wanglab/gogpt-training-data huggingface dataset:
Protein: Minor histocompatibility antigen H13 (EC 3.4.23.-) (Intramembrane protease 1) (IMP-1) (IMPAS-1) (hIMP1) (Presenilin-like protein 3) (Signal peptide peptidase) (Q8TCT9)
Organism: Homo sapiens (Human)
Function: Catalyzes intramembrane proteolysis of some signal peptides after they have been cleaved from a preprotein, resulting in the release of the fragment from the ER membrane into the cytoplasm. Required to generate lymphocyte cell surface (HLA-E) epitopes derived from MHC class I signal peptides. May be necessary for the removal of the signal peptide that remains attached to the hepatitis C virus core protein after the initial proteolytic processing of the polyprotein. Involved in the intramembrane cleavage of the integral membrane protein PSEN1. Cleaves the integral membrane protein XBP1 isoform 1 in a DERL1/RNF139-dependent manner. May play a role in graft rejection (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15998642}; Multi-pass membrane protein {ECO:0000305}. Membrane {ECO:0000269|PubMed:12077416, ECO:0000269|PubMed:15385547}; Multi-pass membrane protein {ECO:0000305}; Lumenal side {ECO:0000269|PubMed:12077416, ECO:0000269|PubMed:15385547}.; SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000250|UniProtKB:Q9D8V0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9D8V0}.
Interaction partners:
- E3 ubiquitin-protein ligase RNF139
- Derlin-1
- Usherin
- Transitional endoplasmic reticulum ATPase
- Protein sel-1 homolog 1
- E3 ubiquitin-protein ligase AMFR
- E3 ubiquitin-protein ligase synoviolin
- Heme oxygenase 1
- Endoplasmin
- Selenoprotein S
Sequence:
MDSALSDPHNGSAEAGGPTNSTTRPPSTPEGIALAYGSLLLMALLPIFFGALRSVRCARGKNASDMPETITSRDAARFPIIASCTLLGLYLFFKIFSQEYINLLLSMYFFVLGILALSHTISPFMNKFFPASFPNRQYQLLFTQGSGENKEEIINYEFDTKDLVCLGLSSIVGVWYLLRKHWIANNLFGLAFSLNGVELLHLNNVSTGCILLGGLFIYDVFWVFGTNVMVTVAKSFEAPIKLVFPQDLLEKGLEANNFAMLGLGDVVIPGIFIALLLRFDISLKKNTHTYFYTSFAAYIFGLGLTIFIMHIFKHAQPALLYLVPACIGFPVLVALAKGEVTEMFSYEESNPKDPAAVTESKEGTEASASKGLEKKEK
Protein: Myotubularin-related protein 9 (Inactive phosphatidylinositol 3-phosphatase 9) (Q9Z2D0)
Organism: Mus musculus (Mouse)
Function: Acts as an adapter for myotubularin-related phosphatases. Increases lipid phosphatase MTMR6 catalytic activity, specifically towards phosphatidylinositol 3,5-bisphosphate, and MTMR6 binding affinity for phosphorylated phosphatidylinositols (By similarity). Positively regulates lipid phosphatase MTMR7 catalytic activity. The formation of the MTMR6-MTMR9 complex, stabilizes both MTMR6 and MTMR9 protein levels (By similarity). Plays a role in the late stages of macropinocytosis possibly by regulating MTMR6-mediated dephosphorylation of phosphatidylinositol 3-phosphate in membrane ruffles (By similarity). Negatively regulates DNA damage-induced apoptosis, in part via its association with MTMR6 (By similarity). Does not bind mono-, di- and tri-phosphorylated phosphatidylinositols, phosphatidic acid and phosphatidylserine (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24591580}. Cell projection, ruffle membrane {ECO:0000269|PubMed:24591580}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96QG7}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q96QG7}. Note=Localizes to ruffles during EGF-induced macropinocytosis (PubMed:24591580). Colocalizes with MTMR6 to the perinuclear region (By similarity). Partially localizes to the endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:Q96QG7, ECO:0000269|PubMed:24591580}.
