wanglab/gogpt-training-data huggingface dataset:
Protein: tRNA-splicing endonuclease subunit Sen2 (EC 4.6.1.16) (tRNA-intron endonuclease Sen2) (HsSen2) (Q8NCE0)
Organism: Homo sapiens (Human)
Function: Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. Isoform 1 probably carries the active site for 5'-splice site cleavage. The tRNA splicing endonuclease is also involved in mRNA processing via its association with pre-mRNA 3'-end processing factors, establishing a link between pre-tRNA splicing and pre-mRNA 3'-end formation, suggesting that the endonuclease subunits function in multiple RNA-processing events. Isoform 2 is responsible for processing a yet unknown RNA substrate. The complex containing isoform 2 is not able to cleave pre-tRNAs properly, although it retains endonucleolytic activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:15109492}. Nucleus, nucleolus {ECO:0000269|PubMed:15109492}. Note=May be transiently localized in the nucleolus.
Interaction partners:
- tRNA-splicing endonuclease subunit Sen34
- tRNA-splicing endonuclease subunit Sen54
- tRNA-splicing endonuclease subunit Sen15
- Polyribonucleotide 5'-hydroxyl-kinase Clp1
- Cdc42-interacting protein 4
- Cleavage stimulation factor subunit 2
- Cleavage and polyadenylation specificity factor subunit 4
- Cleavage and polyadenylation specificity factor subunit 6
- Cleavage and polyadenylation specificity factor subunit 1
- Formin-binding protein 1
Sequence:
MAEAVFHAPKRKRRVYETYESPLPIPFGQDHGPLKEFKIFRAEMINNNVIVRNAEDIEQLYGKGYFGKGILSRSRPSFTISDPKLVAKWKDMKTNMPIITSKRYQHSVEWAAELMRRQGQDESTVRRILKDYTKPLEHPPVKRNEEAQVHDKLNSGMVSNMEGTAGGERPSVVNGDSGKSGGVGDPREPLGCLQEGSGCHPTTESFEKSVREDASPLPHVCCCKQDALILQRGLHHEDGSQHIGLLHPGDRGPDHEYVLVEEAECAMSEREAAPNEELVQRNRLICRRNPYRIFEYLQLSLEEAFFLVYALGCLSIYYEKEPLTIVKLWKAFTVVQPTFRTTYMAYHYFRSKGWVPKVGLKYGTDLLLYRKGPPFYHASYSVIIELVDDHFEGSLRRPLSWKSLAALSRVSVNVSKELMLCYLIKPSTMTDKEMESPECMKRIKVQEVILSRWVSSRERSDQDDL
Protein: Homeobox protein Hox-A5 (Homeobox protein Hox-1C) (P20719)
Organism: Homo sapiens (Human)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Also binds to its own promoter. Binds specifically to the motif 5'-CYYNATTA[TG]Y-3'.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein Hox-A6
- Homeobox protein Hox-A7
- Homeobox protein Hox-B7
- Homeobox protein Hox-D4
- Homeobox protein Hox-B5
- Homeobox protein Hox-B6
- Homeobox protein Hox-A10
- Homeobox protein Hox-C4
- Homeobox protein Hox-C6
- Homeobox protein Hox-B4
Sequence:
MSSYFVNSFCGRYPNGPDYQLHNYGDHSSVSEQFRDSASMHSGRYGYGYNGMDLSVGRSGSGHFGSGERARSYAASASAAPAEPRYSQPATSTHSPQPDPLPCSAVAPSPGSDSHHGGKNSLSNSSGASADAGSTHISSREGVGTASGAEEDAPASSEQASAQSEPSPAPPAQPQIYPWMRKLHISHDNIGGPEGKRARTAYTRYQTLELEKEFHFNRYLTRRRRIEIAHALCLSERQIKIWFQNRRMKWKKDNKLKSMSMAAAGGAFRP
