit) (DNA primase 48 kDa subunit) (P10363)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication. In a complex with DNA polymerase alpha (DNA polymerase alpha:primase) constitutes a replicative polymerase. Both primase components participate in formation of the active center, but the ATP-binding site is exclusively located on p48.
Interaction partners:
- DNA polymerase alpha subunit B
- DNA polymerase alpha catalytic subunit A
- DNA primase large subunit
- DNA polymerase epsilon catalytic subunit A
- DNA polymerase delta catalytic subunit
- DNA polymerase epsilon subunit B
- DNA polymerase zeta catalytic subunit
- Replication factor A protein 2
- DNA polymerase delta small subunit
- DNA polymerase epsilon subunit D
Sequence:
MTNSVKTNGPSSSDMEYYYKSLYPFKHIFNWLNHSPKPSRDMINREFAMAFRSGAYKRYNSFNSVQDFKAQIEKANPDRFEIGAIYNKPPRERDTLLKSELKALEKELVFDIDMDDYDAFRTCCSGAQVCSKCWKFISLAMKITNTALREDFGYKDFIWVFSGRRGAHCWVSDKRARALTDVQRRNVLDYVNVIRDRNTDKRLALKRPYHPHLARSLEQLKPFFVSIMLEEQNPWEDDQHAIQTLLPALYDKQLIDSLKKYWLDNPRRSSKEKWNDIDQIATSLFKGPKQDSHIIKLRECKEDLVLMTLYPKLDVEVTKQTIHLLKAPFCIHPATGNVCVPIDESFAPEKAPKLIDLQTEMEKNNDVSLTALQPFINQFQAYVSSLLKNELGSVKREREDDDEPASLDF
Protein: Far upstream element binding protein 1 (C9JSZ1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MADYSTVPPPSSGSAGGGGGGGGGGGVNDAFKDALQRARQIAAKIGGDAGTSLNSNDYGYGGQKRPLEDGDGSWTSPSSTTHWEGMPSPFKDQPDAKKVAPQNDSFGTQLPPMHQQQRSVMTEEYKVPDGMVGFIIGRGGEQISRIQQESGCKIQIAPDSGGLPERSCMLTGTPESVQSAKRLLDQIVEKGRPAPGFHHGDGPGNAVQEIMIPASKAGLVIGKGGETIKQLQERAGVKMVMIQDGPQNTGADKPLRITGDPYKVQQAKEMVLELIRDQGGFREVRNEYGSRIGGNEGIDVPIPRFAVGIVIGRNGEMIKKIQNDAGVRIQFKPDDGTTPERIAQITGPPDRCQHAAEIITDLLRSVQAGNPGGPGPGGRGRGRGQGNWNMGPPGGLQEFNFIVPTGKTGLIIGKGGETIKSISQQSGARIELQRNPPPNADPNMKLFTIRGTPQQIDYARQLIEEKIGGPVNPLGPPVPHGPHGVPGPHGPPGPPGPGTPMGPYNPAPYNPGPPGPAPHGPPAPYAPQGWGNAYPHWQQQAPPDPAKAGTDPNSAAWAAYYAHYYQQQAQPPPAAPAGAPTTTQTNGQGDQQNPAPAGQVDYTKAWEEYYKKMGQAVPAPTGAPPGGQPDYSAAWAEYYRQQAAYYAQTSPQGMPQHPPAPQCLPRPSTLGSAAKSTSAEDAASTKS
Protein: Methylcytosine dioxygenase TET (EC 1.14.11.80) (A0A2R8Q4R6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
Interaction partners:
- G/T mismatch-specific thymine DNA glycosylase
- G/T mismatch-specific thymine DNA glycosylase
- DNA
- DNA
- E3 ubiquitin-protein ligase UHRF1
