wanglab/gogpt-training-data huggingface dataset:
Protein: SHC-transforming protein 3 (Neuronal Shc) (N-Shc) (Protein Rai) (SHC-transforming protein C) (Src homology 2 domain-containing-transforming protein C3) (SH2 domain protein C3) (Q92529)
Organism: Homo sapiens (Human)
Function: Signaling adapter that couples activated growth factor receptors to signaling pathway in neurons. Involved in the signal transduction pathways of neurotrophin-activated Trk receptors in cortical neurons.
Interaction partners:
- BDNF/NT-3 growth factors receptor
- Epidermal growth factor receptor
- Growth factor receptor-bound protein 2
- High affinity nerve growth factor receptor
- Proto-oncogene tyrosine-protein kinase Src
- Receptor tyrosine-protein kinase erbB-2
- Son of sevenless homolog 1
- Receptor tyrosine-protein kinase erbB-3
- Insulin-like growth factor 1 receptor
- Receptor tyrosine-protein kinase erbB-4
Sequence:
MLPRTKYNRFRNDSVTSVDDLLHSLSVSGGGGKVSAARATPAAAPYLVSGEALRKAPDDGPGSLGHLLHKVSHLKLSSSGLRGLSSAARERAGARLSGSCSAPSLAAPDGSAPSAPRAPAMSAARKGRPGDEPLPRPPRGAPHASDQVLGPGVTYVVKYLGCIEVLRSMRSLDFSTRTQITREAISRVCEAVPGAKGAFKKRKPPSKMLSSILGKSNLQFAGMSISLTISTASLNLRTPDSKQIIANHHMRSISFASGGDPDTTDYVAYVAKDPVNRRACHILECCDGLAQDVIGSIGQAFELRFKQYLQCPTKIPALHDRMQSLDEPWTEEEGDGSDHPYYNSIPSKMPPPGGFLDTRLKPRPHAPDTAQFAGKEQTYYQGRHLGDTFGEDWQQTPLRQGSSDIYSTPEGKLHVAPTGEAPTYVNTQQIPPQAWPAAVSSAESSPRKDLFDMKPFEDALKNQPLGPVLSKAASVECISPVSPRAPDAKMLEELQAETWYQGEMSRKEAEGLLEKDGDFLVRKSTTNPGSFVLTGMHNGQAKHLLLVDPEGTIRTKDRVFDSISHLINHHLESSLPIVSAGSELCLQQPVERKQ
Protein: At3g47490 (HNH endonuclease) (Q9SN88)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDWPTTTLISRRICNLLIFFVKLNHKNLSIDSDNPQHSAMKPDPTRRRNRALSSSSPSKTRPELSSGSPNRNTGEARGGKVKTSATLLDREEMGLFPGSGYGDPNPEPRSFPYSVKQQCWEKAEKIKGRDPERWRRDHLGNIVFRKLVGCPGCLCHDYDHIVPYSKGGKSTLENCQVLQAKVNRSKGNKTDISRSELIQRSSYCRVAGRDMDLIELTAYGNVQRAPTSSGCRIQ
Protein: NEDD4-like E3 ubiquitin-protein ligase WWP1 (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase WWP1) (WW domain-containing protein 1) (Q8BZZ3)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Ubiquitinates and promotes degradation of SMAD2 in response to TGF-beta signaling, which requires interaction with TGIF (By similarity). Ubiquitinates ERBB4 isoforms JM-A CYT-1 and JM-B CYT-1, KLF2, KLF5 and TP63 and promotes their proteasomal degradation. Ubiquitinates RNF11 without targeting it for degradation. Ubiquitinates and promotes degradation of TGFBR1; the ubiquitination is enhanced by SMAD7. Ubiquitinates SMAD6 and SMAD7.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15735697}. Cell membrane {ECO:0000269|PubMed:15735697}; Peripheral membrane protein {ECO:0000269|PubMed:15735697}. Nucleus {ECO:0000269|PubMed:15735697}. Cell junction {ECO:0000250|UniProtKB:Q9H0M0}. Note=Translocates to the plasma membrane in response to increased cell-cell contact inhibition and subsequent interaction with the Crumbs complex. {ECO:0000250|UniProtKB:Q9H0M0}.
