wanglab/gogpt-training-data huggingface dataset:
Protein: Fimbrin-5 (AtFIM5) (Fimbrin-like protein 2) (Fimbrin5) (Q9FKI0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cross-links actin filaments (F-actin) in a calcium independent manner. Induces the formation of actin bundles. Stabilizes and prevents F-actin depolymerization mediated by latrunculin B (LatB).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q7G188}.
Interaction partners:
- Putative cysteine-rich repeat secretory protein 14
- Villin-1
- Actin cross-linking protein, putative
- Actin-depolymerizing factor 5
- Actin-depolymerizing factor 7
- Formin-like protein 5
- LIM domain-containing protein PLIM2c
- LIM domain-containing protein PLIM2b
- LIM domain-containing protein PLIM2a
- F-actin-capping protein subunit beta
Sequence:
MSSYVGVLVSDPWLQSQFTQVELRTLKSKFVSNKTQLGRFTVGDLPPVFEKLKAFNGTIDEDEIKSVLDKSYPNADDEVDFEFFLRAFLSVQARGVEKSGGSKGASSFLKTSTTTVHHAINESEKASYVSHVNNYLRDDPFLKSYLPIDPATNAFFDLVKDGVLLCKLINVAVPGTIDERAINTKKTLNPWERNENLTLGLNSAKAIGCTVVNIGTQDIAEGRPYLVLGLISQIIKIQMLADLNFKKTPSLFQLVDDTQDAEELMGLAPEKVLLKWMNFHLKKAGYEKQVTNFSSDLKDGEAYAYLLNALAPEHSTHVALETKDPTERAKKVLEQAEKLDCKRYLSPKDIVDGSANLNLAFVAQIFQHRNGLTVDDSKTSFAEMMTDDVETSREERCFRLWINSLGTATYVNNVFEDLRNGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNEVIKIGKELRFSLVNVAGNDIVQGNKKLLLAFLWQLMRYTMLQLLRNLRSHSQGKEITDADILNWANRKVKRGGRTSQADSFRDKNLSSGMFFLELLSAVEPRVVNWSLVTNGETEEDKKLNATYIISVARKLGCSIFLLPEDIIEVNQKMMLILAASIMYWSLQQQSDTESTVSEDATDDGDANSVAGEISNLSIDGASESSPTVQDQELLTKADNDEDEVDGENNKDA
Protein: Zgc:136383 (Q1RM99)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MLPLSSSMSSSRMSKTATIMEPFRKFHKDRYLAPHSATKDTSSGSAAASFEQMQKKNRFLGNDIPPVFAIIARAVRADQKLLGYQLAAYFDKPTARVQLIASSIAENDNMKICADGALLSKHKVTAKFSWGAECKQYAVFAKAEAGVLGEYPAARLEVEWERLPKIASTYAKKVSKYILNAAYDTGFRFERATNSEKEIELTAALPSQKSLNVIARIPEITMSRRDIYLPVTVPINPDGTFTIDKDFLSWIHKYINED
Protein: Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase (EC 2.4.1.258) (Asparagine-linked glycosylation protein 6) (Dol-P-Man-dependent alpha(1-3)-mannosyltransferase) (Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase) (A2RA94)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Function: Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man(5)GlcNAc(2)-PP-Dol.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P38179}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDWMRLIRDLCFNPRHTKWMAPLLVLGDAFLCALIIWKVPCKATAKLRSHPFATRERDYTLIRGSTGPLVYPAAHVYSYTALYHLTDEGRDIFFGQILFAVLYLITLVVVLCCYRQSGAPPYLLPLLVLSKRLHSVYVLRLFNDGLAALAMWVAILLFMNRKWTAAVAVWSTGVAIKMTLLLLAPAIAVVTVLSLSLGPSVGLGVLAVLVQVLLAIPFLQNNPAGYLSRAFELTRQFMFKWTVNWRFVGEEVFLSKSFSLALLAVHIVLLGAFAVTGWLRYSRSSLPAFIRNLLAGRHRTVSLPKPYIMSVMLSSLTVGLLCARSLHYQFFAYLSWATPFLLWRAGFHPILLYLIWAMQEWAWNTFPSTNLSSIIVVLSLATQSFGVLANSASAFYTMRSNPSGKEHNQ
Protein: ADP-ribosylation factor-like protein 8a (AtARL8a) (ADP-ribosylation factor-like A1C) (AtARLA1C) (Q8VY57)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in lysosome motility. May play a role in chromosome segregation.
