wanglab/gogpt-training-data huggingface dataset:
Protein: Progonadoliberin-2 (Progonadoliberin II) [Cleaved into: Gonadoliberin-2 (Gonadoliberin II) (Gonadotropin-releasing hormone II) (GnRH II) (Luliberin II) (Luteinizing hormone-releasing hormone II) (LH-RH II); GnRH-associated peptide 2 (GnRH-associated peptide II)] (O43555)
Organism: Homo sapiens (Human)
Function: Stimulates the secretion of gonadotropins; it stimulates the secretion of both luteinizing and follicle-stimulating hormones.
Subcellular location: Secreted.
Interaction partners:
- Progonadoliberin-1
- Gonadotropin-releasing hormone receptor
- Mitogen-activated protein kinase 3
- RAC-alpha serine/threonine-protein kinase
- Mitogen-activated protein kinase 1
- RAC-gamma serine/threonine-protein kinase
- RAC-beta serine/threonine-protein kinase
- Metastasis-suppressor KiSS-1
- KiSS-1 receptor
- Small ribosomal subunit protein uS2
Sequence:
MASSRRGLLLLLLLTAHLGPSEAQHWSHGWYPGGKRALSSAQDPQNALRPPGRALDTAAGSPVQTAHGLPSDALAPLDDSMPWEGRTTAQWSLHRKRHLARTLLTAAREPRPAPPSSNKV
Protein: NAD(P)H-dependent anabolic L-arginine dehydrogenase DauB (EC 1.4.1.25) (Q9HXE4)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Involved in the anabolism of D-lysine and D-arginine. Under aerobic conditions, the arginine succinyltransferase (AST) and arginine transaminase (ATA) pathways are 2 major routes for L-arginine utilization as the sole source of carbon and nitrogen. The D-to-L racemization of arginine by DauA and DauB is necessary, before to be channeled into the AST and/or ATA pathways. DauB catalyzes the synthesis of L-arginine from 2-ketoarginine (2-KA) and ammonium.
Interaction partners:
- FAD-dependent catabolic D-arginine dehydrogenase DauA
- Transcriptional regulator DauR
- Probable dihydrodipicolinate synthetase
- L-cysteine desulfhydrase Cds1
- Cysteine synthase
- RidA family protein
- Argininosuccinate lyase
- Uncharacterized protein
- Arginine biosynthesis bifunctional protein ArgJ
- Ornithine carbamoyltransferase, anabolic
Sequence:
MSAATPLIVQQAEAEQLLARIDVLQAMRQLFLDLAAGQALQPAQQLVEFPAGRGDFINYLGVLAQEQVYGVKTSPYIVREQGPLVTAWTLLMSMQTGQPLLLCDAARLTTARTAATTAVAVDALAPAEACRLALIGSGPVAHAHLQYVKGLRDWQGVRVHSPCLDERRLQSLRAIDPRAEAAGSLEEALDEADVILLCTSSARAVIDPRQLKRPALVTSISTNAPRAHEVPAESLAAMDVYCDYRHTTPGSAGEMLIAAEQHGWSPEAIRGDLAELLSAQAPRPEYRRPAFFRSIGLGLEDVALANALYRLRQAG
Protein: tRNA-dihydrouridine(20) synthase [NAD(P)+] (EC 1.3.1.91) (mRNA-dihydrouridine synthase dus2) (EC 1.3.1.-) (tRNA-dihydrouridine synthase 2) (O74731)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Also able to mediate dihydrouridylation of some mRNAs, thereby affecting their translation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P53720}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- E3 ubiquitin-protein ligase itt1
