wanglab/gogpt-training-data huggingface dataset:
Protein: Centromere protein I (CENP-I) (FSH primary response protein 1) (Follicle-stimulating hormone primary response protein) (Interphase centromere complex protein 19) (Leucine-rich primary response protein 1) (Q92674)
Organism: Homo sapiens (Human)
Function: Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. Required for the localization of CENPF, MAD1L1 and MAD2 (MAD2L1 or MAD2L2) to kinetochores. Involved in the response of gonadal tissues to follicle-stimulating hormone.
Subcellular location: Nucleus. Chromosome, centromere. Note=Localizes exclusively in the centromeres. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex.
Interaction partners:
- Centromere protein T
- Centromere protein N
- Centromere protein L
- Centromere protein M
- Histone H3-like centromeric protein A
- Centromere protein P
- Centromere protein O
- Centromere protein Q
- Centromere protein H
- Centromere protein U
Sequence:
MSPQKRVKNVQAQNRTSQGSSSFQTTLSAWKVKQDPSNSKNISKHGQNNPVGDYEHADDQAEEDALQMAVGYFEKGPIKASQNKDKTLEKHLKTVENVAWKNGLASEEIDILLNIALSGKFGNAVNTRILKCMIPATVISEDSVVKAVSWLCVGKCSGSTKVLFYRWLVAMFDFIDRKEQINLLYGFFFASLQDDALCPYVCHLLYLLTKKENVKPFRVRKLLDLQAKMGMQPHLQALLSLYKFFAPALISVSLPVRKKIYFKNSENLWKTALLAVKQRNRGPSPEPLKLMLGPANVRPLKRKWNSLSVIPVLNSSSYTKECGKKEMSLSDCLNRSGSFPLEQLQSFPQLLQNIHCLELPSQMGSVLNNSLLLHYINCVRDEPVLLRFYYWLSQTLQEECIWYKVNNYEHGKEFTNFLDTIIRAECFLQEGFYSCEAFLYKSLPLWDGLCCRSQFLQLVSWIPFSSFSEVKPLLFDHLAQLFFTSTIYFKCSVLQSLKELLQNWLLWLSMDIHMKPVTNSPLETTLGGSMNSVSKLIHYVGWLSTTAMRLESNNTFLLHFILDFYEKVCDIYINYNLPLVVLFPPGIFYSALLSLDTSILNQLCFIMHRYRKNLTAAKKNELVQKTKSEFNFSSKTYQEFNHYLTSMVGCLWTSKPFGKGIYIDPEILEKTGVAEYKNSLNVVHHPSFLSYAVSFLLQESPEERTVNVSSIRGKKWSWYLDYLFSQGLQGLKLFIRSSVHHSSIPRAEGINCNNQY
Protein: RAP domain-containing protein, chloroplastic (AtRAP) (Q8VZE7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: RNA-binding protein required for chloroplast 16S rRNA maturation, an important process which supports chloroplast gene expression and biogenesis. Binds to 16S rRNA precursor and is involved in its 5'-end processing. May act as negative regulator of defense response against bacterial pathogens.
Subcellular location: Plastid, chloroplast stroma, chloroplast nucleoid {ECO:0000269|PubMed:24585838}.
Interaction partners:
- At2g18210
- 5'-3' exoribonuclease 4
- Protein argonaute 7
- Large ribosomal subunit protein uL11z
- Small RNA 2'-O-methyltransferase
- Uncharacterized aarF domain-containing protein kinase At5g05200, chloroplastic
Sequence:
MECVVPFRRCFCLNPPETRHRIVNHNHRNLHISLSSSSFASGILPLSNKKYRFVGPLAQRSSLHRRTDSLKHLPFSVNASVIGNSEEEVEEEDDDGDWEAEFLGEIDPLDIQPPKKRKKQKNSKALEDTEGMDWCVRARKIALKSIEARGLSSRMAEVMPLKKKKKKKSKKVIVKKDKVKSKSIPEDDFDTEDEDLDFEDGFVEDKMGDLRKRVSSLAGGMFEEKKEKMKEQLAQRLSQFSGPSDRMKEINLNKAIIEAQTAEEVLEVTAETIMAVAKGLSPSPLSPLNIATALHRIAKNMEKVSMMRTRRLAFARQREMSMLVALAMTCLPECSAQGISNISWALSKIGGELLYLTEMDRVAEVATSKVGEFNSQNVANIAGAFASMRHSAPELFAELSKRASTIINTFKGQEIAQLLWSFASLYEPADPLLESLDSAFKSSDQFKCYLTKEITNSDEVVDAEVSDDVSRSPALSFNRDQLGNIAWSYAVLGQVERPFFANIWNTLTTLEEQRLSEQYREDVMFASQVYLVNQCLKLECPHLQLSLCQELEEKISRAGKTKRFNQKITSSFQKEVGRLLISTGLDWAKEHDVDGYTVDVALVEKKVALEIDGPTHFSRNSGLPLGHTMLKRRYVAAAGWKVVSLSLQEWEEHEGSHEQLEYLREILTGCI
Protein: Interferon regulatory factor (B5X8L4)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR038196}.