Subcellular location: Late endosome membrane {ECO:0000250|UniProtKB:Q9NVJ2}. Lysosome membrane {ECO:0000250|UniProtKB:Q9NVJ2}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9NVJ2}. Note=Localizes with microtubules at the spindle mid-zone during mitosis. {ECO:0000250|UniProtKB:Q9NVJ2}.
Interaction partners:
- Protein TOM THREE HOMOLOG 1
- Kinesin-like protein KIN-14E
- Serine carboxypeptidase-like 7
- Protein DJ-1 homolog B
- Tobamovirus multiplication protein 3
- Tobamovirus multiplication protein 2A
- Ras-related protein RABA1f
- Tobamovirus multiplication protein 1
- Ran-binding protein 1 homolog b
- Elicitor peptide 4
Sequence:
MGLLEAFLNWLRSLFFKQEMELSLIGLQNAGKTSLVNVVATGGYSEDMIPTVGFNMRKVTKGNVTIKLWDLGGQPRFRSMWERYCRAVSAIVYVVDAADPDNLSVSKSELHDLLSKTSLNGIPLLVLGNKIDKPGALSKEALTDEMGLTSLTDREVCCFMISCKNSTNIDQVIDWLVKHSKSKN
Protein: Polynucleotide 5'-hydroxyl-kinase grc3 (EC 2.7.1.-) (Q9UU96)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Polynucleotide 5'-kinase required for both rRNA processing and heterochromatic gene silencing.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:21385875}. Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:21385875}. Chromosome {ECO:0000269|PubMed:10759889}. Note=Nuclear dots. {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:21385875}.
Interaction partners:
- Pre-rRNA-processing protein crb3/ipi3
- Pre-rRNA-processing protein las1
- 5'-3' exoribonuclease 2
- Pre-rRNA-processing protein ipi1
- Midasin
- Decapping nuclease din1
- Ubiquitin-like-specific protease 1
- Exosome complex exonuclease dis3
- Exosome complex exonuclease rrp6
- Large ribosomal subunit protein uL30C
Sequence:
MVKRQRIESSNVPLSAFAVRQLTLSKAARKKDNSSGKKRSVSEEESQDKYEDEMKTEGEFPSYKHTLVQVVVPGVDHRTKLHSESSKNDSEITPDINRSKVNPQEYSEFSVASPQTISPSLPLNLDDETVSENVPHSPQSSNDAIPVIKITEENSFRVKDTLYVGLHKDQKLAMVGTFIFRSVRGKFQLFGATYSSACMSWFPLNAPLAFATPVFSAIDNALPAMQISEYEEDSLNLRSFAVPSYSPKEHEYELEPKDILPNFETVIAFRENENGLSKIARVLPFAKRLFSFKNLLQDASSISNNFEITPESWCSFSNQLLFSTSKSDYVVPRLMVCGPKGSGKSSFSRYITNRLLQQYRHIAYLDLDPGQPEVVPSGHISLYYINSPLQGPVFARMLFPTYMLRLHLGDISPQKDPDHYIACVTRLFAEYKDYIFNQEISQKEIIPLIINCPGWIRGGGAELLSSIVDICQPTEVVYMSREDMKSSHREKKSIYQHKEYMPDFLSSRDEFQLTLLESTWQYLPDPNVNKVTSADNRMLGLLSYLYFNCNLQRWDFTTSLTACQPIATAFKGSSKGIDAVNIIGEPLNVNDVAKTINGTLMALYACDTASLDNSNTQRIVSSPEGIPLIINDGLPLDPNTSHCLGLIVLRTIDLKRNEFHFVGPLNLELIKDAYAKSLKIVLERGRLELPVYAMLDHRLAQYSELPYLDRNHDRVAVGAHRRRVRRNIIRRSTFVG
Protein: Transcription initiation factor TFIID subunit 2 (150 kDa cofactor of initiator function) (RNA polymerase II TBP-associated factor subunit B) (TBP-associated factor 150 kDa) (Transcription initiation factor TFIID 150 kDa subunit) (TAF(II)150) (TAFII-150) (TAFII150) (Q6P1X5)
Organism: Homo sapiens (Human)
Function: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription. TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. TAF2 forms a promoter DNA binding subcomplex of TFIID, together with TAF7 and TAF1.