- Putative acyl carrier protein, mitochondrial
Sequence:
MGLLNYSNKVCLAPMVRIGELPMRLLALRYGANLVWGPEIVDKALLSGTPVERVVNDRINCIDFVKPPSNKVLFRVHPLEANRLIFQLGSASPELAVEAAKLVANDVAGIDLNCGCPKHFSVHAGMGAGLLKNQDRLVSILDALVNEIGKPYKISISCKIRLLETKEDTLKLVERICDTGVRAITVHCRTTPMRNTEPADRSYLSEIVGVCRNKDVSILVNGDVLSYNDGLDVIEKYGVDGVLIARAAERNVSCFRIEGPLSSFKVAEEFLKMALEVDNNFGNTKYCLNQIMQGSFRKNVRQLAQTAKTYEDLKKAFEIEYKHSDASSVCPTLEKEKSLVISFVDLPSFLESLLASNILKQLSRLHFTKIFAVSEEEDICKQLDDIHEKFLCHGIALSLISADNLASAIASAHLVICMEKDESIMNEAVCDQKITIRLPINSNTNEAVVECENKSMQSKHALDIIQERIKDLEEKAQVV
Protein: Eukaryotic translation initiation factor 2-alpha kinase (EC 2.7.11.1) (PRKR-like endoplasmic reticulum kinase) (DmPEK) (PEK) (PERK) (Q9NIV1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Phosphorylates the alpha subunit of eukaryotic translation-initiation factor 2 (EIF2), leading to its inactivation and thus to a rapid reduction of translational initiation and repression of global protein synthesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit 1
- Cryptocephal, isoform A
- non-specific serine/threonine protein kinase
- X-box-binding protein 1
- Endoplasmic reticulum chaperone BiP
- Atf6, isoform C
- Eukaryotic translation initiation factor 2 subunit 2
- GH11727p
Sequence:
MQDDLDGIVRHRRRSLSFLQIVTLTMAGLVAFDPAQVLAGHPTTDSELQTAGSPRPPGLEHCVDQEERRVARRLLYISTLDGRLSALDIAKSGKLRWSVPTGPGPLISSSIHRLELTNNGQFVRMIPSLSGGIYKFDGDSIDPIPITAEHLLSSSAKFSDDLVISGGKETRSYGVSVRTGQLLYECSLNGCVNSTEEGLAIDDTIREPDEEDQLEDGEQLRDEAGYIVRHDPLLDDVIIVRRQTQTVRAVESRTGVERWNFSVGQHELDLVRPSECQLQPRDELELAVLDVDIKVVVPEGIICAFSKSEPQTMLWKYKFDHPIVSAWNTNADDELQPIDLFSSAQWLWDQDENDTELPNAPQSPPSIYLGMYDKQLYIQESIRLRQEIMDQTKVYQQLTGDTSLMPRIPWKPISASSKSLVIFRKDQEDPEMIAEGAVAQGGELVPYDDENFAVAAQSVLNASEFVNGNGFYFYTTGDLNGPQECSTQNNPTDLPAITAPTSPTNATSEGTEATGNHSVNDDLGFSLDDIDAPVKVVILSLWFWWKEIVVIAFTSAVILNIFMGQRNQRVEREYLVIERHVPVQTAIEATEASTQALLGPVVPMQRPGNRFSFPPGQANQRTISESTTHSGEHYTSRFQSDFELMQCLGRGGFGVVFEAKNKLDENRYAIKRITLPNKESSRQRVLREARTLASCEHHNIVRYFHSWTETPPTGWQEEEDRKLLAHELSTSIQIETPDDSTMPSLTEQLKEKRQQQLLSWVSDAANSTACSHDFHLPGESSLKNIREEYDYDEEEDSLIEFRSESQSAALRAEEEDDTDDDYEEDEEQQGDHEKRHRSSVSIDIHSASFDLKNINYSQHQLVSNSFQIESVRPKSSGSDDANDDNKARRKPLTLALAQNHNNNQNGSQPTPSSATILNGTVAKPSKVYLYIQMQLCRKESLRDWLRDNRSETRAAHIGDIFHQIVDAVDYVHLKGLIHRDLKPSNIFFSQDGQIKIGDFGLVTDMADIPNLVAKCGDQSGLPSCARHTQQVGTHLYMSPEQLLGQHYDYKVDIYSLGLIFFELHVYFSTEMERIKTLRSLRDGQYPKDFAVNYPQQYDLLQQMLSAQPEQRPQTKQLKSQLRNILQLPHLLSEGQSEQAELAERARRLSRSRTFSSSSEPHQ
Protein: Neutrophil cytosolic factor 1 (NCF-1) (F1M707)
Organism: Rattus norvegicus (Rat)
Function: NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P14598}. Membrane {ECO:0000250|UniProtKB:P14598}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14598}; Cytoplasmic side {ECO:0000250|UniProtKB:P14598}.