Interaction partners:
Sequence:
MSVSRMRMRPWLEEKIESNSISGLVWVDKDNKIFSVPWKHAARHGWDLNKDACLFKQWAMHTEEVKDKSINRGSGAVRVYKMKNIYSKPNNKRSKANNVKKNKKGSQIKTGGMAYSETNCPENLNTNTHLQEDSMTQESIVDSTGNLGDFTFAPECSTNVEIGPDSTNNFYASFQVSPDHSTDYEDGHQETLIGMTHHWEQGSVNDKGFQSNEVGTAESFDTAESYHSQESQWSDNSETEIELRLYTELSSGLPIIDDILSYTDYWTLNNNTSSYPQQITCPL
Protein: Mothers against decapentaplegic homolog 5 (MAD homolog 5) (Mothers against DPP homolog 5) (Dwarfin-C) (Dwf-C) (SMAD family member 5) (SMAD 5) (Smad5) (mSmad5) (P97454)
Organism: Mus musculus (Mouse)
Function: Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD5 is a receptor-regulated SMAD (R-SMAD) (By similarity). Required for angiogenesis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q99717}. Nucleus {ECO:0000250|UniProtKB:Q99717}. Mitochondrion {ECO:0000250|UniProtKB:Q99717}. Note=Cytoplasmic in the absence of ligand. Migrates to the nucleus when complexed with SMAD4. {ECO:0000250|UniProtKB:Q99717}.
Interaction partners:
- Mothers against decapentaplegic homolog 4
- Mothers against decapentaplegic homolog 9
- Bone morphogenetic protein receptor type-1A
- Mothers against decapentaplegic homolog 1
- Activin receptor type-1
- Bone morphogenetic protein receptor type-1B
- Bone morphogenetic protein receptor type-2
- E3 ubiquitin-protein ligase SMURF1
- Mothers against decapentaplegic homolog 7
- Mothers against decapentaplegic homolog 3
Sequence:
MTSMASLFSFTSPAVKRLLGWKQGDEEEKWAEKAVDALVKKLKKKKGAMEELEKALSSPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLDICEFPFGSKQKEVCINPYHYKRVESPVLPPVLVPRHNEFNPQHSLLVQFRNLSHNEPHMPQNATFPDSFHQPNNAPFPLSPNSPYPPSPASSTYPNSPASSGPGSPFQLPADTPPPAYMPPDDQMAPDNSQPMDTSSNMIPQTMPSISSRDVQPVAYEEPKHWCSIVYYELNNRVGEAFHASSTSVLVDGFTDPSNNKSRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLSDSSIFVQSRNCNFHHGFHPTTVCKIPSSCSLKIFNNQEFAQLLAQSVNHGFEAVYELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPLNPISSVS
Protein: Conidiogenone synthase PrP450 (EC 1.-.-.-) (Conidiogenone biosynthesis cluster protein PrP450) (Cytochrome P450 monooxygenase PrP450) (W6Q9B3)
Organism: Penicillium roqueforti (strain FM164)
Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of conidiogenone, a diterpene known to induce the conidiation. The bifunctional terpene synthase PrDS converts isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) into deoxyconidiogenol. The C-terminal prenyltransferase (PT) domain of PrDS catalyzes formation of GGPP, whereas the N-terminal terpene cyclase (TC) domain catalyzes the cyclization of GGPP into deoxyconidiogenol. The cytochrome P450 monooxygenase PrP450 then catalyzes two rounds of oxidation to furnish conidiogenone.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- DNA 3'-5' helicase
