wanglab/gogpt-training-data huggingface dataset:
Protein: Protein ZNF365 (DISC1-binding zinc-finger protein) (Protein su48) (Q70YC5)
Organism: Homo sapiens (Human)
Function: Involved in the regulation of neurogenesis. Negatively regulates neurite outgrowth. Involved in the morphogenesis of basket cells in the somatosensory cortex during embryogenesis. Involved in the positive regulation of oligodendrocyte differentiation during postnatal growth. Involved in dendritic arborization, morphogenesis of spine density dendrite, and establishment of postsynaptic dendrite density in cortical pyramidal neurons (By similarity). Involved in homologous recombination (HR) repair pathway. Required for proper resolution of DNA double-strand breaks (DSBs) by HR. Is required for recovery of stalled replication forks, and directly contributes to genomic stability. Interacts with PARP1 and mediates MRE11-dependent DNA end resection during replication fork recovery. Contributes to genomic stability by preventing telomere dysfunction.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:16617106}. Note=localizes to the centrosome at all stages of the cell cycle. {ECO:0000269|PubMed:16617106}.
Interaction partners:
- Disrupted in schizophrenia 1 protein
- Nuclear distribution protein nudE homolog 1
- Fasciculation and elongation protein zeta-1
Sequence:
MQQKAFEESRYPWQESFENVAVCLPLRCPRCGDHTRFRSLSSLRAHLEFSHSYEERTLLTKCSLFPSLKDTDLVTSSELLKPGKLQSSGNVVKQKPSYVNLYSISHEHSKDRKPFEVVAERPVSYVQTYTAMDLHADSLDGTRSGPGLPTSDTKASFEAHVREKFNRMVEAVDRTIEKRIDKLTKELAQKTAELLEVRAAFVQLTQKKQEVQRRERALNRQVDVAVEMIAVLRQRLTESEEELLRKEEEVVTFNHFLEAAAEKEVQGKARLQDFIENLLQRVELAEKQLEYYQSQQASGFVRDLSGHVLTDISSNRKPKCLSRGHPHSVCNHPDLKAHFHPKGRNHLKKAKDDRASMQPAKAIHEQAESSRDLCRPPKKGELLGFGRKGNIRPKMAKKKPTAIVNII
Protein: Large ribosomal subunit protein uL11 (50S ribosomal protein L11) (P9WHE5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
Interaction partners:
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein bL25
- Uncharacterized protein Rv0500B
- Large ribosomal subunit protein uL1
- Small ribosomal subunit protein bS6
- Large ribosomal subunit protein uL3
- Transcription termination/antitermination protein NusG
- Large ribosomal subunit protein uL22
Sequence:
MAPKKKVAGLIKLQIVAGQANPAPPVGPALGQHGVNIMEFCKAYNAATENQRGNVIPVEITVYEDRSFTFTLKTPPAAKLLLKAAGVAKGSAEPHKTKVAKVTWDQVREIAETKKTDLNANDVDAAAKIIAGTARSMGITVE
Protein: Small ribosomal subunit protein eS4 (40S ribosomal protein S4) (P46299)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Cytoplasm.