Protein: Cell cycle and apoptosis regulator 2 (KIAA1967, isoform CRA_b) (G3V119)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLFVDDMAEPRETPEHPLKQIKFLLGRKEEEAVLVGGEWSPSLDGLDPQADPQVLVRTAIRCAQAQTGIDLSGCTKWWRFAEFQYLQPGPPRRLQTVVVYLPDVWTIMPTLEEWEALCQQKAAEAAPPTQEAQGETEPTEQAPDALEQAADTSRRNAETPEATTQQETDTDLPEAPPPPLEPAVIARPGCVNLSLHGIVEDRRPKERISFEVMVLAELFLEMLQRDFGYRVYKMLLSLPEKVVSPPEPEKEEAAKEEATKEEEAIKEEVVKEPKDEAQNEGPATESEAPLKEDGLLPKPLSSGGEEEEKPRGEASEDLCEMALDPELLLLRDDGEEEFAGAKLEDSEVRSVASNQSEMEFSSLQDMPKELDPSAVLPLDCLLAFVFFDANWCGYLHRRDLERILLTLGIRLSAEQAKQLVSRVVTQNICQYRSLQYSRQEGLDGGLPEEVLFGNLDLLPPPGKSTKPGAAPTEHKALVSHNGSLINVGSLLQRAEQQDSGRLYLENKIHTLELKLEESHNRFSATEVTNKTLAAEMQELRVRLAEAEETARTAERQKSQLQRLLQELRRRLTPLQLEIQRVVEKVRWGWTRRQHSSFP
Protein: Polyamine-transporting ATPase 13A2 (EC 7.6.2.-) (Q9CTG6)
Organism: Mus musculus (Mouse)
Function: ATPase which acts as a lysosomal polyamine exporter with high affinity for spermine (By similarity). Also stimulates cellular uptake of polyamines and protects against polyamine toxicity (By similarity). Plays a role in intracellular cation homeostasis and the maintenance of neuronal integrity (By similarity). Contributes to cellular zinc homeostasis (By similarity). Confers cellular protection against Mn(2+) and Zn(2+) toxicity and mitochondrial stress (By similarity). Required for proper lysosomal and mitochondrial maintenance (By similarity). Regulates the autophagy-lysosome pathway through the control of SYT11 expression at both transcriptional and post-translational levels. Facilitates recruitment of deacetylase HDAC6 to lysosomes to deacetylate CTTN, leading to actin polymerization, promotion of autophagosome-lysosome fusion and completion of autophagy. Promotes secretion of exosomes as well as secretion of SCNA via exosomes (By similarity). Plays a role in lipid homeostasis (By similarity).
Subcellular location: Lysosome membrane {ECO:0000250|UniProtKB:Q9NQ11}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:Q9NQ11}; Multi-pass membrane protein {ECO:0000255}. Endosome, multivesicular body membrane {ECO:0000250|UniProtKB:Q9NQ11}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q9NQ11}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Parkinson disease protein 7 homolog
- Lysosomal acid glucosylceramidase
- Alpha-synuclein
- Serine/threonine-protein kinase PINK1, mitochondrial
- Vacuolar protein sorting-associated protein 35
- F-box only protein 7
- 85/88 kDa calcium-independent phospholipase A2
- Intermembrane lipid transfer protein VPS13C
- E3 ubiquitin-protein ligase parkin