- Nitrate reductase
Sequence:
MLLLWFGFFSFIFGVVIYRLYFHPLSKFPGPKLAALTSLYEFYYNVVLGGRYLWEIERMHEKYGPIVRITPHELHVADPNFYTEIYAGPTRRRDKDPRLVRLAGQPTSMFATVDHGLHSSRRAILNSYFSKKSIAGLEDMIQGKVQKLVKRLSMACDQGTVVKLDAASSALTADIISEYAHGFFPFLLDLSKFIPDKVLEKLWFHAANILRLQKLVRAQADVALQNGGKVDGQATMFGALCDPSLPVQERTLDRLQDEGFSLIGGGTETTTGTLKIVMFHLLNEKALLLKLREELEQYPSSTWADLEKLPYMRGTINEGLRLSGVITRLPRRAPDEALVYKQWTIPPNSLMSTSSHFVHTNSDLFPNPLAFDPERWIRAEAAGQRLEHMIVTFSKGSRQCMGNHLALAELYLVISTLVRRFDMDLYGVTADNIVTHREYGFGVPKERGEGLRVSITRVRDP
Protein: S-methyl-5'-thioadenosine phosphorylase (EC 2.4.2.28) (5'-methylthioadenosine phosphorylase) (MTA phosphorylase) (MTAP) (MTAPase) (C8VP37)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03155}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03155}.
Interaction partners:
- adenine phosphoribosyltransferase
- SPEE_NEUCR Spermidine synthase
- Epoxide hydrolase, putative
- Epoxide hydrolase, putative
- Epoxide hydrolase, putative
- Methylthioribose-1-phosphate isomerase
- Nicotinamide-nucleotide adenylyltransferase
- Xanthine-guanine phosphoribosyl transferase Xpt1, putative
Sequence:
MFLRSVSSITKPFRRIESPKQLARRMAVLPDTYADPVRIAVIGGTGLRELPGFTQVASLNIQTPWGTPSSPITILHHTHKDKTVAVAFLSRHGLHHQIAPHEVPARANIAALRSIGVRTIIAFSAVGSLQEEIKPRDFVVPDQVIDRTKGIRPFTFFEGGVVGHVPFGDPFDESVAKIVRACGHSLEGEGVKLHDRGTLICMEGPQFSTRAESKLYRSWGGSVINMSCLPEAKLAREAEIAYQMICMSTDYDCWHESTEDVTVEMVMGNMKANAVNAKHFVTAVLDELADDRNAELVQAKQYAGSVKFGLSTAQANWSPEARERMNWLFPGYFEIDLYIRYLLLIQRDIDLTSWN
Protein: Translationally-controlled tumor protein (A0A0P1J1R0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MIIYRDLISHDEMFSDIYKIREIADGLCLEVEGKMVSRTEGNIDDSLIGGNASAEGPEGEGTESTVITGVDIVMNHHLQETSFTKEAYKKYIKDYMKSIKGKLEEQRPERVKPFMTGAAEQIKHILANFKNYQFFIGENMNPDGMVALLDYREDGVTPYMIFFKDGLEMEKC
Protein: Autophagy-related protein 34 (Q12292)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Cargo-receptor protein involved in the cytoplasm to vacuole transport (Cvt) and in autophagy. Recognizes cargo proteins, such as AMS1 and delivers them to the pre-autophagosomal structure for eventual engulfment by the autophagosome and targeting to the vacuole.
Subcellular location: Preautophagosomal structure membrane {ECO:0000269|PubMed:20639194}; Peripheral membrane protein {ECO:0000269|PubMed:20639194}. Note=Membrane-associated protein found in pre-autophagosomal structure and other perivacuolar punctate structures.