Interaction partners:
- Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR6
- Phosphatidylinositol-3-phosphate phosphatase MTMR7
Sequence:
MEFAELIKTPRVDNVVLHRPFYTAVEGTLCLTGHHLILSSRQDNTEELWLLHSNIDAIDKRFVGSLGTIIIKCKDFRIIQLDIPGMEECLNIASSIEALSTLDSVTLMYPFFYRPMFEVIEDGWHSFLPEQEFEFYSSATSEWRLSYINKDFSICPSYPPTVIVPKSVDDEALRKVAAFRHGGRFPVLSYYHKKNGMVIMRSGQPLTGTNGRRCKEDEKLINATLRAGKRGYLIDTRSLNVAQQARAKGGGFEQEAHYPQWRRIHKSIERYHVLQESLIKLVEACNEQTHNMDRWLGKLEASNWLTHIKEILTTACLAAQCIDREGASVLIHGTEGTDSTLQVTSLAQIILEPRSRTIRGFEALIEREWLQAGHPFQQRCAQSAYCSSKQKWEAPVFLLFLDCVWQILRQFPCSFEFNEHFLIMLFEHAYASQFGTFLGNNESERCKLKLQQKTMSLWSWVNRPGELSKFTNPLFEANNLVIWPSVAPQSLQLWEGIFLRWSRSSKYLDEAYEEMVNIIEYNKELQAKVNVLRRQLAELETEDGL
Protein: Bone morphogenetic protein 15 (BMP-15) (Growth/differentiation factor 9B) (GDF-9B) (Q9Z0L4)
Organism: Mus musculus (Mouse)
Function: May be involved in follicular development. Oocyte-specific growth/differentiation factor that stimulates folliculogenesis and granulosa cell (GC) growth (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Bone morphogenetic protein receptor type-2
- Bone morphogenetic protein receptor type-1B
- Growth/differentiation factor 9
- Follistatin
- Factor in the germline alpha
- Homeobox protein NOBOX
- Follicle-stimulating hormone receptor
- Muellerian-inhibiting factor
- Lutropin-choriogonadotropic hormone receptor
- Inhibin alpha chain
Sequence:
MALLTILRILLWGVVLFMEQRVQMAKPGWPSTALLADDPTLPSILDLAKEAPGKEMKQWPQGYPLRYMLKLYHRSADPHGHPRENRTIGAKMVRLVKPSANTVRPPRGSWHVQTLDFPLASNQVAYELIRATVVYRHQLHLVNYHLSCHVETWVPKCRTKHLPSSKSGSSKPSPMSKAWTEIDITHCIQQKLWNRKGRSVLRLRFMCQQQKGNETREFRWHGMTSLDVAFLLLYFNDTDDRVQGKLLARGQEELTDRESSFLMRSVRQACSIESDASCPSQEHDGSVNNQCSLHPYKVSFHQLGWDHWIIAPRLYTPNYCKGICTRVLPYGLNSPNHAIIQSLVNELVNHSVPQPSCVPYNFLPMSILLIETNGSILYKEYEGMIAQSCTCR
Protein: AF4/FMR2 family member 2 (Protein FMR-2) (FMR2P) (Protein Ox19) (O55112)
Organism: Mus musculus (Mouse)
Function: RNA-binding protein. Might be involved in alternative splicing regulation through an interaction with G-quartet RNA structure.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:19136466}. Note=When splicing or transcription are inhibited, accumulates in large, rounded speckles and in the nucleolus. {ECO:0000250}.