Sequence:
MHKLRGGPGPPVQDIYEFSLDEEDPKVFLGARSARVVSPADDYIRSEHEQAGMFSLSQMEDQEPIEPVVAQKKKRKRCGVCGPCMRKENCGTCSNCLNRKIGHQICKLRKCDELKRKKSPWEVEYFEDKNTQPVIPNLAKETVSVVGSVDGPRGKGQMEIGSHERLEEGLLNQELSNGLSKHASNEENVCDNEDRDATKEQHQHNFHEGAGSISQTPGWVLEHTGKLSNPESQQGVWSGQNASTTVNDVDMEDAQTLVAFSVGSLPPYTNHQPSPTPTAQLYERFNQEMSNGGEEAKKKGVDGAFCPPEDLNTLQAALSKARHGHKPPNCDCDGPDCPDYLEWLEKQIKLVTNCQNKTSCNLSGTAQQPLEQHHYSQSQPQQCGGKPLCVQDTNPQPLVNKPSTPRPFGPPAPIPCSPSVLSIAKERNVSLQTAIAIEALTQLSATVPQTVVPPGESSLANHHQHLPTSYHQNMPQVVSSSPGPLLSSSATSAIPQSNHYPQQELTTWEQQRPQSKGEAPTANIFPSSSHYSSSYPSSKPPFTNMHASSPNPRPQQWNQGTASSCEKNSPRNAWMMANTDSKQHFAKPSHESSDPVSELKQLLGDTGGKHPFKFPFPHPSLQDVHKGSFTGMPHIKQEVETKEYLGSECSVMGQEGMLNGQQQFQGQQLSSTIRHSTQAALQQHLHHKRNLFSNSPTYGPLAHMACQDLRKWWPQTIPENLINIKQEHKEPKKKKGAQSSHLKQPAGGPFGPLGTPLPKPKPIVIKKHKQKASQPTFLPQIQITISKPPLISPGYAPSRAQLVPSLPGMEAGLPPTQVAESHPAPAQSQESIINCSSAPISENSHSSTNPVSVLAPSTQKVIACPGSAGSNDSIPTTSITPQTSTTQPSPSLAGLSNLDPKFEELIRQFEEEFGDTAASAAETPENGPVQPVVTESHPNSGQLRPESPSLKQPNNCPPVPTNESEPMNEGQKDIPERQKEKTPLPPEELCTVKQESEECALDVKPSGELLSEFLKQQNPFVAPFSPPNKRMKIESSNGVTVLSTTACFSADREGDDFNTPTKDIFPSSPSLKGFLESPLRYLDTPTKNLLDTPGKDVQPDFPICDCVDQVLEKDEGPYYNHLGSGRDIPSVRQLMEDRYGEKGEAVRIEKVVYTGREGKSSQGCPIAKWVLRRSSEKEKVLCVVKQRPGHHCANTVIVVVILAWEGVPRALGDKLYREVTETITKYGNPTSRRCGLNEDRTCACQGKDPETCGASFSFGCSWSMYFNGCKYARSKVPRKFRLQGEHPKEEDNLRDNFQALATHVAPLYKKLAPQAYSNQCLHEDVASDCRLGLKEGRPFSGITACMDFCAHAHKDQHNLHNGCTVVCTLTKEDNRTVGTIPEDEQLHVLPLYKLATTDEFGSEENQRLKMQTGAIQVLANFRREVRKLPEPAKSCRQRRLEAKKAASEKKNRKLQLAETPEKTVKMEIRHAESPHIQQGNKAIPKQEVKPTIKKEPVDHFQPFNGAIHGYQALGNGKTNPDPHNMNSSFSYPGNYARGRIPGNSHPPAQNPINGFHPNLQDIRYGYYNYPSSALFSPELLRYDKGAWPKNGEPSAQAFEQKPDVQCLQANLAQAYPTHHGQSQAQMADASIQGYPQPSDISQCRTPSMSLEQTHRSKPIVKQEPMDVPLYEARSDGQAQSCPTTPSTTPTPEGWHGHKPNGSLVPKGWDGNIRAASNNSPFTPDKQRLHQQHQHEHPQYPQQQQWNSYSCPNTPMASPAPSPSPSLKAGLSPAPSPHPSTPRQWGSPAPSPQPKAWGPYGPMGYGAGVIRQGNPAGAYPDNMLSQAGVNCGSAPLGLQEKAWKSGGGSAAGSTPSPAPEGRLFPDALQRSDGQACWDSGAETQSERDPEEDEVWSDSEHNFLDPNIGGVAVAPAHGCVLIECARRELHATTPLKKPDRTHPSRISLVFYQHKNLNQPCHGLALWESKMKILAERARQRQQEAALLGLSQEEIKAYGKKRKWAAGSASPSPGQTKDKREGVVTRMAPTQHSTTIVTVSPYPSTHLTGPYSRFV
Protein: Metallothionein-1E (MT-1E) (Metallothionein-IE) (MT-IE) (P04732)
Organism: Homo sapiens (Human)
Function: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.