Interaction partners:
- Alpha-mannosidase
- Vacuolar aminopeptidase 1
- Autophagy-related protein 11
- Autophagy-related protein 19
- Autophagy-related protein 8
- Autophagy-related protein 39
- Autophagy-related protein 36
- Autophagy-related protein 40
- Autophagy-related protein 32
- Aspartyl aminopeptidase 4
Sequence:
MKIAVETTLFDFFVIDQFKKSTFSAPNTKVDTIKGCINKFIEQFNVYDEQHIFWQPPGKSNVRLLSNANDFGQLGNFLHKKIKCNIFIGEEALRKYDLNICGPYDKFVENSDPSVKKVVNRDDVMLSRKCLNIISEQLSILEKSISKAQNQVLQSSEVEGKKCIILPEDKPELIKFFSKFETSVQLQEVYEGYKVYEKLLQKFGGQKKRMESFLNENTPMSGAEAIKQINISEELKEKGERLTTPNDPLLHVEVSNEDNSLHFILYNKTNIIIPGNCTFEFSSQISEVFSIKMGPHEIGIKGQKELWFFPSLPTPLSNYTMKVVNQDGETILVGKCADSNEITLKSPLASFSTGSFQTGSFHTLQDPTNVFRADALSSPDESSIMSTPFLGETDEVYNSGSTLSRPFTWEEI
Protein: Rho guanine nucleotide exchange factor 2 (Guanine nucleotide exchange factor H1) (F1RLP5)
Organism: Sus scrofa (Pig)
Subcellular location: Cell junction, tight junction {ECO:0000256|ARBA:ARBA00004435}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}. Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00004541}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
Sequence:
MSRIESLTRARIDRSKELASKTREKEKMKEAKDARYTNGHLFTTISVSGMTMCYACNKSITAKEALICPTCNVTIHNRCKDTLANCTKVKQKQQKAALLKNNTALQSVSLRSKTTTRERPSSAIYPSDSFRQSLLGSRRGRSSLSLAKSVSTTNIAGHFNDESPLGLRRILSQSTDSLNMRNRTLSVESLIDEAEVIYNELMSDFEMGEKDFAADSWSLAVDSSFLQQHKKEVMKQQDVIYELIQTELHHVRTLKIMTRLFRTGMLEELQLEPGVVQGLFPCVDELSDIHTRFLSQLLERRRQALCPGSPRNFVIHRLGDLLITQFSGPSADQMRKTYSEFCSRHTKALKLYKELYARDKRFQQFIRKVTRSAVLKRHGVQECILLVTQRITKYPVLISRILQHTHGIEEERQDLTTALGLVKELLSNVDQDVHELEKGARLQEIYNRMDPRAQTPVPGKGPFGREELLRRKLIHDGCLLWKTAAGRFKDVLMLLMTDVLVFLQEKDQKYIFPALDKPSVVSLQNLIVRDIANQEKGMFLISAAPPEMYEVHTASRDDRSTWIRVIQQSVRVCPSREDFPLIETEDEAYLRRIKMELQQKDRALVELLQEKVGLFAEMTHFQVEEDGGGGMPLPTLPRGLFRSESLESPRGERLLQDAIREVEGLKDLLVGPGVELLLTSREPALPVETDSGGNTSPGVTANGEARTFNGSIELCRADSDSSQKDRNGNQLRSPQEEALQRLVNLYGLLHGLQAAVAQQDTLMEARFPEGPERREKLTRANSRDGEAGRAGAAPVAPEKQATELALLQRQHALLQEELRRCRRLGEERATEAGSLEARLRESEQARALLEREVEEARRQLAALGHTEPLPAEAPWARRPLDPRRRSLPAGDALYLSFTPPQPSRGHDRLDLPVTIRSVHRPFEDRERQELGSPDERLQDSSDPDTGSEEEGSSSRLSPPHSPRDFTRMQDIPEETESRDGEPVASES
Protein: Chromodomain helicase DNA binding protein 8 (H0YJG4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XKRIQSRHPELKRVNRPQASAWKKLELSHEYKNRNQLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYHGSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRRLKEDVEKNLAPKQETIIEVELTNIQKKYYRAILEKNFSFLSKGAGHTNMPNLLNTMMELRKCCNHPYLINGAEEKILTEFREACHIIPHDFHLQAMVRSAGKLVLIDKLLPKLKAGGHKVLIFSQMVRCLDILEDYLIQRRYLYERIDGRVRGNLRQAAIDRFSKPDSDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAVLQSMSGRDGNITGIQQFSKKEIEDLLRKGAYAAIMEEDDEGSKFCEEDIDQILLRRTTTITIESEGKGSTFAKASFVASENRTDISLDDPNFWQKWAKKADLDMDLLNSKNNLVIDTPRVRKQTRHFSTLKDDDLVEFSDLESEDDERPRSRRHDRHHAYGRTDCFRVEKHLLVYGWGRWRDILSHGRFKRRMTERDVETICRAILVYCLLHYRGDENIKGFIWDLISPAENGKTKELQNHSVFDVSPFPGLSIPVPRGRKGKKVKSQSTFDIHKADWIRKYNPDTLFQDESYKKHLKHQCNKVLLRVRMLYYLRQEVIGDQAEKVLGGAIASEIDIWFPVVDQLEVPTTWWDSEADKSLLIGVFKHGYEKYNTMRADPALCFLEKAGRPDDKAIAAEHRVLDNFSDIVEGVDFDKDCEDPEYKPLQGPPKDQDDEGDPLMMMDEEISVIDGDEAQVTQQPGHLFWPPGSALTARLRRLVTAYQRSYKREQMKIEAAERGDRRRRRCEAAFKLKEIARREKQQRWTRREQTDFYRVVSTFGVEYDPDTMQFHWDRFRTFARLDKKTDESLTKYFHGFVAMCRQVCRLPPAAGDEPPDPNLFIEPITEERASRTLYRIELLRRLREQVLCHPLLEDRLALCQPPGPELPKWWEPVRHDGELLRGAARHGVSQTDCNIMQDPDFSFLAARMNYMQNHQAGAPAPSLSRCSTPLLHQQYTSRTASPLPLRPDAPVEKSPEETATQVPSLESLTLKLEHEVVARSRPTPQDYEMRVSPSDTTPLVSRSVPPVKLEDEDDSDSELDLSKLSPSSSSSSSSSSSSSSTDESEDEKEEKLTDQSRSKLYDEESLLSLTMSQDGFPNEDGEQMTPELLLLQERQRASEWPKDRVLINRIDLVCQAVLSGKWPSSRRSQEMVTGGILGPGNHLLDSPSLTPGEYGDSPVPTPRSSSAASMAEEEASAVSTAAAQFTKLRRGMDEKEFTVQIKDEEGLKLTFQKHKLMANGVMGDGHPLFHKKKGNRKKLVELEVECMEEPNHLDVDLETRIPVINKVDGTLLVGEDAPRRAELEMWLQGHPEFAVDPRFLAYMEDRRKQKWQRCKKNNKAELNCLGMEPVQTANSRNGKKGHHTETVFNRVLPGPIAPESSKKRARRMRPDLSKMMALMQGGSTGSLSLHNTFQHSSSGLQSVSSLGHSSATSASLPFMPFVMGGAPSSPHVDSSTMLHHHHHHPHPHHHHHHHPGLRAPGYPSSPVTTASGTTLRLPPLQPEEDDDEDEEDDDDLSQGYDSSERDFSLIDDPMMPANSDSSEDADD
Protein: Cytohesin-2 (ARF nucleotide-binding site opener) (Protein ARNO) (PH, SEC7 and coiled-coil domain-containing protein 2) (CLM2) (SEC7 homolog B) (mSec7-2) (P63034)
Organism: Mus musculus (Mouse)
Function: Acts as a guanine-nucleotide exchange factor (GEF). Promotes guanine-nucleotide exchange on ARF1, ARF3 and ARF6. Activates ARF factors through replacement of GDP with GTP. The cell membrane form, in association with ARL4 proteins, recruits ARF6 to the plasma membrane (By similarity). Involved in neurite growth.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q99418}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q99418}. Cytoplasm {ECO:0000269|PubMed:25326380}. Cell projection {ECO:0000269|PubMed:25326380}. Cell projection, growth cone {ECO:0000269|PubMed:25326380}. Cell junction, tight junction {ECO:0000269|PubMed:20080746}. Cell junction, adherens junction {ECO:0000269|PubMed:20080746}. Note=Recruited to the cell membrane through its association with ARL4A, ARL4C and ARL4D. Also requires interaction with phosphoinositides for targeting to plasma membrane (By similarity). In differentiating neuroblastoma cells, colocalizes with CCDC120 in both neurite shaft and growth cone areas. {ECO:0000250, ECO:0000269|PubMed:25326380}.
