wanglab/gogpt-training-data huggingface dataset:
Protein: Ethanolamine kinase 1 (EKI 1) (EC 2.7.1.82) (Q9HBU6)
Organism: Homo sapiens (Human)
Function: Highly specific for ethanolamine phosphorylation. May be a rate-controlling step in phosphatidylethanolamine biosynthesis.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:11044454}.
Interaction partners:
- Ethanolamine-phosphate cytidylyltransferase
- Ethanolamine-phosphate phospho-lyase
- Glycerophosphocholine phosphodiesterase GPCPD1
- Transcription factor SOX-5
- Ethanolaminephosphotransferase 1
Sequence:
MLCGRPRSSSDNRNFLRERAGLSSAAVQTRIGNSAASRRSPAARPPVPAPPALPRGRPGTEGSTSLSAPAVLVVAVAVVVVVVSAVAWAMANYIHVPPGSPEVPKLNVTVQDQEEHRCREGALSLLQHLRPHWDPQEVTLQLFTDGITNKLIGCYVGNTMEDVVLVRIYGNKTELLVDRDEEVKSFRVLQAHGCAPQLYCTFNNGLCYEFIQGEALDPKHVCNPAIFRLIARQLAKIHAIHAHNGWIPKSNLWLKMGKYFSLIPTGFADEDINKRFLSDIPSSQILQEEMTWMKEILSNLGSPVVLCHNDLLCKNIIYNEKQGDVQFIDYEYSGYNYLAYDIGNHFNEFAGVSDVDYSLYPDRELQSQWLRAYLEAYKEFKGFGTEVTEKEVEILFIQVNQFALASHFFWGLWALIQAKYSTIEFDFLGYAIVRFNQYFKMKPEVTALKVPE
Protein: Beta-pinacene synthase (PcS) (EC 4.2.3.-) (EC 4.2.3.200) (EC 4.2.3.46) (EC 4.2.3.47) (Terpene synthase 5) (Q54TW4)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Terpene synthase that converts its substrate geranylgeranyl diphosphate (GGPP) into the diterpene beta-pinacene. Is also able to convert farnesyl diphosphate (FPP) into the sesquiterpene (E)-beta-farnesene as well as (E,E)-alpha-farnesene and beta-elemene as minor products.
Interaction partners:
Sequence:
MLCFNDFNFPKEWEVVPNSFKYIDIVIKEIIGFGLIKENDQELKMIVNQAISIAAYFWPYANEEQMVMGGSVLCWCVLFDDPLDTNKLDEKKGLEIVSRTEKLLLTRTLPNNPTNLEKYGFTIFEKCLKYCGTNTHMYDMLIKLTVQWIYSIIPFNKLNESPVHPETLKYIRKINIGIEFTQSIFYIINSNNKVDLIVLANPLYQKLVDLSSLNISFVNDAASFCKEIKDGGSDNNLFIILMKRLGGIEFIKEAYKQLTDLSNGYIDEFCYYEKLLLSSLSKQQQNEIQIFIDHLKYLMKGNQIWSTKTIRYATEDHPIIQLRNSTNKLIENNINMDKVSLTNKNYI
Protein: RAB6A-GEF complex partner protein 2 (Retrograde Golgi transport protein RGP1 homolog) (Q92546)
Organism: Homo sapiens (Human)
Function: The RIC1-RGP1 complex acts as a guanine nucleotide exchange factor (GEF), which activates RAB6A by exchanging bound GDP for free GTP and may thereby required for efficient fusion of endosome-derived vesicles with the Golgi compartment. The RIC1-RGP1 complex participates in the recycling of mannose-6-phosphate receptors.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:23091056}. Membrane {ECO:0000269|PubMed:23091056}.
