wanglab/gogpt-training-data huggingface dataset:
Protein: Transient receptor potential cation channel subfamily V member 6 (TrpV6) (Calcium transport protein 1) (CaT1) (Epithelial calcium channel 2) (ECaC2) (Q9R186)
Organism: Rattus norvegicus (Rat)
Function: Calcium selective cation channel that mediates Ca(2+) uptake in various tissues, including the intestine. Important for normal Ca(2+) ion homeostasis in the body, including bone and skin (By similarity). The channel is activated by low internal calcium level, probably including intracellular calcium store depletion, and the current exhibits an inward rectification. Inactivation includes both a rapid Ca(2+)-dependent and a slower Ca(2+)-calmodulin-dependent mechanism; the latter may be regulated by phosphorylation. In vitro, is slowly inhibited by Mg(2+) in a voltage-independent manner. Heteromeric assembly with TRPV5 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:10428857, ECO:0000269|PubMed:17197020, ECO:0000269|PubMed:27296226, ECO:0000269|PubMed:28878326, ECO:0000269|PubMed:29258289}; Multi-pass membrane protein {ECO:0000269|PubMed:27296226, ECO:0000269|PubMed:28878326, ECO:0000269|PubMed:29258289}.
Interaction partners:
- Calmodulin-1
- Protein S100-G
- Short transient receptor potential channel 1
- Plasma membrane calcium-transporting ATPase 1
- Protein S100-A10
- Transient receptor potential cation channel subfamily M member 8
- Transient receptor potential cation channel subfamily M member 4
- non-specific serine/threonine protein kinase
- Transient receptor potential cation channel subfamily M member 7
- Short transient receptor potential channel 3
Sequence:
MGPLQREGRPALGDANVAPGSSPGGVWHQPQPPKDSAFHPMGWSLPKEKGLILCLWNKFCRWFHRRESWAQSRDEQNLLQQKRIWESPLLLAAKENNVQALIKLLKFEGCEVHQKGAMGETALHIAALYDNLEAAMVLMEAAPELVFEPMTSELYEGQTALHIAVINQNVNLVRALLARGASVSARATGSVFHYRPHNLIYYGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSLGNTVLHILILQPNKTFACQMYNLLLSYDGGDHLKSLELVPNNQGLTPFKLAGVEGNIVMFQHLMQKRKHIQWTYGPLTSTLYDLTEIDSSGDDQSLLELIVTTKKREARQILDQTPVKELVSLKWKRYGRPYFCVLGAIYVLYIICFTMCCVYRPLKPRITNRTNPRDNTLLQQKLLQEAYVTPKDDLRLVGELVSIVGAVIILLVEIPDIFRLGVTRFFGQTILGGPFHVIIVTYAFMVLVTMVMRLTNSDGEVVPMSFALVLGWCNVMYFARGFQMLGPFTIMIQKMIFGDLMRFCWLMAVVILGFASAFYIIFQTEDPDELGHFYDYPMALFSTFELFLTIIDGPANYDVDLPFMYSITYAAFAIIATLLMLNLLIAMMGDTHWRVAHERDELWRAQVVATTVMLERKLPRCLWPRSGICGREYGLGDRWFLRVEDRQDLNRQRIRRYAQAFQQQDDLYSEDLEKDSGEKLEMARPFGAYLSFPTPSVSRSTSRSSTNWDRLRQGALRKDLQGIINRGLEDGEGWEYQI
Protein: Elongator complex protein 5 (Protein iki1) (O94495)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the elongator complex, a multiprotein complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Elongator complex protein 4
- Elongator complex protein 2
- Elongator complex protein 1
- Elongator complex protein 3
- Elongator complex protein 6 homolog
- Cytoplasmic tRNA 2-thiolation protein 1
- Protein kti12
- Adenylyltransferase and sulfurtransferase uba4
