<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functionⁱ

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

1. poly(A) RNA binding Source: Ensembl

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Ligandⁱ

Enzyme and pathway databases

<p>Provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.</p><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>Provides information on the location and the topology of the mature protein in the cell.</p><p><a href='../manual/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componentⁱ

1. endoplasmic reticulum Source: UniProtKB-SubCell
2. integral component of membrane Source: UniProtKB-KW
3. mitochondrial outer membrane Source: UniProtKB-SubCell
4. mitochondrion Source: MGI

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 14651853
   • 18614015

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Cellular componentⁱ

<p>Describes post-translational modifications (PTMs) and/or processing events.</p><p><a href='../manual/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the extent of a transit peptide.</p><p><a href='../manual/transit' target='_top'>More...</a></p>Transit peptidei	1 – 29	29	MitochondrionBy similarity			Add BLAST
<p>Describes the extent of a polypeptide chain in the mature protein following processing.</p><p><a href='../manual/chain' target='_top'>More...</a></p>Chaini	30 – 857	828	A-kinase anchor protein 1, mitochondrial		PRO_0000016660	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	55 – 55	1	Phosphoserine2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.6 "Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; SER-101 AND SER-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.7 "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis." Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H. J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	101 – 101	1	Phosphoserine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.6 "Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; SER-101 AND SER-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	103 – 103	1	Phosphoserine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.6 "Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; SER-101 AND SER-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	164 – 164	1	PhosphoserineBy similarity
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	401 – 401	1	PhosphothreonineBy similarity
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	487 – 487	1	PhosphothreonineBy similarity

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>Provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.</p><p><a href='../manual/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>Provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.</p><p><a href='../manual/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

Gene expression databases

<p>Provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.</p><p><a href='../manual/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>Provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.</p><p><a href='../manual/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

Protein-protein interaction databases

<p>Provides information on the tertiary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure databases

<p>Provides information on sequence similarities with other proteins and the domain(s) present in a protein.</p><p><a href='../manual/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.</p><p><a href='../manual/domain' target='_top'>More...</a></p>Domaini	561 – 625	65	KHPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi PROSITE-ProRule:PRU00117			Add BLAST
<p>Describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.</p><p><a href='../manual/domain' target='_top'>More...</a></p>Domaini	712 – 771	60	TudorPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi PROSITE-ProRule:PRU00211			Add BLAST

Region

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes a region of interest that cannot be described in other subsections.</p><p><a href='../manual/region' target='_top'>More...</a></p>Regioni	306 – 319	14	PKA-RII subunit binding domain			Add BLAST

<p>Provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.</p><p><a href='../manual/domain_cc' target='_top'>More...</a></p>Domainⁱ

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>Displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequences (6)ⁱ

<p>Indicates if the canonical sequence displayed by default in the entry is complete or not.</p><p><a href='../manual/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

<p>Indicates if the canonical sequence displayed by default in the entry is in its mature form or if it represents the precursor.</p><p><a href='../manual/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 6<p>Lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.</p><p><a href='../manual/alternative_products' target='_top'>More...</a></p> isoformsⁱ produced by alternative splicing. Align