Interaction partners:
- small monomeric GTPase
- NADPH oxidase 4
- NADPH oxidase activator 1
- Cytochrome b-245 light chain
- NADPH oxidase 2
- Neutrophil cytosol factor 4
- NADPH oxidase 1
- NADPH oxidase organizer 1
- NADPH oxidase 3
- Ras-related C3 botulinum toxin substrate 1
Sequence:
MGDTFIRHIALLGFEKRFVPSQHYVYMFLVKWQDLSEKVVYRKFTEIYEFHKMLKEMFPIEAGEIHTENRVIPHLPAPRWYDGQRAAESRQGTLTEYFNSLMGLPMKISRCPHLLNFFKVRPDDLKLPNDSQVKKPETYLTAKDGKNNVADITGPIILQTYRAIADYEKGSKTEMTVATGDVVDVVEKSESGWWFCQMKTKRGWVPASYLEPLDSPDEAEDPDPNYAGEPYVTIKAYAAVEEDEVSLSEGEAIEVIHKLLDGWWVVRKGDITGYFPSMYLQKAGEEITQAQRQIRSRGAPPRRSTIRNAQSIHQRSRKRLSQDTYRRNSVRFLQQRRRPARPGPQSPDSKDNPSTPRAKPQPAVPPRPSSDLILHRCTESTKRKLTSAV
Protein: 66 kDa U4/U6.U5 small nuclear ribonucleoprotein component (Q12420)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the U4/U6.U5 tri-snRNP particle, one of the building blocks of the spliceosome. Required for pre-mRNA splicing.
Subcellular location: Nucleus {ECO:0000269|PubMed:11290703, ECO:0000269|PubMed:14562095}.
Interaction partners:
- LSM complex subunit LSM2
- RDS3 complex subunit 10
- Pre-mRNA-processing factor 31
- 13 kDa ribonucleoprotein-associated protein
- Spliceosomal protein DIB1
- Protein HSH49
- LSM2-LSM8 complex subunit LSM8
- Cold sensitive U2 snRNA suppressor 1
- LSM complex subunit LSM4
- Small nuclear ribonucleoprotein Sm D3
Sequence:
MNKTENLSIEETNEIREKLGMKPIPVFQEKNTDHKESLSIEETNELRASLGLKLIPPQQNFNSSPPNVHNTSKIDELREKITKFQKKANAPLRMAHLLEETNVNDDSSWLENMDAIPSSHESKRSSTLPRKGATKEDENIDLHNVQVSYNIEALSPKKDTILTLKESSIFDDTDSTEVLENVKAAEENADREKLRLRQMNKDRRQKKKILNVSSLDIEEEEEGEKHSITTTHLIIGAEQGVMKAPNTISAKPPTGKVKVNFDSANNMSDEDGGDFKPLKIKKRKIKDPRSTKARKSKITDKMEIVKLVDEDESLSWMEEEQPVTIINPRTSSNNELKGPEDLAREIEKARDEEKRRTESILKMREISNSIVVDEKVTFLNTLDTSLSERSATENKVKVHGEGEKNIGDVTNGHTKEGSGNNTLTEAVNNEPNYEGDAENAPNFFSGLASTLGYLRKKSVFTTGDVDLKPGKDVNNSESLRRDVRNKEHTGTGTYTKDKLHGLEQFTSSDSSNANTHSKRQDHYDPDIKLVYRDEKGNRLTTKEAYKKLSQKFHGTKSNKKKRAKMKSRIEARKNTPENGSLFEFDDN
Protein: Protein YIF1 (E9PS11)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU368073}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU368073}. Golgi apparatus membrane {ECO:0000256|RuleBase:RU368073}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU368073}.