Interaction partners:
- Transcription factor HIVEP3
- Spartin
- Receptor tyrosine-protein kinase erbB-4
- Polyubiquitin-B
- Mothers against decapentaplegic homolog 7
- Ubiquitin-conjugating enzyme E2 L3
- Ubiquitin-ribosomal protein eL40 fusion protein
- E3 ubiquitin-protein ligase Itchy
- Polyubiquitin-C
- Ubiquitin-ribosomal protein eS31 fusion protein
Sequence:
MATASPRSDTSDIHSGRLQLKVTVSSAKLKRKKNWFGTAIYTEVIVDGEVKKTAKSSSSSNPKWDEQLIVNVTPQTTLEFRVWSHHTLKADALLGKATVDLKQVLLTHNRKLEKVKEQLKLSLENKNGIVQTGELTVVLDGLVIEQEPVTNRSSSPPIEIQQNGDALHENGDPATRTTPRLPVEGTIGIDNHVSTNTVVPNSCCSHVVNGENTPSSPSQVAARPKNAPAPKPVTSAPTSDTVNGESSSVLADNTSTMGTLLPSEDTTSTSNCTSTTTQEPPVQEPPASSEHSECIPSASAEVGPEARSLIDPDSDSRNNSVFDKVRQPEGCVEPLRPQSGNTNTEALPSGWEQRKDPHGRTYYVDHNTRTTTWERPQPLPPGWERRVDDRGRVYYVDHNTRTTTWQRPTMESVRNFEQWQSQRNQLQGAMQQFNQRYLYSASMLAAENDPYGPLPPGWEKRVDSTDRVYFVNHNTKTTQWEDPRTQGLPNEEPLPEGWEIRYTREGVRYFVDHNTRTTTFKDPRNGKSSVTKGGPQIAYERSFRWKLAHFRYLCQSNALPSHVKINVSRQTLFEDSFQQIMALKPYDLRRRLYVIFRGEEGLDYGGLAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASTINPDHLSYFCFIGRFIAMALFHGKFIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFSVDMEILGKVTSHDLKLGGSNILVTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYFDEKELEVMLCGMQEVDLADWQRNTVYRHYTRNSKQIIWFWQFVKETDNEVRMRLLQFVTGTCRLPLGGFAELMGSNGPQKFCIEKVGKDTWLPRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFGQE
Protein: Uncharacterized protein (Q38FR8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MNRSCLEVNVSDYICLERIGGDYEWSNTLARVIGLPTSQHVRVELFDRVDAVPGGFEPYAEKLGELAVQQDRLDGLNELKALQQQYQQLVEDEDRSSERLCRAREVTQEKQAIAAAFTRQQMVELDQVRAAIEQVPARSWRIIRNINNPSEELFSLVRALMIALQEDHNGSWESMQIVMRQSDFVGRIMELDCTVAPLSKLQRKKIKNELALVPAESLKERRGKSDSFPKLLRGAPLPVVIRRWLNVQMACSRAREAEERVADRLVVKHDRIAALLSEVNGLRGKIAMLGVQISEKKQALIGEEPLNLLNDEEEPINVEGCYVQRTTNGRVVSDIVSLDSVLLVFGPKESKTLLGKEIPVYVQLQPEEVLKMQQTVRTVNDLYDIDELEALFAAEERDDQEKRELQLRMEELSKKELFTEDDEEEMRQLDAFLTDVDRRHERTVWRRRCLEKAGRDKLYLEKRRRIENIVYSDLHIFFTGDKWQEVLDNEEHREYLDAAFKEDASATLRLPKENFTNLTFEGYPLEASFTTEHDKSTPKEELQALLERCAFPTVCAFYHSLTGGTTESVEGEDVDG
Protein: Glutathione S-transferase U26 (AtGSTU26) (EC 2.5.1.18) (GST class-tau member 26) (Q9SHH8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB). May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.
Subcellular location: Cytoplasm, cytosol {ECO:0000305}.