Interaction partners:
Sequence:
MDPNCSCATGGSCTCAGSCKCKECKCTSCKKSCCSCCPVGCAKCAQGCVCKGASEKCSCCA
Protein: Cardiac voltage-gated potassium channel accessory subunit isoform 3a (Cardiac voltage-gated potassium channel accessory subunit isoform 3b) (Potassium voltage-gated channel subfamily E regulatory subunit 3) (Q2N1I1)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
METTNGTETWYESLHAVLKALNATLHSNLLCRPGPGLGPDNQTEERRASLPGRDDNSYMYILFVMFLFAVTVGSLILGYTRSRKVDKRSDPYHVYIKNR
Protein: R3H domain-containing protein (Q383A2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAATGSREEMMEALNKARQAMARRVPTPTASTVQSSSEHDPSANVGVLQIYDAADTSLCRHARPSEAKDNRAHFFETWCKKIEVFVADPTKTTLELPPELCANDRRELHNLAEKYNLSHHSRGTGATRHLVLKKDALHYRMPDAAPANIEAIKRDPGTKESKFHLRRVKQNPEAPAGSMGAFGDETTAAMVHRLVRATDEYRRAVNVGYTQDELLAFETGESVEGILRSGGERDAQPATNADVEDPTGLCASPPRARITGGADYEARAKDSSAGEKSKAVYDEMCLRCQTRSRVDYDIQKWDCNGYCAKCTAQTIWKLVEVENSTGMRSAQRKHTREEFEKADEALPQEVQQPEEIDKDNDEDDTITVEDVVDMASMNDFSAADVNWIRRFAVHHSSKEVCCSLSTHIVFCIEFNDLLTMRIFRPFLKLQGSTDSSDEKKRTKNECGASSDGSTLTETHGAWFVWLREVKPAGVALSTLLDELAGCTPEGYDRLCVAFPNMSVYGTEASCVCLVKPGVLNMEGLQAMRQKYGEQNFRLAQELEVALAGDSKPA
Protein: Oxytocin-neurophysin 1 (OT-NPI) [Cleaved into: Oxytocin (Ocytocin); Neurophysin 1] (P35454)
Organism: Mus musculus (Mouse)
Function: Neurophysin 1 specifically binds oxytocin.
Interaction partners:
- Oxytocin receptor
- Vasopressin V1a receptor
- Hypocretin neuropeptide precursor
- Pro-thyrotropin-releasing hormone
- Vasopressin V1b receptor
- Pro-MCH
- Vasopressin-neurophysin 2-copeptin
- Pro-opiomelanocortin
- D
- 5-hydroxytryptamine receptor 1A
Sequence:
MACPSLACCLLGLLALTSACYIQNCPLGGKRAVLDLDMRKCLPCGPGGKGRCFGPSICCADELGCFVGTAEALRCQEENYLPSPCQSGQKPCGSGGRCAATGICCSPDGCRTDPACDPESAFSER
Protein: Protein Nef (Q5QGG3)
Organism: Simian immunodeficiency virus (SIV)
Interaction partners:
Sequence:
MGGAISMRRSRPSGDLRQRLLRARGETYGRLLGEVEDGYSQSPGGLDKGLSSLSCEGQKYNQGQYMNTPWRNPAEEREKLAYRKQNMDDIDEZDDDLVGVSVRPKVPLRTMSYKLAIDMSHFIKEKGGLEGIYYSARRHRILDIYLEKEEGIIPDWQDYTSGPGIRYPKTFGWLWKLVPVNVSDEAQEDEEHYLMHPAQTSQWDDPWGEVLAWKFDPTLAYTYEAYVRYPEEFGSKSGLSEEEVRRRLTARGLLNMADKKETR
Protein: Neuropilin-1 (Vascular endothelial cell growth factor 165 receptor) (CD antigen CD304) (O14786)
Organism: Homo sapiens (Human)
Function: Cell-surface receptor involved in the development of the cardiovascular system, in angiogenesis, in the formation of certain neuronal circuits and in organogenesis outside the nervous system. Mediates the chemorepulsant activity of semaphorins. Recognizes a C-end rule (CendR) motif R/KXXR/K on its ligands which causes cellular internalization and vascular leakage. It binds to semaphorin 3A, the PLGF-2 isoform of PGF, the VEGF165 isoform of VEGFA and VEGFB. Coexpression with KDR results in increased VEGF165 binding to KDR as well as increased chemotaxis. Regulates VEGF-induced angiogenesis. Binding to VEGFA initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development (By similarity). Regulates mitochondrial iron transport via interaction with ABCB8/MITOSUR.
