wanglab/gogpt-training-data huggingface dataset:
Protein: Major DNA-binding protein (F5HDQ6)
Organism: Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5)
Function: Plays several crucial roles in viral infection. Participates in the opening of the viral DNA origin to initiate replication by interacting with the origin-binding protein. May disrupt loops, hairpins and other secondary structures present on ssDNA to reduce and eliminate pausing of viral DNA polymerase at specific sites during elongation. Promotes viral DNA recombination by performing strand-transfer, characterized by the ability to transfer a DNA strand from a linear duplex to a complementary single-stranded DNA circle. Can also catalyze the renaturation of complementary single strands. Additionally, reorganizes the host cell nucleus, leading to the formation of prereplicative sites and replication compartments. This process is driven by the protein which can form double-helical filaments in the absence of DNA.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04007}. Note=In the absence of DNA replication, found in the nuclear framework-associated structures (prereplicative sites). As viral DNA replication proceeds, it migrates to globular intranuclear structures (replication compartments). {ECO:0000255|HAMAP-Rule:MF_04007}.
Interaction partners:
Sequence:
MSHEELTALAPVGPAAFLYFSRLNAETQEILATLSLCDRSSSVVIAPLLAGLTVEADFGVSVRTPVLCYDGGVLTKVTSFCPFALYFHHTQGIVAFTEDHGDVHRLCEDARQKYALEAYTPEADRVPTDLAALCAAVGCQASETTVHVVVGNGLKEFLFAGQLIPCVEEATTVRLHGGEAVRVPLYPPTLFNSLQLDAEADEVSLDARSAFVEARGLYVPAVSETLFYYVYTSWCQSLRFSEPRVLIEAALRQFVHDSQQSVKLAPHKRYLGYMSQRLSSLEKDHLMLSDAVVCELAFSFASVFFDSAYQPAESMLFSEWPLVTNATDHRDLIRALTELKLHLSTHVAALVFSANSVLYQHRLVYLQSSARHPSAGGTASQETLLKAIQFTNGLSAACEDVYNDARKVLKFQGAPLKDERYGPQHLALVCGTCPQLVSGFVWYLNRVSVYNTGLSGSSTLTNHLVGCAAGLCEACGGTCCHTCYQTAFVRVRTRLPVVPKQPKKEPCVITVQSRFLNDVDILGSFGRRYNVDAKDGGLDGKGDDGVPGGGAGGGGGRDVSGGPSDGLGGGRGGGGGGDSGGMMGRGGRMLGASVDRTYRLNRILDYCRKMRLIDPVTGEDTFSAHGKSDFVAVFSALNKFVDDEALGFVSEVRLKSSRDEVAGATQAFNLDLNPYAVAFQPLLAYAYFRSVFYVIQNVALITATSYIVDNPLTTNLVSKWMTQHFQSIHGAFSTTSSRKGFLFTKQIKSSKNSDHDRLLDFRLYAQGTYAVVPMEIKLSRLSVPTLIMVRVKNRPIYRAGKGNAGSVFFRRDHVPRRNPAKGCLGFLLYRHHERLFPECGLPCLQFWQKVCSNALPKNVPIGDMGEFNAFVKFLVAVTADYQEHDLLDVAPDCVLSYVESRFHNKFLCYYGFKDYIGSLHGLTTRLTTQNHAQFPHVLGASPRFSSPAEFALHVKGLKTAGVPAPMAATVARESLVRSVFEHRSLVTVPVSVEKYAGINNSKEIYQFGQIGYFSGNGVERSLNVSSMSGQDYRFMRQRYLLATRLADVLIKRSRRENVLFDADLIKNRVMLALDAENLDCDPEVMAVYEILSVREEIPASDDVLFFVDGCEALAASLMDKFAALQEQGVEDFSLENLRRVLDADAQRLTDAAGGEVHDLSALFAPSGVGAASGVGGGGLLLGESVAGNSICFGVPGETGGGCFLVNAGEDEAGGVGGSSGGGGGSGLLPAKRSRL
Protein: Anionic trypsin-2 (EC 3.4.21.4) (Anionic trypsin II) (Pretrypsinogen II) (Serine protease 2) (P00763)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space.