Interaction partners:
- 40S ribosomal protein S30
- S12
- S12
- 40S ribosomal protein S28-like
- 40S ribosomal protein S28
- 40S ribosomal protein S25
- 40S ribosomal protein S25
- 40S ribosomal protein S25
- 40S ribosomal protein S25
- 40S ribosomal protein S29-like
Sequence:
MARGLKKHLKRLNAPRHWMLDKLGGAFAPKPSSGPHKSRECLPLILILRNRLKYALTYREVIAILMQRHVMVDGKVRTDKTYPAGFMDVVSIPKTNEDFRLLYDTKGRFCLHAITGDETKFKLCKVRSVQFGQKGIPYLNTYDGRTIRYPDPLIKANDTIKLDLESNKIVDFIKFDVGNVVMVTGGRNRGRVGVIKNREKHKGSFETIHVQDAAGHEFATRLGNVFTIGKGTKPWVSLPKRKGIKLSIIEEARKRLAAQNAA
Protein: Endoplasmic reticulum lectin 1 (ER lectin) (Q8MQY6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
Sequence:
MGKSYVIIARIALLLNLIIAAVSHEAKDFDDSILYKIDFEVPDLDVQPSLGNQLRTFYTPDKEKYDCLIPTLEHQKEEEKSDKPELSPITLLQPIFSALTCTYRIEAYWSYEICHGHHVRQYHEEREGKNVKFQEYYLGKWTDEKMEILTKAWQADIKAGVKPKYKSLKIDNTRYPYFEMEYSDGTMCDIINAPRTTMVRYVCYPHGKNDIYSFKETSSCNYEAIILSSALCPIRALHAEETKELSIQCFNSESKPHRPLSMLRSELKEWVESEADLLVFKEKATENLWPKTDGDLVTLNYGGDMEKVLLEHFRNGDLKVDGDFQQLLLSIAASETGPTPITDLTPLKDFISGKNCLTGGNGWWKYEFCYGRHVRQFHKDKTSEVELFLGYFSEEAHRAWSNANPDKGARRSGFTTSI
Protein: Pescadillo homolog (Nucleolar protein 7 homolog) (O60164)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the NOP7 complex, which is required for maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S ribosome.
Subcellular location: Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03028}. Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03028, ECO:0000269|PubMed:10759889}.
Interaction partners:
- GTPase grn1
- Ribosome biogenesis protein erb1
- Probable nucleolar GTP-binding protein 1
- Ribosome biogenesis protein ytm1
- Uncharacterized NOC2 family protein C1142.04
- Ribosome biogenesis protein nsa2
- Probable rRNA-processing protein ebp2
- Ribosome biogenesis protein nsa1
- Ribosome assembly factor mrt4
- ATP-dependent RNA helicase has1
Sequence:
MARVKQKGKAGAARIYITRNQALKKLQLTLADFRRICILKGVYPREPKNKKKANKGSTAPVTFYYTKDIQYLLHEPIVQKFREYKVFARKLSKALGKGELETAKRLEARKPTYSLDHIIKERYPTFHDALKDIDDALSMLFLFSTMPVTDKIGAATVANCERLCAEFQHYVIRSNSLRKAFLSIKGIYYQAEIFGEQITWIVPYKFAQSVPTDVDFRIMHTFLEFYQALMGFVNFKLYNTLGLRYPPKIDVAKSESAAGLAAYELEESSSLPAIVHGNNKNARKNIATLKSKIRDIVNSDANVVEQSEKTTEDADEEPETEENLDEFKPADGADNEDSKSLVSHISSSNTSLFSNFTFFLSREVPRFSLEFVIRAFGGKVGWDPILGSGSPFSESDPVITHHICDRPHISQKYEGRIYIQPQWVYDSINKGILERTDLYACGATLPPHLSPFVKVGENDYDPEAELSAEENDDVSEALDDNISGEAVPISKKNDEPENVEQIDDAEEEDLEHQRELEAEAGGVAYSEYVKQNSKSAKKTKKRQRDTLTAEEKEEKEAKELSKMMMSNKQRKLYSKLKNENSKNENYNNALRNRKRDIEKRKKLKVEN
Protein: Uncharacterized protein (Q389D5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSVSPKRSLQASHSSTFVGKTVPSYVLSPVIEQHHLLWQWRTVLWRKRLHAVPFLLHWAPGVPAKQPFLHHTTAELILTSGQEVASAPAAANYRNSPHRFGELIVPSPAGGLHATISGQAGEVHPLTRWVDDLFDFPQQSAIPGEAVVNHEESISSTDSWRHVPSIYHNVVGCGLAELILAVDRLAALLARRHITLANACWAVLADSKADLKPFLRYSALDIEREVLVMAKAHEMINVSLGDAMRRPLLTIEDYPSMAGW
