wanglab/gogpt-training-data huggingface dataset:
Protein: Adhesion G protein-coupled receptor F5 (G-protein coupled receptor 116) (Q8IZF2)
Organism: Homo sapiens (Human)
Function: Receptor that plays a critical role in lung surfactant homeostasis. May play a role in controlling adipocyte function.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23590306, ECO:0000269|PubMed:23684610}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Surfactant protein C
- Pulmonary surfactant-associated protein B
- Receptor activity-modifying protein 2
Sequence:
MKSPRRTTLCLMFIVIYSSKAALNWNYESTIHPLSLHEHEPAGEEALRQKRAVATKSPTAEEYTVNIEISFENASFLDPIKAYLNSLSFPIHGNNTDQITDILSINVTTVCRPAGNEIWCSCETGYGWPRERCLHNLICQERDVFLPGHHCSCLKELPPNGPFCLLQEDVTLNMRVRLNVGFQEDLMNTSSALYRSYKTDLETAFRKGYGILPGFKGVTVTGFKSGSVVVTYEVKTTPPSLELIHKANEQVVQSLNQTYKMDYNSFQAVTINESNFFVTPEIIFEGDTVSLVCEKEVLSSNVSWRYEEQQLEIQNSSRFSIYTALFNNMTSVSKLTIHNITPGDAGEYVCKLILDIFEYECKKKIDVMPIQILANEEMKVMCDNNPVSLNCCSQGNVNWSKVEWKQEGKINIPGTPETDIDSSCSRYTLKADGTQCPSGSSGTTVIYTCEFISAYGARGSANIKVTFISVANLTITPDPISVSEGQNFSIKCISDVSNYDEVYWNTSAGIKIYQRFYTTRRYLDGAESVLTVKTSTREWNGTYHCIFRYKNSYSIATKDVIVHPLPLKLNIMVDPLEATVSCSGSHHIKCCIEEDGDYKVTFHTGSSSLPAAKEVNKKQVCYKHNFNASSVSWCSKTVDVCCHFTNAANNSVWSPSMKLNLVPGENITCQDPVIGVGEPGKVIQKLCRFSNVPSSPESPIGGTITYKCVGSQWEEKRNDCISAPINSLLQMAKALIKSPSQDEMLPTYLKDLSISIDKAEHEISSSPGSLGAIINILDLLSTVPTQVNSEMMTHVLSTVNVILGKPVLNTWKVLQQQWTNQSSQLLHSVERFSQALQSGDSPPLSFSQTNVQMSSMVIKSSHPETYQQRFVFPYFDLWGNVVIDKSYLENLQSDSSIVTMAFPTLQAILAQDIQENNFAESLVMTTTVSHNTTMPFRISMTFKNNSPSGGETKCVFWNFRLANNTGGWDSSGCYVEEGDGDNVTCICDHLTSFSILMSPDSPDPSSLLGILLDIISYVGVGFSILSLAACLVVEAVVWKSVTKNRTSYMRHTCIVNIAASLLVANTWFIVVAAIQDNRYILCKTACVAATFFIHFFYLSVFFWMLTLGLMLFYRLVFILHETSRSTQKAIAFCLGYGCPLAISVITLGATQPREVYTRKNVCWLNWEDTKALLAFAIPALIIVVVNITITIVVITKILRPSIGDKPCKQEKSSLFQISKSIGVLTPLLGLTWGFGLTTVFPGTNLVFHIIFAILNVFQGLFILLFGCLWDLKVQEALLNKFSLSRWSSQHSKSTSLGSSTPVFSMSSPISRRFNNLFGKTGTYNVSTPEATSSSLENSSSASSLLN
Protein: Variant surface glycoprotein (VSG), putative (Q38G20)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MCAPCHYSKASIDCRGMTSKRAVSLLLLALASASSSSASHVAVKSELWKPQCELAKELRKTAGITISKLSAKLTAIDNLNKMSMRLLLFGQRTSPLDNQVTALALALAAQKKAAKIQSTVSDSVKTGLLATQYSGELAGGIVSAVHFLKHASDGAHYCLNSNGKKGDGRPAVDTTGCATLTATEVSTETGFNKGDINDDGFVKLTALTTTDGAGQTGTCGVFETASGSGSTTAGIQISAGAKVHLAFGAIEGTTSQQPTRPALNKFEGANLEAEQTFFGKAHKSLKALTLDTTENALEDPKAMLKQLATEAEAMEALYTVLSGASPNKKPTEFSAQNQQLKIRYFGADGEKTEKLWEQITAGKTIGAGEDPHKFSNLSEVSTADDLSKALFFYTAATLTATRELKSENSRLKETTAKAEKTQEQICNAIQNEKDCGNNENCKYDKDKTEGPKCILSDKGKKAAEKANQEPGGKDGKTTTNTTGSNSFVINKAPLLLAVFLL
Protein: Fibroblast growth factor-binding protein 1 (FGF-BP) (FGF-BP1) (FGF-binding protein 1) (FGFBP-1) (Growth factor-binding protein 1) (Q9QY10)
Organism: Rattus norvegicus (Rat)
Function: Acts as a carrier protein that release fibroblast-binding factors (FGFs) from the extracellular matrix (EM) storage and thus enhance the mitogenic activity of FGFs. Enhances FGF2 signaling during tissue repair, angiogenesis and in tumor growth (By similarity).
