wanglab/gogpt-training-data huggingface dataset:
Protein: Gap junction gamma-1 protein (Connexin-45) (Cx45) (Gap junction alpha-7 protein) (P36383)
Organism: Homo sapiens (Human)
Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Subcellular location: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction.
Interaction partners:
- Gap junction alpha-1 protein
- Gap junction alpha-5 protein
- Gap junction delta-2 protein
- Gap junction beta-6 protein
- Gap junction epsilon-1 protein
- Tight junction protein 1
- Gap junction alpha-4 protein
- Gap junction beta-2 protein
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4
- Consortin
Sequence:
MSWSFLTRLLEEIHNHSTFVGKIWLTVLIVFRIVLTAVGGESIYYDEQSKFVCNTEQPGCENVCYDAFAPLSHVRFWVFQIILVATPSVMYLGYAIHKIAKMEHGEADKKAARSKPYAMRWKQHRALEETEEDNEEDPMMYPEMELESDKENKEQSQPKPKHDGRRRIREDGLMKIYVLQLLARTVFEVGFLIGQYFLYGFQVHPFYVCSRLPCPHKIDCFISRPTEKTIFLLIMYGVTGLCLLLNIWEMLHLGFGTIRDSLNSKRRELEDPGAYNYPFTWNTPSAPPGYNIAVKPDQIQYTELSNAKIAYKQNKANTAQEQQYGSHEENLPADLEALQREIRMAQERLDLAVQAYSHQNNPHGPREKKAKVGSKAGSNKSTASSKSGDGKTSVWI
Protein: Mitochondrial import inner membrane translocase subunit Tim9 (Q9Y5J7)
Organism: Homo sapiens (Human)
Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. May also be required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:11489896, ECO:0000269|PubMed:14726512}; Peripheral membrane protein {ECO:0000269|PubMed:11489896, ECO:0000269|PubMed:14726512}; Intermembrane side {ECO:0000269|PubMed:11489896, ECO:0000269|PubMed:14726512}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit Tim22
- Mitochondrial import inner membrane translocase subunit Tim10
- Mitochondrial import inner membrane translocase subunit Tim8 A
- Mitochondrial import inner membrane translocase subunit Tim13
- Mitochondrial import inner membrane translocase subunit Tim10 B
- Mitochondrial import inner membrane translocase subunit Tim29
- Acylglycerol kinase, mitochondrial
- Mitochondrial intermembrane space import and assembly protein 40
- Mitochondrial import inner membrane translocase subunit Tim8 B
- Mitochondrial import inner membrane translocase subunit Tim23
Sequence:
MAAQIPESDQIKQFKEFLGTYNKLTETCFLDCVKDFTTREVKPEETTCSEHCLQKYLKMTQRISMRFQEYHIQQNEALAAKAGLLGQPR
Protein: Inter-alpha-inhibitor H4 heavy chain (O35802)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MKSPAPAHMWNIVLVLLSLLAVLPITTTEKNGIDIYSLTVDSRVSSRFAHTVVTSRVVNRADTVQEATFQVELPRKAFITNFSMIIDGVTYPGLSKRRLKPEAIHCCCGRGESAGLVKTTGRKTEQFEVSVNVAPGSKTTFELIYQELLQRRLGMYELLLKVRPEQLVKHLQMTSTSLSPQGISTLETESTFMTQELANALTTSQNKTKAHIQFKPTLSQQRKSQNEQDTVLDGDFTVRYDVDRSSTGGYLQIENGYFVHHFAPEDLPTMAKNVLFVIDKSGSMAGKKIQQTREALIKILKDLSTQDQFNIIVFSGEANQWEQLLVQATEENLNRAVDYASKIPAQGGTNINKAVLSAVELLDKSNQAELLPSKSVSLIILLTDGEPTVGETNPKIIQKNTQEAINGRYSLFCLGFGFDVNYPFLEKLALDNGGLARRIYEDSDSALQLQDFYQEVANPLLSSVTFEYPSNAVEDVTRYNFQHHFKGSEMVVAGKLRDQGPDVLLAKVSGQMHLQNITFQTEASIAQQEKEFQGPKYIFHNFMERLWALLTIQQQLEQRISASGAELEALEAQVLNLSLKYNFVTPLTHMVVTKPEDQEQFQVAEKPTEVDGGVWSILSAVQRHFKTPTTGSKLLTSRLRGNRFQTLSRLGDGLVGSRQYMPPPGLPGPPGLPGPPGPPGHPHFASSIDYGRQPSLGRVLDLPSLSSQDPAGPSLAMLPKVVEQEGTTPEESPNPDHPRAPTIILPLPGSGVDQLCVDILHSEKPMKLFVDINQGLEVVGKYEKNIGFSWIEVTILKPHLQVHATPERLVVTRGRKNSEYKWKKTLFSVLPGLKMTMDKTGLLQLSGPDKVTISLLSLDDPQRGLMLLLNDTHHFSNDITGELGQFYQDIIWDDTKQTVRVLGIDYPATRELKLSYQDGFPGTEISCWTVKI
Protein: Zinc finger FYVE domain-containing protein 16 (Endofin) (Endosome-associated FYVE domain protein) (Q7Z3T8)
Organism: Homo sapiens (Human)
Function: May be involved in regulating membrane trafficking in the endosomal pathway. Overexpression induces endosome aggregation. Required to target TOM1 to endosomes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11546807}. Early endosome membrane {ECO:0000269|PubMed:11546807}; Peripheral membrane protein {ECO:0000269|PubMed:11546807}. Note=Localized to early endosomes. Membrane-associated, probably via its association with phosphatidylinositol 3-phosphate (PI3P).