Protein: RE47242p (Q9VGR0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Cell division cycle 5, isoform A
Sequence:
MASKKYSDVNLYDLLGISLESDQNEIRKAYRKKALECHPDKNPDNPKAVERFHELSKALEILTDESARAAYDKVLKAKKAAELRSRQLDGKRQKLKLELEERERAALHKLAKSQPYSTVAKSDEEVLHEQIERLRREGSRLLEEEQRAMQEQFRRNHAEQQKLQQQPVQFDSAQHRIKMKWKAEPGQDYTQQELLKYLKKYGDVVALVVNSKRRGRAMVELATREACDMVLAYEKGDPAKPLHFEWVTPPAADKQTTKSATTGCSASSTDYEDLVMRKLRQAEERKRLIEQMMKDEEGE
Protein: Programmed cell death protein 4 (Neoplastic transformation inhibitor protein) (Nuclear antigen H731-like) (Protein 197/15a) (Q53EL6)
Organism: Homo sapiens (Human)
Function: Inhibits translation initiation and cap-dependent translation. May excert its function by hindering the interaction between EIF4A1 and EIF4G. Inhibits the helicase activity of EIF4A. Modulates the activation of JUN kinase. Down-regulates the expression of MAP4K1, thus inhibiting events important in driving invasion, namely, MAPK85 activation and consequent JUN-dependent transcription. May play a role in apoptosis. Tumor suppressor. Inhibits tumor promoter-induced neoplastic transformation. Binds RNA (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q61823}. Cytoplasm {ECO:0000250|UniProtKB:Q61823}. Note=Shuttles between the nucleus and cytoplasm (By similarity). Predominantly nuclear under normal growth conditions, and when phosphorylated at Ser-457 (PubMed:16357133). {ECO:0000269|PubMed:16357133}.
Interaction partners:
- Eukaryotic initiation factor 4A-I
- Eukaryotic initiation factor 4A-II
- Eukaryotic translation initiation factor 4 gamma 1
- F-box/WD repeat-containing protein 1A
- Ribonuclease 3
- Ribosomal protein S6 kinase beta-1
- Protein argonaute-2
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Eukaryotic translation initiation factor 4E
- Small ribosomal subunit protein uS15
Sequence:
MDVENEQILNVNPADPDNLSDSLFSGDEENAGTEEIKNEINGNWISASSINEARINAKAKRRLRKNSSRDSGRGDSVSDSGSDALRSGLTVPTSPKGRLLDRRSRSGKGRGLPKKGGAGGKGVWGTPGQVYDVEEVDVKDPNYDDDQENCVYETVVLPLDERAFEKTLTPIIQEYFEHGDTNEVAEMLRDLNLGEMKSGVPVLAVSLALEGKASHREMTSKLLSDLCGTVMSTTDVEKSFDKLLKDLPELALDTPRAPQLVGQFIARAVGDGILCNTYIDSYKGTVDCVQARAALDKATVLLSMSKGGKRKDSVWGSGGGQQSVNHLVKEIDMLLKEYLLSGDISEAEHCLKELEVPHFHHELVYEAIIMVLESTGESTFKMILDLLKSLWKSSTITVDQMKRGYERIYNEIPDINLDVPHSYSVLERFVEECFQAGIISKQLRDLCPSRGRKRFVSEGDGGRLKPESY
Protein: Tlr5b protein (B3DIN1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MGYTFILILFGLCLNTEVVKSTSVCSVIGYNAICINRGLHQVPELPAHVNYVDLSLNSIAELNETSFSRLQDLQFLKVEQQTPGLVIRNNTFRGLSSLIILKLDYNQFLQLETGAFNGLANLELLTLTQCNLDGAVLSGNFFKPLTSLEMLVLRDNNIQKIQPASFFLNMRRFHVLDLTFNKVKSICEEDLLNFQGKHFTLLRLSSITLQDMNEYWLGWEKCGNPFRNSSITTLDLSGNGFKESMAKRFFDAIAGTKIQSLILSNSYNMGSSFGHTNFKDPDNFTFKGLEASGVKTCDLSKSKIFALLKSVFSHFTDLEQLTLAQNEINKIDDDAFWGLTHLLKLNLSQNFLGSIDSRMFENLDKLEVLDLSYNHIRALGDQSFLGLPNLRNLNLTGNAVESVHTFAALPNLNKLYLGKNRISSVSSLPNIAHNLSTLDLEFNKLHALSDLYTILREFPQIENIFLQGNTFSSCYNQKQIVLSDKLQLLHLGLSSMQLIWSEEKCLNVFADLHQLQQLSLTANGLQSLPKDIFKDLTSLFFLDLSFNSLKYLPTDVFPKSLQILNLDYNSIYSVDPNLFSTLGYLSLMNNDFRCDCDLKDFQTWLNQTNVTFVHSIEDVTCASPEDQYMVPVVRSSIQCEDEEEERRTEKLRLVLFISCTVLIILFTASTIVYISRRGVIFKMYKKLIGELVDEKREEPDPDRFLYDVYLCFSSKDMKWVERALLKRLDSQFSEHNTLRCCFEERDFIPGEDHLTNMRSAIQNSRKTICVVSEHFLKDGWCLETFTLAQKRMQAELEDILVVLVVGNIPQYRLLKYKQVRSFIENRSYLVWPDDGQDLEWFYDQLLHKIRKDIKINQTTKETKREEANFNTNTAV
Protein: Pyridoxine/pyridoxal/pyridoxamine kinase (PN/PL/PM kinase) (EC 2.7.1.35) (B6-vitamer kinase) (Pyridoxal kinase 1) (PL kinase 1) (P40191)
Organism: Escherichia coli (strain K12)
Function: B6-vitamer kinase involved in the salvage pathway of pyridoxal 5'-phosphate (PLP). Catalyzes the phosphorylation of pyridoxine (PN), pyridoxal (PL), and pyridoxamine (PM), forming their respective 5'-phosphorylated esters, i.e. PNP, PLP and PMP.
Interaction partners:
- Pyridoxine/pyridoxamine 5'-phosphate oxidase
- Pyridoxine 4-dehydrogenase
- Pyridoxine 5'-phosphate synthase
- Pyridoxal kinase PdxY
- Pyridoxal phosphate homeostasis protein
- Erythronate-4-phosphate dehydrogenase
Sequence:
MSSLLLFNDKSRALQADIVAVQSQVVYGSVGNSIAVPAIKQNGLNVFAVPTVLLSNTPHYDTFYGGAIPDEWFSGYLRALQERDALRQLRAVTTGYMGTASQIKILAEWLTALRKDHPDLLIMVDPVIGDIDSGIYVKPDLPEAYRQYLLPLAQGITPNIFELEILTGKNCRDLDSAIAAAKSLLSDTLKWVVVTSASGNEENQEMQVVVVTADSVNVISHSRVKTDLKGTGDLFCAQLISGLLKGKALTDAVHRAGLRVLEVMRYTQQHESDELILPPLAEA
Protein: Crossover junction endodeoxyribonuclease RuvC (EC 3.1.21.10) (Holliday junction endonuclease RuvC) (Holliday junction nuclease RuvC) (Holliday junction resolvase RuvC) (P0A814)
Organism: Escherichia coli (strain K12)
Function: The RuvA-RuvB-RuvC complex processes Holliday junctions during genetic recombination and DNA repair. Endonuclease that resolves Holliday junction (HJ) intermediates. Cleaves cruciform DNA by making single-stranded nicks across the junction at symmetrical positions within the homologous arms, leaving a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C>G/A)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange, although there is some flexibility in the position cleaved. The cleavage reactions can be uncoupled; incision requires the presence of two consensus cleavage sequences, although they do not have to be identical. The presence of a 5'-phosphate in a half-cut site accelerates cleavage of the second site, ensuring the second cleavage occurs within the lifetime of a single RuvC-HJ complex. Binds to cruciform DNA in a sequence non-specific manner.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00034, ECO:0000269|PubMed:21219465}. Note=In 15% of cell localizes to discrete nucleoid foci (probable DNA damage sites) upon treatment with mitomycin C (MMC) for 2 hours.