Subcellular location: Secreted, extracellular space {ECO:0000250|UniProtKB:Q14512}. Cell membrane {ECO:0000250|UniProtKB:Q14512}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14512}. Note=Extracellular and plasma membrane-associated. {ECO:0000250|UniProtKB:Q14512}.
Interaction partners:
- Fibroblast growth factor 10
- Fibroblast growth factor
- Fibroblast growth factor 7
- Fibroblast growth factor 2
- Fibroblast growth factor 1
- Fibroblast growth factor
- Fibroblast growth factor 20
- Fibroblast growth factor 18
- Fibroblast growth factor 5
- Fibroblast growth factor
Sequence:
MRIHGLILLSFLLLAAQVLSEKVRKTAKNVPDSTTEEDMSPSLGKARNKQRSRTSKSMTHGRFVTKDQATCRWAVTEEELGINLKVQCTRADQEFSCVFAGDPTGCLKYDKDQTYWKQVARTLRKQKNICENSKSVLKTRVCRKKFPESNLKVVNPRKEKAEVSPREHNKVQEAVSMEPNKVKVDITTSPAATVAVKDSECLEDPDVLTQRKTALEFCGESWSSFCTFFLNMLQATSC
Protein: Katanin p60 ATPase-containing subunit A1 (Katanin p60 subunit A1) (EC 5.6.1.1) (p60 katanin) (Q5RII9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000255|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O75449}. Note=Predominantly cytoplasmic. Also localized to the interphase centrosome and the mitotic spindle poles. Enhanced recruitment to the mitotic spindle poles requires microtubules and interaction with katnb1. {ECO:0000255|HAMAP-Rule:MF_03023}.
Interaction partners:
- Katanin p80 WD40 repeat-containing subunit B1
- Glycerol-3-phosphate dehydrogenase, mitochondrial
Sequence:
MSLGEINENVKLAREYALLGNYSSAVVCYQGVLEQIKKYLYSVRDSSLQQKWQQVWQEINEETKQVREIMTTLESFQMESTPSKPSSFAQDNDIMPVHVEHRSSPCVVRKSSVPYKDSKGHGNRLSVGPRGQARPSPRVANGDKGKPQKSKEKKENPSKPKEDKNKAEAVETEVKRFDRGGEDKDLIDALERDIISQNPNVTWDDIADLEEAKKLLKEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECRTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKAELLVQMDGVGGTSENDPSKMVMVLAATNFPWDIDEALRRRLEKRIYIPLPSAKGRVDLLKINLKELDLANDVNMDKIAEQMEGYSGADITNVCRDASLMAMRRRIEGLTPEEIRNLPKDEMHMPTTMEDFETALKKVSKSVSAADLEKYEKWIAEFGSC
Protein: ER membrane protein complex subunit 1 (Q8C7X2)
Organism: Mus musculus (Mouse)
Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors. By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8N766}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8N766}.