Interaction partners:
- Tyrosine-protein phosphatase non-receptor type 23
- Target of Myb1 membrane trafficking protein
- Mothers against decapentaplegic homolog 3
- Mothers against decapentaplegic homolog 2
- Zinc finger FYVE domain-containing protein 9
- TOM1-like protein 2
- TOM1-like protein 1
- Mothers against decapentaplegic homolog 4
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
Sequence:
MDSYFKAAVSDLDKLLDDFEQNPDEQDYLQDVQNAYDSNHCSVSSELASSQRTSLLPKDQECVNSCASSETSYGTNESSLNEKTLKGLTSIQNEKNVTGLDLLSSVDGGTSDEIQPLYMGRCSKPICDLISDMGNLVHATNSEEDIKKLLPDDFKSNADSLIGLDLSSVSDTPCVSSTDHDSDTVREQQNDISSELQNREIGGIKELGIKVDTTLSDSYNYSGTENLKDKKIFNQLESIVDFNMSSALTRQSSKMFHAKDKLQHKSQPCGLLKDVGLVKEEVDVAVITAAECLKEEGKTSALTCSLPKNEDLCLNDSNSRDENFKLPDFSFQEDKTVIKQSAQEDSKSLDLKDNDVIQDSSSALHVSSKDVPSSLSCLPASGSMCGSLIESKARGDFLPQHEHKDNIQDAVTIHEEIQNSVVLGGEPFKENDLLKQEKCKSILLQSLIEGMEDRKIDPDQTVIRAESLDGGDTSSTVVESQEGLSGTHVPESSDCCEGFINTFSSNDMDGQDLDYFNIDEGAKSGPLISDAELDAFLTEQYLQTTNIKSFEENVNDSKSQMNQIDMKGLDDGNINNIYFNAEAGAIGESHGINIICEIVDKQNTIENGLSLGEKSTIPVQQGLPTSKSEITNQLSVSDINSQSVGGARPKQLFSLPSRTRSSKDLNKPDVPDTIESEPSTADTVVPITCAIDSTADPQVSFNSNYIDIESNSEGGSSFVTANEDSVPENTCKEGLVLGQKQPTWVPDSEAPNCMNCQVKFTFTKRRHHCRACGKVFCGVCCNRKCKLQYLEKEARVCVVCYETISKAQAFERMMSPTGSNLKSNHSDECTTVQPPQENQTSSIPSPATLPVSALKQPGVEGLCSKEQKRVWFADGILPNGEVADTTKLSSGSKRCSEDFSPLSPDVPMTVNTVDHSHSTTVEKPNNETGDITRNEIIQSPISQVPSVEKLSMNTGNEGLPTSGSFTLDDDVFAETEEPSSPTGVLVNSNLPIASISDYRLLCDINKYVCNKISLLPNDEDSLPPLLVASGEKGSVPVVEEHPSHEQIILLLEGESFHPVTFVLNANLLVNVKFIFYSSDKYWYFSTNGLHGLGQAEIIILLLCLPNEDTIPKDIFRLFITIYKDALKGKYIENLDNITFTESFLSSKDHGGFLFITPTFQKLDDLSLPSNPFLCGILIQKLEIPWAKVFPMRLMLRLGAEYKAYPAPLTSIRGRKPLFGEIGHTIMNLLVDLRNYQYTLHNIDQLLIHMEMGKSCIKIPRKKYSDVMKVLNSSNEHVISIGASFSTEADSHLVCIQNDGIYETQANSATGHPRKVTGASFVVFNGALKTSSGFLAKSSIVEDGLMVQITPETMNGLRLALREQKDFKITCGKVDAVDLREYVDICWVDAEEKGNKGVISSVDGISLQGFPSEKIKLEADFETDEKIVKCTEVFYFLKDQDLSILSTSYQFAKEIAMACSAALCPHLKTLKSNGMNKIGLRVSIDTDMVEFQAGSEGQLLPQHYLNDLDSALIPVIHGGTSNSSLPLEIELVFFIIEHLF
Protein: PTS-dependent dihydroxyacetone kinase 2, dihydroxyacetone-binding subunit DhaK (EC 2.7.1.121) (Q92EU2)
Organism: Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262)
Function: Dihydroxyacetone binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone via a phosphoryl group transfer from DhaL-ATP.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:22773791}.