Interaction partners:
- Holliday junction branch migration complex subunit RuvB
- Holliday junction branch migration complex subunit RuvA
- UvrABC system protein A
- UvrABC system protein B
- UvrABC system protein C
- Probable transcriptional regulatory protein YebC
- Single-stranded-DNA-specific exonuclease RecJ
- Protein RecA
- DNA replication and repair protein RecF
- ATP-dependent DNA helicase RecG
Sequence:
MAIILGIDPGSRVTGYGVIRQVGRQLSYLGSGCIRTKVDDLPSRLKLIYAGVTEIITQFQPDYFAIEQVFMAKNADSALKLGQARGVAIVAAVNQELPVFEYAARQVKQTVVGIGSAEKSQVQHMVRTLLKLPANPQADAADALAIAITHCHVSQNAMQMSESRLNLARGRLR
Protein: ADP-ribosylation factor-like protein 6-interacting protein 4 (ARL-6-interacting protein 4) (Aip-4) (Splicing factor SRrp37) (Q9JM93)
Organism: Mus musculus (Mouse)
Function: Involved in modulating alternative pre-mRNA splicing with either 5' distal site activation or preferential use of 3' proximal site.
Subcellular location: Nucleus, nucleolus {ECO:0000250}. Nucleus speckle {ECO:0000250}.
Interaction partners:
- 2-oxoglutarate and iron-dependent oxygenase domain-containing protein 2
Sequence:
MAHVGSRKRSRSRSRSRSGRRGSEKRSKRSSKDASRNCSASRSQGHKAGSASGVEERSKHKAQRTSRSSSTSSSSSSSSSASSSSSSDGRKKRAKHKEKKRKKKKKKRKKKLKKRVKEKAVAVHQAEALPGPSLDQWHRSAGEDNDGPVLTDEQKSRIQAMKPMTKEEWDARQSVIRKVVDPETGRTRLIKGDGEVLEEIVTKERHREINKQATRGDGLAFQMRTGLLP
Protein: Cone-rod homeobox protein (Q9XSK0)
Organism: Bos taurus (Bovine)
Function: Transcription factor that binds and transactivates the sequence 5'-TAATC[CA]-3' which is found upstream of several photoreceptor-specific genes, including the opsin genes. Acts synergistically with other transcription factors, such as NRL, RORB and RAX, to regulate photoreceptor cell-specific gene transcription. Essential for the maintenance of mammalian photoreceptors (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Photoreceptor-specific nuclear receptor
- Recoverin
- Rhodopsin
- Neural retina-specific leucine zipper protein
- Aryl-hydrocarbon-interacting protein-like 1
- Guanine nucleotide-binding protein G
- Arrestin-C
- SIX homeobox 3
- Guanine nucleotide-binding protein G
- Tubby-like protein
Sequence:
MMAYMNPGPHYSVNALALSGPSVDLMHPAVSYPSAPRKQRRERTTFTRSQLEELEALFAKTQYPDVYAREEVALKINLPESRVQVWFKNRRAKCRQQRQQQKQQQQPPGAQAKARPAKRKAGTSPRSSTDVCPDPLGISDSYSPPLPGPSGSPTTAVATVSIWSPASESPLPEAQRAGLVASGPSLTSAPYAMTYAPASAFCSSPSAYGSPSSYFSGLDPYLSPMVPPLGGPALSPLSGPSVGPSLTQSPTSLSGQSYGTYSPVDSLEFKDPTGTWKFTYNPMDPLDYKDQSAWKFQIL
Protein: Threonylcarbamoyl-AMP synthase (TC-AMP synthase) (EC 2.7.7.87) (L-threonylcarbamoyladenylate synthase) (t(6)A37 threonylcarbamoyladenosine biosynthesis protein sua5) (tRNA threonylcarbamoyladenosine biosynthesis protein sua5) (O94530)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Likely catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate. Required for normal translation, by ensuring translation fidelity at the level of codon recognition, appropriate translation initiation selection and maintenance of reading frame. Also involved in telomere replication. Binds to single-stranded telomeric (ssTG) DNA and positively regulates telomere length (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Chromosome, telomere {ECO:0000250}.