Interaction partners:
- ER membrane protein complex subunit 3
- ER membrane protein complex subunit 2
- ER membrane protein complex subunit 4
- ER membrane protein complex subunit 6
- Endoplasmic reticulum membrane protein complex subunit 7
- ER membrane protein complex subunit 5
- ER membrane protein complex subunit 10
- ER membrane protein complex subunit 8
- ER membrane protein complex subunit 9
- Membrane magnesium transporter 2
Sequence:
MAVAVASGFWIWAAVLLVPAAAVYEDQVGKFDWRQQYVGKIKFASLEFSPGSKKLVVATEKNVIAALNSRTGEILWRHVDKGTAEGAVDAMLVHGQDAITVSNGGRLMRSWETNIGGLNWEITLDTGSFQALGLVGLQESVRYIAVLKKTTLTLHHLSSGHLKWVEHLPESDSILYQMVYSYGSGVVWALGIVPFSHVNIVKFNVEDGEIVQQVRVWTPWLQHLTGACGVVDEAVLVCPDPSSHSLHTLALETEWELRQIPLQSPDLEFGSGFQPQVLPTQPSPVAPSRAQFFLQLSPSHYALLHYHHGAVTLLKNFPQATLVSFATTGEKTVAAVMTCRTEVQKPVSAGDGSVASFPETSGAQDSLACFNQTYTINLYLVETGRRLLDTSISFSLEQKGTRPEQLYIQVFLKKDDSVGYRALVQTQDHLQLFLQQLAGKVVLWSREESLAEVVCLEMVDLPLTGAQAELEGEFGKKAAIQDGLLGMFLKRLSSQLILLQAWTSHLWKMFYDARKPRSQIKNEINIDTLARDEFNLQKMMVTVTASGKLFGIESSSGTILWKQYLPNVKPDSSFKLMVQRTTAHFPHPPQCTLLVKDKETGMSSLFVFNPIFGKWSQVAPPVLKRPILQSLLLPVMDQDYAKVLLLVDDEYKVTAFPATRNVLRQLHELAPSIFFYLVDAEQGRLSGYQLRKDLTTELSWELTIPPEVQRVVKVKGKRSSEHVHSQGRVMGDRSVLYKSLNPNLLAVVTESTDVHHERTFIGIFLIDGVTGRIIHSSVQKKARGPVHLVHSENWVVYQYWNSKARRNELTALELYEGTEQYNATAFSSLDRPQLPQVLQQSYIFPSSISAMEATITERGITSRHLLIGLPSGAILSLPKALLDPRRPEIPTEQSREENLIPYSPDVQVHAERFINYNQTVSRMRGIYTAPSGLESTCLVVAYGLDIYQTRVYPSKQFDVLKDDYDYVLISSVLFGLVFATMITKRLAQVKLLNRAWR
Protein: Sec translocon accessory complex subunit YajC (P0ADZ7)
Organism: Escherichia coli (strain K12)
Function: The SecYEG-SecDF-YajC-YidC holo-translocon (HTL) protein secretase/insertase is a supercomplex required for protein secretion, insertion of proteins into membranes, and assembly of membrane protein complexes. The SecYEG complex is essential for assembly of a number of proteins and complexes, assembly is facilitated in the presence of the SecDF-YajC-YidC subcomplex.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:27435098}; Single-pass membrane protein {ECO:0000269|PubMed:16079137}.
Interaction partners:
- Protein translocase subunit SecF
- Protein translocase subunit SecD
- Membrane protein insertase YidC
- Protein translocase subunit SecE
- Protein translocase subunit SecA
- Protein translocase subunit SecY
- Protein-export membrane protein SecG
- Signal recognition particle receptor FtsY
- Protein-export protein SecB
- Signal recognition particle protein
Sequence:
MSFFISDAVAATGAPAQGSPMSLILMLVVFGLIFYFMILRPQQKRTKEHKKLMDSIAKGDEVLTNGGLVGRVTKVAENGYIAIALNDTTEVVIKRDFVAAVLPKGTMKAL
Protein: Growth hormone secretagogue receptor type 1 (GH-releasing peptide receptor) (Ghrelin receptor) (A8CGH3)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MRSWPNRTDCLSPVNCSWEDNYWNYYFNGSYQGPVPPENLFPIPVLMGITITCTLLFLAGVAGNVMTILVVSKYRDMRTTTNLYLCSMAVSDLLIFLCMPPDVYRLWKYRPWIFGDTFCKLFQFVSECCTYSTILNITALSVERYLAICFPLRAKRLVTKRRVRALILFLWLVSLLSAGPVFVLVGVEHETRPAAGNSVTAGGAEGQTEIDTSECKPTQYAVESGLLAAMALVSSVFFFLPVFCLTVVYSLIGRRLWKRRRENNIGANVAHRDKSNRQTVKMLGRVQYMLLIFKTILTTA
Protein: Macrosialin (Gp110) (CD antigen CD68) (P34810)
Organism: Homo sapiens (Human)
Function: Could play a role in phagocytic activities of tissue macrophages, both in intracellular lysosomal metabolism and extracellular cell-cell and cell-pathogen interactions. Binds to tissue- and organ-specific lectins or selectins, allowing homing of macrophage subsets to particular sites. Rapid recirculation of CD68 from endosomes and lysosomes to the plasma membrane may allow macrophages to crawl over selectin-bearing substrates or other cells.