Subcellular location: Nucleus {ECO:0000269|PubMed:9774672}.
Interaction partners:
- Transcription initiation factor TFIID subunit 11
- Transcription initiation factor TFIID subunit 13
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 5
- Transcription initiation factor TFIID subunit 4
- TATA-box-binding protein
- Transcription initiation factor TFIID subunit 7
- Transcription initiation factor TFIID subunit 6
Sequence:
MPLTGVEPARMNRKKGDKGFESPRPYKLTHQVVCINNINFQRKSVVGFVELTIFPTVANLNRIKLNSKQCRIYRVRINDLEAAFIYNDPTLEVCHSESKQRNLNYFSNAYAAAVSAVDPDAGNGELCIKVPSELWKHVDELKVLKIHINFSLDQPKGGLHFVVPSVEGSMAERGAHVFSCGYQNSTRFWFPCVDSYSELCTWKLEFTVDAAMVAVSNGDLVETVYTHDMRKKTFHYMLTIPTAASNISLAIGPFEILVDPYMHEVTHFCLPQLLPLLKHTTSYLHEVFEFYEEILTCRYPYSCFKTVFIDEAYVEVAAYASMSIFSTNLLHSAMIIDETPLTRRCLAQSLAQQFFGCFISRMSWSDEWVLKGISGYIYGLWMKKTFGVNEYRHWIKEELDKIVAYELKTGGVLLHPIFGGGKEKDNPASHLHFSIKHPHTLSWEYYSMFQCKAHLVMRLIENRISMEFMLQVFNKLLSLASTASSQKFQSHMWSQMLVSTSGFLKSISNVSGKDIQPLIKQWVDQSGVVKFYGSFAFNRKRNVLELEIKQDYTSPGTQKYVGPLKVTVQELDGSFNHTLQIEENSLKHDIPCHSKSRRNKKKKIPLMNGEEVDMDLSAMDADSPLLWIRIDPDMSVLRKVEFEQADFMWQYQLRYERDVVAQQESILALEKFPTPASRLALTDILEQEQCFYRVRMSACFCLAKIANSMVSTWTGPPAMKSLFTRMFCCKSCPNIVKTNNFMSFQSYFLQKTMPVAMALLRDVHNLCPKEVLTFILDLIKYNDNRKNKFSDNYYRAEMIDALANSVTPAVSVNNEVRTLDNLNPDVRLILEEITRFLNMEKLLPSYRHTITVSCLRAIRVLQKNGHVPSDPALFKSYAEYGHFVDIRIAALEAVVDYTKVDRSYEELQWLLNMIQNDPVPYVRHKILNMLTKNPPFTKNMESPLCNEALVDQLWKLMNSGTSHDWRLRCGAVDLYFTLFGLSRPSCLPLPELGLVLNLKEKKAVLNPTIIPESVAGNQEAANNPSSHPQLVGFQNPFSSSQDEEEIDMDTVHDSQAFISHHLNMLERPSTPGLSKYRPASSRSALIPQHSAGCDSTPTTKPQWSLELARKGTGKEQAPLEMSMHPAASAPLSVFTKESTASKHSDHHHHHHHEHKKKKKKHKHKHKHKHKHDSKEKDKEPFTFSSPASGRSIRSPSLSD
Protein: Cyclic nucleotide phosphodiesterase 7B3 (EC 3.1.4.17) (Phosphodiesterase 7B, isoform CRA_a) (Q8VIE3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MTPQAPLHLLDEDYLGQARHMLSKVGMWDFDIFLFDRLTNGNSLVTLLCHLFNSHGLIHHFKLDMVTLHRFLVMVQEDYHGHNPYHNAVHAADVTQAMHCYLKEPKLASFLTPLDIMLGLLAAAAHDVDHPGVNQPFLIKTNHHLANLYQNMSVLENHHWRSTIGMLRESRLLAHLPKEMTQDIEQQLGSLILATDINRQNEFLTRLKAHLHNKDLRLENIQDRHFMLQIALKCADICNPCRIWEMSKQWSERVCEEFYRQGDLEQKFELEISPLCNQQKDSIPSIQIGFMTYIVEPLFREWARFTGNSTLSESMLNHLAHNKAQWKSLLSNQHRRRGSGQDPAGTAPETLEQTEGATP
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 (DAD-1) (Oligosaccharyl transferase subunit DAD1) (Defender against apoptotic cell death 1) (Defender against cell death 1) (Q9VLM5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity (By similarity). Probably as part of the N-glycosylation pathway, plays a role in the regulation of tissue growth and apoptosis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:27693235}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- GH11935p