Interaction partners:
- Amyloid-beta precursor protein
- Mannose-binding protein C
- Mannose-binding protein A
- Proteinase-activated receptor 2
- Proteinase-activated receptor 1
- Chymotrypsinogen B
Sequence:
MRALLFLALVGAAVAFPVDDDDKIVGGYTCQENSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKSRIQVRLGEHNINVLEGNEQFVNAAKIIKHPNFDRKTLNNDIMLIKLSSPVKLNARVATVALPSSCAPAGTQCLISGWGNTLSSGVNEPDLLQCLDAPLLPQADCEASYPGKITDNMVCVGFLEGGKDSCQGDSGGPVVCNGELQGIVSWGYGCALPDNPGVYTKVCNYVDWIQDTIAAN
Protein: Olfactomedin 2 (K7EIS8)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MEVLELRTYRDLQYVRGMETLMRSLDARLRAADGSLSAKSFQELKDRMTELLPLSSVLEQYKADTRTIVRLREEVRNLSGSLAAIQEEMGAYGYEDLQQRVMALEARLHACAQKLGCGKLTGVSNPITVRAMGSRFGSWMTDTMAPSADSRVWYMDGYYKGRRVLEFRTLGDFIKGQNFIQHLLPQPWAGTGHVVYNGSLFYNKYQSNVVVKYHFRSRSVLVQRSLPGAGYNNTFPYSWGGFSDMDFMVDESGLWAVYTTNQNAGNIVVSRLDPHTLEVMRSWDTGYPKRSAGEAFMICGVLYVTNSHLAGAKVYFAYFTNTSSYEYTDVPFHNQYSHISMLDYNPRERALYTWNNGHQVLYNVTLFHVISTSGDP
Protein: DNA polymerase iota (EC 2.7.7.7) (Rad30 homolog B) (Q6R3M4)
Organism: Mus musculus (Mouse)
Function: Error-prone DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Favors Hoogsteen base-pairing in the active site. Inserts the correct base with high-fidelity opposite an adenosine template (By similarity). Exhibits low fidelity and efficiency opposite a thymidine template, where it will preferentially insert guanosine (By similarity). May play a role in hypermutation of immunoglobulin genes (By similarity). Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but may not have lyase activity (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Note=Binding to ubiquitin mediates localization to replication forks after UV-induced DNA damage. {ECO:0000269|PubMed:16357261}.
Interaction partners:
- DNA repair protein REV1
- RNA polymerase I-specific transcription initiation factor RRN3
- Proliferating cell nuclear antigen
- Nucleolar transcription factor 1
- DNA polymerase zeta catalytic subunit
- NAD-dependent protein deacetylase sirtuin-7
- Polyubiquitin-C
- Cellular tumor antigen p53
- Mitotic spindle assembly checkpoint protein MAD2B
- Ubiquitin-ribosomal protein eS31 fusion protein
Sequence:
MEPLHAGAAGSSRAVCSQGPPTQISSSRVIVHVDLDCFYAQVEMISNPELKDRPLGVQQKYLVVTCNYEARKLGVRKLMNVRDAKEKCPQLVLVNGEDLSRYREMSYKVTELLEEFSPAVERLGFDENFVDLTEMVEKRLQQLPSEEVPSVTVFGHVYNNQSVNLHNIMHRRLVVGSQIAAEMREAMYNQLGLTGCAGVAPNKLLAKLVSGVFKPNQQTVLLPESCQHLIHSLNHIKEIPGIGYKTAKRLEVLGINSVHDLQTFPIKTLEKELGIAIAQRIQQLSFGEDKSPVTPSGPPQSFSEEDTFKKCSSEVEAKAKIEELLSSLLTRVCQDGRKPHTVRLVIRRYSDKHCNRESRQCPIPSHVIQKLGTGNHDSMPPLIDILMKLFRNMVNVKMPFHLTLMSVCFCNLKALSSAKKGPMDCYLTSLSTPAYTDKRAFKVKDTHTEDSHKEKEANWDCLPSRRIESTGTGESPLDATCFPKEKDTSDLPLQALPEGVDQEVFKQLPADIQEEILYGKSRENLKGKGSLSCPLHASRGVLSFFSTKQMQASRLSPRDTALPSKRVSAASPCEPGTSGLSPGSTSHPSCGKDCSYYIDSQLKDEQTSQGPTESQGCQFSSTNPAVSGFHSFPNLQTEQLFSTHRTVDSHKQTATASHQGLESHQGLESRELDSAEEKLPFPPDIDPQVFYELPEEVQKELMAEWERAGAARPSAHR
Protein: Transmembrane protein 176A (Gene signature 188) (Kidney-expressed gene 2 protein) (Q9DCS1)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Transmembrane protein 176B
- Membrane-spanning 4-domains, subfamily A, member 18
Sequence:
MSTDMETAVVGKVDPEAPQPTHIDVHIHQESALAKLLLAGCSLLRIPASASTQSQGSSRVLVASWVVQTVLGALSVVLGGTLYIGHYLAMYSEGAPFWTGIVAMLAGAVAFLHKKRGGTCWALMRTLLVLASFCTAVAAIVIGSRELNFYWYFLGDDVCQRDSSYGWSTMPRTTPVPEEADRIALCIYYTSMLKTLLMSLQAMLLGIWVLLLLASLTPVCVYIWKRFFTKAETEEKKLLGAAVI
Protein: Cytotoxic necrotizing factor 1 (A0A1W5T566)
Organism: Escherichia coli
Interaction partners:
Sequence:
LENDNKQLLSQHFSLYSRQDGITYAGVNSVLNAIENDGVFNESYFLYSNKRINNKDVFDAVAFSVKKRSFSDGDTVIKSNSEAQRDYALTILQTILSMTPIFDVAIPEVSVTLGLGIIASSMGISFDQLINGDTYEERRSAIPGLATNAALLGLSFAIPFLISKAG
Protein: Transcription factor MYB32 (Myb-related protein 32) (AtMYB32) (O49608)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
Interaction partners:
- Trans-cinnamate 4-monooxygenase
- NAC domain-containing protein 12
- Dihydroflavonol 4-reductase
- NAC domain-containing protein 43
- Transcription factor TT8
Sequence:
MGRSPCCEKDHTNKGAWTKEEDDKLISYIKAHGEGCWRSLPRSAGLQRCGKSCRLRWINYLRPDLKRGNFTLEEDDLIIKLHSLLGNKWSLIATRLPGRTDNEIKNYWNTHVKRKLLRKGIDPATHRPINETKTSQDSSDSSKTEDPLVKILSFGPQLEKIANFGDERIQKRVEYSVVEERCLDLNLELRISPPWQDKLHDERNLRFGRVKYRCSACRFGFGNGKECSCNNVKCQTEDSSSSSYSSTDISSSIGYDFLGLNNTRVLDFSTLEMK
Protein: Integrin-linked protein kinase 1 (EC 2.7.11.1) (Ankyrin protein kinase 1) (F4IS56)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as a link between plant defense pathways, stress responses and potassium homeostasis. Promotes osmotic stress sensitivity, responses to the bacterial-derived pathogen-associated molecular pattern (PAMP) flg22, and resistance to bacterial pathogens. Promotes the accumulation of POT5/HAK5, a potassium transporter that mediates high-affinity uptake during potassium deficiency.
Subcellular location: Cell membrane {ECO:0000269|PubMed:27208244}; Peripheral membrane protein {ECO:0000269|PubMed:27208244}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:27208244}; Peripheral membrane protein {ECO:0000269|PubMed:27208244}.