Interaction partners:
Sequence:
MILSVLTGLLFGSDGYYVALAWTSSALMYFIVRSLRTAALGPDSMGGPVPRQRLQLYLTLGAAAFQPLIIYWLTFHLVR
Protein: FI06908p (FI07108p) (Heterochromatin protein 1b, isoform A) (Heterochromatin protein 1b, isoform B) (Heterochromatin protein 1b, isoform C) (Q9W396)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Histone-lysine N-methyltransferase Su
- G9a, isoform B
- Heterochromatin protein 1c
- Polycomb protein Sfmbt
- Telomere-binding protein cav
- Heterochromatin protein 1
Sequence:
MAEFSVERVEDKRTVNGRTEYYLKWKGYPRSENTWEPVENLDCPDLIANFEESLKNNKKETKKRLSTSSTPESIRSKRKSFLEDDTEEQKKLIGFERGLEASKILGATDSSGHLMFLMKWKGSDHADLVPAKLANTRCPQVVIQFYEERLTWHTGSGNGNGNTNSVNLGSSGGLGSVGGSGAGDDTAPGSVGTTGGGSNIDGGDEEDPEPASPIGSINQDENIKPDESSELDNGQPDADD
Protein: Dedicator of cytokinesis protein 2 (Protein Hch) (Q8C3J5)
Organism: Mus musculus (Mouse)
Function: Involved in cytoskeletal rearrangements required for lymphocyte migration in response of chemokines. Activates RAC1 and RAC2, but not CDC42, by functioning as a guanine nucleotide exchange factor (GEF), which exchanges bound GDP for free GTP. May also participate in IL2 transcriptional activation via the activation of RAC2.
Subcellular location: Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalizes with F-actin. {ECO:0000250}.
Interaction partners:
- Engulfment and cell motility protein 1
- Ras-related C3 botulinum toxin substrate 2
- Engulfment and cell motility protein 2
- Engulfment and cell motility protein 3
- Ras-related C3 botulinum toxin substrate 3
- Proto-oncogene tyrosine-protein kinase Src
- Tyrosine-protein kinase HCK
- Tyrosine-protein kinase Fgr
- Tyrosine-protein kinase Lyn
- Adapter molecule crk
Sequence:
MAPWRKTDKERHGVAIYNFQGSEAQHLTLQIGDVVRIQETCGDWYRGYLIKHKLSQGIFPTSFIHLKEVTVEKRRNIENIIPAEIPLAQEVTTTLWEWGSIWKQLYVASKKERFLQVQSMMYDLMEWRSQLLSGTLPKDELKELKQKVTSKIDYGNKILELDLIVRDEDGNILDPDKTSVISLFHAHEEATYKITERIKEEMSKDQPDYGVYSRISSSPTHSLYVFVRNFVCRIGEDAELFMSLYDPHKQTVISENYLVRWGSKGFPKEIEMLNNLKVVFTDLGNKDLNRDKIFLICQIVRIGKMDLKDINAKKCTQGLRRPFGVAVMDITDIIKGKAESDEEKQHFIPFHPVSAENDFLHSLLGKVIASKGDSGGQGLWVTMKMLVGDIIQIRKDYPHLVDRTTVVARKLGFPEIIMPGDVRNDIYITLLQGDFDKYTKTTQRNVEVIMCVCTEDGKVLPNAICVGAGDKAMNEYHSVVYYQVKQPRWMETVKVAVPIEDMQRIHLRFMFRHRSSLESKDKGEKNFAMSYVKLMKEDGTTLHDGYHELVVLKGDSKKMEDASAYLTLPSYRHPVENKGATLSRSSSSVGGLSVSSRDVFSISTLVCSTKLTQNVGLLGLLKWRMKPQLLQENLEKLKIVDGEEVVKFLQDTLDALFNIMMEHSQSNEYDILVFDALIYIIGLIADRKFQHFNTVLEAYIQQHFSATLAYKKLMTVLKTYLDTSSRGEQCEPILRTLKALEYVFKFIVRSRTLFSQLYEGKEQMEFEESMRRLFESINNLMKSQYKTTILLQVAALKYIPSVLHDVETVFDAKLLSQLLYEFYTCIPPVKLQKQKVQSMNEIVQSNLFKKQECRDILLPVITKELKELLEQRDDGQHQAEKKHCVELLNSILEVLSCQDAAFTYDHIQEIMVQLLRTVNRTVITMGRDHALISHFVACMTAILDQMGDQHYSFYIETFQTSSDLVDFLMETFIMFKDLIGKNVYPGDWMAMSMVQNRVFLRAINKFAETMNQKFLEHTSFEFQLWNNYFHLAVAFITQDSLQLEQFTHAKYNKILNKYGDMRRLIGFSIRDMWYKLGQNKICFIPGMVGPILEMTLIPEAELRKATIPIFFDMMLCEYQRTGAFKKFENEIILKLDHEVEGGRGDEQYMQLLESILMECTAEHPTIAKSVENFVSLVKGLLEKLLDYRGVMTDESKDNRMSCTVNLLNFYKDNNREEMYIRYLYKLRDLHLDCENYTEAAYTLLLHTWLLKWSDEQCASQVMQTGQQHPQTHRQLKETLYETIIGYFDKGKMWEEAISLCKELAEQYEMEIFDYELLSQNLTQQAKFYENIMKILRTKPDYFAVGYYGQGFPSFLRNKVFIYRGKEYERREDFQMQLLSQFPNAEKMNTTSAPGDDVRNAPGQYIQCFTVQPVLDEHPRFKNKPVPDQIINFYKSNYVQKFHYSRPVRRGKVDPENEFASMWIERTSFLTAYKLPGILRWFEVVHMSQTTISPLENAIETMSTVNEKILMMINQYQSDESLPINPLSMLLNGIVDPAVMGGFAKYEKAFFTEEYSREHPEDQDKLSHLKDLIAWQIPFLGAGIKIHEKRVSDNLRPFHDRMEECFKNLKMKVEKEYGVREMPDFEDRRVGRPRSMLRSYRQMSVISLASMHSDCSTPSKVPAESFDLESAPPKTPKVEEEPISPGSTLPEVKLRRSKKRTKRSSVVFADEKAATESDLKRLSRKQEFMSDTNLSEHAAIPARVSILSQMSFASQSMPTIPALTLSVAGVPGLDEANTSPRLSQTFFQVSDGDKKTLKKKKVNQFFKTMLASKSSEESKQIPDFLSTNM
Protein: Mortality factor 4-like protein 2 (MORF-related gene X protein) (Protein MSL3-2) (Transcription factor-like protein MRGX) (Q15014)
Organism: Homo sapiens (Human)
Function: Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histone H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when directly recruited to sites of DNA damage. Also a component of the MSIN3A complex which acts to repress transcription by deacetylation of nucleosomal histones.
Subcellular location: Nucleus.
Interaction partners:
- MRG/MORF4L-binding protein
- Transformation/transcription domain-associated protein
- Histone acetyltransferase KAT5
- YEATS domain-containing protein 4
- Bromodomain-containing protein 8
- Mortality factor 4-like protein 1
- Chromatin modification-related protein MEAF6
- DNA methyltransferase 1-associated protein 1
- Enhancer of polycomb homolog 1
- Inhibitor of growth protein 3
Sequence:
MSSRKQGSQPRGQQSAEEENFKKPTRSNMQRSKMRGASSGKKTAGPQQKNLEPALPGRWGGRSAENPPSGSVRKTRKNKQKTPGNGDGGSTSEAPQPPRKKRARADPTVESEEAFKNRMEVKVKIPEELKPWLVEDWDLVTRQKQLFQLPAKKNVDAILEEYANCKKSQGNVDNKEYAVNEVVAGIKEYFNVMLGTQLLYKFERPQYAEILLAHPDAPMSQVYGAPHLLRLFVRIGAMLAYTPLDEKSLALLLGYLHDFLKYLAKNSASLFTASDYKVASAEYHRKAL
Protein: Protein P78/83 (Q03209)
Organism: Autographa californica nuclear polyhedrosis virus (AcMNPV)
Function: Plays a role in the transport of the nucleocapsids from the cytoplasm toward the host nucleus together with the host actin-polymerizing Arp2/3 complex.
Subcellular location: Host cytoplasm {ECO:0000269|PubMed:17053146}. Host nucleus {ECO:0000269|PubMed:17053146}.