Interaction partners:
- RNA polymerase II elongation factor ELL
Sequence:
MDLFDFFRDWDLEQQCHYEQDRSALKKREWERRNQEVQQEEDLFSSGFDLFGEPYKVAEYTNKGDALANRVQNTLGSYDEMKDLLSNHSSQNHLVGIPKNSAPQTPISKSEASFYPEQKNRMIPSHQETTHSSTPMPPPSVVILNSTLIHSNRKSKSEWPRDSHNTSPAQASQTSSQPNKMQTSTQDPPQTRLEDFFVYPAEQPQIGTVEKSNPSSKEENNPNSGGEDTFKEIFQSNSPEESEFTVQAPGSPLVASSLLAPSSGLSVPTFPPGLYCKTSMGQQKPTAYVRPMDGQDQATDISPTLKPSIEFENSFGNLSFGSLLDGKPSAVSSKTKLPKFTILQTSEVSLTSDPSCVEEILRESQHLTPGFTLQKWSDPSSRASTKMLEDDLKLSSDEDDLEPVKTLTTQCTANELYQAVEKAKPKNNPVNPLLATPQSTPATQTNVGSGSSSESESSSESDSDTESSTTDSESNEAPRVATPEPEPPSTNKWQLDKWLNKVTSQNKSFICGQNETPTETISLPPPIIQPVEVQVKVKPNPSQAVAVPKERPLLSLIREKARPRPTQKTPETKALKHKLSTSVDTVSQRTIGKKQPKKVEKNTSFEEFTWPKPNITNSTPKEKGSVELPDPPRSRNKATAHKPVPRKEPRPHVPLATEKKKYRGPGKIVPKSREFIETDSSTSDSNTDQEETLQIKVLPPCITSKSKETSNASLTLSTLTNGNSNNLSTSNEETAFSPPPAMQTELLSPLRDHENPKNLWVKIDLDLLSRVPGQNSVPVTPAKTDYKETASKPKRQTAATAVEKPAPKGKRKHKPAETAEKIPEKKQRLEDNTTICLLPPCISPAPPHKPPSTRENSSRRANRKKEEKLFPPALSPLAEDPPRRRNVSGNNGHFGQDKNISMAGQITSSKPKRSEGKFCATFKGISINEGDAPKKAASATVTVANMALATATATATVPAIVTATVTATATTTATATTTTTTTTISSITPTITSGLMDSSHLEMTSWAALPLLSSSSANVRRPKLTFDDSVHNADFYMQEAKKLKHKADALFEKFGKAVNYADAALSFTECGNAMERDPLEAKSPYTMYSETVELLRYAMRLKNFASPLASDGDKKLAVLCYRCLSLLYLRMFKLKKDHAMKYSRSLMEYFKQNASKVTQIPSPWVGNGKNTPSPVSLNNVSPINSVGNCNNGPVTIPQRIHHMAASHVNITSNVLRGYEHWDMADKLTRDNKEFFGDLDTLMGPLTQHSSMTNLVRYVRQGLCWLRIDAHLL
Protein: Clathrin adaptor complexes medium subunit family protein (F4KHJ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}. Membrane, coated pit {ECO:0000256|ARBA:ARBA00004277}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004277}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004277}.
Interaction partners:
Sequence:
MPVAASAIYFLNLRGDVLINRTYRDDVGGNMVDAFRTHIMQTKELGNCPVRQIGGCSFVYMRISNVYIVIVVSSNANVACGFKFVVEAVALFKSYFGGAFDEDAIRNNFVLIYELLDEIMDFGYPQNLSPEILKLYITQEGVRSPFSSKPKDKPVPNATLQVTGAVGWRREGLAYKKNEVFLDIVESVNLLMSSKGNVLRCDVTGKVLMKCFLSGMPDLKLGLNDKIGLEKESEMKSRPAKSGKTIELDDVTFHQCVNLTRFNSEKTVSFVPPDGEFELMKYRITEGVNLPFRVLPTIKELGRTRMEVNVKVKSVFGAKMFALGVVVKIPVPKQTAKTNFQVTTGRAKYNPSIDCLVWKIRKFPGQTESTLSAEIELISTMGEKKSWTRPPIQMEFQVPMFTASGLRVRFLKVRIVIYAFESTILPKNAMLSSRISKPLCH
Protein: Putative secretin GspD (Putative general secretion pathway protein D) (Putative type II secretion system protein D) (T2SS protein D) (P45758)
Organism: Escherichia coli (strain K12)
Function: Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of folded proteins across the outer membrane. This subunit would form the outer membrane channel.
Subcellular location: Cell outer membrane {ECO:0000305|PubMed:28067918}. Note=Most of the protein is in the periplasm which it traverses to contact proteins of the cell inner membrane. {ECO:0000305|PubMed:28067918}.