Subcellular location: [Isoform 2]: Secreted {ECO:0000269|PubMed:10688880}.; SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305|PubMed:30623799}; Single-pass type I membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:30623799}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:30623799}.
Interaction partners:
- Semaphorin-3B
- Plexin-A1
- Semaphorin-3F
- Plexin-A4
- Semaphorin-3A
- Neural cell adhesion molecule L1
- Vascular endothelial growth factor receptor 2
- Plexin-A3
- Plexin-A2
- Semaphorin-3D
Sequence:
MERGLPLLCAVLALVLAPAGAFRNDKCGDTIKIESPGYLTSPGYPHSYHPSEKCEWLIQAPDPYQRIMINFNPHFDLEDRDCKYDYVEVFDGENENGHFRGKFCGKIAPPPVVSSGPFLFIKFVSDYETHGAGFSIRYEIFKRGPECSQNYTTPSGVIKSPGFPEKYPNSLECTYIVFVPKMSEIILEFESFDLEPDSNPPGGMFCRYDRLEIWDGFPDVGPHIGRYCGQKTPGRIRSSSGILSMVFYTDSAIAKEGFSANYSVLQSSVSEDFKCMEALGMESGEIHSDQITASSQYSTNWSAERSRLNYPENGWTPGEDSYREWIQVDLGLLRFVTAVGTQGAISKETKKKYYVKTYKIDVSSNGEDWITIKEGNKPVLFQGNTNPTDVVVAVFPKPLITRFVRIKPATWETGISMRFEVYGCKITDYPCSGMLGMVSGLISDSQITSSNQGDRNWMPENIRLVTSRSGWALPPAPHSYINEWLQIDLGEEKIVRGIIIQGGKHRENKVFMRKFKIGYSNNGSDWKMIMDDSKRKAKSFEGNNNYDTPELRTFPALSTRFIRIYPERATHGGLGLRMELLGCEVEAPTAGPTTPNGNLVDECDDDQANCHSGTGDDFQLTGGTTVLATEKPTVIDSTIQSEFPTYGFNCEFGWGSHKTFCHWEHDNHVQLKWSVLTSKTGPIQDHTGDGNFIYSQADENQKGKVARLVSPVVYSQNSAHCMTFWYHMSGSHVGTLRVKLRYQKPEEYDQLVWMAIGHQGDHWKEGRVLLHKSLKLYQVIFEGEIGKGNLGGIAVDDISINNHISQEDCAKPADLDKKNPEIKIDETGSTPGYEGEGEGDKNISRKPGNVLKTLDPILITIIAMSALGVLLGAVCGVVLYCACWHNGMSERNLSALENYNFELVDGVKLKKDKLNTQSTYSEA
Protein: Glycine cleavage system H protein (Q38E17)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion {ECO:0000256|RuleBase:RU364055}.
Interaction partners:
- Aminomethyltransferase
- Glycine cleavage system P protein
- lipoyl
- Lipoyl synthase, mitochondrial
- Dihydrolipoyl dehydrogenase
- Dihydrolipoamide dehydrogenase, putative
- Dihydrolipoamide dehydrogenase, putative
- Acyl carrier protein
- Dihydrolipoamide dehydrogenase, point mutation
- Lipoate-protein ligase, putative
Sequence:
MRRALFCPAATVAATIRFYTTRFFTDSHEWVEHGDGIATIGITAHAQENLGDVVYVALPNVGDKITERDMLGEVESVKATSNVYCPVTGVVHAVNEKVKDEPSLINRSAEADGWLVKVKCDEIPKGLMTADEYNKFIE
Protein: Ethylene response sensor 1 (AtERS1) (EC 2.7.11.-) (EC 2.7.13.3) (Protein ERS1) (Q38846)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ethylene receptor related to bacterial two-component regulators. Acts as a redundant negative regulator of ethylene signaling.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:10938361}; Multi-pass membrane protein {ECO:0000305|PubMed:10938361}.