Sequence:
MSKFLLNRCIRDLSPLTVLKDNLQQTAKPILNYYAKNAASRGIKVLFISYETLEKEAPEGIDCFLYATSWEKVKSLKELYEHISSWRTQGKQHIVMIDTINPILNTSISSFTMFFGSVLALGSICFLTSFHKDVTLENYPSYLPPCEVFLDFTSTCTVSLIGMQHLSVEHDAKMRSLPNPLLEELQDDKIISLLGSNCETAIVLHVEFRKKSGRIIKESCVLKNGKLEPYTPFEETARGPEPADNQIDFNVSFNLNVSEKERKERDKVFLPYFSAQMVGSQHKSSFVDEGTIIYHADEADDFDEEEDADEDLLI
Protein: Vigilin (A0A024R4E5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSSVAVLTQESFAEHRSGLVPQQIKVATLNSEEESDPPTYKDAFPPLPEKAACLESAQEPAGAWGNKIRPIKASVITQVFHVPLEERKYKDMNQFGEGEQAKICLEIMQRTGAHLELSLAKDQGLSIMVSGKLDAVMKARKDIVARLQTQASATVAIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPDDPSNQIKITGTKEGIEKARHEVLLISAEQDKRAVERLEVEKAFHPFIAGPYNRLVGEIMQETGTRINIPPPSVNRTEIVFTGEKEQLAQAVARIKKIYEEKKKKTTTIAVEVKKSQHKYVIGPKGNSLQEILERTGVSVEIPPSDSISETVILRGEPEKLGQALTEVYAKANSFTVSSVAAPSWLHRFIIGKKGQNLAKITQQMPKVHIEFTEGEDKITLEGPTEDVNVAQEQIEGMVKDLINRMDYVEINIDHKFHRHLIGKSGANINRIKDQYKVSVRIPPDSEKSNLIRIEGDPQGVQQAKRELLELASRMENERTKDLIIEQRFHRTIIGQKGERIREIRDKFPEVIINFPDPAQKSDIVQLRGPKNEVEKCTKYMQKMVADLVENSYSISVPIFKQFHKNIIGKGGANIKKIREESNTKIDLPAENSNSETIIITGKRANCEAARSRILSIQKDLANIAEVEVSIPAKLHNSLIGTKGRLIRSIMEECGGVHIHFPVEGSGSDTVVIRGPSSDVEKAKKQLLHLAEEKQTKSFTVDIRAKPEYHKFLIGKGGGKIRKVRDSTGARVIFPAAEDKDQDLITIIGKEDAVREAQKELEALIQNLDNVVEDSMLVDPKHHRHFVIRRGQVLREIAEEYGGVMVSFPRSGTQSDKVTLKGAKDCVEAAKKRIQEIIEDLEAQVTLECAIPQKFHRSVMGPKGSRIQQITRDFSVQIKFPDREENAVHSTEPVVQENGDEAGEGREAKDCDPGSPRRCDIIIISGRKEKCEAAKEALEALVPVTIEVEVPFDLHRYVIGQKGSGIRKMMDEFEVNIHVPAPELQSDIIAITGLAANLDRAKAGLLERVKELQAEQEDRALRSFKLSVTVDPKYHPKIIGRKGAVITQIRLEHDVNIQFPDKDDGNQPQDQITITGYEKNTEAARDAILRIVGELEQMVSEDVPLDHRVHARIIGARGKAIRKIMDEFKVDIRFPQSGAPDPNCVTVTGLPENVEEAIDHILNLEEEYLADVVDSEALQVYMKPPAHEEAKAPSRGFVVRDAPWTASSSEKAPDMSSSEEFPSFGAQVAPKTLPWGPKR
Protein: At1g75300 (NADPH oxidoreductase, putative; 10572-9197) (NmrA-like negative transcriptional regulator family protein) (Putative NADPH oxidoreductase) (Q9FRM1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MTTEKSKILVIGGTGYMGEFIVEGSAKAGNPTFALVREASLSDPVKSKTIQSFKDLGVTILHGDLNDHESLVKAIKQVDVVISTIGHKQIFDQTKIISAIKEAGNVKRFLPAEFGIDVERTSAVEPAKSLFAGKVQIRRAIEAEGIPYTYVVSNCSAGFYLRTLLQFESGLISHTRDKAIIFGDKNVPPRDKVTILGDGNAKVVINKEEDVAAYMIKAVDDLRTLNKTLYISPPNNILSMNEMVTLWEKKIGKSLEKTHISEEQILKSIQVPIDVFKSINHAVFVKGDQTSFTIEPWFGEEASVLYPDVKYTSIDEYLSQFT
Protein: Collagen alpha-1(XVIII) chain [Cleaved into: Endostatin; Non-collagenous domain 1 (NC1)] (P39061)
Organism: Mus musculus (Mouse)
Function: Probably plays a major role in determining the retinal structure as well as in the closure of the neural tube.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:9687493}.; SUBCELLULAR LOCATION: [Non-collagenous domain 1]: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000305|PubMed:9687493}. Secreted {ECO:0000269|PubMed:10626789}.; SUBCELLULAR LOCATION: [Endostatin]: Secreted {ECO:0000269|PubMed:10626789, ECO:0000305|PubMed:9008168}. Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000305}.
