wanglab/gogpt-training-data huggingface dataset:
Protein: Interferon regulatory factor (B5X185)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR038196}.
Interaction partners:
Sequence:
MPVERMRMRPWLVEQINSSLIPGLIWINREKRIFQIPWMHAARHGWDLEKDAPLFMNWAIHTGKYQLGIDKPDPKTWKANFRCAMNSLPDIEEVKDKSIKKGTNAFRVYKMLSASERQTKKGKKRTEKGGKNKQVEPGFPAMESMNGSVGDHRGPVLKVEVKEEVKEDYFTDCTEYLHQSSHSPGYDQLIVDDLPCVCQTIEVTTENEEQSVSSSHPYPLQISPVSSYGESDPDSVHSEEDSKEDLRGGLWESSFTSSVLRVPSCSLPSMATFVTGGKVTNFKVTSTRDPMPLISYSNSPWTRDMPAAQHPPSEEASSSQASAAETRASVIMKTPDVSSVKTC
Protein: Sodium channel regulatory subunit beta-2 (O60939)
Organism: Homo sapiens (Human)
Function: Crucial in the assembly, expression, and functional modulation of the heterotrimeric complex of the sodium channel. The subunit beta-2 causes an increase in the plasma membrane surface area and in its folding into microvilli. Interacts with TNR may play a crucial role in clustering and regulation of activity of sodium channels at nodes of Ranvier (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:35277491}; Single-pass type I membrane protein {ECO:0000269|PubMed:36823201}. Cell projection, axon {ECO:0000250|UniProtKB:P54900}. Note=Clusters at the axon initial segment and node of Ranvier, the specialized neuronal subcellular domains involved in action potentials generation and propagation. {ECO:0000250|UniProtKB:P54900}.
Interaction partners:
- Sodium channel regulatory subunit beta-1
- Sodium channel protein type 3 subunit alpha
- Sodium channel protein type 2 subunit alpha
- Sodium channel protein type 9 subunit alpha
- Sodium channel regulatory subunit beta-3
- Sodium channel protein type 1 subunit alpha
- Sodium channel protein type 5 subunit alpha
- Sodium channel protein type 8 subunit alpha
- Sodium channel protein type 10 subunit alpha
- Sodium channel protein type 4 subunit alpha
Sequence:
MHRDAWLPRPAFSLTGLSLFFSLVPPGRSMEVTVPATLNVLNGSDARLPCTFNSCYTVNHKQFSLNWTYQECNNCSEEMFLQFRMKIINLKLERFQDRVEFSGNPSKYDVSVMLRNVQPEDEGIYNCYIMNPPDRHRGHGKIHLQVLMEEPPERDSTVAVIVGASVGGFLAVVILVLMVVKCVRRKKEQKLSTDDLKTEEEGKTDGEGNPDDGAK
Protein: Transglutaminase, isoform B (EC 2.3.2.13) (Q8IPH0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSYWYRNYTPSWLQRWWPNSQPRRVNPFRNTRPSADLEDGASSAVLGVLKVDLCLEDNHEEHHTSHFYAAAAKEALVVRRGEPFRLKIHFNRDYSPSKDAISFIFTVADDTKPSPGHGTLNALVPHDGIDYLGDTLEWGAGIESHEGQTLTVLIKPPSTCPVTEWKLDIDTKLLGDGSRSYPLPLPIYVLFNPWCPDDQVYLEDRDQRKEYVMHDTTLIWRGSYNRLRPSVWKIGQFERHVLECSLKVLGTVGRIPPAYRGDPVRVARALSALVNSVDDDGVLLGNWSEDFSGGVAPTKWTGSVEILQQFYKTQKSVKFAQCWNFSGVLTTIARSLGIPSRIITCYSSAHDTQASLTVDVFIDANNKKLDAETTDSIWNYHVWNELWMQRPDLGVGEHGTFDGWQVVDATPQEASDNMYRVGPASVAAVKNGDILRPFDGGFVFAEVNADKLYWRYNGPSQPLKLLRKDTLAIGHLISTKAVLKWEREDITDTYKHAERSEEERSTMLKALKQSRHAFSRYYLNDNFNDIEFDMELKDDIKIGQSFSVVLKVSNKSESRTHMATGQISCDAVLYTGVGAVEVKTLGFELELEPKSSDYVRMEVIFEEYYDKLSSQAAFQISAAAKVKDTDYDYYAQDDFRVRKPDIKFQLGEAAIVAQKELDVILRLENPLPIPLHKGVFTVEGPGIEQPLKFKIAEIPVGGTAAATFKYTPPYAGRGTMLAKFTSKELDDVDGYRHYEIEPRPEDLLQPNGSHRSSNIIRRRTDVIA
Protein: Transcription elongation factor SPT5 (A0A8I5ZR84)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR036945}.