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- dolichyl-diphosphooligosaccharide--protein glycotransferase
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- DSec61alpha
- Transmembrane protein 258
- Protein transport protein Sec61 subunit beta
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4
Sequence:
MVELSSVISKFYNDYVQNTPKKLKLVDIYLGYILLTGIIQFVYCCLVGTFPFNSFLSGFISTVSCFVLAVCLRLQANPQNKSVFAGISPERGFADFIFAHVILHLVVMNFIG
Protein: At2g40070 (En/Spm-like transposon protein) (Flocculation FLO11-like protein) (Q494P4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein SPIRAL1-like 3
- Subtilisin-like protease SBT3.11
- Mutator-like transposase
- Mutator-like transposase
- TRIO/F-actin-binding protein
- At3g53320
- Protein SPIRAL1
Sequence:
MNRSFRAKESLLLDSAERQRQQLRASMMAEKDEELSLFLEMRRREKEQDNLLLNNNPDEFETPLGSKHGTSPVFNISSGAPPSRKAAPDDFLNSEGDKNDYEWLLTPPGTPLFPSLEMESHRTMMSQTGDSKSRPATLTSRLANSSTESAARNHLTSRQQTSSPGLSSSSGASRRPSSSGGPGSRPATPTGRSSTLTANSKSSRPSTPTSRATVSSATRPSLTNSRSTVSATTKPTPMSRSTSLSSSRLTPTASKPTTSTARSAGSVTRSTPSTTTKSAGPSRSTTPLSRSTARSSTPTSRPTLPPSKTISRSSTPTRRPIASASAATTTANPTISQIKPSSPAPAKPMPTPSKNPALSRAASPTVRSRPWKPSDMPGFSLETPPNLRTTLPERPLSATRGRPGAPSSRSGSVEPGGPPGGRPRRQSCSPSRGRAPMYSSGSSVPAVNRGYSKASDNVSPVMMGTKMVERVINMRKLAPPRSDDKGSPHGNLSAKSSSPDSAGFGRTLSKKSLDMAIRHMDIRRTIPGNLRPLMTNIPASSMYSVRSGHTRGRPMNVSDSSPLATSSNASSEISVCNNNGICLEASEKEDDAGSERGCRSPASLQGR
Protein: Polyketide cyclase / dehydrase and lipid transport protein (Q1G3L2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- MLP-like protein 165
- Abscisic acid receptor PYL5
Sequence:
MSATAILSVNNPKDLVTGFGNRTFHSRSNFAKPSSRLFPSSSSPMKPLTLASRFSPLISTNRSFKSSVFRRFDTLMEWQECKVKMKVEVPVSVAYGLYSERESIPKWMTFISSVKVLKDKPDLSRWTLKYKAFGQNLEYAWLAKNLQPLPNQKIHWISLEGLPNKGTVRFFPLGPSSCDVELTFAYEVPLLLIPFAAALQPLMQGLIKNSLEQFAEIAKSTKTT
Protein: Putative potassium channel regulatory protein sup-10 (Suppressor of unc-93 protein 10) (Q17374)
Organism: Caenorhabditis elegans
Function: May contribute to coordination of muscle contraction as regulatory subunit of a nonessential potassium channel complex.
Subcellular location: Membrane {ECO:0000303|PubMed:14534247}; Single-pass type I membrane protein {ECO:0000303|PubMed:14534247}. Note=In body-wall muscle cells, localizes to dense body-like structure which connect the myofibril lattice to the cell membrane. Colocalizes with sup-18. {ECO:0000269|PubMed:14534247, ECO:0000269|PubMed:24586202}.