Subcellular location: [Isoform Short]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform Long]: Endosome membrane; Single-pass type I membrane protein. Lysosome membrane; Single-pass type I membrane protein.
Interaction partners:
- Lysosome-associated membrane glycoprotein 3
- Scavenger receptor cysteine-rich type 1 protein M130
- Lysosome-associated membrane glycoprotein 1
- T-cell surface glycoprotein CD1e, membrane-associated
- T-cell surface glycoprotein CD1a
- T-cell surface glycoprotein CD1b
- T-cell surface glycoprotein CD4
- Integrin alpha-M
- T-cell surface glycoprotein CD8 alpha chain
- T-cell surface glycoprotein CD1c
Sequence:
MRLAVLFSGALLGLLAAQGTGNDCPHKKSATLLPSFTVTPTVTESTGTTSHRTTKSHKTTTHRTTTTGTTSHGPTTATHNPTTTSHGNVTVHPTSNSTATSQGPSTATHSPATTSHGNATVHPTSNSTATSPGFTSSAHPEPPPPSPSPSPTSKETIGDYTWTNGSQPCVHLQAQIQIRVMYTTQGGGEAWGISVLNPNKTKVQGSCEGAHPHLLLSFPYGHLSFGFMQDLQQKVVYLSYMAVEYNVSFPHAAQWTFSAQNASLRDLQAPLGQSFSCSNSSIILSPAVHLDLLSLRLQAAQLPHTGVFGQSFSCPSDRSILLPLIIGLILLGLLALVLIAFCIIRRRPSAYQAL
Protein: 3-phenylpropionate/cinnamic acid dioxygenase subunit beta (EC 1.14.12.19) (Q47140)
Organism: Escherichia coli (strain K12)
Function: Part of the multicomponent 3-phenylpropionate dioxygenase. Converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (CI-dihydrodiol), respectively.
Interaction partners:
- 3-phenylpropionate/cinnamic acid dioxygenase subunit alpha
- 3-phenylpropionate-dihydrodiol/cinnamic acid-dihydrodiol dehydrogenasepropanoate dehydrogenase)
- 3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD
- 3-phenylpropionate/cinnamic acid dioxygenase ferredoxin subunit
- 2-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolase
- Flavodoxin/ferredoxin--NADP reductase
- Carnitine monooxygenase oxygenase subunit
- 2-keto-4-pentenoate hydratase
- 2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase
- Acetaldehyde dehydrogenase
Sequence:
MSAQVSLELHHRISQFLFHEASLLDDWKFRDWLAQLDEEIRYTMRTTVNAQTRDRRKGVQPPTTWIFNDTKDQLERRIARLETGMAWAEEPPSRTRHLISNCQISETDIPNVFAVRVNYLLYRAQKERDETFYVGTRFDKVRRLEDDNWRLLERDIVLDQAVITSHNLSVLF
Protein: Exportin-7 (Exp7) (Ran-binding protein 16) (Q9EPK7)
Organism: Mus musculus (Mouse)
Function: Mediates the nuclear export of proteins (cargos) with broad substrate specificity. In the nucleus binds cooperatively to its cargo and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. XPO7 then return to the nuclear compartment and mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9UIA9}. Nucleus {ECO:0000250|UniProtKB:Q9UIA9}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250|UniProtKB:Q9UIA9}.