Interaction partners:
- Protein GRAVITROPIC IN THE LIGHT 1
Sequence:
MENITAQLKRGISRQFSTGSIRRTLSRQFTRQSSLDPRRTNMRFSFGRQSSLDPIRRSPDSSKSDDEPHMSVPENLDSTMQLLFMASKGDVRGIEELLDEGIDVNSIDLDGRTALHIAACEGHLGVVKALLSRRANIDARDRWGSTAAADAKYYGNLDVYNLLKARGAKVPKTRKTPMTVSNPREVPEYELNPLEVQVRKSDGISKGAYQVAKWNGTRVSVKILDKDSYSDPERINAFRHELTLLEKVRHPNVIQFVGAVTQNIPMMIVVEYNPKGDLSVYLQKKGRLSPSKALRFALDIARGMNYLHECKPDPIIHCDLKPKNILLDRGGQLKISGFGMIRLSKISQDKAKVANHKAHIDLSNYYIAPEVYKDEIFDLRVDAHSFGVILYEITEGVPVFHPRPPEEVARMMCLEGKRPVFKTKSRSYPPDIKELIEKCWHPEAGIRPTFSEIIIRLDKIVANCSKQGWWKDTFKFPWK
Protein: Sulfur oxidation protein SoxX (Q8KDN0)
Organism: Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) (Chlorobium tepidum)
Interaction partners:
- L-cysteine S-thiosulfotransferase subunit SoxA
- Sulfur oxidation protein SoxY
- Sulfur oxidation protein SoxB
- Sulfur oxidation protein SoxZ
- Cytochrome bc complex cytochrome b subunit
- Uncharacterized protein
- Cytochrome b6-f complex iron-sulfur subunit
- Polysulfide reductase, subunit A, putative
- Sulfide dehydrogenase, flavoprotein subunit
- DoxX family protein
Sequence:
MARGFAAGDHGFSLKQVFNSLNKRGHMKSSGIIAAAAVLLLPSLGKAAAPAAVDSSVEKGKALALDTNKGNCIACHMMGDGEFPGNYGPPLSQMKERYPDRAVLRKQVWDASAINPKSIMPPFGKNGILNDSEIDNIVDYLYTL
Protein: Cyclic di-GMP phosphodiesterase NbdA (EC 3.1.4.52) (NO-induced biofilm dispersion locus A) (Q9HYT3)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:23729646}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- EAL domain-containing protein
Sequence:
MPFLPGKMPKPAVCRRPATSFHADLAGGSRYLYWKHNATPSPHPRRPRVFRVQGDTAMDWQGLRFLGESPVDGYVLQNCTYSPSLVALAFLVACLAGYTALDMVERVGNSLSHPRLWQWIGAFCLGSGIWATHFVAMLAFHAPIALRYDLPITGLSLLIAVAASYLTMYMTARPRFGLLPCLLAACCIGLGIAAMHYTGMAAMRSVATQYYQPSLFALSVLIAIGAAFTALAAVPYLRGRRSARYRYMKLIASLLLAGAIAAMHFTGMAALVLSVPAGTPLELQASADSLRLGWLTGVLASAIAACGIWAAWSEKQRERRLSENSRVNALLNQLDHAHASLRQMARYDSLTGLQNRTAFNEVFVQHLENCRLRGKGLAVMFLDLDHFKRINDSLGHDSGDQLLKIVSERIRSVLRDSDVVARFAGDEFCVLADLTQDHEAHILSQRLMQKMKEPIALDGRTLVMTASVGVSLYPNDGEQCEELLKNAGLALHQSKACGRNNAQFFSRQLLVRATQELQMEEELRQALRDDQLELHYQPILALADGEVHQLEALVRWRHPTQGLLGPDRFIGLAEANGMIDQLDDWVLRRACRDLRSLHLAGHERLRVAVNCCASNLGRASLVDEVRHALEQAGLAACFLELEVTEDALMYNIDQTIPLLERLRELGVSLSIDDFGTGYSSLAYLRRLPLDALKVDRSFIMDIPASQRDMEIAQAIIAMAQKLHLKVVAEGVETPQQLAFLRENHCELVQGYLFSRPLPLAALEEFLRAYRFDAAPPLRSLNQA
Protein: Dolichyl N-acetyl-alpha-D-glucosaminyl phosphate 3-beta-D-2,3-diacetamido-2,3-dideoxy-beta-D-glucuronosyltransferase (EC 2.4.1.335) (Glc-2,3-diNAcA glycosyltransferase) (UDP-Glc-2,3-diNAcA glycosyltransferase) (B3VA59)
Organism: Methanococcus voltae
Function: Involved in the assembly of an N-linked disaccharide that decorates the S-layer glycoprotein and flagellins. AglC catalyzes the transfer of 2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronic acid (Glc-2,3-diNAcA) from uridine 5'-diphospho 2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronic acid (UDP-Glc-2,3-diNAcA) to the AglK product Dol-P-GlcNAc to yield Dol-P-GlcNAc-Glc-2,3-diNAcA. AglC is specific for the monophosphate-linked Dol-P-GlcNAc.