Interaction partners:
- Glutathione S-transferase DHAR1, mitochondrial
- Methylesterase 8
- Glutathione S-transferase DHAR3, chloroplastic
- Glutathione S-transferase DHAR2
- Phospholipid hydroperoxide glutathione peroxidase 1, chloroplastic
- Probable phospholipid hydroperoxide glutathione peroxidase 6, mitochondrial
- Mannosyltransferase APTG1
- Glutathione S-transferase U1
- Glutathione S-transferase TCHQD
- Glutathione synthetase, chloroplastic
Sequence:
MANDQVILLDYWPSMFGMRTKMALAEKGVKYEYKETDPWVKTPLLIEMNPIHKKIPVLIHNGKPICESLIQLEYIDEVWSDASPILPSDPYQKSRARFWAEFIDKKFYDPSWKVWATMGEEHAAVKKELLEHFKTLETELGDKPYYGGEVFGYLDIALMGYYSWFKAMEKFGEFSIETEFPILTTWTKRCLERESVVKALADSDRIIEYVYVLRKKFGAA
Protein: SD03917p (Q8T3I9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MQHSPNPAMVATTMAHEMGHNFGMEHDTSDCHCRDEKCVMAASSTSFIPVNWSSCSIDQLTIAFSRGMNYCLRNKPERLFESPTCGNGFVEPGEQCDCGLPEHCENACCNAQTCMLHSKNATCATGECCDLTTCRPKLAGSACREAENECDLPEYCTGESEYCPADVFRRDTEPCDGGQAYCFHGTCRSHSNQCRTLWGPTGDNSEHCYNKNTEGTRLGNCGYNRLNKTFLRCEEQHVNCGMLHCIHLNERLEFGMESAAVLSHSYISHDRKIVACRTALVDLGLQTTDPGLTPNGAKCGVDKMCVDQRCLPVDAVRQKGMGKPCPEDCNGNGICNSRGHCHCDVGFGGESCSKAGSGGSPDSGPATDPNGSVGFKRFLYVLFFFVLPVVALFWFLYHCYKNGMLTRGKLADNMYVSTSSFSIGSKEDTSPDSSISTTLAHKQTPARTAPPPLPLHTNRQLSGIVTNTAPATITNIHAILPRHKSNPDVVHQLNIPPPSVPKSHSTHEVRPKAATLKPLTLLHSTHSTSNNNNTESLNQNDKSNTNNSTLRRKLDITAPRLNATTNPLALTEGAQFIQSDPARCAKN
Protein: RanBP-type and C3HC4-type zinc finger-containing protein 1 (EC 2.3.2.31) (Heme-oxidized IRP2 ubiquitin ligase 1 homolog) (HOIL-1) (Protein kinase C-binding protein beta-15) (RBCC protein interacting with PKC) (RING-type E3 ubiquitin transferase HOIL-1) (Ubiquitin-conjugating enzyme 7-interacting protein 3) (Q62921)
Organism: Rattus norvegicus (Rat)
Function: E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2L3/UBCM4, and then transfers it to substrates (By similarity). Functions as an E3 ligase for oxidized IREB2 and both heme and oxygen are necessary for IREB2 ubiquitination (By similarity). Promotes ubiquitination of TAB2 and IRF3 and their degradation by the proteasome. Component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation (By similarity). LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways (By similarity). Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation (By similarity). LUBAC is recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex (By similarity). The LUBAC complex is also involved in innate immunity by conjugating linear polyubiquitin chains at the surface of bacteria invading the cytosol to form the ubiquitin coat surrounding bacteria (By similarity). LUBAC is not able to initiate formation of the bacterial ubiquitin coat, and can only promote formation of linear polyubiquitins on pre-existing ubiquitin (By similarity). The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation (By similarity). Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis (By similarity). Binds polyubiquitin of different linkage types (By similarity).