Interaction partners:
- PEP-dependent dihydroxyacetone kinase 2, ADP-binding subunit DhaL
- PEP-dependent dihydroxyacetone kinase 2, phosphoryl donor subunit DhaM
- PEP-dependent dihydroxyacetone kinase 1, ADP-binding subunit DhaL
- PEP-dependent dihydroxyacetone kinase 1, phosphoryl donor subunit DhaM
- NAD-dependent glycerol dehydrogenase
- PTS-dependent dihydroxyacetone kinase 1, dihydroxyacetone-binding subunit DhaK
- Triosephosphate isomerase 2
- Ribose-5-P isomerase B
- Glycerol-3-phosphate dehydrogenase
- Glycerol-3-phosphate dehydrogenase [NAD
Sequence:
MRRLVNDGYEAVEEMLAGYVAAQGKYVDFAENDKRVIVSKQMSEEPRVRIIVGGGSGHEPLFLGYVGKDFADAAVVGNINTSPSPEPCYNAVKAVDSGKGCLYMYGNYAGDVMNFDMGAEMAADDGIRVETVLVTDDIYSAENVEDRRGVAGDLIVFKAAASAAAKGLDLDAVKQAAEKANANTFSMGVALSSSTLPVTGKAIFEMKEGEMEVGMGIHGEPGIKRTSIEPADKVVDQIMGYLIEEMKLTAGEEVHVLINGLGGLPVMDQYICYRRVDEILKEKGVHIHSPLVGNYATSMDMIGMSITLVRLDDELKDLLDTPCDTPYFKVD
Protein: Glutamine synthetase (EC 6.3.1.2) (A8WCU7)
Organism: Gossypium raimondii (Peruvian cotton) (Gossypium klotzschianum subsp. raimondii)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- glutamate synthase
- glutamate synthase
- Ferredoxin--nitrite reductase, chloroplastic
- glutamine--fructose-6-phosphate transaminase
- glutamate dehydrogenase
- Aldehyde dehydrogenase domain-containing protein
- Formamidase
- Carbamoyl phosphate synthase small chain, chloroplastic
- Carbamoyl phosphate synthase arginine-specific large chain, chloroplastic
- Carbamoyl phosphate synthase small chain, chloroplastic
Sequence:
MSLLTDLVNLNLSDCTDKIIAEYIWIGGSGMDLRSKARTLSGPVSDPSKLPKWNYDGSSTGQAPGEDSEVILYPQAIFKDPFRRGNNILVMCDAYTPAGEPIPTNKRCNAAKIFSHPDVAAEEPWYGIEQEYTLLQKDVKWPIGWPLGGYPGPQGPYYCGVGVDKAYGRDIVDSHYKACLYAGINISGINGEVMPGQWEFQVGPAVGISAGDELWVARYILERITETAGVVLSFDPKPIQGDWNGAGAHTNYSTKSMRSDGGYEVIKKAIEKLGLRHKEHIAAYGEGNERRLTGRHETADINTFLWGVANRGASIRVGRDTEKAGKGYFEDRRPASNMDPYVVTSMIAETTILWKP
Protein: Calpain-7 (EC 3.4.22.-) (PalB homolog) (PalBH) (Q9R1S8)
Organism: Mus musculus (Mouse)
Function: Calcium-regulated non-lysosomal thiol-protease.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Calpain small subunit 2
- Calpain small subunit 1
- Calpastatin
Sequence:
MDASALERDAVQFARLAVQRDHEGRYSEAVFYYKEAAQALIYAEMAGSSLERIQEKINEYLERVQALHSAVQSKSTDPLKSKHQLDLERAHFLVTQAFDEDEKGNVEDAIELYTEAVELCLKTSSETADKTLQNKLKQLARQALDRAEALSEPLTKPFCKLKSANMKTKTPPVRTHFPLGPNPFVEKPQAFISPQSCDAQGQKYTAEEIEVLRTTSKINGVEYVPFMSVDLRERFAYPMPFCDRLGKLPLSPKQKTTFSKWVRPEDLTNNPTMIYTVSSFSIKQTIVSDCSFVASLAISAAYERRFNKKLITSIIYPQNKDGEPEYNPCGKYMVKLHLNGVPRKVIIDDQLPVDHKGELLCSYSNNKSELWVSLIEKAYMKVMGGYDFPGSNSNIDLHALTGWIPERIAMHSDSQTFSKDNSFRMLYQRFHKGDVLITASTGVMTEAEGEKWGLVPTHAYAVLDIREFKGLRFIQLKNPWSHLRWKGRYSENDVKNWTPELQKYLNFDPRTAQKIDNGIFWISWDDLCQYYDVVYLSWNPALFKESTCIHSTWDAKQGPVKDAYSLANNPQYKLEVQCPQGGAAVWVLLSRHITDKDDFANNREFITMVVYKTDGKKVYYPADPPPYIDGIRINSPHYLTKIKLTTPGTHTFTLVVSQYEKQNTIHYTVRVYSACSFTFSKIPSPYTLSKRINGKWSGQSAGGCGNFQETHKNNPIYQFHIDKTGPLLIELRGPRQYSVGFEVVAVSIMGDPGPHGFQRKSSGDYRCGFCYLELENIPAGIFNIIPSTFLPKQEGPFFLDFNSTVPIKTTQLQ
Protein: Metal transporter nramp1 homolog (Natural resistance-associated membrane protein 1) (Q869V1)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Depletes iron from the phagolysosome in an ATP-dependent process. May rather act as a symporter of protons and metal cations in an ATP-dependent process. Nramp1 overexpression protected cells from L.pneumophila infection.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Located at vesicles of variable size, which are distributed all over the cytoplasm, in part clustered at a perinuclear site. Several tiny vesicles travel rapidly outward from and towards the perinuclear cluster. These vesicles are part of the endo- and phagolysosomal pathway. {ECO:0000269|PubMed:16445684}.