Subcellular location: Cell membrane {ECO:0000305|PubMed:23624439}; Multi-pass membrane protein {ECO:0000305|PubMed:23624439}.
Interaction partners:
Sequence:
MNFISIIIPTFNEEKYITKCLENWFNQDYPKENYEILIFDGKSTDKTLDVIKELQKKHNFENIKIYTNEKRKQVYAFNEGIKNANGDFFIIFGAHAYPEQDFLKNNIETYQRIKKEEPKLAGVGGIINKISENMSAEIAKVIYSTPLSGGSSFWYAKEGFFSNTVVYGMYDTKMIKESEILFDTDFITGQDFEFNLHLIKEGFKLYTNPNIVSSYYTRSSVKKFIKQTISYGAAKGLMIRKGYFNILWLFPFGFLFMLLSIIITGLLIFIYIMAILIDTIRLLIKTREPLYIALPILLFLFHCLISYGFFKGLIKGNSTFK
Protein: Sulfotransferase (EC 2.8.2.-) (Q6DHH8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Progestin and adipoQ receptor family member 4
- ADP-ribosylarginine hydrolase
- Serine/threonine-protein phosphatase
- Protein pelota homolog
- Mid1-interacting protein 1A
- Mitochondrial tRNA translation optimization 1
- Calcium-transporting ATPase
Sequence:
MEQEPLSYEEAITRAADAIQRFPLKDVQGVPLMSTIADNWKSISEFCPDPSDLLISTYPKAGTTWTQEIVDLLLNNGDAQVCKRAPTAVRIPFLEICAPPPIPSGLELLKQMKPPRVIKTHLPIQLVPVGFWQNKCKVIYMARNAKDNLVSYFHFDRMNLTQPEPGPWDGYIHKFMKGQLGWGSWYDHVKGYWKESKERNILYILYEDMKENPSREIKRIMHYLDLSVSEDVINKIVQLTSFHVMKDNPMANYSYIPKAVFDQSISAFMRKGEVGDWVNHFTPAQSKMFDEDYTNQMKDVDIPFRLNI
Protein: Isoamylase 3, chloroplastic (AtISA3) (EC 3.2.1.68) (Q9M0S5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in starch catabolism. ISA3 removes different branches than ISA1-ISA2, namely short chains that prevent amylopectin crystallization. May be the debranching enzyme required to assist beta-amylases for starch degradation in leaves at night.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:16495218, ECO:0000269|PubMed:18431481}. Note=Localizes to granule-like structures inside the chloroplast.