Interaction partners:
Sequence:
MSDSEDSNFSEEEDSERSSEAEEAEVEEDRRSAAGSEKEEEPEEEEEEEEEEYDEEEEEEDDDRPPKKPRHGGFILDEADVDDEYEDEDQWEDGAEDILEKEEIEASNIDNVVLDEDRSGARRLQNLWRDQREEELGEYYMKKYAKSSVGETVYGGSDELSDDITQQQLLPGVKDPNLWTVKCKIGEERATAISLMRKFIAYQFTDTPLQIKSVVAPEHVKGYIYVEAYKQTHVKQAIEGVGNLRLGYWNQQMVPIKEMTDVLKVVKEVANLKPKSWVRLKRGIYKDDIAQVDYVEPSQNTISLKMIPRIDYDRIKARMSLKDWFAKRKKFKRPPQRLFDAEKIRSLGGDVASDGDFLIFEGNRYSRKGFLFKSFAMSAVITEGVKPTLSELEKFEDQPEGIDLEVVTESTGKEREHNFQPGDNVEVCEGELINLQGKVLSVDGNKITIMPKHEDLKDMLEFPAQELRKYFKMGDHVKVIAGRFEGDTGLIVRVEENFVILFSDLTMHELKVLPRDLQLCSETASGVDVGGQHEWGELVQLDPRTVGVIVRLERETFQVLNMHGKVVTVRHQAVTQKKDNRFAVALDSDQNNIHVKDIVKVIDGPHSGREGEIRHLYRSFAFLHCKKLVENGGMFVCKARHLVLAGGSKPRDVTNLTVGGFTPMSPRISSPMHPSAEGEMGSEFRDWSWEEPYLFNLRALGQSGVWKGLGFTEQVEELLTQLGGLTLVERDLRMSWLWAQHKRDKHNSWAPTSSHPTGQHGGFGSPGGMSRGRGRRDNELIGQTVRISQGPYKGYIGVVKDATESTARVELHSTCQTISVDRQRLTTVDSQRPGGMTSTYGRTPMYGSQTPMYGSGSRTPMYGSQTPLQDGSRTPHYGSQTPLHDGSRTPAQSGAWDPNNPNTPSRAEEEYEYAFDDEPTPSPQAYGGTPNPQTPGYPDPSSPQVNPQYNPQTPGTPAMYNTDQFSPYAAPSPQGSYQPSPSPQSYHQVAPSPAGYQNTHSPASYHPTPSPMAYQASPSPSPVGYSPMTPGAPSPGGYNPHTPGSGIEQNSSDWVTTDIQVKVRDTYLDTQIVGQTGVIRSVTGGMCSVYLKDSEKVVSISSEHLEPITPTKNNKVKVILGEDREATGVLLSIDGEDGIIRMDLEDQQIKILNLRFLGKLLEA
Protein: Voltage-gated delayed rectifier potassium channel KCNH1 (Ether-a-go-go potassium channel 1) (EAG channel 1) (r-eag) (Potassium voltage-gated channel subfamily H member 1) (Voltage-gated potassium channel subunit Kv10.1) (Q63472)
Organism: Rattus norvegicus (Rat)
Function: Pore-forming (alpha) subunit of a voltage-gated delayed rectifier potassium channel. Channel properties are modulated by subunit assembly. Mediates IK(NI) current in myoblasts. Involved in the regulation of cell proliferation and differentiation, in particular adipogenic and osteogenic differentiation in bone marrow-derived mesenchymal stem cells (MSCs) (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:24495567, ECO:0000269|PubMed:27516594, ECO:0000269|PubMed:7925287, ECO:0000269|PubMed:9400421}; Multi-pass membrane protein {ECO:0000269|PubMed:27516594}. Nucleus inner membrane {ECO:0000250|UniProtKB:O95259}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O95259}. Cell projection, dendrite {ECO:0000269|PubMed:24495567}. Cell projection, axon {ECO:0000269|PubMed:24495567}. Presynaptic cell membrane {ECO:0000269|PubMed:25556795}. Perikaryon {ECO:0000269|PubMed:24495567}. Postsynaptic density membrane {ECO:0000269|PubMed:24495567}. Early endosome membrane {ECO:0000250|UniProtKB:O95259}. Note=Perinuclear KCNH1 is located to NPC-free islands. {ECO:0000250|UniProtKB:O95259}.