Interaction partners:
- Vascular endothelial growth factor receptor 2
- Basement membrane-specific heparan sulfate proteoglycan core protein
- 72 kDa type IV collagenase
- Matrix metalloproteinase-9
- Nucleolin
- Protein Dr1
- Collagen alpha-1
- Plasminogen
- Collagenase 3
- Glypican-1
Sequence:
MAPDPSRRLCLLLLLLLSCRLVPASADGNSLSPLNPLVWLWPPKTSDSLEGPVSKPQNSSPVQSTENPTTHVVPQDGLTEQQTTPASSELPPEEEEEEDQKAGQGGSPATPAVPIPLVAPAASPDMKEENVAGVGAKILNVAQGIRSFVQLWDEDSTIGHSAGTEVPDSSIPTVLPSPAELSSAPQGSKTTLWLSSAIPSSPDAQTTEAGTLAVPTQLPPFQSNLQAPLGRPSAPPDFPGRAFLSSSTDQGSSWGNQEPPRQPQHLEGKGFLPMTARSSQQHRHSDVHSDIHGHVPLLPLVTGPLVTASLSVHGLLSVPSSDPSGQLSQVAALPGFPGTWVSHVAPSSGTGLSNDSALAGNGSLTSTSRCLPLPPTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLAPSCGPGPPPPLPPCRQFCEALEDECWNYLAGDRLPVVCASLPSQEDGYCVFIGPAAENVAEEVGLLQLLGDPLPEKISQIDDPHVGPAYIFGPDSNSGQVAQYHFPKLFFRDFSLLFHVRPATEAAGVLFAITDAAQVVVSLGVKLSEVRDGQQNISLLYTEPGASQTQTGASFRLPAFVGQWTHFALSVDGGSVALYVDCEEFQRVPFARASQGLELERGAGLFVGQAGTADPDKFQGMISELKVRKTPRVSPVHCLDEEDDDEDRASGDFGSGFEESSKSHKEDTSLLPGLPQPPPVTSPPLAGGSTTEDPRTEETEEDAAVDSIGAETLPGTGSSGAWDEAIQNPGRGLIKGGMKGQKGEPGAQGPPGPAGPQGPAGPVVQSPNSQPVPGAQGPPGPQGPPGKDGTPGRDGEPGDPGEDGRPGDTGPQGFPGTPGDVGPKGEKGDPGIGPRGPPGPPGPPGPSFRQDKLTFIDMEGSGFSGDIESLRGPRGFPGPPGPPGVPGLPGEPGRFGINGSYAPGPAGLPGVPGKEGPPGFPGPPGPPGPPGKEGPPGVAGQKGSVGDVGIPGPKGSKGDLGPIGMPGKSGLAGSPGPVGPPGPPGPPGPPGPGFAAGFDDMEGSGIPLWTTARSSDGLQGPPGSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPGREGAAGSPGPKGEKGMPGEKGNPGKDGVGRPGLPGPPGPPGPVIYVSSEDKAIVSTPGPEGKPGYAGFPGPAGPKGDLGSKGEQGLPGPKGEKGEPGTIFSPDGRALGHPQKGAKGEPGFRGPPGPYGRPGHKGEIGFPGRPGRPGTNGLKGEKGEPGDASLGFSMRGLPGPPGPPGPPGPPGMPIYDSNAFVESGRPGLPGQQGVQGPSGPKGDKGEVGPPGPPGQFPIDLFHLEAEMKGDKGDRGDAGQKGERGEPGAPGGGFFSSSVPGPPGPPGYPGIPGPKGESIRGPPGPPGPQGPPGIGYEGRQGPPGPPGPPGPPSFPGPHRQTVSVPGPPGPPGPPGPPGAMGASAGQVRIWATYQTMLDKIREVPEGWLIFVAEREELYVRVRNGFRKVLLEARTALPRGTGNEVAALQPPLVQLHEGSPYTRREYSYSTARPWRADDILANPPRLPDRQPYPGVPHHHSSYVHLPPARPTLSLAHTHQDFQPVLHLVALNTPLSGGMRGIRGADFQCFQQARAVGLSGTFRAFLSSRLQDLYSIVRRADRGSVPIVNLKDEVLSPSWDSLFSGSQGQLQPGARIFSFDGRDVLRHPAWPQKSVWHGSDPSGRRLMESYCETWRTETTGATGQASSLLSGRLLEQKAASCHNSYIVLCIENSFMTSFSK
Protein: Serine/threonine-protein kinase pim-2 (EC 2.7.11.1) (Kinase pim-1) (Q9YHZ5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation.