Interaction partners:
- Serine/threonine-protein kinase CTR1
- Protein REVERSION-TO-ETHYLENE SENSITIVITY1
- Protein RTE1-HOMOLOG
- Ethylene-insensitive protein 2
- Protein ETHYLENE INSENSITIVE 3
- ETHYLENE INSENSITIVE 3-like 1 protein
- EIN3-binding F-box protein 1
- Ethylene response sensor 2
- EIN3-binding F-box protein 2
- Telomere repeat-binding protein 1
Sequence:
MESCDCFETHVNQDDLLVKYQYISDALIALAYFSIPLELIYFVQKSAFFPYKWVLMQFGAFIILCGATHFINLWMFFMHSKAVAIVMTIAKVSCAVVSCATALMLVHIIPDLLSVKNRELFLKKKADELDREMGLILTQEETGRHVRMLTHGIRRTLDRHTILRTTLVELGKTLCLEECALWMPSQSGLYLQLSHTLSHKIQVGSSVPINLPIINELFNSAQAMHIPHSCPLAKIGPPVGRYSPPEVVSVRVPLLHLSNFQGSDWSDLSGKGYAIMVLILPTDGARKWRDHELELVENVADQVAVALSHAAILEESMHARDQLMEQNFALDKARQEAEMAVHARNDFLAVMNHEMRTPMHAIISLSSLLLETELSPEQRVMIETILKSSNLVATLISDVLDLSRLEDGSLLLENEPFSLQAIFEEVISLIKPIASVKKLSTNLILSADLPTYAIGDEKRLMQTILNIMGNAVKFTKEGYISIIASIMKPESLQELPSPEFFPVLSDSHFYLCVQVKDTGCGIHTQDIPLLFTKFVQPRTGTQRNHSGGGLGLALCKRFVGLMGGYMWIESEGLEKGCTASFIIRLGICNGPSSSSGSMALHLAAKSQTRPWNW
Protein: CMRF35-like molecule 3 (CLM-3) (CD300 antigen-like family member H) (CD300 molecule-like family member D3) (Q6SJQ5)
Organism: Mus musculus (Mouse)
Function: Acts as an activating receptor inducing cytokine production in mast cells. Can act as a positive regulator of TLR9 signaling in macrophages, leading to enhanced production of pro-inflammatory cytokines.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Early endosome {ECO:0000269|PubMed:21940676}. Lysosome {ECO:0000269|PubMed:21940676}.
Interaction partners:
Sequence:
MWQFPALLFLFLPGCCTAQDPVTGPEEVSGQEQGSLTVQCRYDSGWKDYKKYWCRGAYWKSCEILVETDASEQLVKENRVSIRDDQTDFIFTVTMEDLRMSDADIYWCGITKAGTDPMFKVNVNIDPEISTTIMTTTATVLPSTVLTSTVLTSTVLTPTTPTTESIGTENIGQVTQNSLFIWSLLSSISFLLMVFVVVPLLLSMLSAVLWVNRPQRHYGGGEIGLVETHRSDALDGEKHFPGDEK
Protein: L-malyl-CoA/beta-methylmalyl-CoA lyase (EC 4.1.3.24) ((3S)-malyl-CoA/beta-methylmalyl-CoA lyase) (Q5V463)
Organism: Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Function: Involved in the methylaspartate cycle. Catalyzes the reversible cleavage of beta-methylmalyl-CoA to propionyl-CoA and glyoxylate, as well as the reversible cleavage of (S)-malyl-CoA to acetyl-CoA and glyoxylate. In addition, it has a small malyl-CoA thioesterase activity. It can also catalyzes the cleavage of (S)-citramalyl-CoA to acetyl-CoA and pyruvate.
Interaction partners:
- Mesaconyl-CoA hydratase
- Glutamate mutase sigma subunit 1
- Acetyl-CoA carboxylase biotin carboxylase subunit
- Acetyl-CoA carboxylase biotin carboxylase subunit
- Acetyl-CoA carboxylase alpha subunit
- Acetyl-CoA carboxylase alpha subunit
- Aminotransferase class V
- Succinyl-CoA:mesaconate CoA-transferase
- Apparent malate synthase
- 2-dehydro-3-deoxyphosphogluconate aldolase/4-hydroxy-2-oxoglutarate aldolase
Sequence:
MTRLCRTFQTAPAAIPNDNSAKFLVSGLTSKGFQAPDWLVPDIEDGTAPSMKDEAVDNIIEHIPDHADDFAGDILPRVEWAYDDANARERGIEQVTRLAEAVGEELDGFVFPKVGRLDDVRDAAGVIADAERDAGLPEGTLEMAIILETAPGRSDLREICQYATDSRLSGLVFGPVDYTAELGGRTLDGERPRWDGLLEALSNETSAADIVAIGGPFDQLFHERAGVTYYNAEGYADQVAYEATIGIDGSWSLHPKQTEQANRIHMPTVEEMERDLHKIESFNEAKREGTGAVVVDGQMVDEATYKNFANTVKTVRAIDETHPAQTEAYYDDDLLARARDVELIFG
Protein: Low amplitude and bright protein LabA (Q31LZ8)
Organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (Anacystis nidulans R2)
Function: Functions in an output pathway of the circadian clock. One of three clock output pathways. Involved in negative feedback regulation of KaiC; deletion leads to overexpression of KaiC protein and decreases the amplitude of the circadian reponse. Overexpression reduces the expression of circadian genes.