Interaction partners:
- Exportin-6
- Exportin-1
- Exportin-T
- Exportin-2
Sequence:
MADHVQSLAQLENLCKQLYETTDTTTRLQAEKALVEFTNSPDCLSKCQLLLERGSSSYSQLLAATCLTKLVSRTNNPLPLEQRIDIRNYVLNYLATRPKLATFVTQALIQLYARITKLGWFDCQKDDYVFRNAITDVTRFLQDSVEYCIIGVTILSQLTNEINQADTTHPLTKHRKIASSFRDSSLFDIFTLSCNLLKQASGKNLNLNDESQHGLLMQLLKLTHNCLNFDFIGTSTDESSDDLCTVQIPTSWRSAFLDSSTLQLFFDLYHSIPPSFSPLVLSCLVQIASVRRSLFNNAERAKFLSHLVDGVKRILENPQSLSDPNNYHEFCRLLARLKSNYQLGELVKVENYPDVIRLIANFTVTSLQHWEFAPNSVHYLLSLWQRLAASVPYVKATEPHMLETYTPEVTKAYITSRLESVHIILRDGLEDPLEDTGLVQQQLDQLSTIGRCEYEKTCALLVQLFDQSAQSYQELLQSASASPMDIAVQEGRLTWLVYIIGAVIGGRVSFASTDEQDAMDGELVCRVLQLMNLTDSRLAQAGNEKLELAMLSFFEQFRKIYIGDQVQKSSKLYRRLSEVLGLNDETMVLSVFIGKVITNLKYWGRCEPITSKTLQLLNDLSIGYSSVRKLVKLSAVQFMLNNHTSEHFSFLGINNQSNLTDMRCRTTFYTALGRLLMVDLGEDEDQYEQFMLPLTAAFEAVAQMFSTNSFNEQEAKRTLVGLVRDLRGIAFAFNAKTSFMMLFEWIYPSYMPILQRAIELWYHDPACTTPVLKLMAELVHNRSQRLQFDVSSPNGILLFRETSKMITMYGNRILTLGEVPKDQVYALKLKGISICFSMLKAALSGSYVNFGVFRLYGDDALENALQTFIKLLLSIPHSDLLDYPKLSQSYYSLLEVLTQDHMNFIASLEPHVIMYILSSISEGLTALDTMVCTGCCSCLDHIVTYLFKQLSRSTKKRTTPLNRESDCFLHIMQQHPAMIQQMLSTVLNIIIFEDCRNQWSMSRPLLGLILLNEKYFSDLRNSIVNSQPPEKQQAMHLCFENLMEGIERNLLTKNRDRFTQNLSAFRREVNDSMKNSTYGVNSNDMMS
Protein: Roundabout guidance receptor 2 (A0A8I6A1P7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MTPLMFTLLLLFGFLCIRTDGSRLRQEDFPPRIVEHPSDVIVSKGEPTTLNCKAEGRPTPTIEWYKDGERVETDKDDPRSHRMLLPSGSLFFLRIVHGRRSKPDEGTYVCVARNYLGEAVSRNASLEVALLRDDFRQNPTDVVVAAGEPAILECQPPRGHPEPTIYWKKDKVRIDEKEERISIRGGKLMISNTRKSDAGMYTCVGTNMVGERDSDPAELTVFERPTFLRRPINQVVLEDEPAEFRCQVQGDPQPTVRWKKDDADLPRGRYDIKDDYTLRIKKAISADEGTYVCIAENRVGKVEASATLTVRAPPQFVVRPRDQIVAQGRTVTFPCETKGNPQPAVFWQKEGSQNLLFPNQPQQPNSRCSVSPTGDLTITNIQRSDAGYYICQALTVAGSILAKAQLEVTDVLTDRPPPIILQGPINQTLAVDGTALLKCKATGEPLPVISWLKEGFTFLGRDPRATIQDQGTLQIKNLRISDTGTYTCVATSSSGETSWSAVLDVTESGATISKNYDTNDLPGPPSKPQVTDVTKNSVTLSWQPGTPGVLPASAYIIEAFSQSVSNSWQTVANHVKTTLYTVRGLRPNTIYLFMVRAINPQGLSDPSPMSDPVRTQDISPPAQGVDHRQVQKELGDVTVRLHNPVVLTPTTVQVTWTVDRQPQFIQGYRVMYRQTSGLQASTVWQNLDAKVPTERSAVLVNLKKGVTYEIKVRPYFNEFQGMDSESKTIRTTEEAPSAPPQSVTVLTVGSHNSTSISVSWDPPPADHQNGIIQEYKIWCLGNETRFHINKTVDATIRSVVIGGLFPGIQYRVEVAASTSAGVGVKSEPQPIIIGGRNEVVITENNNSITEQITDVVKQPAFIAGIGGACWVILMGFSIWLYWRRKKRKGLSNYAVTFQRGDGGLMSNGSRPGLLNTGDPSYPWLADSWPATSLPVNNSNSGPNEIGNFGRGDVLPPVPGQGDKTATMLSDGAIYSSIDFTTKTTYNSSSQITQATPYATTQILHSNSIHELAVDLPDPQWKSSVQQKSDLMGFAYSLPDQNKGNNGGKGGKKKKTKNSSKAQKNNGSTWANVPLPPPPVQPLPGTELGHYPAEQENGYDSDSWCPPLPVQTYLHQGMEDELEEDEDRVPTPPVRGVASSPAISFGQQSTATLTPSPREEMQPMLQAHLDELTRAYQFDIAKQTWHIQSNTPPPQPPVPPLGYASGALISDLETDVPDEDADDEEEPLEIPRPLRALDQTPGSSMDNLDSSVTGKAFTSSQRQRPTSPFSTDSNTSAAQNQSQRPRPTKKHKGGRMDPQPVLPHRREGMPDEESLVPYSKPSFPSPGGHSSSGTASSKGSTGPRKAEILRGSHQRNANDLLDIGYVGSNSQGQFTGEL