- Leucine-rich repeat serine/threonine-protein kinase 2
Sequence:
MSADSSLLMGSTPPSYGTLTTGTSIDPLSSSASSVRLSGYCGSPWRAIGYHAAVWMLAGIPWLLFRWKPLWGVRLRLKPCSLAHAETLVIEIKDKEGSSRQLFTVQVQTEAVVQGSLELPPQAQAEDGRSQAAVGVTPEGTWQDTSELHRQEEAKQVLRYYVLQGQRYVWMETQQAFCQVSLLDHGRTCDDVHCSSSGLSLQDQATRKTIYGPNVISIPVKSYLQLLADEALNPYYGFQAFSIALWLADHYYWYALCIFLISAISICLALYKTRKQSLTLRDMVKLSVRVQVCRPGGEEEWVDSSELVPGDCLVLPQEGGVMPCDAALVAGECVVNESSLTGESTPVLKTALPEGPKPYCPETHRRHTLFCGTLILQARAYVGPRVLAVVTRTGFCTAKGGLVSSILHPRPISFKFYKHSMKFVAALSVLALLGTVYSIIILYRNRVPVREIVIRALDLVTVVVPPALPAAMTVCTLYAQSRLRTQGIFCIHPLRINLGGKLRLVCFDKTGTLTEDGLDVMGVVPLKGQVLLPLVPEPCHLPLGPLLRALATCHALSQLHDTPVGDPMDLKMVESTGWVLEEGPAAGSAPGSQVLVVMRPPPGGPRQQEEPPVPVSVLCRFPFSSALQRMDVVVTWPGATQPEAYVKGSPELVASLCSPETVPSDFSQVLQSYTAAGYRVVALAGKPLPIAPSLAAAQQLTRDTVERELSLLGLLVMRNLLKPQTAPVIQTLRKTGIRTVMVTGDNLQTAVTVARACGMVGAQEHLAVIHATHPEQGQPAALEFLPTESSAVMNGAKATGYPTVPEPQSCHLALSGSTFAVLRKHFPKLLPKVLVQATVFARMAPEQKTELVCELQRLQYCVGMCGDGANDCGALKAADVGISLSQAEASVVSPFTSSMASIECVPTVIREGRCSLDTSFSVFKYMALYSLTQFISVLILYTINTNLGDLQFLAIDLVITTTVAVLMSRTGPALTLVRARPPGALLSVPVLGSLLLQVALVAGIQLGGYFLVIAQPWFVPLNRTVPAPDNLPNYENTVVFSLSGFQYLILAAAVSKGAPFRQPLYTNVPFLVALALLGSVLVGLILVPGLLQGPLGLRNIVDSSFKLLLLGLVAFNFVGAFMLESVLDQCLPACLRWLRPKRASKKQFKRLQQELAEHPWPTLPVGSVR
Protein: Organic anion transporting polypeptide 33Eb (RE09129p) (Q9VK82)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- FI06409p
- RE54577p
Sequence:
MAHNTRNSDLSQIAVNANNIPDDSVDCGIKGLGWCRGPGCQKYARLRTFILVLAISGTLQGACESYFRVSAKQASFQFGWNPLIVDWLLVASGLFQAVFALAFAYWADVYHPIKWLVGTLMLQAVTCVVAVIPSIMNFADGNQAKDALLDANMCATSLAQFQRLTLTEAQSSSLTLAMLFVLQLALGMGGLAYYTLGVSYIDDNSLSQDSPAVIGAALAARVFGQQAGSFLVLGVGLTHVGWWLGWVILAPFIFVGAVLLGLFPKRLPKTVIHQAAQRIIEQSSMRRFGSQFSTYMDDSDFWPSLKRLFNNRLLMFNLLSIMCVQSAVVNYGLQEESYLQSRFFLPYNEQDGLAAEWRSAFVSYFLKPPVMALGMLISGLVISKAKLSARKITGINIALSIHLVAIFIGLIFVQCDVGAIAGVEGGKLKQPYCSSQCLCTPTAFMPVCPENSSVTYFSPCYAGCTKKTTINSFQLFEGCSCSGDQSLNSTGQMRATAGACSSDNCQSAIIIFQIMSISVAFLMGVGAIGKTLITLRAVLPQDKSLALAFELMIVGLFAYVPVHLSYDIVTRTTCVYWAPNYERCLLRETPKHGNILDILTASLILASVLFDILVYIFAKGLNLYNCKVTDNNYTPSLYAPIPHEDATTSPSAPRGGSPVTTTTTSSPIQRRDAAPEPRTETAVFRNPSSVTTSSGGAQSIVEPSESGVTYAQVVFPPDRRKPDDGSTSPKRLAVPANVPLHLLSESDVRSQLGNLKSFNPPKQEADRGLDTVDTDDVVVTQPQVQAVLPITRDLHPNHQPQPESPRPQSPETDF
Protein: Eukaryotic translation initiation factor 3 subunit I (eIF3i) (Eukaryotic translation initiation factor 3 subunit 2) (eIF-3-beta) (Q54MT0)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03008}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 3 subunit K
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit D
Sequence:
MRPISLRLHERPITQVLFNREGDLLFVAAKDKLVSLWYTTNGERIGSYQCGGVVYSIDVSQDSKYLITASADAKARVWDVSSGRQLDSTDFEVSARSIEFSQGDKQILVVTDQVMGCQAKIHVFDFDKDEVRKLNKSYTLPSPQCKITQATWGPLNKTIFASCEDGAVRIYCTEKRELIKTILDHNKLVTRIEWTKHRIMFMTCSKDGTAKLYDTKTLKLLRTFDTGRPINAAGISPLKPHVILGGGQSAESVTTTKVDASQFKVRFFHIVYGEELGGLIGHIGPVHSICFTPDGKTFATGGEEGLVQVNHLDESYFEFDDDLVYNPPVQH
Protein: Rhoptry-associated protein 3 (Q8I485)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MIRKFLISLFLIFLCLNNVVIGNKCKKALIDIDTKDLSLSSILRAHKPDNTTLGSWVYFFFNHFSNVDEAIEYLKGLNINVLDIEDHACFARAFSVYLLHFYAKDLKMMIRNEEHESFFKNKLSEINNIISGDFLSTLKHEYFFDKLPSIIVKEKDASHIVKRTDFLQDILEKADLNNHAIYKNDPTKVFIFNEINFFRTFQLEGKPHIPDDQLSFMRDYALLIYLGTKENYYNSDITEYAQGNYNISKNRTRLGLKKRSKTFSLDDPQKNSNIFAFCEKNGKEEFFGTPDDLISSFFSDMKAKMVKGHKRFLMEFDYAVKNRTYALPKVKGFRFLKQLFQRKNLKNFVGMYINLLSTEIDFLAEDFVEMFDTTMNCYGRQHAARAADHYMDMKLSNIFK
Protein: Inositol polyphosphate-5-phosphatase F (D3ZKG7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Inositol polyphosphate 5-phosphatase OCRL
- Phosphatidylinositol 3-kinase regulatory subunit gamma
- Phosphatidylinositol 4-kinase type 2-alpha
- Type II inositol 1,4,5-trisphosphate 5-phosphatase
- Myotubularin
- Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Phosphatidylinositol 4-kinase alpha
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Type II inositol 1,4,5-trisphosphate 5-phosphatase
Sequence:
MELFQAKDHYILQQGERALWCSRRDGGLQLRPATDLLLAWNPICLGLVEGVIGKIQLHSDLPWWLILIRQKALVGKLPGDHEVCKVTKIAVLSLSEMEPQELELELCKKHHFGINKPEKIVPSPDDSKFLLKTFTNIKSNVSAPNKKKVKESKEKEKLERRLLEELLKMFMDSESFYYSLTYDLTNSVQRQSTGEKDGRPLWQKVDDRFFWNKYMIQDLSEIGTPDVDFWIIPIIQGFVQIEELVVNYEPSDDDKSSPETPPQEATCVDDIHPRFLVALISRRSRHRAGMRYKRRGVDKNGNVANYVETEQLIHVHNHTLSFIQTRGSVPVFWSQVGYRYNPRPRLDKSEKETVDCFCAHFEEQLKIYKKQVIVNLVDQAGREKIIGDAYLKQVLLFNNPRLTYVSFDFHEHCRGMKFENVQTLTDAIHDIILDMKWCWVDQAGVICKQEGIFRVNCMDCLDRTNVVQAAIARVVMEQQLKKLGVMPPEQPLPVKCNRTYQIMWANNGDSISRQYAGTAALKGDFTRTGERKLAGVMKDGVNSANRYYLSRFKDAYRQAVIDLMQGIPVTEDLYSIFTKEKEHEALQKETQRSHQELISQLLQSYMQLLLPGDEKFHGGWALIDCDPSLTDAAHRDVDVLLLLSNSAYYVAYYDDEVDKVSQYQRRSLEDLEKIEIGPEPTLFGKPKFSCMRLHYTCKEAGGYFHTLRAVPRSPEEDGKDTLQCIAEMLQITKQAMGLHVPIIERKLERKSSKPHEDIIGIRSQNQGSLAQGKSFLMSKFSSLNQKVKQTKSNVNIGNLRKLGNFTKPEVKVNFLKPNLKVNLWKSDSSLETMENPGVMGNKVQGESDGDVSSDNDSYHSDELLTNSRSEEGKQLANSLESAGPTDYLLPSCGIIASAPRLGSRSQSASSTDVSIHAPSEATVGHGHELGKGLESPLKKSPSADNIHTLTGFAKPMDVYCQRFVQDAQNKMNALSEVRAVAQNSEEGNHKTNPVSNEETQSESVEQMPSRPSQLNVSCSVTGPQLLSVEPAHPAVSQKTPGSGSSLLDLEAGLCVTPSSESSSRAVSPFAKIRSSMVQVANITQAGLTHGINLAVAKVQKSPAEPEVVNEIQQNELKNMFTQCQTRIIQI
Protein: Hydrolethalus syndrome protein 1 homolog (H2KYG1)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MANFTTENELEDILHQMGHHIHDKNQFATFKNEIDNLLDRELCLSDADEDVMNESLFASLSVDPAAQFIRQERNFPTENLNIQSPIVSRKRQGKRFIYENVELQSDFDDESSNEYPERNLLVDRAWRSIHRAMETCNGATEVLTFSFFFLLKNADFHSRFFP