Interaction partners:
- tRNA N6-adenosine threonylcarbamoyltransferase
- EKC/KEOPS complex subunit SPAP27G11.07c
- EKC/KEOPS complex subunit cgi121
- EKC/KEOPS complex subunit SPAC4H3.13
- Uncharacterized protein C14G10.01
- Ribosome quality control complex subunit 2
- tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial
- tRNA threonylcarbamoyladenosine dehydratase
- EKC/KEOPS complex subunit gon7
Sequence:
METKIQTVDTRLISFEKPSNDSEHPFEHTRVSIPPSETRSALENAANILRNTDYPVAFPTETVYGLGADARRTEAVLSIYKAKNRPADNPLIVHVASLDQLRRLLLSAYPKAKSEVKNQAHDSEEIIPKVYLPLIKKFWPGPLSILLPVVDEANPPVSPIVTAGQKTFAVRMPQHPVALALISISDSPLAAPSANASTRPSPTLAKHVYNDLQGKIPLILDGGACGVGVESTVVNGLCDPPVILRPGGISLEEIQSSGGAWERTKVFVAKKSDMETDFIPQTPGMKYRHYSPTAKVLLFVNYTESDAYGVFEKYLSEQGITKEKQKIGVLCSKRWNEESFPSHCPFVFLHMGRDGHEITKNLFAQLRDLDLQGVDFVLVEGVSEENEGLAIMNRLGKAASVVFEGPSH
Protein: E3 ubiquitin-protein ligase MYLIP (EC 2.3.2.27) (Inducible degrader of the LDL-receptor) (Idol) (Myosin regulatory light chain interacting protein) (MIR) (RING-type E3 ubiquitin transferase MYLIP) (Q8WY64)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC), LDLR, VLDLR and LRP8. Activity depends on E2 enzymes of the UBE2D family. Proteasomal degradation of MRLC leads to inhibit neurite outgrowth in presence of NGF by counteracting the stabilization of MRLC by saposin-like protein (CNPY2/MSAP) and reducing CNPY2-stimulated neurite outgrowth. Acts as a sterol-dependent inhibitor of cellular cholesterol uptake by mediating ubiquitination and subsequent degradation of LDLR.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:14550572}. Cell membrane {ECO:0000269|PubMed:14550572}; Peripheral membrane protein {ECO:0000269|PubMed:14550572}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 D1
- Low-density lipoprotein receptor
- Protein canopy homolog 2
- Solute carrier family 53 member 1
- Phospholipid-transporting ATPase ABCA1
- Oxysterols receptor LXR-alpha
- Myosin regulatory light chain 12B
- Very low-density lipoprotein receptor
- Myosin regulatory light chain 11
- ATP-binding cassette sub-family G member 1
Sequence:
MLCYVTRPDAVLMEVEVEAKANGEDCLNQVCRRLGIIEVDYFGLQFTGSKGESLWLNLRNRISQQMDGLAPYRLKLRVKFFVEPHLILQEQTRHIFFLHIKEALLAGHLLCSPEQAVELSALLAQTKFGDYNQNTAKYNYEELCAKELSSATLNSIVAKHKELEGTSQASAEYQVLQIVSAMENYGIEWHSVRDSEGQKLLIGVGPEGISICKDDFSPINRIAYPVVQMATQSGKNVYLTVTKESGNSIVLLFKMISTRAASGLYRAITETHAFYRCDTVTSAVMMQYSRDLKGHLASLFLNENINLGKKYVFDIKRTSKEVYDHARRALYNAGVVDLVSRNNQSPSHSPLKSSESSMNCSSCEGLSCQQTRVLQEKLRKLKEAMLCMVCCEEEINSTFCPCGHTVCCESCAAQLQSCPVCRSRVEHVQHVYLPTHTSLLNLTVI
Protein: dynamin GTPase (EC 3.6.5.5) (F1S593)
Organism: Sus scrofa (Pig)
Interaction partners:
Sequence:
MGNRGMEELIPLVNKLQDAFSSIGQSCHLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFSKTEYAEFLHCKSKKFTDFEEVRQEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIKDMILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRAALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLPALRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSGDQVDTLELSGGARINRIFHERFPFELVKMEFDEKDLRREISYAIKNIHGVRTGLFTPDMAFEAIVKKQIVKLKEPSLKCVDLVVSELATVIKKCAEKLSSYPRLREETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFANAQQRSTQLNKKRAIPNQVVIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKDLRQIELACDSQEDVDSWKASFLRAGVYPEKDQAENEDGAQENTFSMDPQLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESADQAQRRDDMLRMYHALKEALNIIGDISTSTVSTPVPPPVDDTWLQSTSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPVPVGAAASFSAPPIPSRPGPHPGVFANNDPFSAPPQIPSRPARIPPGIPPGVPSRRPPAAPSRPTIIRPAEPSLLD
Protein: Transmembrane protein 240 (B2RWJ3)
Organism: Mus musculus (Mouse)
Subcellular location: Synapse {ECO:0000269|PubMed:22645316}. Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MSMSANTMIFMILGASIVMAIACLMDMNALLDRFHNYILPHLRGEDRVCHCNCGRHHIHYVIPYDGDQSVVDASENYFVTDNVTKQEIDLMLGLLLGFCISWFLVWMDGVLHCAVRAWRAGRRYDGSWTWLPKLCSLRELGRRPHRPFEEPTGNMVHVKQKLYHNGHPSPRHL
Protein: Spastin (EC 5.6.1.1) (Q54KQ7)
Organism: Dictyostelium discoideum (Social amoeba)
Function: ATP-dependent microtubule severing protein. Microtubule severing may promote reorganization of cellular microtubule arrays and the release of microtubules from the microtubule organizing center following nucleation.
Subcellular location: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Note=Forms an intramembrane hairpin-like structure in the membrane. {ECO:0000255|HAMAP-Rule:MF_03021}.
Interaction partners:
- IST1-like protein
- UBX domain-containing protein 7 homolog
- Tubulin beta chain
- HECT-type E3 ubiquitin transferase
- Charged multivesicular body protein 3
Sequence:
MLFDLINSFLKNGINNSNNNNNNNNNKNNFYNSLEDDDYLLNNQTTKVSLYLYFFIFAFMFLVVDLIMLYYKHRENIESRETDLSLKLNKMLIDFENDNKIKSSPTTSTTTTTITPTTTSSSQLRQPSTPKTTTKTINSPPSTPKSPPPLPSLESKLLYKDDIKQQLSLNEAKSQIDSAKQLDESLKYNSCIKLYIDGIEKLMALFSSYNSKEYRDYIDFYLKRAEYLKNELKKGTNLKSITNFNNFSKEYQINYNNKILEQQQQQQQQSSSTYRNSLNLSSSKSNSTINNRHSISSLSSLNSTTATTTTPSNTSTITSPGNKYGLQKSLSSTTLSLKKSSNSTNFQQPSPPSMVIPDIKGIDKSMVTLIMNEIMDRKNPVKWDDVVGLDKVKQSLMESVILPNLRPDVFTGLRAPPKGLLLFGPPGNGKTMIAKAVAYESKVTFFSISSSSLTSKYVGDGEKLVRALFAVATHFQPSIIFIDEIDSLLTERSSNESEASRRLKTEILVQFDGARTNGDERVLVMGATNRPEDLDDAALRRLVKRIYVGLPELETRLQIIQHLLVGQRHSLTKQQINSLAEVTQGYSGFDLAALCKDAAYEPIRRLGIGIKDLELNEISLISFKDFANSLKQIRPSVTSQSLKSFEKWNQKFGTI
Protein: 5-hydroxytryptamine receptor 3D (5-HT3-D) (5-HT3D) (Serotonin receptor 3D) (Q70Z44)
Organism: Homo sapiens (Human)
Function: This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor is a ligand-gated ion channel, which when activated causes fast, depolarizing responses. It is a cation-specific, but otherwise relatively nonselective, ion channel.