Interaction partners:
- Guanine nucleotide exchange factor subunit RIC1
- Ragulator complex protein LAMTOR2
- Ragulator complex protein LAMTOR4
- Ragulator complex protein LAMTOR5
- Ragulator complex protein LAMTOR3
- Ragulator complex protein LAMTOR1
- Guanine nucleotide exchange protein SMCR8
- WD repeat-containing protein 41
- Dedicator of cytokinesis protein 1
- Kinase non-catalytic C-lobe domain-containing protein 1
Sequence:
MIEVVAELSRGPVFLAGEALECVVTVTNPLPPTATSASSEALAWASAQIHCQFHASESRVALPPPDSSQPDVQPDSQTVFLPHRGERGQCILSTPPKILFCDLRLDPGESKSYSYSEVLPIEGPPSFRGQSVKYVYKLTIGCQRVNSPITLLRVPLRVLVLTGLQDVRFPQDEAVAPSSPFLEEDEGGKKDSWLAELAGERLMAATSCRSLHLYNISDGRGKVGTFGIFKSVYRLGEDVVGTLNLGEGTVACLQFSVSLQTEERVQPEYQRRRGAGGVPSVSHVTHARHQESCLHTTRTSFSLPIPLSSTPGFCTAIVSLKWRLHFEFVTSREPGLVLLPPVEQPEPTTWTGPEQVPVDTFSWDLPIKVLPTSPTLASYAAPGPSTSTITI
Protein: Leucine-rich repeat receptor-like protein kinase PXL1 (EC 2.7.11.1) (Protein PHLOEM INTERCALATED WITH XYLEM-LIKE 1) (Q9FRS6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the regulation of procambium maintenance and polarity during vascular-tissue development. Phosphorylates HIRD11 and LHCA1 in vitro.
Subcellular location: Cell membrane {ECO:0000269|PubMed:25602612}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- CLAVATA3/ESR
- CLAVATA3/ESR
- WUSCHEL-related homeobox 14
- Dehydrin HIRD11
- EPIDERMAL PATTERNING FACTOR-like protein 4
- NADPH:quinone oxidoreductase
- WUSCHEL-related homeobox 4
- EPIDERMAL PATTERNING FACTOR-like protein 6
Sequence:
MAIPRLFFLFYYIGFALFPFVSSETFQNSEQEILLAFKSDLFDPSNNLQDWKRPENATTFSELVHCHWTGVHCDANGYVAKLLLSNMNLSGNVSDQIQSFPSLQALDLSNNAFESSLPKSLSNLTSLKVIDVSVNSFFGTFPYGLGMATGLTHVNASSNNFSGFLPEDLGNATTLEVLDFRGGYFEGSVPSSFKNLKNLKFLGLSGNNFGGKVPKVIGELSSLETIILGYNGFMGEIPEEFGKLTRLQYLDLAVGNLTGQIPSSLGQLKQLTTVYLYQNRLTGKLPRELGGMTSLVFLDLSDNQITGEIPMEVGELKNLQLLNLMRNQLTGIIPSKIAELPNLEVLELWQNSLMGSLPVHLGKNSPLKWLDVSSNKLSGDIPSGLCYSRNLTKLILFNNSFSGQIPEEIFSCPTLVRVRIQKNHISGSIPAGSGDLPMLQHLELAKNNLTGKIPDDIALSTSLSFIDISFNHLSSLSSSIFSSPNLQTFIASHNNFAGKIPNQIQDRPSLSVLDLSFNHFSGGIPERIASFEKLVSLNLKSNQLVGEIPKALAGMHMLAVLDLSNNSLTGNIPADLGASPTLEMLNVSFNKLDGPIPSNMLFAAIDPKDLVGNNGLCGGVLPPCSKSLALSAKGRNPGRIHVNHAVFGFIVGTSVIVAMGMMFLAGRWIYTRWDLYSNFAREYIFCKKPREEWPWRLVAFQRLCFTAGDILSHIKESNIIGMGAIGIVYKAEVMRRPLLTVAVKKLWRSPSPQNDIEDHHQEEDEEDDILREVNLLGGLRHRNIVKILGYVHNEREVMMVYEYMPNGNLGTALHSKDEKFLLRDWLSRYNVAVGVVQGLNYLHNDCYPPIIHRDIKSNNILLDSNLEARIADFGLAKMMLHKNETVSMVAGSYGYIAPEYGYTLKIDEKSDIYSLGVVLLELVTGKMPIDPSFEDSIDVVEWIRRKVKKNESLEEVIDASIAGDCKHVIEEMLLALRIALLCTAKLPKDRPSIRDVITMLAEAKPRRKSVCQVAGDLPIFRNSPVVGLI
Protein: FAD-linked oxidoreductase patO (EC 1.-.-.-) (Patulin synthesis protein O) (A1CFM2)
Organism: Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107)
Function: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (By similarity). PatO acts with patJ in the vacuole to convert gentisyl alcohol to isoepoxydon (By similarity). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable).