Interaction partners:
- Sharpin
- RBR-type E3 ubiquitin transferase
- NF-kappa-B essential modulator
- Tumor necrosis factor receptor superfamily member 1A
- RING-type E3 ubiquitin transferase
- Receptor-interacting serine/threonine-protein kinase 1
- RING-type E3 ubiquitin transferase
- ubiquitinyl hydrolase 1
- TNF receptor-associated factor
- Receptor-interacting serine/threonine-protein kinase 2
Sequence:
MDEKTKKAEEMALSLARAVTGGDEQAAIKYATWLAEQKVPLRVQVKPEVSPTQDIRLCVSVEDAYMHTVTIWLTVRPDMTVASLKDMVFLDYGFPPSLQQWVVGQRLARDQETLHSHGIRRNGDSAYLYLLSARNTSLNPQELQRQRQLRMLEDLGFKDLTLQPRGPLEPVLPKPRTHQETGQPDAAPESPPVGWQCPGCTFINKPTRPGCEMCCRARPEAYQIPASYQPDEEERARLAGEEEALRQYEQRKQQQQEGNYLQHVQLEQRSLVLNTEPAECPVCYSVLAPGEAVVLRECLHTFCRECLQGTIRNSQEAEVSCPFIDNTYSCPGKLLEREIRALLSPEDYQRFLDLGVSIAENRSTLSYHCKTPDCRGWCFFEDDVNEFTCPVCTRVNCLLCKAIHERMNCREYQDDLAHRARNDVAAQQTTEMLRVMLQQGEAMYCPQCRIVVQKKDGCDWIRCTVCHTEICWVTKGPRWGPGGPGDTSGGCRCRVNGIPCHPSCQNCH
Protein: Nitrite oxidoreductase subunit B (EC 1.7.99.4) (Nitrite:nitrate oxidoreductase subunit beta) (Strongly similar to nitrate reductase (NarH)) (Q1PZD5)
Organism: Kuenenia stuttgartiensis
Subcellular location: Cell envelope {ECO:0000256|ARBA:ARBA00004196}.
Interaction partners:
Sequence:
MTLVHNWHLGRRMEYPYFESRPKHQFAAVFNINRCIACQTCTMACKSTWTFNKGQEFMWWNNVETKPYGGFPQSWDVKTLKLIDSPDNIWYTDDKDKETSQYGTGAPYGTYEGDTIFEVAKKKNINQWAVGYIPEDKEWRSPNFGEDTAKSSNQPGEYSTLPEHSRWFFYLQRICNHCTYPGCLAACPRKAIYKRKEDGIVLIDQKRCRGYRKCVEQCPYKKPMYRGLTRVSEKCIACYPRIEGRDSLTDGRPMETRCMSACVGQIRLQGFLDDNPKNPITWLIRHQKIALPLYPQFGTEPNIYYIPPRWAPRAYLRQMFGPGVDEAIEKFMVPSRELLAVMSLFRMTQTIVYEYKIEEGPKVFETEIHGKKFTMYNDTVIGFGEDGKEVVRTTVEEPIHIRPDKHYNSI
Protein: Transcriptional activator BRRF1 (P03207)
Organism: Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Function: Enhances the ability of BRLF1 to induce lytic infection by cooperating with it to transcriptionally activate the BZLF1 promoter.
Interaction partners:
Sequence:
MASSNRGNARPLKSFLHELYLKHYPEVGDVVHLLNTIGVDCDLPPSHPLLTAQRGLFLARVLQAVQQHKLLEDTIVPKILKKLAYFLELLSYYSPKDEQRDIAEVLDHLKTNRDLGLDDRLWALIRKLRQDRHHASVNVLMPGSDYTAVSLQYYDGISIGMRKVIADVCRSGYASMPSMTATHNLSHQLLMASGPSEEPCAWRGFFNQVLLWTVALCKFRRCIYYNYIQGSIATISQLLHLEIKALCSWIISQDGMRLFQHSRPLLTLWESVAANQEVTDAITLPDCAEYIDLLKHTKHVLENCSAMQYK
Protein: Protein SSH4 (Multicopy suppressor of leflunomide protein 4) (Suppressor of SHR3 null mutation protein 4) (P32343)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Components of the endosome-vacuole trafficking pathway that regulates nutrient transport. May be involved in processes which determine whether plasma membrane proteins are degraded or routed to the plasma membrane. Confers leflunomide resistance when overexpressed.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:17287526}; Single-pass type II membrane protein {ECO:0000269|PubMed:17287526}. Endosome membrane {ECO:0000269|PubMed:17287526}; Single-pass type II membrane protein {ECO:0000269|PubMed:17287526}.