Interaction partners:
- Alpha-glucan phosphorylase 2, cytosolic
- 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic
- 4-alpha-glucanotransferase DPE2
- Alpha-glucan phosphorylase 1
- Alpha-amylase 3, chloroplastic
- Alpha-amylase 1
- Probable alpha-amylase 2
- Starch synthase 3, chloroplastic/amyloplastic
- 1,4-alpha-glucan-branching enzyme 2-1, chloroplastic/amyloplastic
- 1,4-alpha-glucan-branching enzyme 3, chloroplastic/amyloplastic
Sequence:
MLTSPSSSSTYDPFSSNFSPSLTNAFSSSFTIPMGLKLSRRVTRARIFSRKIKDRSTLKVTCRRAHERVVEEEASTMTETKLFKVSSGEVSPLGVSQVDKGINFALFSQNATSVTLCLSLSQSGKDDTDDDGMIELVLDPSVNKTGDTWHICVEDLPLNNVLYGYRVDGPGEWQQGHRFDRSILLLDPYAKLVKGHSSFGDSSQKFAQFYGTYDFESSPFDWGDDYKFPNIPEKDLVIYEMNVRAFTADESSGMDPAIGGSYLGFIEKIPHLQDLGINAVELLPVFEFDELELQRRSNPRDHMVNTWGYSTVNFFAPMSRYASGEGDPIKASKEFKEMVKALHSAGIEVILDVVYNHTNEADDKYPYTTSFRGIDNKVYYMLDPNNQLLNFSGCGNTLNCNHPVVMELILDSLRHWVTEYHVDGFRFDLASVLCRATDGSPLSAPPLIRAIAKDSVLSRCKIIAEPWDCGGLYLVGKFPNWDRWAEWNGMYRDDVRRFIKGDSGMKGSFATRVSGSSDLYQVNQRKPYHGVNFVIAHDGFTLRDLVSYNFKHNEANGEGGNDGCNDNHSWNCGFEGETGDAHIKSLRTRQMKNFHLALMISQGTPMMLMGDEYGHTRYGNNNSYGHDTSLNNFQWKELDAKKQNHFRFFSEVIKFRHSHHVLKHENFLTQGEITWHEDNWDNSESKFLAFTLHDGIGGRDIYVAFNAHDYFVKALIPQPPPGKQWFRVADTNLESPDDFVREGVAGVADTYNVAPFSSILLQSK
Protein: Fibroblast growth factor receptor 1 (FGFR-1) (bFGF-R-1) (EC 2.7.10.1) (Basic fibroblast growth factor receptor 1) (MFR) (Proto-oncogene c-Fgr) (CD antigen CD331) (Q04589)
Organism: Rattus norvegicus (Rat)
Function: Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of embryonic development, cell proliferation, differentiation and migration. Required for normal mesoderm patterning and correct axial organization during embryonic development, normal skeletogenesis and normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. Phosphorylates PLCG1, FRS2, GAB1 and SHB. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes phosphorylation of SHC1, STAT1 and PTPN11/SHP2. In the nucleus, enhances RPS6KA1 and CREB1 activity and contributes to the regulation of transcription. FGFR1 signaling is down-regulated by IL17RD/SEF, and by FGFR1 ubiquitination, internalization and degradation (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:15117958}; Single-pass type I membrane protein {ECO:0000269|PubMed:15117958}. Nucleus {ECO:0000269|PubMed:15117958}. Cytoplasm, cytosol {ECO:0000269|PubMed:15117958}. Cytoplasmic vesicle {ECO:0000250}. Note=After ligand binding, both receptor and ligand are rapidly internalized. Can translocate to the nucleus after internalization, or by translocation from the endoplasmic reticulum or Golgi apparatus to the cytosol, and from there to the nucleus (By similarity). {ECO:0000250}.