Interaction partners:
Sequence:
MTPRIESEESAPLVNKNNNNNNDNNNNNNVDEENPLIIESGIPIEDLEQKNKPYLIKVPNIDKPDSKWINFKTLWAFTGPGFLMSIAYLDPGNLESDIQAGAMAGYQLLWVLFWSTVIGFWLQMLASRLGVVTGKHLAEHCREQYPKTPRLLLWLMTELAIIGSDIQEVIGTAIALQILSNGHIPLWAGVLFTAADTFTFLFLEKYGIRKLEAFFCSLIAIMAISFGVEYIISKPDQIEVVKGVFIPLCSQNNISQAVGILGAVVMPHNIYLHSALVQSREIDRKSETQVKIANKYNRLESAFALIISFIINLLLVSVFAKGFYGETTEIGLSSAADFLMDKYGKVAKYIWAIGLFSAGQCSTMTGTYSGQFVMEGFLKLKIAPWKRLLITRCTAIVPAMVVAILSTSHLDSLDQWLNILQSIQLPFAVVPVLLFTSSEKIMGSKFKNHWLNNQFVRFLSLLIIAINIYLIITFSMQISESAWMISIVSISFFFYFIFIVYLSMGQENFNSMTKKIKNLFNNNSNQTYNNINY
Protein: Probable galaptin lec-8 (Q09610)
Organism: Caenorhabditis elegans
Interaction partners:
- Transmembrane protein
- Bacterial colonization factor
Sequence:
MHTINSPDVPSAHAIREQLRAGSEIHVRGHVTHKHHKDFSVELLSGPHIVLHVNFRFEHDHIVAMNTCTNGAWGAEIRHHNPLKHHDHFNLSIHVHEGYYHISVNGEHLADFPHRFPVESVQAIGLKGAAHIDEISFSGFEFGVDWNSQHDFGHAGYNSYGTETYVAPVFQETHSYNAYF
Protein: RNA pyrophosphohydrolase (EC 3.6.1.-) ((Di)nucleoside polyphosphate hydrolase) (Q9X4P2)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage.
Interaction partners:
- Ribonuclease R
- Diaminopimelate epimerase
- NAD-capped RNA hydrolase NudC
- Ribonuclease E
- Bifunctional NAD
- RNA-binding protein Hfq
- Bis
- phosphoenolpyruvate--protein phosphotransferase
- ADP-ribose pyrophosphatase
- Sensor domain-containing diguanylate cyclase
Sequence:
MIDSDGFRPNVGIILANEAGQVLWARRINQEAWQFPQGGINDRETPEEALYRELNEEVGLEAGDVRILACTRGWLRYRLPQRLVRTHSQPLCIGQKQKWFLLRLMSDEARVRMDITSKPEFDGWRWVSYWYPLGQVVTFKREVYRRALKELAPRLLARD
Protein: Exit protein of rhodopsin and TRP B, isoform A (Exit protein of rhodopsin and TRP B, isoform B) (GH25417p) (E1JIQ5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Exit protein of rhodopsin and TRP A
- Endoplasmic reticulum chaperone BiP
- Heat shock protein 27
- Heat shock protein 83
Sequence:
MVGPFMQGLFLIGIIYWYSKGMMSMINDYYRSEFQRKLQTEPAKTRAETPINVDNFMDYVRELDTPDEVARIPAEGTESPPMGNTYCHILRRFLEITGTLPPFDVCLVTSNIR
Protein: G2/mitotic-specific cyclin-B (P20439)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential for the control of the cell cycle at the G2/M (mitosis) transition.