Interaction partners:
- Putative type II secretion system protein C
- Type II secretion system core protein G
- Putative type II secretion system protein F
- Type II secretion system protein J
- Putative type II secretion system protein K
- Putative type II secretion system protein E
- Putative type II secretion system protein L
- Prepilin leader peptidase/N-methyltransferase
- Putative type II secretion system protein I
- Type II secretion system protein H
Sequence:
MKGLNKITCCLLAALLMPCAGHAENEQYGANFNNADIRQFVEIVGQHLGKTILIDPSVQGTISVRSNDTFSQQEYYQFFLSILDLYGYSVITLDNGFLKVVRSANVKTSPGMIADSSRPGVGDELVTRIVPLENVPARDLAPLLRQMMDAGSVGNVVHYEPSNVLILTGRASTINKLIEVIKRVDVIGTEKQQIIHLEYASAEDLAEILNQLISESHGKSQMPALLSAKIVADKRTNSLIISGPEKARQRITSLLKSLDVEESEEGNTRVYYLKYAKATNLVEVLTGVSEKLKDEKGNARKPSSSGAMDNVAITADEQTNSLVITADQSVQEKLATVIARLDIRRAQVLVEAIIVEVQDGNGLNLGVQWANKNVGAQQFTNTGLPIFNAAQGVADYKKNGGITSANPAWDMFSAYNGMAAGFFNGDWGVLLTALASNNKNDILATPSIVTLDNKLASFNVGQDVPVLSGSQTTSGDNVFNTVERKTVGTKLKVTPQVNEGDAVLLEIEQEVSSVDSSSNSTLGPTFNTRTIQNAVLVKTGETVVLGGLLDDFSKEQVSKVPLLGDIPLVGQLFRYTSTERAKRNLMVFIRPTIIRDDDVYRSLSKEKYTRYRQEQQQRIDGKSKALVGSEDLPVLDENTFNSHAPAPSSR
Protein: Phosphatidylinositol 3-kinase regulatory subunit beta (PI3-kinase regulatory subunit beta) (PI3K regulatory subunit beta) (PtdIns-3-kinase regulatory subunit beta) (Phosphatidylinositol 3-kinase 85 kDa regulatory subunit beta) (PI3-kinase subunit p85-beta) (PtdIns-3-kinase regulatory subunit p85-beta) (Q63788)
Organism: Rattus norvegicus (Rat)
Function: Regulatory subunit of phosphoinositide-3-kinase (PI3K), a kinase that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Indirectly regulates autophagy. Promotes nuclear translocation of XBP1 in a ER stress- and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement (By similarity).
Interaction partners:
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- phosphatidylinositol-4,5-bisphosphate 3-kinase
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform-like
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit.
- Phosphatidylinositol 3-kinase regulatory subunit gamma
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Receptor protein-tyrosine kinase
Sequence:
MAGAEGFQYRAVYPFRRERPEDLELLPGDLLVVSRVALQALGVADGGERCPHNVGWMPGFNERTRQRGDFPGTYVEFLGPVALARPGPRPRGPRPLPARPLDGPSESGHTLASLAEQFSPPESAPPILVKLIEAIEQAELDSEFYSRPELPAPRTDWSLSDLEQWDRTTLYDAVKGFLLALPAAVVTPEAASEAYRAMREVTGPVGLVLEPPTLPLHQALTLRFLLQHLGRVARRAPSPATAVHALASAFGPLLLRAPPPGGEGDGSEPAPDFPVLLLERLVQEHVDEQDTAPPALPPKPSKVKPAPTALANGGSTPSLQDAEWYWGDISREEVNERLRDTPDGTFLVRDASSKIQGEYTLTLRKGGNNKLIKVFHRDGHYGFSEPLTFCSVVELISHYRHESLAQYNAKLDTRLLYPVSKYQQDQVVKEDSVEAVGAQLKVYHQQYQDKSREYDQLYEEYTRTSQELQMKRTAIEAFNETILIFEEQGQTQEKCSKEYLERFRREGNEKEMQRILLNSERLKSRIAEIHESRTKLEQDLRAQASDNREIDKRMNSLKPDLMQLRKIRDQYLVWLTQKGARQRKINEWLGIKNETEDQYSLMEDEDALPHHEERTWYVGKINRTQAEEMLSAKRDGTFLIRESSQRGCYACSVVVDGDTKHCVIYRTATGFGFAEPYNLYGSLKELVLHYQHASLVQHNDALTVTLAHPVRAPGPGPPPAAR
Protein: Homeobox expressed in ES cells 1 (Homeobox protein ANF) (hAnf) (Q9UBX0)
Organism: Homo sapiens (Human)
Function: Required for the normal development of the forebrain, eyes and other anterior structures such as the olfactory placodes and pituitary gland. Possible transcriptional repressor. Binds to the palindromic PIII sequence, 5'-AGCTTGAGTCTAATTGAATTAACTGTAC-3'. HESX1 and PROP1 bind as heterodimers on this palindromic site, and, in vitro, HESX1 can antagonize PROP1 activation.