        10         20         30         40         50
MAIQLRSLFP LALPGMLALL GWWWFFSRKK DRLSSSDKQV ETLKVGPAIK 
        60         70         80         90        100
DRRLSEEACP GVLSVAPTVT QPPGREEQRC VDKPSTEPLA LPRTRQVRRR 
       110        120        130        140        150
SESSGNLPSV ADTRSQPGPC RDEIAKVELS LMGDKAKSIP LGCPLLPKDA 
       160        170        180        190        200
SFPYEAVERC KQESALGKTP GRGWPSPYAA SGEKARETGG TEGTGDAVLG 
       210        220        230        240        250
ENVSEEGLLS QECVSEVEKS EFPILAPGGG EGEEVSHGPP QVAELLKKEE 
       260        270        280        290        300
YIVGKLPSSF VEPVHSEPVK DEDALEPQVK GSSNTSDRDL AGELDKDETV 
       310        320        330        340        350
PENDQIKQAA FQLISQVILE ATEEFRATTV GKTVAQVHPT SATQPKGKEE 
       360        370        380        390        400
SCVPASQETS LGQDTSDPAS TRTGATASPS AEALPPKTYV SCLSSPLSGP 
       410        420        430        440        450
TKDQKPKNSA HHISLAPCPP PVTPQRQSLE GASNPRGDDN FVACMANNSQ 
       460        470        480        490        500
SVLSVSSLGQ CSDPVSTSGL EDSCTETISS SGDKAMTPPL PVSTQPFSNG 
       510        520        530        540        550
VLKEELSDLG TEDGWTMDTE ADHSGGSDGN SMDSVDSCCG LTKPDSPQSV 
       560        570        580        590        600
QAGSNPKKVD LIIWEIEVPK HLVGRLIGKQ GRYVSFLKQT SGAKIYISTL 
       610        620        630        640        650
PYTQNIQICH IEGSQHHVDK ALNLIGKKFK ELNLTNIYAP PLPSLALPSL 
       660        670        680        690        700
PMTSWLMLPD GITVEVIVVN QVNAGHLFVQ QHTHPTFHAL RSLDQQMYLC 
       710        720        730        740        750
YSQPGIPTLP TPVEITVICA APGADGAWWR AQVVASYEET NEVEIRYVDY 
       760        770        780        790        800
GGYKRVKVDV LRQIRSDFVT LPFQGAEVLL DSVVPLSDDD HFSPEADAAM 
       810        820        830        840        850
SEMTGNTALL AQVTSYSATG LPLIQLWSVV GDEVVLINRS LVERGLAQWV 

DSYYASL                                             

        10         20         30         40         50
MAIQLRSLFP LALPGMLALL GWWWFFSRKK DRLSSSDKQV ETLKVGPAIK 
        60         70         80         90        100
DRRLSEEACP GVLSVAPTVT QPPGREEQRC VDKPSTEPLA LPRTRQVRRR 
       110        120        130        140        150
SESSGNLPSV ADTRSQPGPC RDEIAKVELS LMGDKAKSIP LGCPLLPKDA 
       160        170        180        190        200
SFPYEAVERC KQESALGKTP GRGWPSPYAA SGEKARETGG TEGTGDAVLG 
       210        220        230        240        250
ENVSEEGLLS QECVSEVEKS EFPILAPGGG EGEEVSHGPP QVAELLKKEE 
       260        270        280        290        300
YIVGKLPSSF VEPVHSEPVK DEDALEPQVK GSSNTSDRDL AGELDKDETV 
       310        320        330        340        350
PENDQIKQAA FQLISQVILE ATEEFRATTV GKTVAQVHPT SATQPKGKEE 
       360        370        380        390        400
SCVPASQETS LGQDTSDPAS TRTGATASPS AEALPPKTYV SCLSSPLSGP 
       410        420        430        440        450
TKDQKPKNSA HHISLAPCPP PVTPQRQSLE GASNPRGDDN FVACMANNSQ 
       460        470        480        490        500
SVLSVSSLGQ CSDPVSTSGL EDSCTETISS SGDKAMTPPL PVSTQPFSNG 
       510        520        530        540 
VLKEELSDLG TEDGWTMDTE ADHSGGRKVL GCFLGESGRG PIIC 

        10         20         30         40         50
MGCKTGPKPF GGGETIRPIR IRRCSYFTST DSKMAIQLRS LFPLALPGML 
        60         70         80         90        100
ALLGWWWFFS RKKDRLSSSD KQVETLKVGP AIKDRRLSEE ACPGVLSVAP 
       110        120        130        140        150
TVTQPPGREE QRCVDKPSTE PLALPRTRQV RRRSESSGNL PSVADTRSQP 
       160        170        180        190        200
GPCRDEIAKV ELSLMGDKAK SIPLGCPLLP KDASFPYEAV ERCKQESALG 
       210        220        230        240        250
KTPGRGWPSP YAASGEKARE TGGTEGTGDA VLGENVSEEG LLSQECVSEV 
       260        270        280        290        300
EKSEFPILAP GGGEGEEVSH GPPQVAELLK KEEYIVGKLP SSFVEPVHSE 
       310        320        330        340        350
PVKDEDALEP QVKGSSNTSD RDLAGELDKD ETVPENDQIK QAAFQLISQV 
       360        370        380        390        400
ILEATEEFRA TTVGKTVAQV HPTSATQPKG KEESCVPASQ ETSLGQDTSD 
       410        420        430        440        450
PASTRTGATA SPSAEALPPK TYVSCLSSPL SGPTKDQKPK NSAHHISLAP 
       460        470        480        490        500
CPPPVTPQRQ SLEGASNPRG DDNFVACMAN NSQSVLSVSS LGQCSDPVST 
       510        520        530        540        550
SGLEDSCTET ISSSGDKAMT PPLPVSTQPF SNGVLKEELS DLGTEDGWTM 
       560        570 
DTEADHSGGR KVLGCFLGES GRGPIIC                       