Interaction partners:
- Calmodulin-1
- Calmodulin 2, pseudogene 2
- Voltage-gated potassium channel subunit beta-1
- Voltage-gated potassium channel subunit beta-2
- Voltage-gated potassium channel subunit beta-3
- A-type voltage-gated potassium channel KCND1
- Potassium voltage-gated channel subfamily B member 1
Sequence:
MTMAGGRRGLVAPQNTFLENIVRRSNDTNFVLGNAQIVDWPIVYSNDGFCKLSGYHRAEVMQKSSACSFMYGELTDKDTVEKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRNEQDKVVLFLCTFSDITAFKQPIEDDSCKGWGKFARLTRALTSSRGVLQQLAPSVQKGENVHKHSRLAEVLQLGSDILPQYKQEAPKTPPHIILHYCVFKTTWDWIILILTFYTAILVPYNVSFKTRQNNVAWLVVDSIVDVIFLVDIVLNFHTTFVGPAGEVISDPKLIRMNYLKTWFVIDLLSCLPYDVINAFENVDEGISSLFSSLKVVRLLRLGRVARKLDHYIEYGAAVLVLLVCVFGLAAHWMACIWYSIGDYEIFDEDTKTIRNNSWLYQLALDIGTPYQFNGSGSGKWEGGPSKNSVYISSLYFTMTSLTSVGFGNIAPSTDIEKIFAVAIMMIGSLLYATIFGNVTTIFQQMYANTNRYHEMLNSVRDFLKLYQVPKGLSERVMDYIVSTWSMSRGIDTEKVLQICPKDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDEVVAILGKGDVFGDVFWKEATLAQSCANVRALTYCDLHVIKRDALQKVLEFYTAFSHSFSRNLILTYNLRKRIVFRKISDVKREEEERMKRKNEAPLILPPDHPVRRLFQRFRQQKEARLAAERGGRDLDDLDVEKGNALTDHTSANHSLVKASVVTVRESPATPVSFQAASTSTVSDHAKLHAPGSECLGPKAGGGDPAKRKGWARFKDACGKGEDWNKVSKAESMETLPERTKASGEATLKKTDSCDSGITKSDLRLDNVGEARSPQDRSPILAEVKHSFYPIPEQTLQATVLEVKHELKEDIKALNAKMTSIEKQLSEILRILMSRGSSQSPQDTCEVSRPQSPESDRDIFGAS
Protein: Candida glabrata strain CBS138 chromosome M complete sequence (Q6FJ80)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Secreted, cell wall {ECO:0000256|ARBA:ARBA00004191}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome A complete sequence
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome F complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- Lysophospholipase 1
Sequence:
MQYKKSLAATALLASSGLAAYVPGNPWSTLTPSGTYKGGLTDYSSTFGIAVQPIATSSSVAKRAVSQIGDGQVQAATKTQAAPVSQIGDGQIQATTKTQAAPVSQIGDGQIQAATKTQAAPVSQIGDGQIQAATKTQAAPVSQIGDGQIQAATKTQAAPVSQIGDGQIQATTKTQAAPVSQIGDGQIQATTKTTQAASQIGDGQVQAATKTASAASQIADGQVQQNKDPKDPVGAVSCKVDGTLQMNLKGGILTDEKGRIGSIVANRQFQFDGPPPQAGAIYAAGWSLTPQGNLALGDSDVFYQCLSGNFYNLYDQSIGAQCHPVHLSAIDLVKC
Protein: Probable prolyl 4-hydroxylase 3 (AtP4H3) (EC 1.14.11.2) (Q9LN20)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in proline-rich peptide sequences of plant glycoproteins and other proteins. Hydroxyprolines are important constituent of many plant cell wall glycoproteins such as extensins, hydroxyproline-rich glycoproteins, lectins and arabinogalactan proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q24JN5}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q24JN5}.