Protein: Putative UDP-arabinose 4-epimerase 2 (EC 5.1.3.5) (UDP-D-xylose 4-epimerase 2) (O64749)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- UDP-sugar pyrophosphorylase
- UDP-D-apiose/UDP-D-xylose synthase 1
- UDP-D-apiose/UDP-D-xylose synthase 2
- Cellulose synthase-like protein D5
- Thylakoid lumenal P17.1 protein
- ADP-glucose phosphorylase
- Probable mannose-1-phosphate guanylyltransferase 3
- ADP-glucose pyrophosphorylase family protein
- Probable mannose-1-phosphate guanylyltransferase 2
- ADP-glucose pyrophosphorylase family protein
Sequence:
MLNLGRARTGRQNRSMSFEGLDFADPKKNNNYMGKIVLVMTLTAMCILLLNQSPTFNTPSVFSRSEPGVTHVLVTGGAGYIGSHAALRLLKDSYRVTIVDNLSRGNLGAVKILQQLFPEPGKLQFIYADLGDANAVNKIFSENAFDAVMHFAAVAYVGESTQFPLKYYHNITSNTLVVLETMAAHGVKTLIYSSTCATYGEPEKMPITEETPQVPINPYGKAKKMAEDIILDFSKNSIMAVMILRYFNVIGSDPEGRLGEAPRPELSEHGRISGACFDAARGIIPGLQIKGTDYKTVDGTCVRDYIDVTDLVDAHVKALEKAKPRKVGIFNVGTGKGSSVKEFVEACKKATGVDIKVDYLERRAGDYAEVYSDPRKIKEELNWTAKHTNLQESLKMAWRWQKLHRSGYGSSSLVSAY
Protein: Kinetoplastid kinetochore protein 8 (Q584J5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRASTPPLYQRQPEGLAPSYNTGLPLAMPDVPTLRIPQHLSATSHAMPPTAAAQGEFVMAATAPRLGSLETSTRATNPAPFITQFPAAQAPNLHGYVSASPRTSGTGTETSASDYFRYAANLMRNTLPPPMTELAALEEEEKSLKREEEELRPQIIELERMREQLEEQTQKVAVELMQMVVLEQQYYVEPIVDYTAQIKNAEVQCVHLASRVEEAKHSLEELQRQHQSYDAVMEEKERLKKETCAVRERFATLENRRRLCMLQSEALFDVESRRGEEAASQAEETENQLMEMRNNEPLLGIKRSRRSSRSMSRGVSFAQKSIVLDTGSDGDDDGYARSTRHTGDTVSGLTQRGSWNSAGAEDEESEQDCDRDDICGISGQSVRYSLNDTKRVQLVVPAV
Protein: Methylosome subunit pICln (Chloride channel, nucleotide sensitive 1A) (Chloride conductance regulatory protein ICln) (I(Cln)) (P35521)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Involved in both the assembly of spliceosomal snRNPs and the methylation of Sm proteins (By similarity). Chaperone that regulates the assembly of spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs (By similarity). Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core) (By similarity). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP (By similarity). Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P54105}. Nucleus {ECO:0000250|UniProtKB:P54105}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P54105}. Note=A small fraction is also associated with the cytoskeleton. {ECO:0000250|UniProtKB:P54105}.