Subcellular location: Nucleus {ECO:0000269|PubMed:26781211}.
Interaction partners:
- Pituitary-specific positive transcription factor 1
- Transcription factor SOX-3
- Transcription factor SOX-2
- Transducin-like enhancer protein 1
- Nuclear receptor corepressor 1
- Prokineticin receptor 2
Sequence:
MSPSLQEGAQLGENKPSTCSFSIERILGLDQKKDCVPLMKPHRPWADTCSSSGKDGNLCLHVPNPPSGISFPSVVDHPMPEERASKYENYFSASERLSLKRELSWYRGRRPRTAFTQNQIEVLENVFRVNCYPGIDIREDLAQKLNLEEDRIQIWFQNRRAKLKRSHRESQFLMAKKNFNTNLLE
Protein: Integrator complex subunit 12 (Int12) (PHD finger protein 22) (Q96CB8)
Organism: Homo sapiens (Human)
Function: Component of the Integrator complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:23904267, ECO:0000269|PubMed:39032490}.
Interaction partners:
- Integrator complex subunit 1
- Integrator complex subunit 5
- Integrator complex subunit 3
- Integrator complex subunit 6
- Integrator complex subunit 11
- Integrator complex subunit 9
- Integrator complex subunit 7
- Integrator complex subunit 10
- Integrator complex subunit 4
- Integrator complex subunit 8
Sequence:
MAATVNLELDPIFLKALGFLHSKSKDSAEKLKALLDESLARGIDSSYRPSQKDVEPPKISSTKNISIKQEPKISSSLPSGNNNGKVLTTEKVKKEAEKRPADKMKSDITEGVDIPKKPRLEKPETQSSPITVQSSKDLPMADLSSFEETSADDFAMEMGLACVVCRQMMVASGNQLVECQECHNLYHRDCHKPQVTDKEANDPRLVWYCARCTRQMKRMAQKTQKPPQKPAPAVVSVTPAVKDPLVKKPETKLKQETTFLAFKRTEVKTSTVISGNSSSASVSSSVTSGLTGWAAFAAKTSSAGPSTAKLSSTTQNNTGKPATSSANQKPVGLTGLATSSKGGIGSKIGSNNSTTPTVPLKPPPPLTLGKTGLSRSVSCDNVSKVGLPSPSSLVPGSSSQLSGNGNSGTSGPSGSTTSKTTSESSSSPSASLKGPTSQESQLNAMKRLQMVKKKAAQKKLKK
Protein: RNA-directed RNA polymerase 2a (protein 2a) (EC 2.7.7.48) (P03594)
Organism: Brome mosaic virus (BMV)
Function: RNA-dependent RNA polymerase which replicates the viral genome composed of 3 RNA segments, RNA1, RNA2 and RNA3.
Interaction partners:
Sequence:
MSSKTWDDDFVRQVPSFQWIIDQSLEDEVEAASLQVQEPADGVAIDGSLASFKLAIAPLEIGGVFDPPFDRVRWGSICDTVQQMVQQFTDRPLIPQAEMARMLYLDIPGSFVLEDEIDDWYPEDTSDGYGVSFAADEDHASDLKLASDSSNCEIEEVRVTGDTPKELTLGDRYMGIDEEFQTTNTDYDITLQIMNPIEHRVSRVIDTHCHPDNPDISTGPIYMERVSLARTEATSHSILPTHAYFDDSYHQALVENGDYSMDFDRIRLKQSDVDWYRDPDKYFQPKMNIGSAQRRVGTQKEVLTALKKRNADVPEMGDAINMKDTAKAIAKRFRSTFLNVDGEDCLRASMDVMTKCLEYHKKWGKHMDLQGVNVAAETDLCRYQHMLKSDVKPVVTDTLHLERAVAATITFHSKGVTSNFSPFFTACFEKLSLALKSRFIVPIGKISSLELKNVRLNNRYFLEADLSKFDKSQGELHLEFQREILLALGFPAPLTNWWSDFHRDSYLSDPHAKVGMSVSFQRRTGDAFTYFGNTLVTMAMIAYASDLSDCDCAIFSGDDSLIISKVKPVLDTDMFTSLFNMEIKVMDPSVPYVCSKFLVETEMGNLVSVPDPLREIQRLAKRKILRDEQMLRAHFVSFCDRMKFINQLDEKMITTLCHFVYLKYGKEKPWIFEEVRAALAAFSLYSENFLRFSDCYCTEGIRVYQMSDPVCKFKRTTEERKTDGDWFHNWKNPKFPGVLDKVYRTIGIYSSDCSTKELPVKRIGRLHEALERESLKLANDRRTTQRLKKKVDDYATGRGGLTSVDALLVKSHCETFKPSDLR
Protein: Myosin-51 (Myosin type V-1) (O74805)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in cytokinesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11112691}. Note=Component of the cytokinetic actin ring (CAR).