Interaction partners:
- Pyrroline-5-carboxylate reductase
- Proline iminopeptidase
- Proline dehydrogenase 2, mitochondrial
- Proline dehydrogenase 1, mitochondrial
- procollagen-proline 3-dioxygenase
- Delta-9 desaturase-like 1 protein
Sequence:
MAKLRHSRFQARKWSTLMLVLFMLFMLTIVLLMLLAFGVFSLPINNDESSPIDLSYFRRAATERSEGLGKRGDQWTEVLSWEPRAFVYHNFLSKEECEYLISLAKPHMVKSTVVDSETGKSKDSRVRTSSGTFLRRGRDKIIKTIEKRIADYTFIPADHGEGLQVLHYEAGQKYEPHYDYFVDEFNTKNGGQRMATMLMYLSDVEEGGETVFPAANMNFSSVPWYNELSECGKKGLSVKPRMGDALLFWSMRPDATLDPTSLHGGCPVIRGNKWSSTKWMHVGEYKI
Protein: Zinc finger CCHC-type containing 7 (X6R4A7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MFGGYETIEAYEDDLYRDESSSELSVDSEVEFQLYSQIHYAQDLDDVIREEEHEEKNSGNSESSSSKPNQKKLIVLSDSEVIQLSDGSEVITLSDEDSIYRCKGKNVRVQAQENAHGLSSSLQSNELVDKKCKSDIEKPKSEERSGVIREVMIIEVSSSEEEESTISEGDNVESWMLLGCEVDDKDDDILLNLVGCENSVTEGQE
Protein: RNA-binding protein, putative (Q57YP5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- MIF4G domain-containing protein
- RRM domain-containing protein
- RNA-binding protein, putative
- RNA-binding protein, putative
- Regulator of nonsense transcripts 1, putative
- Probable eukaryotic initiation factor 4A
- C3H1-type domain-containing protein
- C3H1-type domain-containing protein
- Splicing factor TSR1
- Poly
Sequence:
MEDNLAAEIARIEAELEADRQQREKQQQQQQQQQQQQQHQMSMQNMMPSFGVSAVPQPMQHQHQHQQSQQQSPQQMGVLHGQVSGSTSHAPGQPHHFSKDSDGRSIFVGNLPKGDNGGPTTTPEELAHLFADCGPILNCTLLRDRTTGELKGTAYVEFSTYTGMGKAIDTKNNTMFKGSTLIVC
Protein: Heat stress transcription factor A-3 (AtHsfA3) (AtHsf-17) (Q8GYY1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE). Involved in heat stress response. Activated by DREB2A under heat stress.
Subcellular location: Nucleus {ECO:0000269|PubMed:18261981}. Note=Detected under heat stress condition.
Interaction partners:
- Dehydration-responsive element-binding protein 2A
- Dehydration-responsive element-binding protein 2C
- Heat shock 70 kDa protein 4
- Heat shock protein 90-1
- L-ascorbate peroxidase 2, cytosolic
- Chaperone protein ClpB1
- Heat shock protein 21, chloroplastic
- 18.1 kDa class I heat shock protein
- Multiprotein-bridging factor 1c
- Protein HEAT-STRESS-ASSOCIATED 32
Sequence:
MSPKKDAVSKPTPISVPVSRRSDIPGSLYVDTDMGFSGSPLPMPLDILQGNPIPPFLSKTFDLVDDPTLDPVISWGLTGASFVVWDPLEFARIILPRNFKHNNFSSFVRQLNTYGFRKIDTDKWEFANEAFLRGKKHLLKNIHRRRSPQSNQTCCSSTSQSQGSPTEVGGEIEKLRKERRALMEEMVELQQQSRGTARHVDTVNQRLKAAEQRQKQLLSFLAKLFQNRGFLERLKNFKGKEKGGALGLEKARKKFIKHHQQPQDSPTGGEVVKYEADDWERLLMYDEETENTKGLGGMTSSDPKGKNLMYPSEEEMSKPDYLMSFPSPEGLIKQEETTWSMGFDTTIPSFSNTDAWGNTMDYNDVSEFGFAAETTSDGLPDVCWEQFAAGITETGFNWPTGDDDDNTPMNDP
Protein: Eukaryotic translation initiation factor 4E type 2 (eIF-4E type 2) (eIF4E type 2) (eIF4E-2) (mRNA cap-binding protein type 2) (Eukaryotic translation initiation factor 4E-like 3) (eIF4E-like protein 4E-LP) (Q8BMB3)
Organism: Mus musculus (Mouse)
Function: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation. Acts as a repressor of translation initiation (By similarity). In contrast to EIF4E, it is unable to bind eIF4G (EIF4G1, EIF4G2 or EIF4G3), suggesting that it acts by competing with EIF4E and block assembly of eIF4F at the cap. In P-bodies, component of a complex that promotes miRNA-mediated translational repression (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O60573}. Cytoplasm, P-body {ECO:0000250|UniProtKB:O60573}.