Interaction partners:
Sequence:
MTNRRYESVQSYLFNNRNNKIDAHQFFERVDTAEAQIIKNNIYDNTVVLNRDVLLNILKLANDVFDNKAYMYVDDSEVSRHYNAVVKMKRLVIGVRDPSLRQSLYNTIAYIERLLNIGTVNDSEITMLIADFYDLYSNYNIELPPPQALPRSRRPSVVQPAAPAPVPTIVREQTKPEQIIPAAPPPPPSPVPNIPAPPPPPPPSMSELPPAPPMPTEPQPAAPLDDRQQLLEAIRNEKNRTRLRPVKPKTAPETSTIVEVPTVLPKETFEPKPPSASPPPPPPPPPPPAPPAPPPMVDLSSAPPPPPLVDLPSEMLPPPAPSLSNVLSELKSGTVRLKPAQKRPQSEIIPKSSTTNLIADVLADTINRRRVAMAKSSSEATSNDEGWDDDDNRPNKANTPDVKYVQALFNVFTSSQLYTNDSDERNTKAHNILNDVEPLLQNKTQTNIDKARLLLQDLASFVALSENPLDSPAIGSEKQPLFETNRNLFYKSIEDLIFKFRYKDAENHLIFALTYHPKDYKFNELLKYVQQLSVNQQRTESSA
Protein: Vacuole membrane protein 1 (NF-E2-inducible protein 2) (Protein ni-2) (Q99KU0)
Organism: Mus musculus (Mouse)
Function: Phospholipid scramblase involved in lipid homeostasis and membrane dynamics processes (By similarity). Has phospholipid scramblase activity toward cholesterol and phosphatidylserine, as well as phosphatidylethanolamine and phosphatidylcholine (By similarity). Required for autophagosome formation: participates in early stages of autophagosome biogenesis at the endoplasmic reticulum (ER) membrane by reequilibrating the leaflets of the ER as lipids are extracted by ATG2 (ATG2A or ATG2B) to mediate autophagosome assembly. Regulates ATP2A2 activity to control ER-isolation membrane contacts for autophagosome formation (By similarity). In addition to autophagy, involved in other processes in which phospholipid scramblase activity is required (By similarity). Modulates ER contacts with lipid droplets, mitochondria and endosomes (By similarity). Plays an essential role in formation of cell junctions. Upon stress such as bacterial and viral infection, promotes formation of cytoplasmic vacuoles followed by cell death (By similarity). Involved in the cytoplasmic vacuolization of acinar cells during the early stage of acute pancreatitis (By similarity).
Subcellular location: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q91ZQ0}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q96GC9}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:Q91ZQ0}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96GC9}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Beclin-1
- Autophagy-related protein 13
- Tumor protein p53-inducible nuclear protein 2
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Albumin
- Autophagy-related protein 9A
- Transmembrane protein 41B
- Ubiquitin-like protein ATG12
- Autophagy protein 5
- Beclin 1-associated autophagy-related key regulator
Sequence:
MAENGKNCDQRRIAMSKDQHNGSLTDPSSVHEKKRRDREERQNIVLWRQPLITLQYFSLETLVVLKEWTSKLWHRQSIVVSFLLLLAALVATYYVEGAHQQYVQRIEKQFLLYAYWIGLGILSSVGLGTGLHTFLLYLGPHIASVTLAAYECNSVNFPEPPYPDQIICPEEEGAEGAISLWSIISKVRIEACMWGIGTAIGELPPYFMARAARLSGAEPDDEEYQEFEEMLEHAEAAQDFASRAKLAVQKLVQKVGFFGILACASIPNPLFDLAGITCGHFLVPFWTFFGATLIGKAIIKMHIQKIFVIVTFSKHIVEQMVTFIGAVPGIGPSLQKPFQEYLEAQRQKLHHRSEAGTPQGENWLSWMFEKLVVAMVCYFVLSIINSMAQNYAKRIQQRLNSEEKTK
Protein: Epithelial membrane protein 2 (EMP-2) (F1QIK8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Functions as a key regulator of cell membrane composition by regulating protein surface expression. Also, plays a role in regulation of processes including cell migration, cell proliferation, cell contraction and cell adhesion. May play a role in glomerular filtration.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:O88662}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:P54851}. Apical cell membrane {ECO:0000250|UniProtKB:O88662}. Membrane raft {ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:P54851}. Cytoplasm {ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:P54851, ECO:0000250|UniProtKB:Q66HH2}. Nucleus {ECO:0000250|UniProtKB:Q66HH2}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O88662}.
Interaction partners:
- GRB2-associated and regulator of MAPK protein 1
- Metadherin a
- Lysophosphatidic acid receptor 6
Sequence:
MLVILAFIILFHITSAILLFIATINNAWRIKGDFSMDLWYNCNTTACYDIPKSATYDAAYLQAVQATMILATILCCVGFFVFILQLFRLKQGERFVFTAIIQLLSAFCVMTGASIYTAEGLTFNGQEFKNAEYGYSFVVAWVAFPMTLLSGLMYLVLRKRK
Protein: 45 kDa calcium-binding protein (Cab45) (Stromal cell-derived factor 4) (SDF-4) (Q7ZUC2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: May regulate calcium-dependent activities in the endoplasmic reticulum lumen or post-ER compartment.