Interaction partners:
- Uncharacterized protein C4H3.14c
- Myosin regulatory light chain cdc4
- Actin
- Tropomyosin
- GTP-binding protein ypt3
- Uncharacterized protein P8B7.02
- Myosin regulatory light chain 1
- Ras GTPase-activating-like protein rng2
- Ring assembly protein 3
- Kinesin-like protein 3
Sequence:
MSHARLSVGSECWVSNNNGHWDAARLIEIKDNGGGKVVATVAKSSGVLETVNYQQLQNRNIGQSESPSDLTNLPYLNEPSVLHALHNRYNNKQIYTYSGIVLVSINPYQNLPEFYNDNLIKHFHKDPEAAKVPHLYSIASSCYHALTTDSKNQTIIVSGESGAGKTVAAKYIMRYLTSVQGVDHNGVVKRSVENQVLATNPIMEAFGNAKTIRNDNSSRFGKYVTISFDENLLITGANVNTYLLERSRVVSLLKGERNYHIFYQLITGCTEEQRDKWFLESASSFNYLSQGNCDEISGVDDSNDFTITCRALSTIGISESRQEDVFCLLAALLHLGNIEVCATRNEAQIQPGDGYLQKAALLLGVDSSTLAKWIVKRQLKTRSETIITSSTLEHAISIRDSVAKYLYSALFLWIVHMINASLDHNKVKRAAYKYIGVVDIYGFEHFEKNSMEQFCINYANEKLQQEFNKHVFKLEQEEYVKEGLDWRLIEYSDNQGCISLIEDKLGILSLLDEECRLPSGNHQSFLQKLNNQLPTKHSQFYKKSRFNDGSFMVKHYALDVSYQVHDFLAKNSDAIPDEFISLLQNSKNEFITYLLDFYMQLVSSQNKNPRKTAISRKPTLSSMFKSSLSQLMTTVSSTNVHYIRCIKPNEEKLPWTFSPPMVLSQLRACGVFETIRISSLGFPARFSYEEFAHRFRILLSSKEWEEDNKKLTLNIVNSVIPHDNLNFQVGRSKIFFRSNVIGNFEEAHRATCSKSTVLLQSAIRGFFTRKEYQRTVKFIIKLQSVIMGWLTRQRFEREKIERAAILIQAHWRSYIQRKRYLSLIKCAIVIQSIVRKNIAYSRYINELRESSATLLAKFWRAYNARKTFRGLKKSVIALQCVSRSVLTRRYLRRLQDSAGRTSILYEKQKNLQASITEVSKQLKSNSKKVTVLRNKLNILNNSLSKWKCLIKKPSDFSEPVSMDFTSNDEQLVQLLQAESKLRQASQQLYMAAKKSELGFVQSQTARENLSNYYQALQMTVSEKFEYDTEQLPSRVLFYAMDRYFSIHKKLKQLLELVGVENASLLPNEVVNKQTKDLLYEKRVVFLKQIKQALTVSSLFNAVGYKDGVMRLLETDQNSLLFAGVVNFLIFAGISLDLKTQISEFLSQLCSYFTKIVDGTVIENDKTLDFYEKPLQAVLYWFATLHKIRSFLVHLLSINSHGKQSVVEDLWNPLILKFSKHFSNLENSFHSLVQKLLSCCTEGSINALLNSKCLPEFIDAADENTTPTGMNIYELIDRMNLIHKLLISSALQPNLLELTISHMLQHIGQRAFQTLIHGRSPYTWKSASQVSYNASLLINWCHQKGISYVNSSLLPLMQSPLVFCLRKNDANDLDVILSVCNLLSPFEVVCLLNRYQPCAGENPLPKSFSKAVEALSCKYKQSGFTNGKITNTNGHAIPIAASKNPLLSLENNHIYEELRLSELINLLAKATL
Protein: cysteine-S-conjugate beta-lyase (EC 4.4.1.13) (O53620)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Cystathionine gamma-synthase
- Conserved protein
- O-succinylhomoserine sulfhydrylase
- Putative cystathionine beta-lyase
- Probable O-acetylhomoserine sulfhydrylase MetC
- Methionine synthase
- O-acetylserine sulfhydrylase
- Probable cystathionine beta-synthase Rv1077
- L-cysteine desulfhydrase Cds1
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
Sequence:
MQDSIFNLLTEEQLRGRNTLKWNYFGPDVVPLWLAEMDFPTAPAVLDGVRACVDNEEFGYPPLGEDSLPRATADWCRQRYGWCPRPDWVRVVPDVLKGMEVVVEFLTRPESPVALPVPAYMPFFDVLHVTGRQRVEVPMVQQDSGRYLLDLDALQAAFVRGAGSVIICNPNNPLGTAFTEAELRAIVDIAARHGARVIADEIWAPVVYGSRHVAAASVSEAAAEVVVTLVSASKGWNLPGLMCAQVILSNRRDAHDWDRINMLHRMGASTVGIRANIAAYHHGESWLDELLPYLRANRDHLARALPELAPGVEVNAPDGTYLSWVDFRALALPSEPAEYLLSKAKVALSPGIPFGAAVGSGFARLNFATTRAILDRAIEAIAAALRDIID