Subcellular location: Vacuole lumen {ECO:0000250|UniProtKB:A0A075TR33}.
Interaction partners:
Sequence:
MRLSIYSSILLLRAMCLVRPTFGFPATTCRCMPGDSCWPSSTDWAHFNASIGGRLIATQPLAQACHDPYYNETECQYLQKHWTLPALHDISPSSIMAAAVAKDTCDAFTPRSKPCAPGDMVVYSVNASSPDDFSRTIRFSQQRNIRLVIRNTGHDYLGKSTGAGALSIWTHYLKDIEFVNYTSSSYTGPAFTMAAGVQGSDIYNVANGRGLVVVGGECASVGPVGGYTQGGGHSALSSRFGLAADQVLEWQVVDGTGRLLTASPTQNPDLYWALSGGGGGTYGVVYSMTVKAFPDFPVTGVVLQFDTKNTSSKDFFQAVSYYHRDLPTYTAAGGMAIAQITRSSFLLTPLTLPNKTTEEARSLIAPFIHELETLHIPYQLNITQSATYLEHYKKLIEPNPTQLVQNGQYGGRLLPLNVIESNNTQLTEAVKTITQDGVVFVGIGLNVSSSVVGDVWNSVLPAWRTAALSVLLSTDWPAGANRSTMKTLADRMTSKWVPILTALSPDSGCYMNEADPQQPDWPQTFYGRNYETLYAIKKRYDPFDTFYASTAVGSGDWQVKTDGRLCRVKGNT
Protein: RNA demethylase ALKBH10B (EC 1.14.11.53) (Alkylated DNA repair protein alkB homolog 10B) (Alpha-ketoglutarate-dependent dioxygenase alkB homolog 10B) (Q9ZT92)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Dioxygenase that demethylates RNA by oxidative demethylation: specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes. ALKBH10B-mediated mRNA m6A demethylation stabilizes the mRNA of the key flowering time regulators FT, SPL3 and SPL9, which are involved in the control of floral transition.
Interaction partners:
- FKBP12-interacting protein of 37 kDa
- E3 ubiquitin-protein ligase HAKAI homolog
- N
- YTH domain-containing protein ECT3
- YTH domain-containing protein ECT2
- YTH domain-containing protein ECT4
- 30-kDa cleavage and polyadenylation specificity factor 30
- DNA oxidative demethylase ALKBH2
- Protein virilizer homolog
- Immune-associated nucleotide-binding protein 4
Sequence:
MTIAAAPARQTDRSATGFNPAYVTTAKAVSVPVQVPPATVVSEGLGKDALISWFRGEFAAANAIIDAMCSHLRIAEEAVSGSEYEAVFAAIHRRRLNWIPVLQMQKYHSIAEVAIELQKVAAKKAEDLKQKKTEEEAEEDLKEVVATEEEEVKKECFNGEKVTENDVNGDVEDVEDDSPTSDITDSGSHQDVHQTVVADTAHQIICHSHEDCDARSCEIKPIKGFQAKEQVKGHTVNVVKGLKLYEELLKEDEISKLLDFVAELREAGINGKLAGESFILFNKQIKGNKRELIQLGVPIFGHVKADENSNDTNNSVNIEPIPPLLESVIDHFVTWRLIPEYKRPNGCVINFFEEGEYSQPFLKPPHLEQPISTLVLSESTMAYGRILSSDNEGNFRGPLTLSLKQGSLLVMRGNSADMARHVMCPSQNKRVSITFFRIRPDTYHNHSQPNSPRNDGVMTMWQPYQMTPTPFLNGYDHSIDMMPKLGVLRPPMVMMAPPPVQPMILPSPNVMGTGGGTGVFLPWASVNSSRKHVKHLPPRAQKKRLLPLPPAASSSPAGGSTSEPVITVG
Protein: Fibulin-1 (A0A8I6AAN5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498, ECO:0000256|PIRNR:PIRNR036313}.