Interaction partners:
- ADP-ribosylation factor 6
- ADP-ribosylation factor 1
- ADP-ribosylation factor 2
- General receptor for phosphoinositides 1-associated scaffold protein
- ADP-ribosylation factor 3
- Coiled-coil domain-containing protein 120
- Interactor protein for cytohesin exchange factors 1
- ADP-ribosylation factor-like protein 4D
Sequence:
MEDGVYEPPDLTPEERMELENIRRRKQELLVEIQRLREELSEAMSEVEGLEANEGSKTLQRNRKMAMGRKKFNMDPKKGIQFLVEHELLQNTPEEIARFLYKGEGLNKTAIGDYLGEREELNLSVLHAFVDLHEFTDLNLVQALRQFLWSFRLPGEAQKIDRMMEAFAQRYCLCNPGVFQSTDTCYVLSFAVIMLNTSLHNPNVRDKPGLERFVAMNRGINEGGDLPEDLLRNLYDSIRNEPFKIPEDDGNDLTHTFFNPDREGWLLKLGGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVDDPRKPNCFELYIPNNKGQLIKACKTEADGRVVEGNHMVYRISAPTQEEKDEWIKSIQAAVSVDPFYEMLAARKKRISVKKKQEQP
Protein: Phosphatidylinositol/phosphatidylcholine transfer protein SFH1 (Phosphatidylinositol transfer protein 1) (AtPITP1) (Protein CAN OF WORMS1) (Protein SEC FOURTEEN HOMOLOGS 1) (AtSFH1) (Protein SHORT ROOT HAIR 1) (F4JLE5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for transport of secretory proteins from the Golgi complex (By similarity). Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes in vitro. Plays a role in root hair tip elongation as a key regulator of polarized membrane trafficking. May promote the PtdIns(4,5)P2 synthesis and organization in root hair membrane.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:15728190}; Peripheral membrane protein {ECO:0000269|PubMed:15728190}.
Interaction partners:
- Phosphatidylinositol 4-phosphate 5-kinase 3
- Adenine nucleotide alpha hydrolases-like superfamily protein
- Expansin-A7
- Phosphoinositide phosphatase SAC7
- Leucine-rich repeat extensin-like protein 1
- ADP-ribosylation factor GTPase-activating protein AGD1
- Putative pectinesterase/pectinesterase inhibitor 24
- Uncharacterized protein
- Sec14p-like phosphatidylinositol transfer family protein
- Transcription factor RHD6
Sequence:
MAETKPEIEMSEEERKIVKISSLKKKAINASNRFKNSFKKKGRRSSSRVMSVPIEDDIDAEDLQALDAFRQALILDELLPSKLDDLHMMLRFLRARKFDIEKAKQMWSDMIQWRKDFGADTIIEDFDFEEIDEVMKHYPQGYHGVDKEGRPVYIERLGQIDANKLLQVTTMDRYVKYHVKEFEKTFKVKFPSCSVAANKHIDQSTTILDVQGVGLKNFSKSARELLQRLCKIDNENYPETLNRMFIINAGSGFRLLWSTVKSFLDPKTTAKIHVLGNKYHSKLLEVIDASELPEFFGGACTCEDKGGCMRSDKGPWNDPEVLKIAINREAKCSPISEDEHKHVDQGRSTSGFESLERIKKKTDEDNVYEKQIATIDKSMDMAWLAKTQKAENFPISKGLECYVRKGAPKKGDGLLVGGVMAFVMGIVAMVRLSKDVPRKLTEAALYGNSVCYEESTKSKQNQGQFAAPVSSSEYMLMVKRMAELEDKCMFLDLKPAHVESEKEEKLQAALNRVQVLEQELTETKKALEEALVSQKEILAYIEKKKKKKKLFFGF
Protein: Synaptic vesicle glycoprotein 2B (Synaptic vesicle protein 2B) (Q63564)
Organism: Rattus norvegicus (Rat)
Function: Probably plays a role in the control of regulated secretion in neural and endocrine cells.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:16306227, ECO:0000269|PubMed:7681585}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:12754292}. Note=Associated with synaptic-like microvesicles but not with insulin-containing vesicles in insulin-secreting cells of the pancreas (PubMed:16306227). Localizes to microvesicles in the pinealocytes. Localizes to the acrosome in spermatids (PubMed:12754292). {ECO:0000269|PubMed:12754292, ECO:0000269|PubMed:16306227}.