Protein: CTP-dependent diacylglycerol kinase 1 (EC 2.7.1.174) (Diglyceride kinase 1) (DAG kinase 1) (High-copy suppressor of SLY1 defect protein 1) (Q12382)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: CTP-dependent diacylglycerol kinase that catalyzes the phosphorylation of diacylglycerol (DAG) to phosphatidate (PA). Controls phosphatidate levels at the nuclear envelope. Counteracts the activity of PA phosphatase PAH1/SMP2, controlling the levels of PA and DAG for the synthesis of triacylglycerol and membrane phospholipids. May be involved in vesicle trafficking between the endoplasmic reticulum and the Golgi apparatus. Required to convert triacylglycerol-derived DAG to PA for phospholipid synthesis during growth resumption from stationary phase in the absence of de novo fatty acid synthesis. Involved in the resistance to nickel chloride and nalidixic acid.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11481671, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:18458075}; Multi-pass membrane protein {ECO:0000305|PubMed:11481671, ECO:0000305|PubMed:18458075}. Nucleus membrane {ECO:0000269|PubMed:18458075}; Multi-pass membrane protein {ECO:0000305|PubMed:18458075}.
Interaction partners:
- Phosphatidic acid phosphohydrolase 1
- Protein ICE2
- Lipid phosphate phosphatase 1
- Diacylglycerol pyrophosphate phosphatase 1
- Phosphatidate cytidylyltransferase
- Phospholipase D1
- Choline/ethanolaminephosphotransferase 1
- Lysophospholipid acyltransferase
- Triacylglycerol lipase 4
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
Sequence:
MGTEDAIALPNSTLEPRTEAKQRLSSKSHQVSAKVTIPAKEEISSSDDDAHVPVTEIHLKSHEWFGDFITKHEIPRKVFHSSIGFITLYLYTQGINYKNVLWPLIYAFIILFILDLIRLNWPFFNMLYCRTVGALMRKKEIHTYNGVLWYILGLIFSFNFFSKDVTLISLFLLSWSDTAAATIGRKYGHLTPKVARNKSLAGSIAAFTVGVITCWVFYGYFVPAYSYVNKPGEIQWSPETSRLSLNMLSLLGGVVAALSEGIDLFNWDDNFTIPVLSSLFMNAVIKTFKK
Protein: Uncharacterized protein (Q386Z1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Ribosomal protein L9 domain-containing protein
- Ribosomal protein L9 domain-containing protein
- Large ribosomal subunit protein uL23m
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Ribosomal protein S24/S35 mitochondrial conserved domain-containing protein
- Uncharacterized protein
Sequence:
MLRRFALTSSVALRLRFERDSGHNTVRYRPIPESMQPKHLEDNFTPFPLPKFDESLEYGPVRLRNIPDIEAAKERRRGSRLAATEVLLQETLQEENQFATSGKGDGNMAIAITERHTEDVTTPAADSRFPSQTMSPCSHEEEMRGYVVSRDYPLIDRLHCTRSIEELVAQFEDRPQIESRVAALADMASTVSFRSDEELLRMFTAISAPFSVDGRGLNFLTVKVSKFGRPYYVPNSLLPAYVNLVDATTIALVREQPWRLSASPALFIQVLQFMALIKVFEPNKWFTFSDHAPSNRADYRHAIGVNHSTAFWGTGEELYDFMVELLRVEDDGRIPTMLDLCTREQMVDLLSGFCGVMPGGKAVGDVFKTITDAFLRRVRNDISGSWGAHDWAIVERMYLVTVLCDAGNNEILQLLLSDTASPRGPDFFAAVSRTKDTPTKKRALCLLQEAIDNASVKADKVTLLGLLESGSEFLLSLVDKGVAHTFATQNLFDYRILNSFLHCSLVADRLRVEQSVITSRIPSSLRDVQVQMLMSNERNALNPLTSSLPGNSGAIATAPKLKRPLMTMLSQLEYLNSIDSVFILHSSLMATSTDQLVSAVRRLPSGKDSLIVTMSCLRALSVKSLTSPSMKERIACARALEIVSYELEKGRAVLLPFSEEILLHDAGAYCDEDLMLWTVAAFLARELPLVKVHTLMHSNCTARTPYRFLKGGHNLLVSSRSLYDKGAPLLSSLHSKELRLVTHNVRLRTPVRDRKCTLQYYNPIRARFVYRRDKPLFDKYHVTARNLAPGFSRGALKHDWRALGVYTPDHPQVPYHPLQTWMLGETTVEAE
Protein: Septin-2 (Neural precursor cell expressed developmentally down-regulated protein 5) (NEDD-5) (P42208)
Organism: Mus musculus (Mouse)
Function: Filament-forming cytoskeletal GTPase. Forms a filamentous structure with SEPTIN12, SEPTIN6, SEPTIN2 and probably SEPTIN4 at the sperm annulus which is required for the structural integrity and motility of the sperm tail during postmeiotic differentiation (By similarity). Required for normal organization of the actin cytoskeleton. Plays a role in the biogenesis of polarized columnar-shaped epithelium by maintaining polyglutamylated microtubules, thus facilitating efficient vesicle transport, and by impeding MAP4 binding to tubulin. Required for the progression through mitosis. Forms a scaffold at the midplane of the mitotic splindle required to maintain CENPE localization at kinetochores and consequently chromosome congression. During anaphase, may be required for chromosome segregation and spindle elongation. Plays a role in ciliogenesis and collective cell movements (By similarity). In cilia, required for the integrity of the diffusion barrier at the base of the primary cilium that prevents diffusion of transmembrane proteins between the cilia and plasma membranes: probably acts by regulating the assembly of the tectonic-like complex (also named B9 complex) by localizing TMEM231 protein.
Subcellular location: Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Cleavage furrow {ECO:0000250}. Midbody {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cell projection, cilium membrane. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q15019}. Note=In metaphase cells, localized within the microtubule spindle. At the metaphase plate, in close apposition to the kinetochores of the congressed chromosomes. In cells undergoing cytokinesis, localized to the midbody, the ingressing cleavage furrow, and the central spindle (By similarity). In interphase and postmitotic cells, localized to fibrous or granular structures, depending on the growth state of the cell. Localizes at the base of the cilia near the morphological distinction between the cilia and plasma membranes. Found in the sperm annulus. {ECO:0000250, ECO:0000250|UniProtKB:Q15019}.