        10         20         30         40         50
MGCKTGPKPF GGGETIRPIR IRRCSYFTST DSKMAIQLRS LFPLALPGML 
        60         70         80         90        100
ALLGWWWFFS RKKDRLSSSD KQVETLKVGP AIKDRRLSEE ACPGVLSVAP 
       110        120        130        140        150
TVTQPPGREE QRCVDKPSTE PLALPRTRQV RRRSESSGNL PSVADTRSQP 
       160        170        180        190        200
GPCRDEIAKV ELSLMGDKAK SIPLGCPLLP KDASFPYEAV ERCKQESALG 
       210        220        230        240        250
KTPGRGWPSP YAASGEKARE TGGTEGTGDA VLGENVSEEG LLSQECVSEV 
       260        270        280        290        300
EKSEFPILAP GGGEGEEVSH GPPQVAELLK KEEYIVGKLP SSFVEPVHSE 
       310        320        330        340        350
PVKDEDALEP QVKGSSNTSD RDLAGELDKD ETVPENDQIK QAAFQLISQV 
       360        370        380        390        400
ILEATEEFRA TTVGKTVAQV HPTSATQPKG KEESCVPASQ ETSLGQDTSD 
       410        420        430        440        450
PASTRTGATA SPSAEALPPK TYVSCLSSPL SGPTKDQKPK NSAHHISLAP 
       460        470        480        490        500
CPPPVTPQRQ SLEGASNPRG DDNFVACMAN NSQSVLSVSS LGQCSDPVST 
       510        520        530        540        550
SGLEDSCTET ISSSGDKAMT PPLPVSTQPF SNGVLKEELS DLGTEDGWTM 
       560        570        580        590        600
DTEADHSGGS DGNSMDSVDS CCGLTKPDSP QSVQAGSNPK KVDLIIWEIE 
       610        620        630        640        650
VPKHLVGRLI GKQGRYVSFL KQTSGAKIYI STLPYTQNIQ ICHIEGSQHH 
       660        670        680        690        700
VDKALNLIGK KFKELNLTNI YAPPLPSLAL PSLPMTSWLM LPDGITVEVI 
       710        720        730        740        750
VVNQVNAGHL FVQQHTHPTF HALRSLDQQM YLCYSQPGIP TLPTPVEITV 
       760        770        780        790        800
ICAAPGADGA WWRAQVVASY EETNEVEIRY VDYGGYKRVK VDVLRQIRSD 
       810        820        830        840        850
FVTLPFQGAE VLLDSVVPLS DDDHFSPEAD AAMSEMTGNT ALLAQVTSYS 
       860        870        880        890
ATGLPLIQLW SVVGDEVVLI NRSLVERGLA QWVDSYYASL            