Interaction partners:
Sequence:
ASSPCPSRLARSLPYTANADISMEACCTEGNQMANQHRDCSLSYTSESKECRMVQEQCCHNQLEELHCATGINLASEPDGCASLHNYNSSLETIFIKRCCHCCMLGRAAQARGQTCEPNLMISYQCGLVFRACCVKGQENSDFVRGDGTDLQDPAKIPEEEEQEDPYLNDRCRGGGPCKQQCRDTGDEVICSCFVGYQLQSDGVSCEDINECITGSHNCRLGESCINTVGSFRCQRDSSCGTGYELTEDNNCKDIDECETGIHNCPPDFICQNTLGSFRCRPKLQCKSGFIQDALGNCIDINECLSISAPCPVGQTCINTEGSYTCQKNVPNCGRGYHLNEEGTRCVDVDECSPPAEPCGKGHHCLNSPGSFRCECKAGYYFDGISRTCVDINECQRYPGRLCGHKCENTPGSYHCSCSAGFRLSVDGRSCEDVNECLNSPCSQECANVYGSYQCYCRRGYQLSDVDGVTCEGEGTLCTVGSTLAWLPNSGISESMARACQDVSHIDECVTGIHNCSINETCFNIQGSFRCLSFECPENYRRSADTFRQEKTDTVRCIKSCRPTDEACMRDPVHTVSHTVISLPTFREFTRPEEIIFLRAVTPLYPANQADIIFDITEGNLRDSFDIIKRYEDGMTVGVVRQVRPIVGPFYAVLKLEMNYVLGGVVSHRNVVNVHIFVSEYWF
Protein: 1,4-alpha-glucan branching enzyme GlgB (EC 2.4.1.18) (1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase) (Alpha-(1->4)-glucan branching enzyme) (Glycogen-branching enzyme) (BE) (P9WN45)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Essential enzyme that catalyzes the formation of the alpha-1,6-glucosidic linkages in glucan chains by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position. Is involved in the biosynthesis of both glycogen and capsular alpha-D-glucan.
Interaction partners:
- Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase
- Glycogen phosphorylase
- Trehalose synthase/amylase TreS
- 4-alpha-glucanotransferase
- Glucose-1-phosphate adenylyltransferase
- Maltokinase
- Glycogen synthase
- Alpha-maltose-1-phosphate synthase
- Glycogen operon protein GlgX homolog
- Probable 1,4-alpha-glucan branching enzyme Rv3031
Sequence:
MSRSEKLTGEHLAPEPAEMARLVAGTHHNPHGILGAHEYDDHTVIRAFRPHAVEVVALVGKDRFSLQHLDSGLFAVALPFVDLIDYRLQVTYEGCEPHTVADAYRFLPTLGEVDLHLFAEGRHERLWEVLGAHPRSFTTADGVVSGVSFAVWAPNAKGVSLIGEFNGWNGHEAPMRVLGPSGVWELFWPDFPCDGLYKFRVHGADGVVTDRADPFAFGTEVPPQTASRVTSSDYTWGDDDWMAGRALRNPVNEAMSTYEVHLGSWRPGLSYRQLARELTDYIVDQGFTHVELLPVAEHPFAGSWGYQVTSYYAPTSRFGTPDDFRALVDALHQAGIGVIVDWVPAHFPKDAWALGRFDGTPLYEHSDPKRGEQLDWGTYVFDFGRPEVRNFLVANALYWLQEFHIDGLRVDAVASMLYLDYSRPEGGWTPNVHGGRENLEAVQFLQEMNATAHKVAPGIVTIAEESTPWSGVTRPTNIGGLGFSMKWNMGWMHDTLDYVSRDPVYRSYHHHEMTFSMLYAFSENYVLPLSHDEVVHGKGTLWGRMPGNNHVKAAGLRSLLAYQWAHPGKQLLFMGQEFGQRAEWSEQRGLDWFQLDENGFSNGIQRLVRDINDIYRCHPALWSLDTTPEGYSWIDANDSANNVLSFMRYGSDGSVLACVFNFAGAEHRDYRLGLPRAGRWREVLNTDATIYHGSGIGNLGGVDATDDPWHGRPASAVLVLPPTSALWLTPA