Interaction partners:
- Two pore potassium channel protein sup-9
- Iodotyrosine dehalogenase 1 homolog
- Putative potassium channel regulatory protein unc-93
- Bifunctional glyoxylate cycle protein
Sequence:
MRYAVFIFLIVLIDLIYCWNSKRSFFIPDFLGSGDGTPKSKTESVIEERMEYGRMILLVCNKTCAKHRSDIPLWLKEFNQKKGYQEPETITYYYHTYRQAVSFIDTNETDVFPNLIYFIGVKRVVFNGDVNIREDVNDWIASLDQLILLEPRVYEDLNVILSDTSNCSSKYLLLADRPKCPQPSWSIVARIAQDHGIQPVKIGHPLDGLTHVLLYKRMPYLSEASCHLSVLLYENSYSDFGDDINPLVVSDWITTLLPLEEGSCPALFETYWHPIVDELTELQQIFYSAELEISERNKRPAFVLVGLTGGIAVIILAFSIFWGLNGSGFNKD
Protein: Cytochrome P450 26A1 (Q2PMW7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004406}. Microsome membrane {ECO:0000256|ARBA:ARBA00004174}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004174}.
Interaction partners:
Sequence:
MGLPALLASALCTFVLPLLLFLAALKLWDLYCVSSRDRSCALPLPPGTMGFPFFGETLQMVLQRRKFLQMKRRKYGFIYKTHLFGRPTVRVMGADNVRRILLGEHRLVSVHWPASVRTILGAGCLSNLHDSSHKQRKKVIMQAFNREALQCYVPVIAEEVSGCLEQWLSCGERGLLVYPEVKRLMFRIAMRILLGCEPGPAGGGEDEQQLVEAFEEMTRNLFSLPIDVPFSGLYRGVKARNLIHARIEENIRAKIRRLQAAEPDAGCKDALQLLIEHSWERGERLDMQALKQSSTELLFGGHETTASAATSLITYLGLYPHVLQKVREEIKSKGLLCKSHHEDKLDMETLEQLKYIGCVIKETLRLNPPVPGGFRVALKTFELNGYQIPKGWNVIYSICDTHDVADSFTNKEEFNPDRFTSLHPEDTSRFSFIPFGGGLRSCVGKEFAKILLKIFTVELARRCDWQLLNGPPTMKTSPTFYPVDNLPARFTHFQGDI
Protein: Renin receptor (ATPase H(+)-transporting lysosomal accessory protein 2) (ATPase H(+)-transporting lysosomal-interacting protein 2) (ER-localized type I transmembrane adapter) (Embryonic liver differentiation factor 10) (N14F) (Renin/prorenin receptor) (Vacuolar ATP synthase membrane sector-associated protein M8-9) (ATP6M8-9) (V-ATPase M8.9 subunit) [Cleaved into: Renin receptor N-terminal fragment; Renin receptor C-terminal fragment] (O75787)
Organism: Homo sapiens (Human)
Function: Multifunctional protein which functions as a renin, prorenin cellular receptor and is involved in the assembly of the lysosomal proton-transporting V-type ATPase (V-ATPase) and the acidification of the endo-lysosomal system. May mediate renin-dependent cellular responses by activating ERK1 and ERK2. By increasing the catalytic efficiency of renin in AGT/angiotensinogen conversion to angiotensin I, may also play a role in the renin-angiotensin system (RAS). Through its function in V-type ATPase (v-ATPase) assembly and acidification of the lysosome it regulates protein degradation and may control different signaling pathways important for proper brain development, synapse morphology and synaptic transmission (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29127204}; Single-pass type I membrane protein {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:29127204}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q9CYN9}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, dendritic spine membrane {ECO:0000250|UniProtKB:Q9CYN9}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000250|UniProtKB:Q9CYN9}. Endosome membrane {ECO:0000250|UniProtKB:Q9CYN9}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:Q6AXS4}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q6AXS4}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- V-type proton ATPase subunit d 1
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit S1
- Renin
- V-type proton ATPase subunit C 1
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase 116 kDa subunit a 1
- Ribonuclease kappa
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit F
Sequence:
MAVFVVLLALVAGVLGNEFSILKSPGSVVFRNGNWPIPGERIPDVAALSMGFSVKEDLSWPGLAVGNLFHRPRATVMVMVKGVNKLALPPGSVISYPLENAVPFSLDSVANSIHSLFSEETPVVLQLAPSEERVYMVGKANSVFEDLSVTLRQLRNRLFQENSVLSSLPLNSLSRNNEVDLLFLSELQVLHDISSLLSRHKHLAKDHSPDLYSLELAGLDEIGKRYGEDSEQFRDASKILVDALQKFADDMYSLYGGNAVVELVTVKSFDTSLIRKTRTILEAKQAKNPASPYNLAYKYNFEYSVVFNMVLWIMIALALAVIITSYNIWNMDPGYDSIIYRMTNQKIRMD
Protein: Meiosis regulator and mRNA stability factor 1 (Limkain-b1) (Meiosis arrest female protein 1) (Q8BJ34)
Organism: Mus musculus (Mouse)
Function: Essential regulator of oogenesis required for female meiotic progression to repress transposable elements and preventing their mobilization, which is essential for the germline integrity. Probably acts via some RNA metabolic process, equivalent to the piRNA system in males, which mediates the repression of transposable elements during meiosis by forming complexes composed of RNAs and governs the methylation and subsequent repression of transposons. Also required to protect from DNA double-strand breaks.
Subcellular location: Peroxisome {ECO:0000250}.
Interaction partners:
Sequence:
MEGKGTENPCSRTLGWFHQDNDAKPWLWKFSGCFSRPEQTLPLSSQTKEYMENKKAAVELKDIPSPLHVGSKFFPAVPLPDIRSLQQPKVQLSAIPKVSCCAHCPNEPSTSPMRFGGGSGSSGGSGSLIHTGSLLDSPSTGTVTCQVGSGFAFQSVSSLQNASTRNNLVGLSSDFPSMCVESNLPSCKHLSCCGKLHFQSCHSNVHKLHQFQNLQGCASAGYFPCSDFPSGAPGHLEERLSHSELTPHLCTNSLHLNVAPPVCLKGSLYCEDCLNKPARNSIIDAAKIWPNIPPPSTQPAPPAIPVCNGCGTKGMEKETSLLLATSLGKTASKFGSPEVAVTGQVLETLPPIGVFWDIENCSVPSGRSATTVVQRIREKFFRGHREAEFICVCDISKENKEVIQELNNCQVTVAHINATAKNAADDKLRQSLRRFANTHTAPATVVLVSTDVNFALELSDLRHRHGFHIILVHKNQASEALLHHANQLIRFEEFISDLPPRLPLKIPQCHTLLYVYNLPANKDGKSISNRLRRLSDNCGGKVLSITGCSAILRFINQDSAERAQKRMENEDVFGNRIIVSFTPKHREFFEAKSSNAIADKVKSPKKVKNTKLCLIKDTSEQSPSVKAMPGKVLQANSGSATKTTNIKSLQELCRMESKSGNRNSDHQQGHGRLAALPNSGPTASVPIVKNTGVTEPLYRSSQKKENPSSQSTVNSPVEKKKREETVFQVSYPSAFSKLIASRQVSPLLTSQSWSPRASPLAFNIANPSSGADCPDPFANGVDIQVSNVDYRLSRKELQQLLQEAFSKHGQVKSVELSPHTDYQLKAIVQMRNLHEAICAVNSLHRHKIGSKKILVSLSTGAANKSLSLLSTETMSILQDAPACCLPLFKFIDIYEKKYGHKLNVSDLYKLTDTIAIREQGNGRLVCLLPSNQARQSPLGSSQSHDGSSSNCSPVLFEELEYHEPVCKQHCSNKDFSELVFDPDSYKIPFVVLSLKVFAPQVHSLLQTHQGTVPLLSFPDCYAAEFGDLEITQDSHKGVPLEHFITCIPGVNIATAQNGVKVVKWIHNKPPPPNTDPWLLRSKSPVRNPQLIQFSREVIDLLKTQPSCILPVSNFIPSYHHHFGKQCRVSDYGYSKLIELLEAVPHVLQILGMGSKRLMTLTHRAQVKRFTQDLLKLLKSQASKQVIVRDFSQAYHWCFSKDWDVTEYGVCDLIDIISEIPDTTICLSQQDDDMVICIRKRERTQDEIERTKQFSKDVVDLLRHQPHFRMPFNKFIPSYHHHFGRQCKLAYYGFTKLLELLEAIPEILQVLECGEEKILTLTEVERFKALAAQFVKLLRSQKGNCLMMTDLFTEYAKTFGYTFRLQDYDVSSVSALTQKLCHVVKVADMESGKQIQLINRKSLRSLTAQLLVLLMSWEGDAYLPVDELRRHYETTHSTPLNPCEYGFMTLTELLKSLPYLVEVCTNDKAEEYVKLTSLYLFAKNVRSLLHTYHYQQIFLHEFSMAYNKYVGETLQPKTYGYSSVEELLGAIPQVVWIKGHGHKRIVVLKNDMKNRLSSFDLFSVNHEDQPAVSRQILAVPESHLASELQLRTGTGPSQMEQELLHLASSSPVDLLCAPVPSCLPSPQLRPDPVILKPADLIQFEEHPQEPLGVLVLNQEEKSEVPLPVQKGNLSCDSSPSSPAASPAPPGPSSEAPRPLFSKDAVESPAKKQPKNRVKLAANFSFAPVTKL
Protein: Small ribosomal subunit protein eS27 (40S ribosomal protein S27) (O74330)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein eL39
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL6
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein eL18A
Sequence:
MVLAVDLLNPSHESEMRKHKLKQLVQGPRSFFMDVKCPGCFNITTVFSHAQTVVICGSCASVLCQPTGGKARLMEGCSFRRKN
Protein: PH domain-containing protein (Q54W22)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- RCR-type E3 ubiquitin transferase
- BAR domain-containing protein
- Pleckstrin domain-containing protein
Sequence:
MESSSMTTNNNNNNSTISPSSSTTSISTSKNNDFLTLHKAYIDEWLMVSFLPILKTTYDGENNFYDISNLNIKNVNQRNIPFSEQLFALDRQFQNLINQWEKLSRSDQQRAAKIESYQQSFYTFIDRIKSTLEKTMVELGGSLEDSNFLAAAISLKEKQSKNKRLTIMARSRISPGGTSSTQYQHQMHLTGPISIVWNEILIIITRKVNEEVVRLQTENINNNIKNINNSEFNITNDIYQFNNNNLTQANKLEINNQRQKLYQQALSNIVPMLFEWRIMMANAQKVISEEKRFKVNPFIPTTVYDHNSSSFISAPILISTTNKTATTLLNNLNNNNIINNNNNNNNNNNNNNNNNNNNNNNNNSSSNSNNNNNSPISNSPSSSSPSPSSPTLTNRPSFINYDNQNNENNINNNNNNENNIGNNNINNNNSNENSDNKFSEEINISSSPPGTSGMTNSTSNLPTIASPTSWTKAVKRPAMSSSGGNIPILNNLGTSLNNNNNNKQIQDNNNNNLNTINANSNGNNNNSSNNVNSENNNIPTGGIIKQGWMKKRGTKNKSWKKRYFILDMKKTLRYYKDNSKIPHGNNSNNSGGGSSSNNNNCNSGNNNNGLNGGSGKGDQVNGNNISLPIGNNPHFHSSSGSGIPTTSPSMSSSSTSLENNDILSSFDHLKYKGSIDLYTSLVVAIKPSTFNVNINNSGSFKEDNNSYFGMDIITPSRTWNFCCESSKSMEDWLIVLKSANK