Interaction partners:
- Cyclin-dependent kinase 1
- Serine/threonine-protein kinase polo
- Fizzy-related protein homolog
- G2/mitotic-specific cyclin-B3
- Cell division cycle protein 20 homolog
- G2/mitotic-specific cyclin-A
- Wee1-like protein kinase
- M-phase inducer phosphatase
- Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase
- Cyclin-dependent kinases regulatory subunit
Sequence:
MVGTTLKMRGDENASENFKQVQLKKLTVPSMEATTKRAALGDLQNRGISRPIAAKDAAQKDSKDLKLTDALRNAKARVDSHWKKQPLGSTNGNGNGAVPPKVNEGGVSAFLRSNSVRNRVPTKTTVEPTKVTVKSSSSENVNEPTLKREDSNLSKKSLTKLRAALAKPVMGVSGIRREPVAVSRKEAETKKELPETKKDSLEVKKDATRMPLIRGNSAVTTTTSTMPTTMSLSSKRLAGIEDIDANDKENLVLVSEYVNDIYDYLYQVELEQPIHKDHLAGQKEVSHKMRAVLIDWINEVHLQFHLAAETFQLAVAIIDRYLQVVKDTKRTYLQLVGVTALFIATKYEELFPPAIGDFVFITDDTYTARQIRQMELQIFKAIDCNLSRPLPIHFLRRYSKAAGAEDEHHTMSKYFIELASVDYEMATYRPSEIAAASLFLSLHLLNGNHRAGTGFNDRHWTPTLTFYSRYSAAHLRPITRLIAKLARDAPQAKLKAIYNKYQGSKFQKIALRTELTGALMDSIVGQSQRK
Protein: EID1-like F-box protein 2 (Q9FLZ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein HUA2-LIKE 3
- Phytochrome A-associated F-box protein
- Scarecrow-like protein 30
Sequence:
MIIAKQYRCIHSATCHCTKGHLSEEVLFLMVQHLNWNPNVIATLSCVCKWFDDLAKRLLWKEFCRARAPKMMSDLQSSGSHSVDGSWRALGKLLIYCSGSSKGGLFNDVQISGHFVHRTRFSRTSGRSFLPPQCRTDDILYVSDPCEHLDQGEDGDLGFFRGIFKSFSMSKVRKLLIKKGTPFHPTEVCPYCKAKLWSMLQAKMIPQSASCRLGAYEDSIEYYVCLNGHMLGVCTLLPLSDSEGASEFQ
Protein: At4g33890 (Transcriptional regulator of RNA polII, SAGA, subunit) (O81757)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 10
- SAGA-associated factor 11
- Phosphotransferases/inositol or phosphatidylinositol kinase
- Phosphatidylinositol 3-and 4-kinase family protein with FAT domain-containing protein
- Ubiquitin C-terminal hydrolase 22
- SAGA-associated factor 29 homolog A
- SAGA-associated factor 29 homolog B
Sequence:
MGSNQGSSRLDTLEIKALIYREIGNQRAESYFNQLGRFFALKITKSEFDKLCIKTIGRQNIHLHNRLIRSIIKNACIAKSPPFIKKGGSFVRFGNGDSKKNSQIQPLHGDSAFSPSTRKCRSRKLRDRPSPLGPLGKPHSLTTTNEESMSKAQSATELLSLGSRPPVEVVSVEEGEEVEQIAGGSPSVQSRCPLTAPLGVSMSLRNGATRKSVSNVSMCSRSFNRETCQNNGELPDTRTLRSRLERRLEMEGLKITMDSVSLLNSGLDVFMRRLIEPCLSLANTRCGTDRVREMNYQYTQQSRRLSYVSMSDFRAGMELNTEILGEDWPMHMEKICSRASDK
Protein: Glutamate receptor 3.4 (AtGLR3.4) (Glutamate receptor-like protein 3.4) (Ligand-gated ion channel 3.4) (Q8GXJ4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Glutamate-gated receptor that probably acts as non-selective cation channel, at least in hypocotyls (Probable). Can be triggered by Asn, Ser, Gly and, to a lower extent, Ala, Cys and Glu. May be involved in light-signal transduction and calcium homeostasis via the regulation of calcium influx into cells (Probable). Plays an important role in the calcium-based fast transmission of environmental stress. Acts as negative regulator of lateral root initiation and development. May restrict primordia numbers and position along the root axis by a signaling process originating in the phloem. AtGLR3.4-mediated cytosolic calcium influx may be involved in the regulation of seed germination under salt stress by modulating sodium accumulation through the SOS pathway.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15864638, ECO:0000269|PubMed:21110940, ECO:0000269|PubMed:22447719, ECO:0000269|PubMed:23590882}; Multi-pass membrane protein {ECO:0000255}. Plastid, chloroplast membrane {ECO:0000269|PubMed:21110940}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the plasma membrane. {ECO:0000269|PubMed:15864638, ECO:0000269|PubMed:21110940, ECO:0000269|PubMed:22447719, ECO:0000269|PubMed:23590882}.