Interaction partners:
- Crooked neck-like protein 1
Sequence:
MLDKRIVDVRLDQLEILKAKNGKEHFEKQYTMGNLLGSGGFGSVYSGHRISDGQKVAIKQISRDRIQQWSKMPGEVNPVPNEIALLQSLGGGSGSVPGHRGIIRMLDWFEIPGQEYLIVFEKPQHCQDLFDFITERGALDESLARRFLKQVIEAVQFCHSKGIVHRDIKDENILVDTRTGDIKVIDFGSGATLKDSMYTDFEGTRVYSPPEWILYHKYHALPLTVWSLGVLLYDMVCGDIPFEQDTDIVKAKPSFNKRISNDCRSLICSCLSYNPGDRPSLEQILQHPWMMESSVDNGDLQEESKIKPSL
Protein: Protein S-acyltransferase 24 (EC 2.3.1.225) (Ankyrin repeat-containing S-palmitoyltransferase) (Palmitoyltransferase TIP1) (Protein TIP GROWTH DEFECTIVE 1) (AtTIP1) (Zinc finger DHHC domain-containing protein TIP1) (Q52T38)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Palmitoyltransferase involved in cell growth regulation (Ref.8). Contributes to the palmitoylation of CESA3, thus regulating cellulose biosynthesis.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:22430844}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Aquaporin TIP1-2
- NAC domain-containing protein 91
- Aquaporin TIP1-1
- Aquaporin TIP3-1
- Probable aquaporin TIP2-2
- Aquaporin TIP2-1
- Probable aquaporin TIP5-1
- Aquaporin TIP1-3
- Protein ROOT HAIR DEFECTIVE 3
- PAMP-induced secreted peptide 1
Sequence:
MSSEIEVVEEIQSNPKENGESSSKGIEEESLKNDVYTAAAYGDLEKLHRLVECEGSSVSEPDALGYYALQWSALNNRVAVAQYLIEHGGDVNATDHTGQTALHWSAVRGAIQVAELLLQEGARVDATDMYGYQATHVAAQYGQTAFLCHVVSKWNADPDVPDNDGRSPLHWAAYKGFADSIRLLLFLDAYRGRQDKEGCTPLHWAAIRGNLEACTVLVQAGKKEDLMITDKTGLTPAQLAAEKNHRQVSFFLGNARSLLEKRCDGSSPLGRLSKLGLAPVLWIMILLLLLVYTNSVVLASNLPKLTTGIGALAWLGFILATAGLFLFYRCSRKDPGYIRMNIHDPQTMKDDEPLLKIELNNPALLAGNWTQLCATCKIIRPLRAKHCSTCDRCVEQFDHHCPWVSNCVGKKNKWEFFLFLLLEVLAMLITGGVTLARVLSDPSAPSSFGAWMSHVASNHVGALSFLLVEFCLFFSVAVLTVIQASQISRNITTNEMANALRYSYLRGPGGRFRNPYDLGCRRNCSDFLVKGYNEDIECHEEDATQRPEGISMMQMQRNPNLQNGNGHVAIDVNPTHNSQSAHVHSANCSHSHNSKSKSDNVPLGLGLGLSRNPTRPVVSP
Protein: Major outer membrane porin (MOMP) (P27455)
Organism: Chlamydia pneumoniae (Chlamydophila pneumoniae)
Function: In elementary bodies (EBs, the infectious stage, which is able to survive outside the host cell) provides the structural integrity of the outer envelope through disulfide cross-links with the small cysteine-rich protein and the large cysteine-rich periplasmic protein. It has been described in publications as the Sarkosyl-insoluble COMC (Chlamydia outer membrane complex), and serves as the functional equivalent of peptidoglycan (By similarity).