Protein: Expressed protein (Transmembrane protein) (Q9SJ03)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MIALAASSLGNTPIASFNRHFRFRLHPRNPLIQAAVSPSSSSSSPTASSGFDLSSLESAINKKDSNGVKEALDKLSEEGWAKKWSSQPYLSRRTTSLRELTTLGIKNAETLAIPSVRNDAAFLFTVVGSTGFIAVLAGQLPGDWGFFVPYLVGSISLVVLAVGSVSPGLLQAAISGFSTFFPDYQERIAAHEAAHFLVAYLIGLPILGYSLDIGKEHVNLIDERLAKLIYSGKLDSKELDRLAAVAMAGLAAEGLKYDKVIGQSADLFSLQRFINRSQPKISNEQQQNLTRWAVLYSASLLKNNKTIHEALMAAMSKNASVLECIQTIETAS
Protein: PRA1 family protein 3 (ADP-ribosylation factor-like protein 6-interacting protein 5) (ARL-6-interacting protein 5) (Aip-5) (GTRAP3-18) (Glutamate transporter EAAC1-interacting protein) (Prenylated Rab acceptor protein 2) (Protein JWa) (Q9ES40)
Organism: Rattus norvegicus (Rat)
Function: Regulates intracellular concentrations of taurine and glutamate (Ref.5). Negatively modulates SLC1A1/EAAC1 glutamate transport activity by decreasing its affinity for glutamate in a PKC activity-dependent manner. Plays a role in the retention of SLC1A1/EAAC1 in the endoplasmic reticulum.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11096102}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:11242046}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:11242046}. Cytoplasm, cytoskeleton {ECO:0000269|Ref.5}. Note=Also exists as a soluble form in the cytoplasm (PubMed:11242046). Associated with microtubules (Ref.5). {ECO:0000269|PubMed:11242046, ECO:0000269|Ref.5}.
Interaction partners:
- Excitatory amino acid transporter 3
- ADP-ribosylation factor like GTPase 6 interacting protein 1
Sequence:
MDVNLAPLRAWDDFFPGSDRFARPDFRDISKWNNRVVSNLLYYQTNYLVVAAMMISVVGFLSPFNMILGGIIVVLVFTGFVWAAHNKDILRRMKKQYPTAFVMVVMLASYFLISMFGGVMVFVFGITFPLLLMFIHASLRLRNLKNKLENKMEGIGLKKTPMGIILDALEQQEDSINKFADYISKARE
Protein: Javelin-like, isoform B (Q7KSJ6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MECLPMSSAAHHPHLMAGASAVGAVSASPTATVVVGATYPHHLHHHHLSHHTPYSNSYGSHHIHSEQTKSLQELQHEVGALLEFRDLVIETFPDLKHKMASMSATPSTPTSSVGAIGGSHSVGGGSSSLATSRREWEPGIRMKRKQSHKEPSTSSAAAAPSSGAEASSSSLTRSRSNSHSGKKEPKSGENNNGSVVQDSGFSTETSSSKEGHSASSTNGAMTVAIAANRLSCAESDDELLNLLDVIHRKSNRLREEVEHLQSYERQHGDAQKTGGEGQGASKEGMTAQQFREQVERLNREDIKQLRKERDRLLDKLAEMEAETLTGRIKAAKMSDQVEELVGVKKDLEEQLKLAMAQKLELSSRVQQLQQQQQSKSSSSGSQSDYSSQRNFLSSATTVLSNGSRPSSNVISNNTFQPVVLDQPAQEAFHQSPGSDIPLRKQQQQSLGRLDGIVSTPGTRNSKCRLTDSKRFAAILLETNVLELQRHLLTLTVQNQVLAQKLESSSKSKTLLAKRLDKNSEEFEHLRYQLEEKNIELEGTKAQLRLVESRLQASNSTSNSYLHSSQHDYETNRSSASTTLMLSRRGVSDSVDSTSTAMPAPPVTQISTPSMKAMVPLAMDELQQHSSSTESAHEHENQGLQTPNSTSSPLSKTIINASPCPVGSSTPSNIAARVMSISVGGVSPFEAMTPPPRQNAFRKFGSASKPSKIPLPGSKAAAYFSGKPPTGRPSTAGRSPPSANNSSSTSYGSKSSLSRSTGNLQSLRRAETSASNHSLSTNTSRSSTSSSIPLATTPYSSGSTGNRSQPTAATTPSPRVLQNSPLPKLKRDTISSRVRHLDSLSRAQQTPEGLKGTTTNSTSIAAQLSSTLRKDLQLSGNGTGAPYNQHHLNHRRSGHSPASNSSGSGVSRRYSSASTGGSGGRAIGRDQGEPTTPTSSYGGDSDSGKIQATYPNKRQATLRK