Protein: Insulin-like 3 (Leydig insulin-like peptide) (Ley-I-L) (Relaxin-like factor) [Cleaved into: Insulin-like 3 B chain; Insulin-like 3 A chain] (Q9WUK0)
Organism: Rattus norvegicus (Rat)
Function: Seems to play a role in testicular function. May be a trophic hormone with a role in testicular descent in fetal life. Is a ligand for LGR8 receptor (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Relaxin receptor 2
- Relaxin receptor 1
- Prorelaxin 1
- Relaxin-3/INSL7 receptor 1 long form.
- Relaxin-3
- Steroid 17-alpha-hydroxylase/17,20 lyase
- 17-beta-hydroxysteroid dehydrogenase type 3
- Muellerian-inhibiting factor
- Cholesterol side-chain cleavage enzyme, mitochondrial
- Lutropin-choriogonadotropic hormone receptor
Sequence:
MHALLLLLLLALGSALRSPQPPEARAKLCGHHLVRALVRVCGGPRWSPEATQPVDTRDRELLQWLEQRHLLHALVADADPALDPDPALDPQLPHQASQRQRRSVATNAVHRCCLTGCTQQDLLGLCPH
Protein: Cytochrome P450 monooxygenase paxQ (EC 1.-.-.-) (Paxilline synthesis protein Q) (Q9C450)
Organism: Penicillium paxilli
Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of paxilline, a mycotoxin that acts as an inhibitor of mammalian maxi-K channels. PaxG, the geranylgeranyl diphosphate (GGPP) synthase is proposed to catalyze the first step in paxilline biosynthesis. Condensation of indole-3-glycerol phosphate with GGPP by paxC then forms 3-geranylgeranylindole (3-GGI), followed by epoxidation and cyclization of this intermediate (by paxM and paxB) to form paspaline. Paspaline is subsequently converted to 13-desoxypaxilline by paxP, the latter being then converted to paxilline by paxQ. Finally paxilline can be mono- and di-prenylated by paxD. PaxQ can also utilized beta-paxitriol and alpha-PC-M6 as substrates converting them to alpha-paxitriol.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDFVLSALQRDSWGIAAIILVSIWALHSFHRSRKLQIPVPYVGKCGILGPWISALQWESKARELVQEGYEKHGNFAFKVALLNRWEVCICNEDMIREYKNLMDNQFSAIAVTSELFQIKWTAPGTEEGAHKISIPLLGKALTWQRNRSAAQNDPYFSEFVEEFLYAWKEEVPVPENGDYELPCFETGARVVAHLTARSLVGYPLCRNPEIVNLFTDYGSAVPTSGFFIAMFPEIMKPFVANFCSAPRISKRLQAILLEEFAKRREEGGIESTDIMGWLRNWTDQNEPGVYGDLEITSSIIATIFGAIHTTTQVLVHCLFELATRPEYVEPLRVEIQSALEEHGGWVKEGIEGMVKLDSFIKECQRFNPLDAGSLARRATKDFTFKNGLTIPEGTFVFAPNGPILFDDTLYPEARQFDGYRFYNLGQKTGKPQDFRFAATNQKYLQFGDGRHTCPGRWMASDEIRLMLAHILMNYDIATKDNKGRPENWIFKKILFPDMKAVVILKARKSVSA
Protein: C-C chemokine receptor type 2 (C-C CKR-2) (CC-CKR-2) (CCR-2) (CCR2) (JE/FIC receptor) (MCP-1 receptor) (CD antigen CD192) (P51683)
Organism: Mus musculus (Mouse)