Interaction partners:
- Cytochrome P450 71B8
- Glutamate receptor 3.2
Sequence:
MGFLVMIREVSMAKAIRVVLLCVSVLWVVPKECACRSNFSRNSSSSSSSSLRPLRQRPSSVNVGALFTYDSFIGRAAKPAVKAAMDDVNADQSVLKGIKLNIIFQDSNCSGFIGTMGALQLMENKVVAAIGPQSSGIAHMISYVANELHVPLLSFGATDPTLSSLQFPYFLRTTQNDYFQMHAIADFLSYSGWRQVIAIFVDDECGRNGISVLGDVLAKKRSRISYKAAITPGADSSSIRDLLVSVNLMESRVFVVHVNPDSGLNVFSVAKSLGMMASGYVWIATDWLPTAMDSMEHVDSDTMDLLQGVVAFRHYTIESSVKRQFMARWKNLRPNDGFNSYAMYAYDSVWLVARALDVFFRENNNITFSNDPNLHKTNGSTIQLSALSVFNEGEKFMKIILGMNHTGVTGPIQFDSDRNRVNPAYEVLNLEGTAPRTVGYWSNHSGLSVVHPETLYSRPPNTSTANQRLKGIIYPGEVTKPPRGWVFPNNGKPLRIGVPNRVSYTDYVSKDKNPPGVRGYCIDVFEAAIELLPYPVPRTYILYGDGKRNPSYDNLVNEVVADNFDVAVGDITIVTNRTRYVDFTQPFIESGLVVVAPVKEAKSSPWSFLKPFTIEMWAVTGGFFLFVGAMVWILEHRFNQEFRGPPRRQLITIFWFSFSTMFFSHRENTVSSLGRFVLIIWLFVVLIINSSYTASLTSILTIRQLTSRIEGIDSLVTSNEPIGVQDGTFARNYLINELNILPSRIVPLKDEEQYLSALQRGPNAGGVAAIVDELPYIEVLLTNSNCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLSEEGELEKIHRKWLNYKHECSMQISNSEDSQLSLKSFWGLFLICGITCFMALTVFFWRVFWQYQRLLPESADEERAGEVSEPSRSGRGSRAPSFKELIKVVDKREAEIKEILKQKSSKKLKSTQSAAGTSQSQHGEIT
Protein: Polynucleotide kinase 3'-phosphatase (M0QYI1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGEVEAPGRLWLESPPGGAPPIFLPSDGQALVLGRGPLTQVTDRKCSRTQVELVADPETRTVAVKQLGVNPSTTGTQELKPGLEGSLGVGDTLYLVNGLHPLTLRWEETRTPESQPDTPPGTPLVSQDEKRDAELPKKRMRKSNPGWENLEKLLVFTAAGVKPQGKVAGFDLDGTLITTRSGKVFPTGPSDWRILYPEIPRKLRELEAEGYKLVIFTNQMSIGRGKLPAEEFKAKVEAVVEKLGVPF
Protein: TSC complex subunit 2 (A0A2R8Y5F1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAKPTSKDSGLKEKFKILLGLGTPRPNPRSAEGKQTEFIITAEILRELSMECGLNNRIRMIGQICEVAKTKKFEEHAVEALWKAVADLLQPERPLEARHAVLALLKAIVQGQGERLGVLRALFFKVIKDYPSNEDLHERLEVFKALTDNGRHITYLEEELADFVLQWMDVGLSSEFLLVLVNLVKFNSCYLDEYIARMVQMICLLCVRTASSVDIEVSLQVLDAVVCYNCLPAESLPLFIVTLCRTINVKELCEPCWKLMRNLLGTHLGHSAIYNMCHLMEDRAYMEDAPLLRGAVFFVGMALWGAHRLYSLRNSPTSVLPSFYQAMACPNEVVSYEIVLSITRLIKKYRKELQVVAWDILLNIIERLLQQLQTLDSPELRTIVHDLLTTVEELCDQNEFHGSQERYFELVERCADQRPESSLLNLISYRAQSIHPAKDGWIQNLQALMERFFRSESRGAVRIKVLDVLSFVLLINRQFYEEELINSVVISQLSHIPEDKDHQVRKLATQLLVDLAEGCHTHHFNSLLDIIEKVMARSLSPPPELEERDVAAYSASLEDVKTAVLGLLVILQTKLYTLPASHATRVYEMLVSHIQLHYKHSYTLPIASSIRLQAFDFLLLLRADSLHRLGLPNKDGVVRFSPYCVCDYMEPERGSEKKTSGPLSPPTGPPGPAPAGPAVRLGSVPYSLLFRVLLQCLKQESDWKVLKLVLGRLPESLRYKVLIFTSPCSVDQLCSALCSMLSGPKTLERLRGAPEGFSRTDLHLAVVPVLTALISYHNYLDKTKQREMVYCLEQGLIHRCASQCVVALSICSVEMPDIIIKALPVLVVKLTHISATASMAVPLLEFLSTLARLPHLYRNFAAEQYASVFAISLPYTNPSKFNQYIVCLAHHVIAMWFIRCRLPFRKDFVPFITKGLRSNVLLSFDDTPEKDSFRARSTSLNERPKRIQTSLTSASLGSADENSVAQADDSLKNLHLELTETCLDMMARYVFSNFTAVPKRSPVGEFLLAGGRTKTWLVGNKLVTVTTSVGTGTRSLLGLDSGELQSGPESSSSPGVHVRQTKEAPAKLESQAGQQVSRGARDRVRSMSGGHGLRVGALDVPASQFLGSATSPGPRTAPAAKPEKASAGTRVPVQEKTNLAAYVPLLTQGWAEILVRRPTGNTSWLMSLENPLSPFSSDINNMPLQELSNALMAAERFKEHRDTALYKSLSVPAASTAKPPPLPRSNTDSAVVMEEGSPGEVPVLVEPPGLEDVEAALGMDRRTDAYSRSSSVSSQEEKSLHAEELVGRGIPIERVVSSEGGRPSVDLSFQPSQPLSKSSSSPELQTLQDILGDPGDKADVGRLSPEVKARSQSGTLDGESAAWSASGEDSRGQPEGPLPSSSPRSPSGLRPRGYTISDSAPSRRGKRVERDALKSRATASNAEKVPGINPSFVFLQLYHSPFFGDESNKPILLPNESFERSVQLLDQIPSYDTHKIAVLYVGEGQSNSELAILSNEHGSYRYTEFLTGLGRLIELKDCQPDKVYLGGLDVCGEDGQFTYCWHDDIMQAVFHIATLMPTKDVDKHRCDKKRHLGNDFVSIVYNDSGEDFKLGTIKGQFNFVHVIVTPLDYECNLVSLQCRKDMEGLVDTSVAKIVSDRNLPFVARQMALHANMASQVHHSRSNPTDIYPSKWIARLRHIKRLRQRICEEAAYSNPSLPLVHPPSHSKAPAQTPAEPTPGYEVGQRKRLISSVEDFTEFV
Protein: RE71384p (Q8SZP5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDESQPKTLYVGNLDSSVSEDLLIALFSTMGPVKSCKIIREPGNDPYAFIEYSNYQAATTALTAMNKRLFLEKEIKVNWATSPGNQPKTDISSHHHIFVGDLSPEIETETLREAFAPFGEISNCRIVRDPHTMKSKGYAFVSFVKKAEAENAIQAMNGQWIGSRSIRTNWSTRKLPPPREPSKGGGQGGGMGGGPGNGSGVKGSQRHTFEEVYNQSSPTNTTVYCGGFPPNVISDDLMHKHFVQFGPIQDVRVFKDKGFSFIKFVTKEAAAHAIEHTHNSEVHGNLVKCFWGKENGGDNSANNLNAAAATAAASANVAAVAAANAAVAAGAGMPGQMMTQQQIAAATGAAIPGQMMTPQQIAAQYPYAYQQMGYWYPPATYPTTQMQTQYMQQGYYPYAYPTSAQQAGGVPCIQFSAAGYRMVPPNVAWGVPGTVVPGVTAAAASAAAAANGSLAPQMMYSAAMPQYQTQ
Protein: KLLA0E01827p (Q6CPV9)
Organism: Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- KLLA0F23980p
- ATP-dependent RNA helicase DHH1
- 5'-3' exoribonuclease 1
- Enhancer of mRNA-decapping protein 3
- KLLA0F27357p
- NAD
- KLLA0A01474p
- KLLA0B11297p
- U6 snRNA-associated Sm-like protein LSm4
- U6 snRNA-associated Sm-like protein LSm1
Sequence:
MSTETLEIYRKALNFNVIARYDPKIKQLLFHTPHATVYKWGDDNWNKLEYQGVLAIYLRDVGDKEAILPEVSSYDDTITGQQSEANTPHVLTGHDIYNYGLIIMNRINPDNFSLAIAPNSVLNKRKLFAPNREEELEPMKVEVRDDLVMIKTLKKEVYGIWVHTPEDRQNIYELIKYLLENEPTDSFT
Protein: DNA polymerase epsilon subunit D (DNA polymerase II subunit D) (A0A1D8PG40)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA polymerase epsilon catalytic subunit
- DNA polymerase epsilon subunit B
- DNA polymerase epsilon noncatalytic subunit
- DNA polymerase
- DNA polymerase