Interaction partners:
- E3 ubiquitin-protein ligase RSP5
- Vacuolar lysine transporter YPQ1
- GID complex subunit 8
- Transmembrane E3 ubiquitin-protein ligase 1
- Metal homeostatis protein BSD2
- Secretory component protein SHR3
- E3 ubiquitin-protein ligase PIB1
- GID complex subunit 7
- Vacuolar membrane protein YPL162C
- Uncharacterized protein TRE1
Sequence:
MYVTFNEALDSSFGNLESPNHDFKVGDPNMVPTPPMDSDSAAISLAFLISLSITFAILMLILVVIAAYVTFCGDDESEYDEENALGTRTSGTLHSLFGKKHSGILLDSSFASPGGFDDEIVLQERELEELPKMSAYEVELYIRAKEFQMMSPPMVKDFGTYLDSDDQQFIKDRGIQSYFLLPSINDNIDEYGNFLPSFIVQDKLDIQFSKFNKSSSTVMNYPLPHNRKDAVYFEVKIFRHIQKSNSIFSIGLTTVPYPYFRVPGMAKYSIAYESTGKLRINNPFTASTLLPKLEEGDTVGFGYRYKTGTIFITHNGKKLMDVTQNIGIDLFIGIGAFNAAYTRTYTRDGLLEDPDNVSFREALSEGKDIEVAKDLQRVHDPHDESDEMTSDEVELHVNLGQVGFVFIEANVKKYAFGSVYGQIGIPPAYNGTEIKKDTILQKGEELPPRYADTDNFFGSMKVKEGSSSRITAQTSKPLWSVGTYERISSNFDRENNVYHDSLETDDNNTDNNVNNNDENAGCNENSPLLEDDGNKRPENSNTPREVSDGAINKNPRNKSTKKRQRNRGKSSKKKNRSRK
Protein: Neurite extension and migration factor (XLMR protein related to neurite extension) (XPN) (Q5QGS0)
Organism: Homo sapiens (Human)
Function: Involved in neurite outgrowth by regulating cell-cell adhesion via the N-cadherin signaling pathway. May act by regulating expression of protein-coding genes, such as N-cadherins and integrin beta-1 (ITGB1).
Subcellular location: Nucleus {ECO:0000269|PubMed:24071057}. Cytoplasm {ECO:0000250|UniProtKB:Q5DTT1}.
Interaction partners:
- S-geranylgeranyl-glutathione receptor P2RY8
- E3 ubiquitin-protein ligase RLIM
Sequence:
MDNQQDKAIVASANGENTLINGVKENDSEDQDVAMKSFAALEAAAPIQPTPVAQKETLMYPRGLLPLPSKKPCMQSPPSPLGLIEAPEHAANSASVNAISLTSGIAKGLNTWSLPNECEKAPFAIMEPAGMSALNGDCLMQPSRTCLGCFMESKDAVDPEPGISLKVGDLNRDYETCAVSDIGIQCINAGENMKYGEQLLSDQLLGFPLHKSRAGDRRETEKPDIDLEDPAQKSYYEALLLDKCNTEEALLANSNQDWGYFETFISESKIELLDLCSKNELSVNLFSEEDVDNYMFDDDESTLGSDVCSLKIRYESFQDNVRDKTTLLMQEDAQFNFFPSVFTTCPKRESKSGALKQSSDFSQFKVPDVSIIWGEEDKNLDKKKGKEEGQEDKGVEKKDGKDNGEKPALNKPCSGTEVEQLKNPKQGHLANSLETSGSFSDDSSFIEISYDAMGEIKDCSRYMARDTNSGSSSSQQNYGLRAKRKVRYSEDYLYDVDSLEGEKVNERKEWLPVGSKEEDDDEWCPKKRRKVTRKEPPVIIKYIIINRFKGEKNMLVKLGKVDASETTVNLSENQLNKYAKLAPLKGFWQKKKKQRNTNTDSIKTPFSQKQSFEPGSFEVSFLPPARKRKSKLGNRHRIQRIPSIEISASSKQISLCNDQRHASNHKEDGGLKGTLKSAPLGAPSCANGSHLNDITGPDSVKVKAQDTEFKGPERKVLNKIKFKSEARLKSKKVKAAGQESKPIVQMSPLLENQSSKANLKNEVIPGTSNSSRLSEFHEAKAAKSSTFLPTTCSSEMPLSSANVTTNIPVIPGGYLQTLLDASDLSNNTSISYFSHHSPEQNEGSLTQTEKSFVPLQPTQDCVLTSSSDSELQQSSHNFKMESSNYRNVWPNKATSGTQEFMAEVSREIAPTQSSEFGASQVVSMENNLTPTTYNPICLNSGGSNCNKVLYDSMQDTQLPSDDSYQLCHFNNGEICFPFQQGPVNMDDGRLFSFDSMAPLSVSSSNYCSLSLKSCEKDGDDDITDDFLAHCSPKLVIQQSIDEIAPLKESTDLLDISNFTPDKFRHSSLSEMSPPDTPSLSPQITRCESMKTLGTLKGFQEGVPGPLDSVEKIKWDCSTLSRQVQMEDGFTLNNHQFQFHMFNDEDSVSLLQKNPCLSTFNDPSGQISTNNKVSKSRKKSSPSKSGAMNQSSSQKNTRKKSLKGNNKGIEKPPGKNSRQVPKSTKKGKYMAAINGEKMQIGIGRGGSQTNTISSTGKTLAECIQHGGPMASMKMPSQKGLSGDWALGKESSPGWSDMSMGTNTNSLLDDDQREFQEPSYILSNIASGMADVQRFMMASIEPLWEPMEHHGDPNIFYSPESNSLKLKTLKILAGTPQESKKKINSGSQGATKNHRSIKGVSKSNGKTAIGDPGRANMPGYNEDSRSTFFDKKYSNMSTLGNNGPTHKKLYRHKSSSKALRDEKCKGKHMEREQVHKDESGTASFEKLRDSDYNLLKAETTFWVLPVFEEETRIFQKDI
Protein: Possible bifunctional enzyme: 2-hydroxyhepta-2,4-diene-1,7-dioate isomerase (HHDD isomerase) + cyclase/dehydrase (O86346)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Multifunctional non-homologous end joining DNA repair protein LigD
- Possible oxygenase
- Possible dehydrogenase/reductase
- Phthioceranic/hydroxyphthioceranic acid synthase
- Mycoketide-CoA synthase
- Mycocerosic acid synthase-like polyketide synthase
- Phenolphthiocerol/phthiocerol polyketide synthase subunit C
- Probable multifunctional mycocerosic acid synthase membrane-associated Mas
Sequence:
MKWVTYRSDHGERTGVLSGDAIYAMPPDVSLLDLVGRGADGLRTAGERAVRSPAAVVALDEVTLAAPIPRPPSIRDSLCFLDHMRNCQEAMGGGRVLMDTWYRIPAFYFACPSTVLGPYDDAPTAPGSAWQDFELEIAAVIGTSGKDLTVEQAERSIIGYTIFNDWSARDLQMLEGQLRIGQAKGKDSGITLGPYLVTPDELEPYCRGGKLSLRVIALVNGTVIGSGSTAQMDWSFGEVIAYASRGVTLTPGDVFGSGTVPTCTLVEHLRPPESFPGWLHDGDVVTLQVEGLGETRQTVRTSGTPFPLALRPNPDAEPDRRGVNPAPTRVPFTRGLHEVADRVWAWTLPDGGYGFSNAGLVAGDGASLLVDTLFDLALTREMLAAMKPVTERAPITDALITHSNGDHTHGTQLLDRSVRIIAAKGTSEEIEHGPAPEMLARIQTADLGPVATRYLRDRFGHFDFSGIKLRNADLTFDRDLAIELGGRRVDLLNLGPAHTTADSVVHVADAGVLFAGDLLFIGCTPIVWAGPIANWVAACDAMIALDAPTVVPGHGPVTGPDGIRAVRGYLAHIAEQAEAAYRKGLSLPEAVETIDLGEYASWLDSERVVVNVYQRYRELDPDTPRQDLLALLVMQAEWAARHCT
Protein: Cytoplasmic dynein 1 intermediate chain 2 (Cytoplasmic dynein intermediate chain 2) (Dynein intermediate chain 2, cytosolic) (DH IC-2) (Q13409)
Organism: Homo sapiens (Human)
Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150-glued) DCTN1 (By similarity). Involved in membrane-transport, such as Golgi apparatus, late endosomes and lysosomes (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305|PubMed:36071160}. Cytoplasm {ECO:0000250|UniProtKB:O88487}. Note=Detected in the cytoplasm of pachytene spermatocytes. Localizes to the manchette in elongating spermatids. {ECO:0000250|UniProtKB:O88487}.