Interaction partners:
- Klotho
- Fibroblast growth factor 2
- Fibroblast growth factor 1
- Fibroblast growth factor 23
- Fibroblast growth factor 9
- Fibroblast growth factor 16
- Klotho beta
- Fibroblast growth factor 10
- Fibroblast growth factor 7
- Fibroblast growth factor
Sequence:
MWGWRGLLFWAVLVTATLCTARPAPTLPEQAQPWGVPVEVESLLVHPGDLLQLRCRLRDDVQSINWLRDGVQLAESNRTRITGEEVEVRDSIPADSGLYACVTNSPSGSDTTYFSVNVSDALPSSEDDDDDDDSSSEEKETDNTKPNRRPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPSSGTPSPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYDQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEALEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIIYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVTVSADSSASMNSGVLLVRPSRLSSSGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPNPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWNAVPSQRPTFKQLVEDLDRIVALTSNQEYLDLSMPLDQDSPSFPDTRSSTCSSGEDSVFSHEPFPEEPCLPRHPTQLANGGLNRR
Protein: (R)-2-hydroxyisocaproyl-CoA dehydratase alpha subunit (EC 4.2.1.157) (Q5U924)
Organism: Clostridioides difficile (Peptoclostridium difficile)
Function: Involved in the reductive branch of L-leucine fermentation. Catalyzes the irreversible beta/alpha-elimination of water from (R)-2-hydroxyisocaproyl-CoA to yield isocaprenoyl-CoA. This beta/alpha-dehydration depends on the reductive formation of ketyl radicals on the substrate generated by injection of a single electron from the ATP-dependent activator protein HadI. The enzyme is specific for the R-isomer.
Interaction partners:
Sequence:
MSEKKEARVVINDLLAEQYANAFKAKEEGRPVGWSTSVFPQELAEVFDLNVLYPENQAAGVAAKKGSLELCEIAESKGYSIDLCAYARTNFGLLENGGCEALDMPAPDFLLCCNNICNQVIKWYENISRELDIPLIMIDTTFNNEDEVTQSRIDYIKAQFEEAIKQLEIISGKKFDPKKFEEVMKISAENGRLWKYSMSLPADSSPSPMNGFDLFTYMAVIVCARGKKETTEAFKLLIEELEDNMKTGKSSFRGEEKYRIMMEGIPCWPYIGYKMKTLAKFGVNMTGSVYPHAWALQYEVNDLDGMAVAYSTMFNNVNLDRMTKYRVDSLVEGKCDGAFYHMNRSCKLMSLIQYEMQRRAAEETGLPYAGFDGDQADPRAFTNAQFETRIQGLVEVMEERKKLNRGEI
Protein: Uncharacterized protein (Q57YD4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Manganese/iron superoxide dismutase C-terminal domain-containing protein
- Ubiquitin-like domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MLRSTLTSLNTFLTSSVATPPISVIRTGPKWWADPERMVRQKLMYFTLGVDQLPLRRTAVIQRDLQRFHMCKPPPRVGDSTGYKRSRAAQLNTWYRRIQYQEYHMQHLFTRHVWGLLRVYPGNTTKIQGKADDGYVGYDSVPFHRYNRAPLPFPARELYERRK
Protein: Guanine nucleotide-binding protein G(i) subunit alpha-3 (G(i) alpha-3) (P08753)
Organism: Rattus norvegicus (Rat)
Function: Heterotrimeric guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Signaling by an activated GPCR promotes GDP release and GTP binding. The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal. Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins. Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels. Stimulates the activity of receptor-regulated K(+) channels. The active GTP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P08754}. Cell membrane {ECO:0000250|UniProtKB:P08754}; Lipid-anchor {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P08754}. Note=Localizes in the centrosomes of interphase and mitotic cells. Detected at the cleavage furrow and/or the midbody. {ECO:0000250|UniProtKB:P08754}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Lysophosphatidic acid receptor 1
- Gamma-aminobutyric acid type B receptor subunit 2
- D
- Regulator of G-protein signaling 9
- G-protein-signaling modulator 1
- Apelin receptor
- Sphingosine 1-phosphate receptor 1
- Melatonin receptor type 1B
- Relaxin receptor 1
Sequence:
MGCTLSAEDKAAVERSKMIDRNLREDGEKAAKEVKLLLLGAGESGKSTIVKQMKIIHEDGYSEDECKQYKVVVYSNTIQSIIAIIRAMGRLKIDFGEAARADDARQLFVLAGSAEEGVMTSELAGVIKRLWRDGGVQACFSRSREYQLNDSASYYLNDLDRISQTNYIPTQQDVLRTRVKTTGIVETHFTFKELYFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKRSPLTICYPEYTGSNTYEEAAAYIQCQFEDLNRRKDTKEVYTHFTCATDTKNVQFVFDAVTDVIIKNNLKECGLY
Protein: Sodium channel protein (A0A286YEQ8)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361132}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361132}.