Subcellular location: Golgi apparatus lumen {ECO:0000250|UniProtKB:Q61112}.
Interaction partners:
- Calretinin
- Calbindin 2b.
- Protein S100-B
- Parvalbumin-7
- Calbindin
Sequence:
MFNWRRSQLSCLCASTLAVFVMLALNVQGRPANISALKGKQPNSKEDNEILPPDHLNGVKMEMDGHLNKDFHQEVFLGKEMEEFEEDSEPRRNRKKLIEIFTKVDINKDRSVSAKEMQRWIMEKTEEHFQEAVRENKLSFRAVDPDGDGLVTWDEYRVKFLASKGLNEKEVAEKIKNNEELKVDEETQEVLESLKDRWFQADNPPADQLLNEEEFLSFLHPEHSRGMLRYMVKEIVRDLDQDGDGKLTLAEFISLPMGTVENQQAQDIDDDWVRERKKEFEEVIDANHDTIVTMEELEEYMDPMNEHNALNEAKQMIAVADENQNHNLELEEILKYSEYFTGSKLMDYARNVHEEF
Protein: Abscisic acid receptor PYL5 (ABI1-binding protein 3) (PYR1-like protein 5) (Regulatory components of ABA receptor 8) (Q9FLB1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Receptor for abscisic acid (ABA) required for ABA-mediated responses such as stomatal closure and germination inhibition. Inhibits the activity of group-A protein phosphatases type 2C (PP2Cs) in an ABA-independent manner but more efficiently when activated by ABA. Confers enhanced sensitivity to ABA. Can be activated by both (-)-ABA and (+)-ABA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19624469}. Nucleus {ECO:0000269|PubMed:19624469}. Cell membrane {ECO:0000250|UniProtKB:O49686}. Note=Localizes at the plasma membrane in the presence of a CAR protein. {ECO:0000250|UniProtKB:O80920}.
Interaction partners:
- Protein phosphatase 2C 16
- Protein phosphatase 2C 56
- Protein phosphatase 2C 77
- Protein phosphatase 2C 37
- Protein phosphatase 2C 7
- Probable protein phosphatase 2C 78
- Probable protein phosphatase 2C 24
- Protein phosphatase 2C 3
- Probable protein phosphatase 2C 75
- Serine/threonine-protein kinase SRK2E
Sequence:
MRSPVQLQHGSDATNGFHTLQPHDQTDGPIKRVCLTRGMHVPEHVAMHHTHDVGPDQCCSSVVQMIHAPPESVWALVRRFDNPKVYKNFIRQCRIVQGDGLHVGDLREVMVVSGLPAVSSTERLEILDEERHVISFSVVGGDHRLKNYRSVTTLHASDDEGTVVVESYIVDVPPGNTEEETLSFVDTIVRCNLQSLARSTNRQ
Protein: Splicing factor ESS-2 homolog (Protein Es2) (dEs2) (O44424)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P34420}.
Interaction partners:
- Drosomycin-like 3
- Dro2 protein
Sequence:
MSATTRTPATPGTPGTPGSLAMEVARVQNSALAEFKKPTAMVRHKNKPKILTEEKYIEEMSKIIQRDFFPDLERLRAQNDYLDAESRRDFVQMAEIRERYSLGRISGTGRSTSRRNNAMSPATFETPVSQAKCSNTPLPNSRATDTPFSTDGSEKSDAEGRDTTAKLSLDAFLQKYTSEDNQSFQEIIETAEAKLRQKYAVLYNHEKLSAEQLQRALMLPSIETQFEEPDPLRKIETWNYTNMNSIMYVPDGVEYTEEERVQLAERKQSIQHNATRLPDEAKHREMDTKKLNDEVPQNGAGGATATPKVRGFDLLRSPSPRPGEAFSPIMTWGEIDGTPFRLDGGDTPLRPTQGPSFRINENSRRENIAIALAERVSERMRNQKQMALDTARRNIGSPLIRTNMERLASMSPAAQLLATGKLGIRGTPRLRHTPSPMSGRKRKVTPGVVRSTNTPILGEPKPKQQAKISTPAKNVTIDTGSTLTDDLLKIPTKRRTAADFF
Protein: Delta(14)-sterol reductase LBR (Delta-14-SR) (EC 1.3.1.70) (3-beta-hydroxysterol Delta (14)-reductase) (C-14 sterol reductase) (C14SR) (Integral nuclear envelope inner membrane protein) (Lamin-B receptor) (Sterol C14-reductase) (Q3U9G9)
Organism: Mus musculus (Mouse)
Function: Catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis. Plays a critical role in myeloid cell cholesterol biosynthesis which is essential to both myeloid cell growth and functional maturation. Mediates the activation of NADPH oxidases, perhaps by maintaining critical levels of cholesterol required for membrane lipid raft formation during neutrophil differentiation. Anchors the lamina and the heterochromatin to the inner nuclear membrane (By similarity).