Subcellular location: Cell outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MKKLLKSALLSAAFAGSVGSLQALPVGNPSDPSLLIDGTIWEGAAGDPCDPCATWCDAISLRAGFYGDYVFDRILKVDAPKTFSMGAKPTGSAAANYTTAVDRPNPAYNKHLHDAEWFTNAGFIALNIWDRFDVFCTLGASNGYIRGNSTAFNLVGLFGVKGTTVNANELPNVSLSNGVVELYTDTSFSWSVGARGALWECGCATLGAEFQYAQSKPKVEELNVICNVSQFSVNKPKGYKGVAFPLPTDAGVATATGTKSATINYHEWQVGASLSYRLNSLVPYIGVQWSRATFDADNIRIAQPKLPTAVLNLTAWNPSLLGNATALSTTDSFSDFMQIVSCQINKFKSRKACGVTVGATLVDADKWSLTAEARLINERAAHVSGQFRF
Protein: Phospholipase D alpha 4 (AtPLDalpha4) (PLD alpha 4) (EC 3.1.4.4) (PLDalpha3) (Phospholipase D epsilon) (AtPLDepsilon) (PLD epsilon) (Q9C888)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond to generate phosphatidic acids (PA). Promotes growth and plays a role in nitrogen signaling.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19143999}.
Interaction partners:
- CDP-diacylglycerol--serine O-phosphatidyltransferase 1
- Non-specific phospholipase C1
- Non-specific phospholipase C2
- Non-specific phospholipase C6
- Non-specific phospholipase C5
- Non-specific phospholipase C4
- Phosphatidyl-N-methylethanolamine N-methyltransferase
- Phosphatidylserine decarboxylase proenzyme 2
- Phosphatidylserine decarboxylase proenzyme 3
- Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
Sequence:
MELEEQKKYFHGTLEITIFDATPFSPPFPFNCICTKPKAAYVTIKINKKKVAKTSSEYDRIWNQTFQILCAHPVTDTTITITLKTRCSVLGRFRISAEQILTSNSAVINGFFPLIADNGSTKRNLKLKCLMWFRPAYLEPGWCRALEEASFQGIRNASFPQRSNCRVVLYQDAHHKATFDPRVDDVPFNARNLWEDVYKAIESARHLVYIAGWALNPNLVLVRDNETEIPHAVGVTVGELLKRKSEEGVAVRVMLWNDETSLPMIKNKGVMRTNVERALAYFRNTNVVCRLCPRLHKKLPTAFAHHQKTITLDTRVTNSSTKEREIMSFLGGFDLCDGRYDTEEHSLFRTLGTEADFYQTSVAGAKLSRGGPREPWHDCHVSVVGGAAWDVLKNFEQRWTKQCNPSVLVNTSGIRNLVNLTGPTEENNRKWNVQVLRSIDHISATEMPRGLPVEKSVHDGYVAAIRKAERFIYIENQYFMGSCDHWESKNDKICSGCTNLIPVEIALKIAAKIRARERFAVYIVIPMWPEGPPESETVEEILHWTRETMSMMYQIIGEAIWEVGDKSHPRDYLNFFCLANREEKRDGEFEAVSSPHQKTHYWNAQRNRRFMVYVHSKLMIVDDTYILIGSANINQRSMDGCRDTEIAIGCYQTNTNNTNEIQAYRLSLWYEHTGGKITADDLSSSEPESLECVRGLRTIGEQMWEIYSGDKVVDMLGIHLVAYPISVTGDGAVEEVGDGCFPDTKTLVKGKRSKMFPPVLTT
Protein: Transcription factor SOX-8 (P57074)
Organism: Gallus gallus (Chicken)
Function: Transcription factor that may play a role in central nervous system, limb and facial development. May be involved in male sex determination. Binds the consensus motif 5'-[AT][AT]CAA[AT]G-3'.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
Interaction partners:
- Sulfhydryl oxidase 1
- Oligodendrocyte transcription factor 2
- Forkhead box protein D3
- Transforming protein p68/c-ets-1
- Uncharacterized protein.