Protein: Sodium-dependent transporter bedraggled (Q0E961)
Organism: Drosophila melanogaster (Fruit fly)
Function: Putative sodium-dependent transporter which is required for viability, early imaginal disk development and adult motor coordination. Also has a role in the fate commitment of the R3/R4 photoreceptor cells. May function in ommatidial polarity by regulating the activity of the core polarity genes, acting upstream of (or in parallel to) Vang, dsh, pk, stan, and dgo, but downstream or independently of fz.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSSKEQQAAGRDFKRNSNAYSSLPPTGTGAGCSGAALGSGTGTGKRARSKQHQLEHEQFGLSNSLSSESIRQACAYYDDELSDEDLIEIQQTPQAFHQQTKQPLQLQPISFRLGDELGDERSAFCGSQEMQQVPLSTPIKQAAETDEALCVLSELDAILDVHDVSQLNGTCSSGSVNSGSDDDKVEDYLMDLDNYLEEMDNALNREDSLIIIDGHTSLKREPRTRTLPLSRKKKSSKKKSEDQEAAQGDFQREHQLRKTFSCSLRPTSQIASSSGSLETSTEPVMDVWRRQSMRRALEQEDTKATVAMEREEDDIPTLLVELPPRRDAEMRRCFSQGDCQASVAPTVGSQMLTEAHIFDNLLQTNARASSEEPRPRQYGRRLEGPPTPVRPLILAQSRPQSAPTRVQMREPQLQDTPTHPIMSTCSELSSARSSRMPSPVSLPSDSSSSGSSSAEHDQEPDPVQTTTMCSASSTTPLEPLHQLQLLLREKCGFNSQWPHAGSRTLALIGCTLGVFNMCRFAVLTINFGGNFLLQFLLLSVIFGIPLLWLQMCLGAKIRAGPVSMWKISPICAGVGIALVMQQCFLALYSTVSLAWILVYLRDVFPTAARSGYRWQEMAFPYRYDASNATGNLTQTVAEYFNVVVLQRLHLANHPDASGIRFHVNDRQLAFYLALIWAAVFLILCKGLKSLGKLAYIIYTLPLVALAVVTAKFVYVVDPSRIQNIFAASDFDDFLVNSNSWTAATQETFLTWGLLGASVIAITSRSHTNANKAALRRDAILLVLFTLIGLGLMALLALCCAQILWQHGYVYVPGSFENPDCYTSIYSLQSNTNPYLLSYPRSLIPHYSSFIGETYRRNRTMIHVESGFQALRFISEIFPAVLSLASDSISWVWAAVAFATFAGFGLAQLCVMWKPISSALGNSTSSVLLSCVTGLLLSIPFATEMGISILYYVDFLLGGSWFIPIIWTAQIFGVFLIRGRPYNGDDLVNDLRLCGSMSAFLALSWNVLLPIGLITLSVVDYKASLSNQFYYWRGKSYFTYWSRKMGSLIQIGVLLVIPVTAIIQIYRYLAHGPPDILERIQLLYRPPEEGEEPRRPSARQTASQSRRNALGQTTEGGQHDAQNDAPPKYTPPPSYTTATGARLAKLLRQSIRRSVRRVLGDSSRTRPVLSLDAESASPAAPPDYLTILTNPAGSSFNADPSPASSSSPESIEIDQRPVGYSQRSQSLGRKLHRSGASTLERRPYTAEDVVTILRSSVRHRQSQGGGNLVTASTLPRPPTAAMSTHLEDASFRSIENLVLNAEPPDRTPGVELELELEAGQAEECARNNTSVI
Protein: F-box protein YDR131C (Q03899)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins (By similarity).
Subcellular location: Vacuole {ECO:0000269|PubMed:14562095}.