Interaction partners:
- Eukaryotic translation initiation factor 4 gamma 3
- RNA-binding protein 4
- GRB10-interacting GYF protein 2
- Eukaryotic initiation factor 4A-I
- Eukaryotic translation initiation factor 4 gamma 1
- Eukaryotic translation initiation factor 4 gamma 2
- Eukaryotic translation initiation factor 4E-binding protein 1
- Eukaryotic translation initiation factor 4E
- GRB10-interacting GYF protein 1
- Eukaryotic translation initiation factor 4E type 1B
Sequence:
MNNKFDALKDDDSGDHDQNEENSTQKDGEKEKTDRDKSQSSGKRKAVVPGPAEHPLQYNYTFWYSRRTPGRPTSSQSYEQNIKQIGTFASVEQFWKFYSHMVRPGDLTGHSDFHLFKEGIKPMWEDDANKNGGKWIIRLRKGLASRCWENLILAMLGEQFMVGEEICGAVVSVRFQEDIISIWNKTASDQATTARIRDTLRRVLNLPPNTIMEYKTHTDSIKMPGRLGPQRLLFQNLWKPRLNVP
Protein: Ankyrin repeat domain-containing protein 2 (Skeletal muscle ankyrin repeat protein) (hArpp) (Q9GZV1)
Organism: Homo sapiens (Human)
Function: Functions as a negative regulator of myocyte differentiation. May interact with both sarcoplasmic structural proteins and nuclear proteins to regulate gene expression during muscle development and in response to muscle stress.
Subcellular location: Cytoplasm, myofibril, sarcomere, I band {ECO:0000250}. Cytoplasm, cytosol. Nucleus. Nucleus, PML body. Note=In the sarcoplasm of differentiated striated muscle cells, where it is cytosolic and enriched in the I band. In nucleus and PML bodies of proliferating and undifferentiated myoblasts. Associates with the euchromatin in the nucleus of myocytes upon muscle stress.
Interaction partners:
- Titin
- Telethonin
- Myopalladin
- Y-box-binding protein 1
- Cysteine and glycine-rich protein 3
- LIM domain-binding protein 3
- Myozenin-2
Sequence:
MAKAPSWAGVGALAYKAPEALWPAEAVMDGTMEDSEAVQRATALIEQRLAQEEENEKLRGDARQKLPMDLLVLEDEKHHGAQSAALQKVKGQERVRKTSLDLRREIIDVGGIQNLIELRKKRKQKKRDALAASHEPPPEPEEITGPVDEETFLKAAVEGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKLLSTPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTPTDLVQLWQADTRHALEHPEPGAEHNGLEGPNDSGRETPQPVPAQ
Protein: Uncharacterized protein (Q586Y4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Pre-mRNA-splicing factor SLU7
Sequence:
MASVVAFLFPLIVHQPTPFHVFVSLFFFFFNGLLGSTQAVAAVALVWKRMSATPQLGGETDTSGDVRSRVGSQLLLRKFPLLAKARAYAQETPDDPRAECNLLCYGSDVYRIYSLTSAEMDGSGVIFSNPQKRQRTDDEPSNGDGGALLRSIDDRVALPTQLGFLTLLENELRRSETALRSAAQKSKTPEKETTDDNEKGKKAKNRDGTVSHSQEGGEGKTTQNDSGVERGFPHHKEEDRLILEAIRKPLDGGMRSAGAHNNGSCGSEKAPGGDQNSSRGVAGSGKVEERLQWEIMAESIMSRSEVVAGTEGTGGDAVRSYLRRVAWIEQQKGRQSLTNSAAETAPHGEQLWSNMTEAARVQKEIMRMRAQRKQFHRERKKGE
Protein: Angiotensin-converting enzyme 2 (EC 3.4.17.23) (ACE-related carboxypeptidase) (EC 3.4.17.-) [Cleaved into: Processed angiotensin-converting enzyme 2] (Q56NL1)
Organism: Paguma larvata (Masked palm civet)
Function: Essential counter-regulatory carboxypeptidase of the renin-angiotensin hormone system that is a critical regulator of blood volume, systemic vascular resistance, and thus cardiovascular homeostasis. Converts angiotensin I to angiotensin 1-9, a nine-amino acid peptide with anti-hypertrophic effects in cardiomyocytes, and angiotensin II to angiotensin 1-7, which then acts as a beneficial vasodilator and anti-proliferation agent, counterbalancing the actions of the vasoconstrictor angiotensin II. Also removes the C-terminal residue from three other vasoactive peptides, neurotensin, kinetensin, and des-Arg bradykinin, but is not active on bradykinin. Also cleaves other biological peptides, such as apelins, casomorphins and dynorphin A. Plays an important role in amino acid transport by acting as binding partner of amino acid transporter SLC6A19 in intestine, regulating trafficking, expression on the cell surface, and its catalytic activity.