Subcellular location: Postsynaptic cell membrane {ECO:0000305|PubMed:17392525}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:17392525}; Multi-pass membrane protein {ECO:0000255}. Note=Presumably retained within the endoplasmic reticulum unless complexed with HTR3A. {ECO:0000269|PubMed:17392525}.
Interaction partners:
- 5-hydroxytryptamine receptor 3C
- 5-hydroxytryptamine receptor 3A
- 5-hydroxytryptamine receptor 3B
- 5-hydroxytryptamine receptor 3E
Sequence:
MQKHSPGPPALALLSQSLLTTGNGDTLIINCPGFGQHRVDPAAFQAVFDRKAIGPVTNYSVATHVNISFTLSAIWNCYSRIHTFNCHHARPWHNQFVQWNPDECGGIKKSGMATENLWLSDVFIEESVDQTPAGLMASMSIVKATSNTISQCGWSASANWTPSISPSMDRARAWRRMSRSFQIHHRTSFRTRREWVLLGIQKRTIKVTVATNQYEQAIFHVAIRRRCRPSPYVVNFLVPSGILIAIDALSFYLPLESGNCAPFKMTVLLGYSVFLLMMNDLLPATSTSSHASLVAPLALMQTPLPAGVYFALCLSLMVGSLLETIFITHLLHVATTQPLPLPRWLHSLLLHCTGQGRCCPTAPQKGNKGPGLTPTHLPGVKEPEVSAGQMPGPGEAELTGGSEWTRAQREHEAQKQHSVELWVQFSHAMDALLFRLYLLFMASSIITVICLWNT
Protein: Probable choline kinase 1 (AtCK1) (EC 2.7.1.32) (Q9M9H6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in phospholipid biosynthesis. Catalyzes the first step in phosphatidylcholine biosynthesis (By similarity).
Interaction partners:
- Ethanolamine-phosphate cytidylyltransferase
- Choline-phosphate cytidylyltransferase 2
- Choline-phosphate cytidylyltransferase 1
- Phosphoethanolamine N-methyltransferase 2
- Phosphoethanolamine N-methyltransferase 3
- Phosphoethanolamine N-methyltransferase 1
- Glycerophosphodiester phosphodiesterase GDPD3
- Glycerophosphodiester phosphodiesterase GDPD2
- Glycerophosphodiester phosphodiesterase GDPD1, chloroplastic
- Regulatory-associated protein of TOR 2
Sequence:
MAIKTKTSLIPSCSSPEDLKRVLQTLGSSWGDVVEDLERLEVVPLKGAMTNEVYQINWPTLNGEDVHRKVLVRIYGDGVDLFFNRGDEIKTFECMSHHGYGPKLLGRFSDGRLEEFIHARTLSADDLRVAETSDFIAAKLREFHKLDMPGPKNVLLWERLRTWLKEAKNLASPIEMDKYRLEGLENEINLLEERLTRDDQEIGFCHNDLQYGNVMIDEVTNAITIIDYEYSSFNPIAYDIANHFCEMAANYHSDTPHVLDYTLYPGEGERRRFISTYLGSTGNATSDKEVERLLKDAESYTLANHIFWGLWGIISGHVNKIEFDYMEYARQRFEQYWLRKPLLLEG