Interaction partners:
- Cytoplasmic dynein 1 light intermediate chain 2
- Cytoplasmic dynein 1 heavy chain 1
- Dynein light chain roadblock-type 1
- Dynein light chain 1, cytoplasmic
- Dynactin subunit 1
- Dynactin subunit 2
- Cytoplasmic dynein 1 light intermediate chain 1
- Dynein light chain 2, cytoplasmic
- Dynein light chain Tctex-type 1
- Dynein light chain Tctex-type 3
Sequence:
MSDKSELKAELERKKQRLAQIREEKKRKEEERKKKETDQKKEAVAPVQEESDLEKKRREAEALLQSMGLTPESPIVFSEYWVPPPMSPSSKSVSTPSEAGSQDSGDGAVGSRTLHWDTDPSVLQLHSDSDLGRGPIKLGMAKITQVDFPPREIVTYTKETQTPVMAQPKEDEEEDDDVVAPKPPIEPEEEKTLKKDEENDSKAPPHELTEEEKQQILHSEEFLSFFDHSTRIVERALSEQINIFFDYSGRDLEDKEGEIQAGAKLSLNRQFFDERWSKHRVVSCLDWSSQYPELLVASYNNNEDAPHEPDGVALVWNMKYKKTTPEYVFHCQSAVMSATFAKFHPNLVVGGTYSGQIVLWDNRSNKRTPVQRTPLSAAAHTHPVYCVNVVGTQNAHNLISISTDGKICSWSLDMLSHPQDSMELVHKQSKAVAVTSMSFPVGDVNNFVVGSEEGSVYTACRHGSKAGISEMFEGHQGPITGIHCHAAVGAVDFSHLFVTSSFDWTVKLWTTKNNKPLYSFEDNADYVYDVMWSPTHPALFACVDGMGRLDLWNLNNDTEVPTASISVEGNPALNRVRWTHSGREIAVGDSEGQIVIYDVGEQIAVPRNDEWARFGRTLAEINANRADAEEEAATRIPA
Protein: Intraflagellar transport protein 52 homolog (Protein NGD5 homolog) (Q9Y366)
Organism: Homo sapiens (Human)
Function: Involved in ciliogenesis as part of a complex involved in intraflagellar transport (IFT), the bi-directional movement of particles required for the assembly, maintenance and functioning of primary cilia. Required for the anterograde transport of IFT88.
Subcellular location: Cell projection, cilium {ECO:0000250|UniProtKB:Q62559}.