Subcellular location: [Processed angiotensin-converting enzyme 2]: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9BYF1}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q8R0I0}. Cell projection, cilium {ECO:0000250|UniProtKB:Q9BYF1}. Apical cell membrane {ECO:0000250|UniProtKB:Q9BYF1}. Note=Detected in both cell membrane and cytoplasm in neurons. {ECO:0000250|UniProtKB:Q8R0I0}.
Interaction partners:
Sequence:
MSGSFWLLLSFAALTAAQSTTEELAKTFLETFNYEAQELSYQSSVASWNYNTNITDENAKNMNEAGAKWSAYYEEQSKLAQTYPLAEIQDAKIKRQLQALQQSGSSVLSADKSQRLNTILNAMSTIYSTGKACNPNNPQECLLLEPGLDNIMENSKDYNERLWAWEGWRAEVGKQLRPLYEEYVALKNEMARANNYEDYGDYWRGDYEEEWTGGYNYSRNQLIQDVEDTFEQIKPLYQHLHAYVRAKLMDTYPSRISRTGCLPAHLLGDMWGRFWTNLYPLTVPFGQKPNIDVTDAMVNQNWDARRIFKEAEKFFVSVGLPNMTQGFWENSMLTEPGDGRKVVCHPTAWDLGKGDFRIKMCTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPNHLKTIGLLSPAFSEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGAIPKEQWMQKWWEMKRNIVGVVEPVPHDETYCDPASLFHVANDYSFIRYYTRTIYQFQFQEALCQIAKHEGPLHKCDISNSTEAGKKLLEMLSLGRSEPWTLALERVVGAKNMNVTPLLNYFEPLFTWLKEQNRNSFVGWDTDWRPYSDQSIKVRISLKSALGEKAYEWNDNEMYLFRSSIAYAMREYFSKVKNQTIPFVEDNVWVSDLKPRISFNFFVTFSNNVSDVIPRSEVEDAIRMSRSRINDAFRLDDNSLEFLGIEPTLSPPYRPPVTIWLIVFGVVMGAIVVGIVLLIVSGIRNRRKNDQAGSEENPYASVDLNKGENNPGFQHADDVQTSF
Protein: Glucose-6-phosphate 3-dehydrogenase (EC 1.1.1.361) (O07564)
Organism: Bacillus subtilis (strain 168)
Function: Involved in the biosynthesis of kanosamine (3-amino-3-deoxy-D-glucose), which is known to have antibiotic and antifungal properties, and to be a precursor of the antibiotic neotrehalosadiamine (3,3'-diamino-3,3'-dideoxy-alpha,beta-trehalose (NTD)). Catalyzes the oxidation of glucose 6-phosphate to 3-oxo-D-glucose 6-phosphate. It can only use NAD.