Sequence:
MLNMTEEHDKALEAPCSPAGTTSSMSHVDSDSDSPLSPAGSEGLGCAPAPAPRPPGAAPLGAKVDAAEVDERFPACIRDAVSQVLKGYDWSLVPMPVRGNGSLKAKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLSENEKRPFVEEAERLRVQHKKDHPDYKYQPRRRKSVKAGQSDSDSGAELSHHAGTQIYKADSGLGGMADGHHHGEHAGQPHGPPTPPTTPKTDLHHGSKQELKHEGRRLVESGRQNIDFSNVDISELSSEVINNMETFDVHEFDQYLPLNGHTAMPADHGPGAGFYSTSYSHSAAGAGGAGQVWTHKSPASASPSSADSGQQRPHIKTEQLSPSHYSDQSHGSPAHSDYGSYSTQACATTASTATAAASFSSSQCDYTDLQSSNYYNPYPGYPSSIYQYPYFHSSRRPYATPILNGLSIPPAHSPTANWDQPVYTTLTRP
Protein: Golgi-associated RAB2 interactor protein 1B (Golgi-associated RAB2 interactor-like 1) (GARI-L1) (Q3UZD7)
Organism: Mus musculus (Mouse)
Function: RAB2B effector protein required for accurate acrosome formation and normal male fertility. In complex with RAB2A/RAB2B, seems to suppress excessive vesicle trafficking during acrosome formation.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:34714330}.
Interaction partners:
- Transmembrane protein 270
- RIKEN cDNA 1700013G24 gene
- Spermatogenesis-associated protein 3
Sequence:
MMTSVPPRKSWWTSKKTVKVIRSYPTFPSLNAWEKFRGLLPVDGETNPGVGLGVEEGLLCQMVHSPEFNLFPNSVVFESNFVQVRRSRNWKEIYKASNTMALGVTSSVPCLPLPNILLMARVKWHQGQSQTWNRPSRAPSINLKSILPLKFVELQIWDDQERVLRLRTVTEKIYYLKLHPDHPETVFHFWIRLVQILHKGLSITTKDPTILVTHCLVPKSLCSPGGKTELVQKKSKGLQPSESLTHLMAQGESETLSQIFSDLHQQKQYRSEKMHINKTSSEKATPCEDSIPCTCDLNWRDAFMFGEWERENPSGPQPLSLLGTLAASSRPRLSLTGGNSI
Protein: Phosphate metabolism protein 6 (Q05637)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Vacuole membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Putative cyclin-dependent kinase inhibitor SPL2
- Vacuolar transporter chaperone 3 complex subunit 3
- Inorganic phosphate transporter PHO84
- Phosphate permease PHO89
- Acid phosphatase PHO12
Sequence:
MEDTSRCIDDVLKIGQQEKEIRQAEFSDAQGEREEVKCIDYTVDLEAGLPRHESSGKSNTLKQCYNAVLGFLEELIIVIIIVLLLYSLTMVGLFYVMTMTKFLF
Protein: Pollen receptor-like kinase 2 (AtPRK2) (EC 2.7.11.1) (Q84JQ4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Receptor-like kinase involved in the control of pollen germination and pollen tube polar growth. Phosphorylates ROPGEF1 in its C-terminal region, releasing its auto-inhibition, and thereby activating the ROP1 signaling pathway. May act as a scaffolding protein, recruiting ROPGEF12 to the plasma membrane by binding to its C-terminal domain. Phosphorylates ROPGEF12, releasing its auto-inhibition.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18000057}; Single-pass membrane protein {ECO:0000255}. Note=ROPGEF12 colocalizes with PRK2 at the apical plasma membrane of pollen tube. {ECO:0000269|PubMed:18000057}.
Interaction partners:
- Rop guanine nucleotide exchange factor 1
- Rop guanine nucleotide exchange factor 12
- Rac-like GTP-binding protein ARAC11
- CRIB domain-containing protein RIC4
- Protein RALF-like 15
- CRIB domain-containing protein RIC3
- Rac-like GTP-binding protein ARAC10
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- Interactor of constitutive active ROPs 1
- Rho guanine nucleotide exchange factor 8
Sequence:
MESKCLMFVSIVSVFFMVVNGVSETETLLKFKNSLVIGRANALESWNRRNPPCKWTGVLCDRGFVWGLRLENLELSGSIDIEALMGLNSLRSLSFINNKFKGPFPEFKKLVALKSLYLSNNQFDLEIPKDAFDGMGWLKKLHLEQNNFIGEIPTSLVKSPKLIELRLDGNRFTGQIPEFRHHPNMLNLSNNALAGQIPNSFSTMDPKLFEGNKGLCGKPLDTKCSSPYNHSSEPKSSTKKTSSKFLYIVAAAVAALAASLIIIGVVIFLIRRRKKKQPLLSAEPGPSSLQMRAGIQESERGQGSYHSQNRAAKKMIHTTKLSFLRDDKGKFELQDLLKASAEILGSGCFGASYKTLLSNGSVMVVKRFKHMNSAGIDEFQEHMKRLGRLNHENLLPIVAYYYKKEEKLFVSDFVANGSLAAHLHGHKSLGQPSLDWPTRFNIVKGVGRGLLYLHKNLPSLMAPHGHLKSSNVLLSEKFEPLLMDYGLIPMINEESAQELMVAYKSPEYVKQSRVTKKTDVWGLGVLILEILTGKLLESFSQVDKESEEDLASWVRSSFKGEWTQELFDQEMGKTSNCEAHILNLMRIGLSCCEVDVEKRLDIREAVEKMEDLMKEREQGDDDFYSTYASEADGRSSRGLSSEGINLS
Protein: EBP cholestenol delta-isomerase (C9JJ78)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MTTNAGPLHPYWPQHLRLDNFVPNDRPTWHILAGLFSVTGVLVVTTWLLSGRAAVVPLGTWRRLSLCWFAVCGFIHLVIEGWFVLYYEDLLGDQAFLSQLWKEYAKGDSRYILGDNFTVCMETITACLWGPLSLWVVIAFLRQHPLRFILQLVVSVGQIY
Protein: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3 (EC 3.1.4.11) (Phosphoinositide phospholipase C-delta-3) (Phospholipase C-delta-3) (PLC-delta-3) (Q8N3E9)
Organism: Homo sapiens (Human)
Function: Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) to generate 2 second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of protein kinase C (PKC), while IP3 releases Ca(2+) from intracellular stores. Essential for trophoblast and placental development. May participate in cytokinesis by hydrolyzing PIP2 at the cleavage furrow. Regulates neurite outgrowth through the inhibition of RhoA/Rho kinase signaling (By similarity).
Subcellular location: Membrane; Peripheral membrane protein. Cytoplasm. Cleavage furrow {ECO:0000269|PubMed:17041247}. Note=Localizes at the cleavage furrow during cytokinesis. {ECO:0000269|PubMed:17041247}.
Interaction partners:
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
- Protein kinase C alpha type
- Inositol polyphosphate-5-phosphatase A
- Inositol polyphosphate multikinase
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR2
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4
- Protein kinase C gamma type
Sequence:
MLCGRWRRCRRPPEEPPVAAQVAAQVAAPVALPSPPTPSDGGTKRPGLRALKKMGLTEDEDVRAMLRGSRLRKIRSRTWHKERLYRLQEDGLSVWFQRRIPRAPSQHIFFVQHIEAVREGHQSEGLRRFGGAFAPARCLTIAFKGRRKNLDLAAPTAEEAQRWVRGLTKLRARLDAMSQRERLDHWIHSYLHRADSNQDSKMSFKEIKSLLRMVNVDMNDMYAYLLFKECDHSNNDRLEGAEIEEFLRRLLKRPELEEIFHQYSGEDRVLSAPELLEFLEDQGEEGATLARAQQLIQTYELNETAKQHELMTLDGFMMYLLSPEGAALDNTHTCVFQDMNQPLAHYFISSSHNTYLTDSQIGGPSSTEAYVRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVVQAVRDHAFTLSPYPVILSLENHCGLEQQAAMARHLCTILGDMLVTQALDSPNPEELPSPEQLKGRVLVKGKKLPAARSEDGRALSDREEEEEDDEEEEEEVEAAAQRRLAKQISPELSALAVYCHATRLRTLHPAPNAPQPCQVSSLSERKAKKLIREAGNSFVRHNARQLTRVYPLGLRMNSANYSPQEMWNSGCQLVALNFQTPGYEMDLNAGRFLVNGQCGYVLKPACLRQPDSTFDPEYPGPPRTTLSIQVLTAQQLPKLNAEKPHSIVDPLVRIEIHGVPADCARQETDYVLNNGFNPRWGQTLQFQLRAPELALVRFVVEDYDATSPNDFVGQFTLPLSSLKQGYRHIHLLSKDGASLSPATLFIQIRIQRS
Protein: Tyrosine recombinase XerD (P0A8P8)