Interaction partners:
Sequence:
MEQTVLVPPGPDSFNFFTRESLAAIERRIAEEKAKNPKPDKKDDDENGPKPNSDLEAGKNLPFIYGDIPPEMVSEPLEDLDPYYINKKTFIVLNKGKAIFRFSATSALYILTPFNPLRKIAIKILVHSLFSMLIMCTILTNCVFMTMSNPPDWTKNVEYTFTGIYTFESLIKIIARGFCLEDFTFLRDPWNWLDFTVITFAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCIQWPPTNASLEEHSIEKNITVNYNGTLINETVFEFDWKSYIQDSRYHYFLEGFLDALLCGNSSDAGQCPEGYMCVKAGRNPNYGYTSFDTFSWAFLSLFRLMTQDFWENLYQLTLRAAGKTYMIFFVLVIFLGSFYLINLILAVVAMAYEEQNQATLEEAEQKEAEFQQMIEQLKKQQEAAQQAATATASEHSREPSAAGRLSDSSSEASKLSSKSAKERRNRRKKRKQKEQSGGEEKDEDEFQKSESEDSIRRKGFRFSIEGNRLTYEKRYSSPHQSLLSIRGSLFSPRRNSRTSLFSFRGRAKDVGSENDFADDEHSTFEDNESRRDSLFVPRRHGERRNSNLSQTSRSSRMLAVFPANGKMHSTVDCNGVVSLVGGPSVPTSPVGQLLPEVIIDKPATDDNGTTTETEMRKRRSSSFHVSMDFLEDPSQRQRAMSIASILTNTVEELEESRQKCPPCWYKFSNIFLIWDCSPYWLKVKHVVNLVVMDPFVDLAITICIVLNTLFMAMEHYPMTDHFNNVLTVGNLVFTGIFTAEMFLKIIAMDPYYYFQEGWNIFDGFIVTLSLVELGLANVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKDCVCKIASDCQLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQAMCLTVFMMVMVIGNLVVLNLFLALLLSSFSADNLAATDDDNEMNNLQIAVDRMHKGVAYVKRKIYEFIQQSFIRKQKILDEIKPLDDLNNKKDSCMSNHTAEIGKDLDYLKDVNGTTSGIGTGSSVEKYIIDESDYMSFINNPSLTVTVPIAVGESDFENLNTEDFSSESDLEESKEKLNESSSSSEGSTVDIGAPVEEQPVVEPEETLEPEACFTEGCVQRFKCCQINVEEGRGKQWWNLRRTCFRIVEHNWFETFIVFMILLSSGALAFEDIYIDQRKTIKTMLEYADKVFTYIFILEMLLKWVAYGYQTYFTNAWCWLDFLIVDVSLVSLTANALGYSELGAIKSLRTLRALRPLRALSRFEGMRATFKGWMDIMYAAVDSRNVELQPKYEESLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPGNKFQGMVFDFVTRQVFDISIMILICLNMVTMMVETDDQSEYVTTILSRINLVFIVLFTGECVLKLISLRHYYFTIGWNIFDFVVVILSIVGMFLAELIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKREVGIDDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSKPPDCDPNKVNPGSSVKGDCGNPSVGIFFFVSYIIISFLVVVNMYIAVILENFSVATEESAEPLSEDDFEMFYEVWEKFDPDATQFMEFEKLSQFAAALEPPLNLPQPNKLQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDALRIQMEERFMASNPSKVSYQPITTTLKRKQEEVSAVIIQRAYRRHLLKRTVKQASFTYNKNKIKGGANLLIKEDMIIDRINENSITEKTDLTMSTAACPPSYDRVTKPIVEKHEQEGKDEKAKGK