Interaction partners:
- Septin-7
- Septin-6
- Septin-8
- Septin-11
- Septin-9
- Septin-5
- Septin-4
- Neuronal-specific septin-3
- Septin 12
- Septin-10
Sequence:
MSKQQPTQFINPETPGYVGFANLPNQVHRKSVKKGFEFTLMVVGESGLGKSTLINSLFLTDLYPERIIPGAAEKIERTVQIEASTVEIEERGVKLRLTVVDTPGYGDAINCRDCFKTIISYIDEQFERYLHDESGLNRRHIIDNRVHCCFYFISPFGHGLKPLDVAFMKAIHNKVNIVPVIAKADTLTLKERERLKKRILDEIEEHSIKIYHLPDAESDEDEDFKEQTRLLKASIPFSVVGSNQLIEAKGKKVRGRLYPWGVVEVENPEHNDFLKLRTMLITHMQDLQEVTQDLHYENFRSERLKRGGRKVENEDMNKDQILLEKEAELRRMQEMIARMQAQMQMQMQGGDSDSGALGQHV
Protein: Protein LOT5 (Low temperature-responsive protein 5) (P34234)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Small nuclear ribonucleoprotein Sm D1
- Protein arginine N-methyltransferase HSL7
- Small nuclear ribonucleoprotein Sm D2
- Pre-mRNA-splicing factor BRR1
- Small nuclear ribonucleoprotein E
- Increased recombination centers protein 6
- Small nuclear ribonucleoprotein Sm D3
- Small nuclear ribonucleoprotein-associated protein B
- Small nuclear ribonucleoprotein G
- Small nuclear ribonucleoprotein F
Sequence:
MMKKKPKCQIARTKPSVENVIPYNQFKKTQPRFNGNFSALNNEEYIILFGGGRDLILGSLTPCSSSHLSNQANPQDTSEYGTDLFILNSCIIIWFNGLGYGLEIPYSSVLYHASRRLPDGREGLQLEILLTLERDEVLDMLYQSLAPQACEFDGEEAHAFTVRSVELTIRPKYSIYDRHYNNEIETLFTFENFGVNRGDDLVNNCNEALAVCMDLHGEDVQDQDQEQYQDPSMAFEGAQDLNATYSGLGDTLHGPPVYQNDGLADDLDGDLVMDNVVSRGGPEASMSMEFYANQNLAGRKNSRDNE
Protein: PHD finger protein 23 (I3L410)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKLKDSLFDLDGPKVASPLSPTSLTHTSRPPAALTPVPLSQGDLSHPPRKKDRKNRKLGPGAGAGFGVLRRPRPTPGDGEKRSRIKKSKKRKLKKAERGDRLPPPGPPQAPPSDTDSEEEEEEEEEEEEEEMATVVGGEAPVPVLPTPPEAPRPPATVHPEGVPPADSESKEVGSTETSQDGDASSSEGEMRVMDEDIMVE
Protein: Delta(8)-fatty-acid desaturase 1 (EC 1.14.19.29) (Delta(8)-sphingolipid desaturase 1) (Sphingoid long-chain base desaturase 1) (Sphingoid LCB desaturase 1) (Sphingolipid 8-(E/Z)-desaturase 1) (Q9ZRP7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a major role as delta(8)-fatty-acid desaturase which introduces a double bond at the 8-position in the long-chain base (LCB) of ceramides with or without a hydroxy group at the 4-position. The enzyme produces both the 8E and 8Z isomers (in a 4:1 ratio). This structural modification contributes to the quantitative partitioning of ceramides between the two major sphingolipid classes, glucosylceramides and glycosylinositolphosphoryl ceramides. Sphingolipids are important membrane components involved in environmental stress responses, such as resistance to chilling, and act as cell signaling molecules.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:22023480}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Sphinganine C4-monooxygenase 2