Interaction partners:
- WD repeat domain 77.
- Small nuclear ribonucleoprotein Sm D1
- Protein arginine N-methyltransferase 5
Sequence:
MSFLKSFPPPGSAEGLRQQQPETEAVLNGKGLGTGTLYIAESRLSWLDGSGLGFSLEYPTISLHAVSRDLNAYPREHLYVMVNAKFGEESKESVAEEEDSDDDVEPIAEFRFVPSDKSALEAMFTAMCECQALHPDPEDEDSDDYDGEEYDVEAHEQGQGDIPTFYTYEEGLSHLTAEGQATLERLEGMLSQSVSSQYNMAGVRTEDSTRDYEDGMEVDTTPTVAGQFEDADVDH
Protein: DNA replication licensing factor MCM4 (EC 3.6.4.12) (Protein disc proliferation abnormal) (Q26454)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts as component of the Mcm2-7 complex (Mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the Mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for DNA replication and cell proliferation. Essential role in mitotic DNA replication but not in endoreplication.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Cell division control protein
- DNA replication licensing factor Mcm2
- DNA replication licensing factor Mcm5
- DNA replication licensing factor Mcm3
- CDC45L
- Probable DNA replication complex GINS protein PSF2
- DNA replication complex GINS protein PSF3
- DNA replication complex GINS protein PSF1
- DNA replication complex GINS protein SLD5
- DNA replication licensing factor Mcm7
Sequence:
MSSPARSPSVGGATPKQGARTPTRGIASQDVETPMRMGPGRAVRPSDNISLPPTSPGNISLPATSPARGLGANMSEIDLSSPLNYGTPSSMGSIRTPRSGIRGTPLRARPDIRTDKRIRQVAIGGGSGLEPIPEKGSETTDPVSESSQAPQLVVWGTNVVVSQCKSKFKSFIMRFIDPSAEQDEISENIDVNQPLYLQKLEEIHTLEEPYLNLNCAHLKTFDQDLYRQLICYPQEVIPGFDMAINEMFFERYPAALLEHQIQVRPFNADKTRNMRSLNPEDMDQLISISGMVIRSSNVIPEMREAFFSCNICSFSTTVEVDRGRINQPTLCTNCNTNHCFRLIHNRSEFTDKQLVKLQESPDDMAAGQTPHNVLLYAHNDLVDKVQPGDRVTVTGIYRATPLKTGGLSSSVKSVYKTHVDVVHFRKVDNKRLYEDEEGKDHIFPPERVELLQLLAKKPDIYDRLARAIAPSIYENDDIKKGILLQLFGGTKKKHATLGRQNFRSEIHLLLCGDPGTSKSQMLQYVFNLVPRSQYTSGRGSSAVGLTAYVTKDPETRQLVLQTGALVLADNGVCCIDEFDKMNDSTRSVLHEVMEQQTLSIAKAGIICQLNARTSILAAANPAESQWNKRKNIIDNVQLPHTLLSRFDLIFLVLDPQDEIFDKRLASHLVSLYYVTRHEEEDTMFDMSVLRDYIAYAREHLSPTLSDEAQQRLIQAYVDMRKVGAGRGQISAYPRQLESLIRLSEAHAKVRLSNQVELLDVEEAWRLHREALKQSATDPLSGKIDVGILTTGLSTAARKKRADLVAAIKENLKKKGKVLTVPYQKLFSDIKEGSQIMITREQFEDALKEVQDEGAIVVMGKNTIRIC
Protein: Methyltransferase type 11 domain-containing protein (O53285)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MTRSSNIPADATPNPHATAEQVAAARHDSKLAQVLYHDWEAENYDEKWSISYDQRCVDYARGRFDAIVPDEVIAQLPYDRALELGCGTGFFLLNLIQAGVARRGSVTDLSPGMVKVATRNGQALGLDIDGRVADAEGIPYDDDAFDLVVGHAVLHHIPDVELSLREVVRVLKPGGRFVFAGEPTTVGDGYARTLSTLTWRVVTNATKLPGLRGWRRPQGELDESSRAAALEALVDLHTFTPQDLQRIAHNAGAVEVQTATEEFTAAMLGWPLRTFECTVPPGRLGWGWARFAFTSWKTLGWVDANVWRHVVPKGWFYNVMITGVKPS