- WAC domain-containing protein
- DNA polymerase alpha subunit B
- DNA primase
- DNA primase large subunit
- DNA-directed DNA polymerase
Sequence:
MPPKGWRKNADGQYPQPSSKENELISIDDILFPRTTIQKLAKNIISDDENNAGQMTIAKDSLLALQRSATVFVSHLLFQAKQISKEANRKTVSAQDMLAALERAEFSGFIPEVKQKLSVFEANVASKKQLKAAKPISTEEGEKSVSKKPKLDNESMEIDTEDGDGGKNASRGDDDDDEDDEENSTDGNEEDDENSKQDIEHEDEQDEDEDDDNDETEEDVSNPISALAKEEQELQGVETETEAENKPDSSETEEEEEEEEE
Protein: Collagen alpha-1(I) chain (Alpha-1 type I collagen) (P02452)
Organism: Homo sapiens (Human)
Function: Type I collagen is a member of group I collagen (fibrillar forming collagen).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
Interaction partners:
- Collagen alpha-1
- Collagen alpha-2
- Collagen alpha-2
- Collagen alpha-1
- CD44 antigen
- Integrin beta-1
- Integrin alpha-2
- Lumican
- Collagen alpha-3
- Biglycan
Sequence:
MFSFVDLRLLLLLAATALLTHGQEEGQVEGQDEDIPPITCVQNGLRYHDRDVWKPEPCRICVCDNGKVLCDDVICDETKNCPGAEVPEGECCPVCPDGSESPTDQETTGVEGPKGDTGPRGPRGPAGPPGRDGIPGQPGLPGPPGPPGPPGPPGLGGNFAPQLSYGYDEKSTGGISVPGPMGPSGPRGLPGPPGAPGPQGFQGPPGEPGEPGASGPMGPRGPPGPPGKNGDDGEAGKPGRPGERGPPGPQGARGLPGTAGLPGMKGHRGFSGLDGAKGDAGPAGPKGEPGSPGENGAPGQMGPRGLPGERGRPGAPGPAGARGNDGATGAAGPPGPTGPAGPPGFPGAVGAKGEAGPQGPRGSEGPQGVRGEPGPPGPAGAAGPAGNPGADGQPGAKGANGAPGIAGAPGFPGARGPSGPQGPGGPPGPKGNSGEPGAPGSKGDTGAKGEPGPVGVQGPPGPAGEEGKRGARGEPGPTGLPGPPGERGGPGSRGFPGADGVAGPKGPAGERGSPGPAGPKGSPGEAGRPGEAGLPGAKGLTGSPGSPGPDGKTGPPGPAGQDGRPGPPGPPGARGQAGVMGFPGPKGAAGEPGKAGERGVPGPPGAVGPAGKDGEAGAQGPPGPAGPAGERGEQGPAGSPGFQGLPGPAGPPGEAGKPGEQGVPGDLGAPGPSGARGERGFPGERGVQGPPGPAGPRGANGAPGNDGAKGDAGAPGAPGSQGAPGLQGMPGERGAAGLPGPKGDRGDAGPKGADGSPGKDGVRGLTGPIGPPGPAGAPGDKGESGPSGPAGPTGARGAPGDRGEPGPPGPAGFAGPPGADGQPGAKGEPGDAGAKGDAGPPGPAGPAGPPGPIGNVGAPGAKGARGSAGPPGATGFPGAAGRVGPPGPSGNAGPPGPPGPAGKEGGKGPRGETGPAGRPGEVGPPGPPGPAGEKGSPGADGPAGAPGTPGPQGIAGQRGVVGLPGQRGERGFPGLPGPSGEPGKQGPSGASGERGPPGPMGPPGLAGPPGESGREGAPGAEGSPGRDGSPGAKGDRGETGPAGPPGAPGAPGAPGPVGPAGKSGDRGETGPAGPAGPVGPVGARGPAGPQGPRGDKGETGEQGDRGIKGHRGFSGLQGPPGPPGSPGEQGPSGASGPAGPRGPPGSAGAPGKDGLNGLPGPIGPPGPRGRTGDAGPVGPPGPPGPPGPPGPPSAGFDFSFLPQPPQEKAHDGGRYYRADDANVVRDRDLEVDTTLKSLSQQIENIRSPEGSRKNPARTCRDLKMCHSDWKSGEYWIDPNQGCNLDAIKVFCNMETGETCVYPTQPSVAQKNWYISKNPKDKRHVWFGESMTDGFQFEYGGQGSDPADVAIQLTFLRLMSTEASQNITYHCKNSVAYMDQQTGNLKKALLLQGSNEIEIRAEGNSRFTYSVTVDGCTSHTGAWGKTVIEYKTTKTSRLPIIDVAPLDVGAPDQEFGFDVGPVCFL