- Sphinganine C4-monooxygenase 1
- Delta-9 acyl-lipid desaturase 2
- Sphingolipid delta
- Ceramide synthase LOH2
- Dihydroceramide fatty acyl 2-hydroxylase FAH2
- Palmitoyl-monogalactosyldiacylglycerol delta-7 desaturase, chloroplastic
- Delta
- Delta-9 acyl-lipid desaturase 1
- Omega-6 fatty acid desaturase, chloroplastic
Sequence:
MAEETEKKYITNEDLKKHNKSGDLWIAIQGKVYNVSDWIKTHPGGDTVILNLVGQDVTDAFIAFHPGTAWHHLDHLFTGYHIRDFQVSEVSRDYRRMAAEFRKLGLFENKGHVTLYTLAFVAAMFLGVLYGVLACTSVFAHQIAAALLGLLWIQSAYIGHDSGHYVIMSNKSYNRFAQLLSGNCLTGISIAWWKWTHNAHHLACNSLDYDPDLQHIPVFAVSTKFFSSLTSRFYDRKLTFDPVARFLVSYQHFTYYPVMCFGRINLFIQTFLLLFSKREVPDRALNFAGILVFWTWFPLLVSCLPNWPERFFFVFTSFTVTALQHIQFTLNHFAADVYVGPPTGSDWFEKQAAGTIDISCRSYMDWFFGGLQFQLEHHLFPRLPRCHLRKVSPVVQELCKKHNLPYRSMSWFEANVLTINTLKTAAYQARDVANPVVKNLVWEALNTHG
Protein: Putative spliceosome-associated protein (RNA-binding (RRM/RBD/RNP motifs) family protein) (Q9ZU66)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Nuclear protein-like
- Pliceosome associated protein-like protein
- Proline-rich spliceosome-associated
- Uncharacterized protein At3g23325
- At2g32600/T26B15.16
- Spliceosome-associated protein 130 A
- Cleavage and polyadenylation specificity factor
- Splicing factor SF3a60 homolog
- PHD finger-like domain-containing protein 5A
- U1 small nuclear ribonucleoprotein C
Sequence:
MTTRIAPGVGANLLGQHSAERNQDATVYVGGLDAQLSEELLWELFVQAGPVVNVYVPKDRVTNLHQNYGFIEYRSEEDADYAIKVLNMIKLHGKPIRVNKASQDKKSLDVGANLFIGNLDPDVDEKLLYDTFSAFGVIASNPKIMRDPDTGNSRGFGFISYDSFEASDAAIESMTGQYLSNRQITVSYAYKKDTKGERHGTPAERLLAATNPTAQKSRPHTLFAMGPPSSAPQVNGLPRPFANGSMQPVPIPAPRQPPPPPPQVYQTQPPSWPSQPQQHSMVPPPMQFRPPQGMPPPPPPQFLNHQQGFGGPRPPPPPQAMGMHQHGGWPPQHMQQQGGPPQQQQPPYQHHHMSMPPPPPHQG
Protein: CDKN1A interacting zinc finger protein 1 (H0Y5D5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
PLPMAVSRGLPPQQPQQPLLNLQGTNSASLLNGSMLQRALLLQQLQGNLRGYGMASPGLAAPSLTPPQLATPNLQQFFPQATRQSLLGPPPVGVPMNPSQFNLSGRNPQKQARTSSSTTPNRKTMPVEDKSDPPEGSEEAAEPRMDTPEDQDLPPCPEDIAKEKRTPAPEPEPCEASELPAKRLRSSEEPTEKEPPGQLQVKAQPQARMTVPKQTQTPDLLPEALEAQVLPRFQPRVLQVQAQVQSQTQPRIPSTDTQVQPKLQKQAQTQTSPEHLVLQQKQVQPQLQQEAEPQKQVQPQVQPQAHSQGPRQVQLQQEAEPLKQVQPQVQPQAHSQPPRQVQLQLQKQVQTQTYPQVHTQAQPSVQPQEHPPAQVSVQPPEQTHEQPHTQPQVSLLAPEQTPVVVHVCGLEMPPDAVEAGGGMEKTLPEPVGTQVSMEEIQNESACGLDVGECENRAREMPGVWGAGGSLKVTILQSSDSRAFSTVPLTPVPRPSDSVSSTPAATSTPSKQALQFFCYICKASCSSQQEFQDHMSEPQHQQRLGEIQHMSQACLLSLLPVPRDVLETEDEEPPPRRWCNTCQLYYMGDLIQHRRTQDHKIAKQSLRPFCTVCNRYFKTPRKFVEHVKSQGHKDKAKELKSLEKEIAGQDEDHFITVDAVGCFEGDEEEEEDDEDEEEIEVEEELCKQVRSRDISREEWKGSETYSPNTAYGVDFLVPVMGYICRICHKFYHSNSGAQLSHCKSLGHFENLQKYKAAKNPSPTTRPVSRRCAINARNALTALFTSSGRPPSQPNTQDKTPSKVTARPSQPPLPRRSTRLKT