Interaction partners:
- Intraflagellar transport protein 88 homolog
- Intraflagellar transport protein 80 homolog
- Intraflagellar transport protein 81 homolog
- Intraflagellar transport protein 25 homolog
- Clusterin-associated protein 1
- Intraflagellar transport protein 46 homolog
- Intraflagellar transport protein 74 homolog
- Intraflagellar transport protein 57 homolog
- Intraflagellar transport protein 70B
- Intraflagellar transport protein 22 homolog
Sequence:
MEKELRSTILFNAYKKEIFTTNNGYKSMQKKLRSNWKIQSLKDEITSEKLNGVKLWITAGPREKFTAAEFEILKKYLDTGGDVFVMLGEGGESRFDTNINFLLEEYGIMVNNDAVVRNVYHKYFHPKEALVSSGVLNREISRAAGKAVPGIIDEESSGNNAQALTFVYPFGATLSVMKPAVAVLSTGSVCFPLNRPILAFYHSKNQGGKLAVLGSCHMFSDQYLDKEENSKIMDVVFQWLTTGDIHLNQIDAEDPEISDYMMLPYTATLSKRNRECLQESDEIPRDFTTLFDLSIFQLDTTSFHSVIEAHEQLNVKHEPLQLIQPQFETPLPTLQPAVFPPSFRELPPPPLELFDLDETFSSEKARLAQITNKCTEEDLEFYVRKCGDILGVTSKLPKDQQDAKHILEHVFFQVVEFKKLNQEHDIDTSETAFQNNF
Protein: Insulin-like growth factor binding protein 7 (F1M9B2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Insulin-like growth factor 1
- Insulin-2
- Insulin-1
- Metalloproteinase inhibitor 2
- Insulin-like growth factor 2
- CCN family member 2
Sequence:
MGRARRGSEDAHDGGRPDPRRAEPGGQQADSPPRGGPPRSAGRGSGFKGWPPGPGLLTCALASSHPIMERSPRALLLGAAGLLLLLLPLSSSSSSDACGPCVPASCPALPPLGCPLGETRDACGCCPVCARGEGEPCGGGAAGRGHCAPGMECVKSRKRRKGKAGAAAGGPATLAVCVCKSRYPVCGSDGVTYPSGCQLRAASLRAESRGEKAITQVSKGTCEQGPSIVTPPKDIWNITGAKVYLSCEVIGIPTPVLIWNKVKRDHSGVQRTELLPGDRENLAIQTRGGPEKHEVTGWVLVSPLSKEDTGEYECHASNSQGQASASAKITVVDAIHEIPVKKGEGAQL
Protein: Palmitoyltransferase ZDHHC15 (EC 2.3.1.225) (Acyltransferase ZDHHC15) (EC 2.3.1.-) (Zinc finger DHHC domain-containing protein 15) (DHHC-15) (Q96MV8)
Organism: Homo sapiens (Human)
Function: Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates. Has no stringent fatty acid selectivity and in addition to palmitate can also transfer onto target proteins myristate from tetradecanoyl-CoA and stearate from octadecanoyl-CoA (By similarity). Palmitoylates IGF2R and SORT1, promoting their partitioning to an endosomal membrane subdomain where they can interact with the retromer cargo-selective complex. Thereby, regulates retrograde transport from endosomes to the Golgi apparatus of these lysosomal sorting receptors and plays a role in trafficking of lysosomal proteins. In the nervous system, catalyzes the palmitoylation of DLG4/PSD95 and regulates its synaptic clustering and function in synaptogenesis (By similarity). Could be involved in the differentiation of dopaminergic neurons and the development of the diencephalon (By similarity). Could also catalyze the palmitoylation of GAP43 (By similarity). Could also palmitoylate DNAJC5 and regulate its localization to the Golgi membrane (By similarity). Could also palmitoylate FYN as shown in vitro.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:16647879}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F1QXD3}. Postsynaptic density {ECO:0000250|UniProtKB:Q2TGJ4}.
Interaction partners:
Sequence:
MRRGWKMALSGGLRCCRRVLSWVPVLVIVLVVLWSYYAYVFELCLVTVLSPAEKVIYLILYHAIFVFFTWTYWKSIFTLPQQPNQKFHLSYTDKERYENEERPEVQKQMLVDMAKKLPVYTRTGSGAVRFCDRCHLIKPDRCHHCSVCAMCVLKMDHHCPWVNNCIGFSNYKFFLQFLAYSVLYCLYIATTVFSYFIKYWRGELPSVRSKFHVLFLLFVACMFFVSLVILFGYHCWLVSRNKTTLEAFCTPVFTSGPEKNGFNLGFIKNIQQVFGDKKKFWLIPIGSSPGDGHSFPMRSMNESQNPLLANEETWEDNEDDNQDYPEGSSSLAVETET