Function: Key functional receptor for CCL2 but can also bind CCL7 and CCL12 chemokines. Its binding with CCL2 on monocytes and macrophages mediates chemotaxis and migration induction through the activation of the PI3K cascade, the small G protein Rac and lamellipodium protrusion (By similarity). Also acts as a receptor for the beta-defensin DEFB106A/DEFB106B (By similarity). Regulates the expression of T-cell inflammatory cytokines and T-cell differentiation, promoting the differentiation of T-cells into T-helper 17 cells (Th17) during inflammation. Facilitates the export of mature thymocytes by enhancing directional movement of thymocytes to sphingosine-1-phosphate stimulation and up-regulation of S1P1R expression; signals through the JAK-STAT pathway to regulate FOXO1 activity leading to an increased expression of S1P1R. Plays an important role in mediating peripheral nerve injury-induced neuropathic pain. Increases NMDA-mediated synaptic transmission in both dopamine D1 and D2 receptor-containing neurons, which may be caused by MAPK/ERK-dependent phosphorylation of GRIN2B/NMDAR2B. Mediates the recruitment of macrophages and monocytes to the injury site following brain injury.
Subcellular location: Cell membrane {ECO:0000269|PubMed:8996246}; Multi-pass membrane protein {ECO:0000255}. Note=The chemoattractant receptors are reportedly distributed throughout the cell surface; after stimulation with a ligand, such as CCL2, they are rapidly recruited into microdomain clusters at the cell membrane. {ECO:0000250|UniProtKB:P41597}.
Interaction partners:
- C-C motif chemokine 5
- C-C motif chemokine 12
- C-C motif chemokine 2
- C-C motif chemokine 7
- C-C motif chemokine 8
- C-X-C motif chemokine 10
- Stromal cell-derived factor 1
- Fractalkine
- C-C motif chemokine 3
- Eotaxin
Sequence:
MEDNNMLPQFIHGILSTSHSLFTRSIQELDEGATTPYDYDDGEPCHKTSVKQIGAWILPPLYSLVFIFGFVGNMLVIIILIGCKKLKSMTDIYLLNLAISDLLFLLTLPFWAHYAANEWVFGNIMCKVFTGLYHIGYFGGIFFIILLTIDRYLAIVHAVFALKARTVTFGVITSVVTWVVAVFASLPGIIFTKSKQDDHHYTCGPYFTQLWKNFQTIMRNILSLILPLLVMVICYSGILHTLFRCRNEKKRHRAVRLIFAIMIVYFLFWTPYNIVLFLTTFQESLGMSNCVIDKHLDQAMQVTETLGMTHCCINPVIYAFVGEKFRRYLSIFFRKHIAKRLCKQCPVFYRETADRVSSTFTPSTGEQEVSVGL
Protein: Transcription factor AP-2 beta (Q561Y4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLWKLVENVKYEDIYEDRHDGVPSHSSRLSQLGSVSQGPYSSAPPLSHTPSSDFQPPYFPPPYQPLPYHQSQDPYSHVSDPYSLNALHQPQQHPWGSRQRQDLQGTESGGLLPQPRASLPQLSGLDPRRDYSTVRRPDVLLHSTHHGLEAGMGDGLSLHGLAHGMDDVQAVEDLNGAMNILDRTPLGNSRPSPILEPGIQSCLSHFSFITHGFGSPAICAALTALQNYLTEALKGLDKMFLNNPTPNRHTPADGSKGGEKEEKHRK