Interaction partners:
- E3 ubiquitin-protein ligase HEL1
- Uncharacterized protein YER135C
Sequence:
MFDKLPYEIFKQIAWRIPQEDKISLTYVCKRSYESIIPFIYQNLFLNETYHINGDYDNSFGTCYWSVLNFHYIDEDDSNTKNDMSNRRLAKVKFSYFERTLAESPKRLCPLINRIRCTWHLNEDVMTNVLKLLSEYGSNLKFVDQFVRSSVNKGLEPLSKQLKTLTLTPPTLMPTHNSVSGSYLNKIDRLLLKCDLSRLEKLSIHINALKYFKNTGSPMKIKALVLNLRPDTLNLAEYDASDDFLKELEYIDIFDASTLRQLEILSWYSRDDFPSGEEGGFDRLYVKWGLEGFWKFPNIEKLSLASLVYSEFFLMNCLAVFHNLKILKLDYMGKFDFDVSLINFLSKQVCGKKLQRFDIHCQLNHRLFFPMTDNPLTRLNFDGFCPCSTCKNTIHEVILKKIFPETRSKLLKNPNKFQAHNFFYQMFFENKIMPYTNIIDNESPAMGWDSVPIETFVRKFNENLQSTIENTENITVNKITREDAISLYHLYLHYLKDVFKVFEQSLPNLEYLTINGIPTKIIQVDELQRCAVPLFYNNGYKSNSVYELVDAEALFS
Protein: Src substrate protein p85 (Cortactin) (p80) (Q01406)
Organism: Gallus gallus (Chicken)
Function: Contributes to the organization of the actin cytoskeleton and cell shape (By similarity). Plays a role in the formation of lamellipodia and in cell migration (By similarity). Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones, and may play a role in the regulation of neuronal spine density (By similarity). Plays a role in focal adhesion assembly and turnover (By similarity). Plays a role in intracellular protein transport and endocytosis, and in modulating the levels of potassium channels present at the cell membrane (By similarity). Plays a role in endocytosis via clathrin-coated pits (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:1922035}. Cell projection, lamellipodium {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell projection {ECO:0000250|UniProtKB:Q66HL2}. Cell membrane {ECO:0000269|PubMed:1922035}. Cell projection, podosome {ECO:0000269|PubMed:1922035}. Cell junction {ECO:0000250|UniProtKB:Q66HL2}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q66HL2}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q66HL2}. Cell projection, dendritic spine {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q14247}. Endoplasmic reticulum {ECO:0000269|PubMed:1922035}. Note=Colocalizes transiently with PTK2/FAK1 at focal adhesions (By similarity). Associated with membrane ruffles and lamellipodia. In normal cells, probably in association with the plasma membrane and possibly the endoplasmic reticulum (PubMed:1922035). p80/85 colocalizes with F-actin in peripheral extensions of normal cells and rosettes (podosomes) of src-transformed cells. p80/85 probably associates with components of the cytoskeleton. In response to neuronal activation by glutamate, redistributes from dendritic spines to the dendritic shaft (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q66HL2, ECO:0000269|PubMed:1922035}.
Interaction partners:
- Cofilin-2
- Actin, cytoplasmic 1
- Proto-oncogene tyrosine-protein kinase Src
- Lysozyme C
- Vinculin
- Actin-related protein 2
- Talin-1
- Talin 2.
- WH1 domain-containing protein.
- Scinderin
Sequence:
MTVLLLVVLQMWKATAGHSIAVSQDDGADDWETDPDFVNDVSEKEQRWGAKTVKGSGHQEHINIHQLRENVFQEHQTIKEKELETGPKASHGYGGKFGVEQDRMDKSAVGHEYQSKLSKHCSQVDSVKGFGGKFGVQTDRVDQSAVGFEYQGKTEKHASQKDYSSGFGGKYGVQADRVDKSAVGFDYQGKTEKHESQKDYSKGFGGKYGVDKDKVDKSAVGFEYQGKTEKHESQKDYVKGFGGKFGVQTDRQDKCALGWDHQEKVQLHESQKDYKSGFGGKFGVQTERQDPSAVGFDYKEKLAKHESQQDYSKGFGGKYGVQKDRMDKNAATFEDIEKPTSTYQKTKPVERVANKTSSIRANLENLAKEKEQEDRRKAEAERAQRMAREKQEQEEARRKLEEQAKAKKQTPPPSPTTQPAEPKTPSSPVYQDAVSYDAESAYKNSSTTYSAEHEPESGYKTTGSDYQEAVSQREAEYEPETVYEVAGAGDHYQAEENTYDEYENELGITAIALYDYQAAGDDEISFDPDDIITNIEMIDDGWWRGVCKGRYGLFPANYVELRQ
Protein: MIP05539p (Q8IN49)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Detonator, isoform E
Sequence:
MFPSSILGRSYLLFMLVLAVGVFAQHEWQARDAFDEIKRQFDKVNADNCPIQHHSDLFMPMDAVSHKPDIKEINVNPVFPNRTALLHLQNMALSRSFFWSYILQSRFIRPAINDTYDPGMMYYFLSTVADVSANPHINASAVYFSPNSSYSSSYRGFFNKTFPRFGPRTFRLDDFNDPIHLQKISTWNTFDVQDLGAHHPDSISKDYTHDLYKINEWYRAWLPDNVEGRHDTKITYQVEIRYANNTNETYTFHGPPGSEENPGPIKFTRPYFDCGRSNKWLVAAVVPIADIYPRHTQFRHIEYPKYTAVSVLEMDFERIDINQCPLGEGNKGPNHFADTARCKKETTECEPLQGWGFRRGGYQCRCKPGFRLPNVVRRPYLGEIVERASAEQYYNEYDCLKIGWIQKLPIQWDKASYHIRQKYLDRHPEYRNYTTGSRSLHAEHLNIDQALKYIHGVNYRTCKNFHPQDLILRGDVSFGAKEQFENEAKMAVRLANFISAFLQVSDPNEVYSGKRVADKPLTEDQMIGETLAIVLGDSKVWSATMLWERNKFTNRTYFAPYAYKTELNTRKFKVEDLARLNKTHELYTEKKYFKFLKQRWNTNFDDLETFYMKIKIRHNETGEYQQKYEHYPNSYRAANIKHGYWTQPQFDCDGYVKKWLVTYAVPFFGWDSLKVKLEFKGVVAVSMDMLQLDINQCPDWYYEPNAFKNTHKCDEQSSYCVPIMGRGYETGGYKCECLQGYEYPFEDLITYYDGQLVEAEYQNIVADVETRYDMFKCRLAGASGLQSALGLVVALIGLTLTLLYRFS
Protein: Sine oculis-binding protein homolog (Jackson circler protein 1) (Q0P5V2)
Organism: Mus musculus (Mouse)
Function: Implicated in development of the cochlea.
Interaction partners:
Sequence:
MAEMEKEGRPPENKRSRKPAHPVKREINEEMKNFAENTMNELLGWYGYDKVELKDGEDIEFRSYTTDGESRQHISVLKENSLPKPKLPEDSVISSYNISTGYSGLATGNGLSDSPAGSKDHGNVPIIVPLIPPPFIKPPAEDDVSNVQIMCAWCQKVGIKRYSLSMGSEVKSFCSEKCFAACRRAYFKRNKARDEDGRAETFPQQHYAKETPRLAFKNNCELLVCDWCKHIRHTKEYLDFGDGERRLQFCSAKCLNQYKMDIFYKETQANLPAGLCSTLHPHMESKAEGTGVQLLTPDSWNIPLTDARRKAPSPVTAAGQSQGPGPSSSTTVSPSDTANCSVTKIPTPVPKSLPISETPSIPPVSVQPPASIGPPLGVPPRSPPMVMTNRGPVPLPIFMEQQIIQQIRPPFIRGPPHHASNPNSPLSNPMLPGIGAPPGGPRNLGPTSSPMHRPMLSPHIHPPSTPTMPGNPPGLLPPPPPGAPLPSLPFPPVSMMPNGPMPVPQMMNFGLPSLAPLVPPPTLLVPYPVIVPLPVPIPIPIPIPHVNDSKPPNGFSSNGESFVPSAPGDSSAAGGKAGGRSLSPRDSKQGSSKSADSPPGSSGQALSLAPAERGRGEVVDLTRRAGSPAGAGGQPGFAGVLHGPQDGVIDLTVGHRARLHNVIHRALHAHVKAEREPGAAERRTCGGCRDGHCSPPAAGDPGPGAPAGPEAAAACNVIVNGTRSAPAEAKGAEPPPEQPPPPAPPKKLLSSEEPVVNELESVKENNCASNCHLDGEATKKLMGEEALAGGDKSDPNLNNPADEDHAYALRMLPKTGCVIQPVPKPAEKAAMTPCVISSPMLSAGPEDLEPPLKRRCLRIRNQNK
Protein: Importin subunit alpha-5 (Importin alpha-S1) (Karyopherin subunit alpha-1) (Nucleoprotein interactor 1) (NPI-1) (RAG cohort protein 2) (SRP1-beta) (Q60960)
Organism: Mus musculus (Mouse)
Function: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:8631802}. Nucleus {ECO:0000305|PubMed:8631802}.