Interaction partners:
Sequence:
MDDYRYRDNYEGYAPNDGYYRGNEQNPEEDAQSDVTEGHDEEDEIYEGEYQGIPHPDDVKSKQTKMAPSRADGLRGQADLMAERMEDEEQLAHQYETIIDECGHGRFQWTLFFVLVLALMADGVEVFVVSFALPSAEKDMCLSSSKKGMLGLIVYLGMMAGAFILGGLADKLGRKKVLSMSLAINASFASLSSFVQGYGAFLFCRLISGIGIGGSLPIVFAYFSEFLSREKRGEHLSWLGIFWMTGGIYASAMAWSIIPHYGWGFSMGTNYHFHSWRVFVIVCALPATVSMVALKFMPESPRFLLEMGKHDEAWMILKQVHDTNMRAKGTPEKVFTVSHIKTPKQMDEFIEIQSSTGTWYQRWLVRFMTIFKQVWDNALYCVMGPYRMNTLILAVVWFTMALSYYGLTVWFPDMIRYFQDEEYKSKMKVFFGEHVHGATINFTMENQIHQHGKLVNDKFIKMYFKHVLFEDTFFDKCYFEDVTSTDTYFKNCTIESTTFYNTDLYKHKFIDCRFINSTFLEQKEGCHMDFEEDNDFLIYLVSFLGSLSVLPGNIISALLMDRIGRLKMIGGSMLISAVCCFFLFFGNSESAMIGWQCLFCGTSIAAWNALDVITVELYPTNQRATAFGILNGLCKLGAILGNTIFASFVGITKVVPILLAAASLVGGGLVALRLPETREQVLM
Protein: Small proline-rich protein 3 (Cornifin beta) (O09116)
Organism: Mus musculus (Mouse)
Function: Cross-linked envelope protein of keratinocytes.
Subcellular location: Cytoplasm.
Interaction partners:
- Keratin, type I cytoskeletal 13
- Keratin, type II cytoskeletal 4
- Cornifelin
- Small proline-rich protein 2A3
- Late cornified envelope 3A
- Small proline-rich protein 4
- Protein-glutamine gamma-glutamyltransferase E
- Loricrin
Sequence:
MSSYQQKQPFVPPPQPEQHQVKQPCQPPPQGKFVPIATSEPCHTDVPQPGNTKIPEPCSTKVPEPGNTVVLEPDYTTMPGPCSTNITEPDYTTIPGPCSTNITEPDYTTIPGPCSTNIPGPDRTVVPGSCSTNITEPDYTTIPGPSSTKIPDPGCAMVPGPSPSSTSEPSSEPCSINVREPGYMNASEPTHAKVPDQGYTKIPDQGSSKVPEPCQSRVPEVCPPTVTPVSAKQKTKQK
Protein: PslA (Q9I1N8)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Alginate biosynthesis protein AlgA
- PslD
- dTDP-Rha:alpha-D-Gal-diphosphoundecaprenol alpha-1,3-rhamnosyltransferase
- PslE
- PslJ
- PslH
- PslF
- Alginate biosynthesis protein AlgA
- GDP-mannose 4,6-dehydratase
- PslI
Sequence:
MHSKSVDSLSLTRAGFIEYFLVATKLVHALTAIAPALFLLYYPGLVPVELRSNMLGLLLFFGALTVIMFQALDVYSDDIFSNRLRFRIMFFAWASAFCLLLFMYQGLGLFPYLSSKLVIFWFTGSLLLFGVQRLLVLRLYRAWMKRGMYLQRTVILGFTESGMHLAEYLVRNHDIRSGIIGFIDDRSERVPENYNSLPLLGNTKDLEKLIRQEQVDQVLVALPWFAEGRIGAIVHRLRQLPVNVLLVPDMAAFRHAHNRIVDVSGIPMFNASELPLRGWSPLIKRCEDLVLASIALVLFAPLMALVALAIRLDSKGPVLFRQKRYGYNNRLIWVFKFRSMYTERTDANAERQTTRDDDRITRVGRFIRKTSIDELPQLFNVLAGSMSMVGPRPHATATKAAGIPFEEAVSEYSSRHRVKPGITGWAQINGYRGETDTLHKIKKRVEYDLEYIAKWSVWFDLYILFRTVPAVLLTKEVY
Protein: Thioredoxin-dependent peroxide reductase, mitochondrial (EC 1.11.1.24) (Antioxidant protein 1) (AOP-1) (Peroxiredoxin-3) (Protein SP-22) (Thioredoxin-dependent peroxiredoxin 3) (P35705)
Organism: Bos taurus (Bovine)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol (By similarity). Required for the maintenance of physical strength (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:8089078}. Cytoplasm {ECO:0000250|UniProtKB:P30048}. Early endosome {ECO:0000250|UniProtKB:P30048}. Note=Localizes to early endosomes in a RPS6KC1-dependent manner. {ECO:0000250|UniProtKB:P30048}.