Organism: Escherichia coli (strain K12)
Function: Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Binds cooperatively to specific DNA consensus sequences that are separated from XerC binding sites by a short central region, forming the heterotetrameric XerC-XerD complex that recombines DNA substrates. The complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids at ColE1 xer (or cer) and pSC101 (or psi) sites. In the complex XerD specifically exchanges the bottom DNA strands (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Tyrosine recombinase XerC
- DNA translocase FtsK
- Holliday junction branch migration complex subunit RuvB
- Thiol:disulfide interchange protein DsbC
- Crossover junction endodeoxyribonuclease RuvC
- Single-stranded-DNA-specific exonuclease RecJ
- Arginine repressor
- Holliday junction branch migration complex subunit RuvA
- UvrABC system protein B
- UvrABC system protein C
Sequence:
MKQDLARIEQFLDALWLEKNLAENTLNAYRRDLSMMVEWLHHRGLTLATAQSDDLQALLAERLEGGYKATSSARLLSAVRRLFQYLYREKFREDDPSAHLASPKLPQRLPKDLSEAQVERLLQAPLIDQPLELRDKAMLEVLYATGLRVSELVGLTMSDISLRQGVVRVIGKGNKERLVPLGEEAVYWLETYLEHGRPWLLNGVSIDVLFPSQRAQQMTRQTFWHRIKHYAVLAGIDSEKLSPHVLRHAFATHLLNHGADLRVVQMLLGHSDLSTTQIYTHVATERLRQLHQQHHPRA
Protein: Exocrine gland secreted peptide 8 (F7AMQ8)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MEKVSAMTSFPVMLFLIILLLPSICSEERTQADPTISADNKKNFKTVVDLTDCQCERNFIESLESTLPASNQDQTLFENMTNQHKLNLSKMLSVLSKCCTQKQQVDTVHFRRMPHRIQSTKQNNYKKQVLYPMQEFMNLTRDVLVSRYV
Protein: Hand transcription factor 1 (Q18612)
Organism: Caenorhabditis elegans
Function: Probable transcription factor which regulates early embryonic myogenesis, in cooperation with transcription factors unc-120 and hlh-1. Involved in controlling the number and position of somatic gonadal precursor cells (SGPs) in the gonadal primordium, and embryonic body shape.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Serum response factor homolog
- Helix-loop-helix protein hlh-2
- Zinc finger protein ehn-3
- T-box transcription factor tbx-8
- C2H2-type domain-containing protein
- T-box transcription factor tbx-9
- Nuclear hormone receptor family member nhr-2
Sequence:
MVKSTTAGNNAVSSLESTDSKKSRKEKSREKEHRRAQCINSAFEILQQHIPYLKSEERKSLPKIKTLRLAMQYIDHLKKLLGGNEMLETDCNESRPLTHSDFRVNISNEIRIRNSYRERAHNQELDEATVKRILAREDQRRRCSSVPEGIQRYTPYQSRQFGPISNNVCNFRHVDANQYNTNFMEYQTQMVQVANFPNQFSHEYYNYGTFPVIDPTSLENSNPILQ
Protein: [Butirosin acyl-carrier protein]--L-glutamate ligase (EC 6.2.1.39) (Butirosin biosynthesis protein J) (Q4H4E7)
Organism: Niallia circulans (Bacillus circulans)
Function: ATP-dependent ligase that catalyzes 2 steps in the biosynthesis of the side chain of the aminoglycoside antibiotics in the biosynthetic pathway of butirosin. Mediates the addition of one molecule of L-glutamate to a dedicated acyl-carrier protein. Following decarboxylation of the product by BtrK, adds a second L-glutamate molecule.
Interaction partners:
Sequence:
MKFTHPLDYYRLNGKQILWYMNIGEDQDSQASNYFPSVKDPQSEKIVVQQEQQLLFLARPQDTVFFHTMPEQAFLDYWKERRLSLPSIICCDKLSQVPDLERYTIIPFIVSDQLLELKRRYPHMDIIAPDLAVCREINHKFNTRRLMERNGFNVTTGYFCSDIESLEHAYEQLISAGFSKCVLKVPYGSSGKGLKVIDNERNFRFLLNYIQNRQTNVDLLLEGWHPHRLSLTSQLFITEYEVHLLAVTEQIIDPNGVYKGTNFTPALSQSEAADYREEILRAGELIRQMGYRGVLGIDSILDTNGELIPVIEINARLTQVTYILPLVIEQKKRYEFVESRVLVFNSRADLDFEDYENDLSEVTRDLPVRIDLYNFCKASGAFKNTYKLFVLVSAHNSEQLIKARSLLDELNTKMTTAVH