Interaction partners:
- Importin subunit beta-1
- Signal transducer and activator of transcription 1
- Exportin-2
- Importin subunit alpha-3
- Importin subunit alpha-4
- Importin subunit alpha-7
- Importin subunit alpha-1
- Transcription factor p65
- Nuclear factor NF-kappa-B p105 subunit
- GTP-binding nuclear protein Ran
Sequence:
MSTPGKENFRLKSYKNKSLNPDEMRRRREEEGLQLRKQKREEQLFKRRNVATAEEETEEEVMSDGGFHEAQINNMEMAPGGVITSDMTDMIFSNSPEQQLSATQKFRKLLSKEPNPPIDEVINTPGVVARFVEFLKRKENCTLQFESAWVLTNIASGNSLQTRNVIQAGAVPIFIELLSSEFEDVQEQAVWALGNIAGDSTMCRDYVLNCNILPPLLQLFSKQNRLTMTRNAVWALSNLCRGKSPPPEFAKVSPCLNVLSWLLFVSDTDVLADACWALSYLSDGPNDKIQAVIDAGVCRRLVELLMHNDYKVVSPALRAVGNIVTGDDIQTQVILNCSALQSLLHLLSSPKESIKKEACWTISNITAGNRAQIQTVIDANMFPALISILQTAEFRTRKEAAWAITNATSGGSAEQIKYLVELGCIKPLCDLLTVMDAKIVQVALNGLENILRLGEQEAKRNGSGINPYCALIEEAYGLDKIEFLQSHENQEIYQKAFDLIEHYFGTEDEDSSIAPQVDLSQQQYIFQQCEAPMEGFQL
Protein: Fibroblast growth factor 18 (FGF-18) (zFGF5) (O76093)
Organism: Homo sapiens (Human)
Function: Plays an important role in the regulation of cell proliferation, cell differentiation and cell migration. Required for normal ossification and bone development. Stimulates hepatic and intestinal proliferation.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Fibroblast growth factor receptor 2
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor 3
- Fibroblast growth factor receptor 4
- Klotho
- Pro-epidermal growth factor
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Fibroblast growth factor-binding protein 1
- Decorin
- Epidermal growth factor receptor
Sequence:
MYSAPSACTCLCLHFLLLCFQVQVLVAEENVDFRIHVENQTRARDDVSRKQLRLYQLYSRTSGKHIQVLGRRISARGEDGDKYAQLLVETDTFGSQVRIKGKETEFYLCMNRKGKLVGKPDGTSKECVFIEKVLENNYTALMSAKYSGWYVGFTKKGRPRKGPKTRENQQDVHFMKRYPKGQPELQKPFKYTTVTKRSRRIRPTHPA
Protein: Guanylate-cyclase regulatory protein (Q9EQ72)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSTEPLSAEASLSSDSQRLGKDPTPSMLGLCGSLASIPSCKSLASFKSNECLVSDSLRAAQHSAPAEEQQGQCQPHLPGAMDNCHLLSPPPQATLQEQYPASLRSQLASGL
Protein: Magnesium dechelatase SGRL, chloroplastic (EC 4.99.1.10) (Protein STAY-GREEN LIKE) (Q94AQ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Magnesium chelatase involved in chlorophyll a degradation in the chlorophyll-protein complexes of photosystem I (PSI) and photosystem II (PSII). Contributes to the degradation of PSI and PSII in the thylakoid membranes. Recombinant SGRL possesses high dechelating activity against chlorophyllide a, very low activity against chlorophyll a, and no activity against chlorophyll b. Contributes to abiotic stress-induced chlorophyll degradation and leaf yellowing during vegetative plant growth.
Subcellular location: Plastid, chloroplast thylakoid {ECO:0000269|PubMed:25261252}.
Interaction partners:
- 7-hydroxymethyl chlorophyll a reductase, chloroplastic
- Chlorophyll synthase, chloroplastic
- Chlorophyllide a oxygenase, chloroplastic
- Chlorophyllase-1
- Chlorophyllase-2
- Divinyl chlorophyllide a 8-vinyl-reductase, chloroplastic
- Protochlorophyllide reductase C, chloroplastic
- Protochlorophyllide reductase A, chloroplastic
- Chlorophyll
- Protochlorophyllide reductase B, chloroplastic
Sequence:
MACYIVPYYHHPVLSHPNREIFSHRHHHHHRFCNNLLNRRISVPRSSAISDGGVSYNTLVSEAVRLLVPQANFDSSKLKVEFLGELLENKSNGGIITPRTYILSHCDFTANLTLTISNVINLDQLEGWYKKDDVVAEWKKVNDELRLHIHCCVSGMSLLQDVAAELRYHIFSKELPLVLKAVVHGDSVMFRENPELMDAYVWVYFHSSTPKYNRIECWGPLKDAAKGKQQGNHQGFLSSTTSRKLIRHKSIFHTLFTFLL