Subcellular location: Nucleus inner membrane {ECO:0000269|PubMed:18785926}; Multi-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:Q14739}. Cytoplasm {ECO:0000250|UniProtKB:Q14739}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q14739}. Note=Nucleus; nuclear rim. {ECO:0000250|UniProtKB:Q14739}.
Interaction partners:
- Lamin-B1
- Lamin-B2
- Methyl-CpG-binding protein 2
- Lanosterol 14-alpha demethylase
- Methylsterol monooxygenase 1
- Delta
- Emerin
- Prelamin-A/C
- Importin subunit beta-1
- Chromobox protein homolog 5
Sequence:
MPSRKFVEGEVVRGRWPGSSLYYEVEILSHDNKSQLYTVKYKDGTELELKESDIKPLKSFKQRKSGSISSSPSRRRGSRSRSRSRSRSRSPGRAPKGSRRSVSASHEGDVKEKKEKEMRREILQVKLTPLVLKPFGNSVSVYNGEPEHMEKNATPYKDKQERIILSTEDRYIVTQYSLRPRREEVKAKEIESEEQNLVTKGPAPLGTFQVTTPQRKDLEFGGVPGAVLIMLGLPACVLLLLLQCRQKDPGLLHFPPPLPALHELWEPRVCGVYLLWFFVQALFHLLPVGKVAEGTPLVDGRRLQYRLNGLYAFILTSAALGAAVFWGVELCYLYTHFLQLALAATGFSVLLSAYLYVRSLRAPREELSPASSGNAVYDFFIGRELNPRLGAFDLKFFCELRPGLIGWVVINLVMLLMEMKIQERAAPSLAMILVNSFQLLYVVDALWNEEALLTSMDIMHDGFGFMLAFGDLVWVPFTYSLQAFYLVSHPHDLSWPLASVIIALKLCGYVIFRCANSQKNAFRKNPTDPKLAHLKTIHTSTGKSLLVSGWWGFVRHPNYLGDLIMALAWSLPCGFNHLLPYFYIIYFTALLIHREARDEHQCRRKYGLAWEKYCQRVPYRIFPYIY
Protein: mitogen-activated protein kinase kinase (EC 2.7.12.2) (Q925D6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Mitogen-activated protein kinase 14
- Mitogen-activated protein kinase kinase kinase 7
- mitogen-activated protein kinase
- mitogen-activated protein kinase kinase kinase
- Mitogen-activated protein kinase 13
- Mitogen-activated protein kinase 12
- mitogen-activated protein kinase kinase
- Mitogen-activated protein kinase 3
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 1
- Mitogen-activated protein kinase 1
Sequence:
MSQSKGKKRNPGLKIPREAFEQPQTSSTPPRDLDSKACISIGNQNFEVKADDLEPIVELGRGAYGVVEKMRHVPSGQIMAVKRIRATVNSQEQKRLLMDLDVSMRTVDCPFTVTFYGALFREGDVWICMELMDTSLDKFYKQVIDKGQTIPEDILGKIAVSIVKALEHLHSKLSVIHRDVKPSNVLINTLGQVKMCDFGISGYLVDSVAKTIDAGCKPYMAPERINPELNQKGYSVKSDIWSLGITMIELAILRFPYDSWGTPFQQLKQVVEEPSPQLPADKFSADFVDFTSQCLKKNSKERPTYPELMQHPFFTVHEAKAADVASFVKLILGD