Interaction partners:
- 3-oxo-glucose-6-phosphate:glutamate aminotransferase
- Kanosamine-6-phosphate phosphatase
- Putative oxidoreductase YteT
- Inosose dehydratase
- 5-deoxy-glucuronate isomerase
- 3D-
- Glucose/mannose transporter GlcP
- Uncharacterized protein YfiH
- Uncharacterized protein YezA
- Uncharacterized N-acetyltransferase YhfO
Sequence:
MKKIGIIGAGGIARAHATALSTIKNAELVGVYDINQQNAESFVKTFGGKSFENVDELIDASEGLIVASPNFCHKEHALQALGKHKHVLCEKPMAISLEEASIMKDTAERLSVRASMGFNYRYLSYVNILKSLIINNELGNILSIKVHFKKNSALRRKKFTWRDDANSKKTSGSLGDLGIHLIDMVWYLFESDFITESVRAKMNTNVKTKEDKQVLVDDYAEIYGQLKNKVFVNIITSKCSVPEDCGFSIEVVGHKKEFKYHTGNPHVYKLIDGLNVVDCPVPQSLLNDPPNEFYGWADSFRSELINWIASTQNDWVEIPSFSDGFRSQEVLEMFFEKDSNSQPMSVSAVN
Protein: QWRF motif-containing protein 2 (Q94AI1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Subtilisin-like protease SBT1.4
- T-complex protein 1 subunit gamma
- Protein disulfide isomerase pTAC5, chloroplastic
Sequence:
MVAAAISTTDPRNPPRDRPQSLTNNGGQRRPRGKQVPSRYLSPSPSHSVSSTTTTTTTTTTTTSSSSSSSSSAILRTSKRYPSPSPLLSRSTTNSASNSIKTPSLLPKRSQSVDRRRPSAVSVTVGTEMSAATKMLITSTRSLSVSFQGEAFSLPISKKKETTSTPVSHRKSTPERRRSTPVRDQRENSKPVDQQRWPGASRRGNSESVVPNSLSRSLDCGSDRGKLGSGFVGRSMLHNSMIDESPRVSVNGRLSLDLGGRDEYLDIGDDIQRRPNNGLTSSVSCDFTASDTDSVSSGSTNGVQECGSGVNGEISKSKSLPRNIMASARFWQETNSRLRRLQDPGSPLSSSPGLKTSSISSKFGLSKRFSSDAVPLSSPRGMASPVRGSAIRSASPSKLWATTTSSPARALSSPSRARNGVSDQMNAYNRNNTPSILSFSADIRRGKIGEDRVMDAHLLRLLYNRDLQWRFVNARADSTVMVQRLNAEKNLWNAWVSISELRHSVTLKRIKLLLLRQKLKLASILRGQMGFLEEWSLLDRDHSSSLSGATESLKASTLRLPIVGKTVVDIQDLKHAVSSAVDVMQAMSSSIFSLTSKVDEMNSVMVETVNVTAKEKVLLERCQGCLSRVAAMQVTDCSMKTHIIQLSRIPITSSLTPQL
Protein: Protein FAM98C (Q17RN3)
Organism: Homo sapiens (Human)
Interaction partners:
- ATP-dependent RNA helicase DDX1
- RNA transcription, translation and transport factor protein
Sequence:
MEAVKAEAWEGAAVAQDLLALGYGGVPGAASRGASCPDFRGLCVRLAAELATLGALEQQREAGAEVLSAGDGPGAEEDFLRQLGSLLRELHCPDRALCGGDGAAALREPGAGLRLLRFLCSELQATRLLCLRSLLDPSPRPPLGEGVVEGAGMVQELDLTLQALGLPRPAPGTPASQLLQELHAKISELQPSLPPGSLQPLLSCSLDAPRWEALESLSQSLRDQYRCRRCLLLKRLDLTTSAFHWSDRAEAQGEAMRAVLIPIREVLTPESDISIAHVLAARADLSCLVPATSVAVRRGTCCAINKVLMGNVPDRGGRPNELEPPMPTWRSRREDGGPQCWGRKKKKKK
Protein: Transient receptor potential cation channel, subfamily C, member 5 (A0A0G2K149)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Short transient receptor potential channel 1
- Short transient receptor potential channel 4
- Voltage-dependent T-type calcium channel subunit alpha-1H
- Bone morphogenetic protein receptor type-2
- Voltage-dependent T-type calcium channel subunit alpha-1G
- Short transient receptor potential channel 3
- Stromal interaction molecule 1
- Transient receptor potential cation channel subfamily A member 1
- Na
- Calmodulin-1
Sequence:
MAQLYYKKVNYSPYRDRIPLQIVRAETELSAEEKAFLSAVEKGDYATVKQALQEAEIYYNVNINCMDPLGRSALLIAIENENLEIMELLLNHSVYVGDALLYAIRKEVVGAVELLLSYRKPSGEKQVPTLMMDTQFSEFTPDITPIMLAAHTNNYEIIKLLVQKRVTIPRPHQIRCNCVECVSSSEVDSLRHSRSRLNIYKALASPSLIALSSEDPILTAFRLGWELKELSKVENEFKAEYEELSQQCKLFAKDLLDQARSSRELEIILNHRDDHSEELDPQKYHDLAKLKVAIKYHQKEFVAQPNCQQLLATLWYDGFPGWRRKHWVVKLLTCMTIGFLFPMLSIAYLISPRSNLGLFIKKPFIKFICHTASYLTFLFMLLLASQHIVRTDLHVQGPPPTVVEWMILPWVLGFIWGEIKEMWDGGFTEYIHDWWNLMDFAMNSLYLATISLKIVAYVKYNGSRPREEWEMWHPTLIAEALFAISNILSSLRLISLFTANSHLGPLQISLGRMLLDILKFLFIYCLVLLAFANGLNQLYFYYETRAIDEPNNCKGIRCEKQNNAFSTLFETLQSLFWSVFGLLNLYVTNVKARHEFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFARTKLWMSYFDEGGTLPPPFNIIPSPKSFLYLGNWFNNTFCPKRDPDGRRRRHNLRSFTPEKKTEYLFVRYVAAMIRNSKTNEGLTEENFKELKQDISSFRYEVLDLLGNRKHPRRSFSTSSAEFSQRDDTNDGSGGARAKSKSVSFNLGCKKKACQGAPLIRTMPRASGAQGKPKAESSGKRSFMGPSFKKLGLLFSKFNGQTSEPTSEPMYTISDGIAQQHSMWQDIRYSQMEKGKAEACSQSEMNLSEVELGEIRGAARSSECPLACSSSLHCASGICSSNSKLLDSSEDVFETWGEACDLLMHKWGDGQEEQVTTRL
Protein: Candida glabrata strain CBS138 chromosome A complete sequence (Q6FYB2)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- ATP-dependent RNA helicase SUB2
- mRNA export factor MEX67
- THO complex subunit 2
- ATP-dependent RNA helicase FAL1
- Candida glabrata strain CBS138 chromosome K complete sequence
- Candida glabrata strain CBS138 chromosome J complete sequence
- Candida glabrata strain CBS138 chromosome G complete sequence
- Pre-mRNA-splicing factor CWC22
- Nucleoporin NSP1
- Pre-mRNA-splicing factor SLU7
Sequence:
MSANLDKSLDEIIGSKKTARPSNRTRAGHAARPKRAAKQINPRRRVVPGRRAVSKPVAAPASAAVARAASLLHGTREARVTVEGLPRDIKQDAVREFFQSQVGGVQRVLLSYNERGQSTGMANVTFRNGELAKKAVAQFSGAPIDGGKSRLRLNIVVDPTVQPARPLTERIRAISRERVVAQKAKPVKGPSKKAAAVKARKQKPKAKKEKQPKKNLEDLDKEMADYFGEGKN
Protein: Bardet-Biedl syndrome 10 protein (Bbs10 protein) (A4QP63)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MQQQLECVSLQVCVSVLGPLESVVRRCLGPEGGSVLFTRDTGETLISRHGQRVLSTLHLEHPMARMVLDCVCAHAKSTGDGTKSFILLLSALLRAIQGSAHMRRKASWSNPALQNLANRLMALSRNELDDIIIYQVTPYASSYCSHHSDKLEHSILDYLISGYISGRTGAGQAEILKHILCEFYYKSKRDQNTTETISFIHSHFNVLHTRVAGLPVGCSEVIEGLVVTRDWSVWTELRGPIKALVLYESFGSSLGDNITVCFQQDWLSRTESITKQKLAYLLELQVNVVLSSVKQPECVLQWARMNHVALLECVDSDQLDFLCNISFPETLSHLQHIVMLKYCKRLQLGGLRCAQLGIYSNVHTLVLCAPAPGLLDQTVCVSRGVFLMLQHITRTLESNQFKSSSVDQSQCTVSSQGLWRAVMQAGGVLPVGGVFEFLLHHFLLTRRTSDPESCRLLAEALLCVPRALYAHNHRRFLNIQTCFFNDLKKWDRTSVGDPVKFEFGFSEGLCLESVSGKQQLVVSVLECLHRLLCVGAILYTRSLLRPQIYSEEDEEEEEEVHTNSI
Protein: Keratin-associated protein 9-7 (Keratin-associated protein 9-like 1) (A8MTY7)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins (By similarity).
Interaction partners:
Sequence:
MTHCCSPCCQPTCCRTTCWKPTTVTTCSSTPCCQPSCCVSSCCQPCCHPTCCQNTCCRTTCCQPTCVTSCCQPSCCSTPCCQPICCGSSCCGQTSCGSSCCQPSSCAPIYCRRTCYHPTSVYLPGCLNQSCGSSCCQPCCRPACCETTCCRTTCFQPTCVTSCCQPACC