Interaction partners:
- Peroxiredoxin-5, mitochondrial
- Thioredoxin, mitochondrial
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- Thioredoxin
- Non-selective voltage-gated ion channel VDAC1
- Superoxide dismutase, mitochondrial
- Sulfiredoxin 1.
- Thioredoxin
- Thioredoxin reductase 2, mitochondrial
- Adrenodoxin, mitochondrial
Sequence:
MAATAGRLFRASLIRHVSAIPWGISASAALRPAASRRMCLTNALWSGSDQAKFAFSTSSSYHAPAVTQHAPYFKGTAVVSGEFKEISLDDFKGKYLVLFFYPLDFTFVCPTEIIAFSDKASEFHDVNCEVVAVSVDSHFSHLAWINTPRKNGGLGHMNIALLSDLTKQISRDYGVLLEGPGLALRGLFIIDPNGVIKHLSVNDLPVGRSVEETLRLVKAFQFVEAHGEVCPANWTPESPTIKPHPTASREYFEKVNQ
Protein: Non-structural maintenance of chromosome element 5 (Non-SMC element 5) (Q03718)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks.
Subcellular location: Nucleus {ECO:0000269|PubMed:14690591}. Chromosome {ECO:0000250|UniProtKB:O94668}.
Interaction partners:
- DNA repair protein KRE29
- E3 SUMO-protein ligase MMS21
- Structural maintenance of chromosomes protein 5
- Structural maintenance of chromosomes protein 6
- Non-structural maintenance of chromosome element 3
- Non-structural maintenance of chromosome element 4
- Non-structural maintenance of chromosomes element 1
- Regulator of Ty1 transposition protein 107
- SUMO-conjugating enzyme UBC9
- E3 SUMO-protein ligase SIZ2
Sequence:
MDGALINSVLYVSPRNGAHYFVELTEKHLLAFEMLNSMCLLENYDHVLLFLECQFGKSHNLAVIPFDIILVLFTLSTLSEYYKEPILRANDPYNTSRETLSRRALKLLQKYLAILKEFDSEQYNLYDLELLRCQFFLAIDTLTPKKQKWGFDRFRRTKSESGVTYRQNASVDPELDQAKTFKNPYRSYISCLEQRNTILGNRLLNLKLNEPGEFINMILWTLSNSLQESTPLFLSSHEIWMPLLEILIDLFSCRQDYFIQHEVAQNVSKSLFVQRLSESPLAVFFESLNTRNFANRFSEYVFLNCDYKLPSDNYATPVHPVYNGENTIVDTYIPTIKCSPLYKSQKSLALRRKLIGSCFKLLLRVPDGHRLITPRIVADDVIQGISRTLASFNDILQFKKFFMTENLSQESYFIPLLAEGTLSEILKDTQECVVILTLVENLSDGVSFCNEVIGLVKSKCFAFTEQCSQASYEEAVLNIEKCDVCLLVLLRYLLHLIGTEAILDAKEQLEMLHAIEKNDSGRRQWAKALNLGNDPPLLYPIVSQMFGVHDKSVIIE