Interaction partners:
- Circadian input-output histidine kinase CikA
- Light dependent period A
- Circadian clock oscillator protein KaiC
- Circadian clock oscillator protein KaiA
- Circadian phase modifier
- tRNA
- tRNA uridine
Sequence:
MAFRPSRLAIFIDGNNMFYAQQKNGWFFDPRRVLNYFANRPEIELVNAYWYTGLKDPQDQRGFRDALVSLGYTVRTKMLKEFHDESNGNRYFQRANLDIEIVIDMFNTVEQYDEIVLFSGDGDFERAIELLRAKQTHITVVSTDGMIARELRNATDRYIDLNDIRSFIEKTERPEPFVSAPVIAPA
Protein: B-cell linker protein (B-cell adapter containing a SH2 domain protein) (B-cell adapter containing a Src homology 2 domain protein) (Cytoplasmic adapter protein) (Src homology 2 domain-containing leukocyte protein of 65 kDa) (SLP-65) (Q8WV28)
Organism: Homo sapiens (Human)
Function: Functions as a central linker protein, downstream of the B-cell receptor (BCR), bridging the SYK kinase to a multitude of signaling pathways and regulating biological outcomes of B-cell function and development. Plays a role in the activation of ERK/EPHB2, MAP kinase p38 and JNK. Modulates AP1 activation. Important for the activation of NF-kappa-B and NFAT. Plays an important role in BCR-mediated PLCG1 and PLCG2 activation and Ca(2+) mobilization and is required for trafficking of the BCR to late endosomes. However, does not seem to be required for pre-BCR-mediated activation of MAP kinase and phosphatidyl-inositol 3 (PI3) kinase signaling. May be required for the RAC1-JNK pathway. Plays a critical role in orchestrating the pro-B cell to pre-B cell transition. May play an important role in BCR-induced B-cell apoptosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9697839}. Cell membrane {ECO:0000269|PubMed:9697839}. Note=BCR activation results in the translocation to membrane fraction.
Interaction partners:
- Tyrosine-protein kinase Lyn
- Proto-oncogene vav
- Growth factor receptor-bound protein 2
- Tyrosine-protein kinase BTK
- Tyrosine-protein kinase SYK
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
- B-cell antigen receptor complex-associated protein alpha chain
- SH3 domain-containing kinase-binding protein 1
- Lymphocyte cytosolic protein 2
- E3 ubiquitin-protein ligase CBL
Sequence:
MDKLNKITVPASQKLRQLQKMVHDIKNNEGGIMNKIKKLKVKAPPSVPRRDYASESPADEEEQWSDDFDSDYENPDEHSDSEMYVMPAEENADDSYEPPPVEQETRPVHPALPFARGEYIDNRSSQRHSPPFSKTLPSKPSWPSEKARLTSTLPALTALQKPQVPPKPKGLLEDEADYVVPVEDNDENYIHPTESSSPPPEKAPMVNRSTKPNSSTPASPPGTASGRNSGAWETKSPPPAAPSPLPRAGKKPTTPLKTTPVASQQNASSVCEEKPIPAERHRGSSHRQEAVQSPVFPPAQKQIHQKPIPLPRFTEGGNPTVDGPLPSFSSNSTISEQEAGVLCKPWYAGACDRKSAEEALHRSNKDGSFLIRKSSGHDSKQPYTLVVFFNKRVYNIPVRFIEATKQYALGRKKNGEEYFGSVAEIIRNHQHSPLVLIDSQNNTKDSTRLKYAVKVS