        10         20         30         40         50
MAIQLRSLFP LALPGMLALL GWWWFFSRKK DRLSSSDKQV ETLKVGPAIK 
        60         70         80         90        100
DRRLSEEACP GVLSVAPTVT QPPGREEQRC VDKPSTEPLA LPRTRQVRRR 
       110        120        130        140        150
SESSGNLPSV ADTRSQPGPC RDEIAKVELS LMGDKAKSIP LGCPLLPKDA 
       160        170        180        190        200
SFPYEAVERC KQESALGKTP GRGWPSPYAA SGEKARETGG TEGTGDAVLG 
       210        220        230        240        250
ENVSEEGLLS QECVSEVEKS EFPILAPGGG EGEEVSHGPP QVAELLKKEE 
       260        270        280        290        300
YIVGKLPSSF VEPVHSEPVK DEDALEPQVK GSSNTSDRDL AGELDKDETV 
       310        320        330        340        350
PENDQIKQAA FQLISQVILE ATEEFRATTV GKTVAQVHPT SATQPKGKEE 
       360        370        380        390        400
SCVPASQETS LGQDTSDPAS TRTGATASPS AEALPPKTYV SCLSSPLSGP 
       410        420        430        440        450
TKDQKPKNSA HHISLAPCPP PVTPQRQSLE GASNPRGDDN FVACMANNSQ 
       460        470        480        490        500
SVLSVSSLGQ CSDPVSTSGL EDSCTETISS SGDKAMTPPL PVSTQPFSNG 
       510        520        530        540 
VLKEELSDLG TEDGWTMDTE ADHSGVAAPP QERGHFGNGG CTGFFEC 

        10         20         30         40         50
MAIQLRSLFP LALPGMLALL GWWWFFSRKK DRLSSSDKQV ETLKVGPAIK 
        60         70         80         90        100
DRRLSEEACP GVLSVAPTVT QPPGREEQRC VDKPSTEPLA LPRTRQVRRR 
       110        120        130        140        150
SESSGNLPSV ADTRSQPGPC RDEIAKVELS LMGDKAKSIP LGCPLLPKDA 
       160        170        180        190        200
SFPYEAVERC KQESALGKTP GRGWPSPYAA SGEKARETGG TEGTGDAVLG 
       210        220        230        240        250
ENVSEEGLLS QECVSEVEKS EFPILAPGGG EGEEVSHGPP QVAELLKKEE 
       260        270        280        290        300
YIVGKLPSSF VEPVHSEPVK DEDALEPQVK GSSNTSDRDL AGELDKDETV 
       310        320        330        340        350
PENDQIKQAA FQLISQVILE ATEEFRATTV GKTVAQVHPT SATQPKGKEE 
       360        370        380        390        400
SCVPASQETS LGQDTSDPAS TRTGATASPS AEALPPKTYV SCLSSPLSGP 
       410        420        430        440        450
TKDQKPKNSA HHISLAPCPP PVTPQRQSLE GASNPRGDDN FVACMANNSQ 
       460        470        480        490        500
SVLSVSSLGQ CSDPVSTSGL EDSCTETISS SGDKAMTPPL PVSTQPFSNG 
       510        520        530        540        550
VLKEELSDLG TEDGWTMDTE ADHSGGSDGN SMDSVDSCCG LTKPDSPQSV 
       560        570        580        590        600
QAGSNPKKVD LIIWEIEVPK HLVGRLIGKQ GRYVSFLKQT SGAKIYISTL 
       610        620        630 
PYTQNIQICH IEGCVSVLTR RLSAPCRQSS ELDWEEV            

Experimental Info

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	80 – 80	1	C → S in AAC27100. 1 Publication Ref.2 Huang L.J.-S., Durick K., Taylor S.S. Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION. Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	80 – 80	1	C → S in AAB53740. (PubMed:9182549)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	80 – 80	1	C → S in AAB53741. (PubMed:9182549)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	220 – 220	1	S → I in AAC27100. 1 Publication Ref.2 Huang L.J.-S., Durick K., Taylor S.S. Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION. Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	325 – 325	1	F → L in AAC27100. 1 Publication Ref.2 Huang L.J.-S., Durick K., Taylor S.S. Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION. Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	325 – 325	1	F → L in AAB53740. (PubMed:9182549)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	325 – 325	1	F → L in AAB53741. (PubMed:9182549)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	327 – 327	1	A → P in AAB53740. (PubMed:9182549)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	327 – 327	1	A → P in AAB53741. (PubMed:9182549)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	340 – 340	1	T → I in AAC27100. 1 Publication Ref.2 Huang L.J.-S., Durick K., Taylor S.S. Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION. Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	340 – 340	1	T → I in AAB53740. (PubMed:9182549)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	340 – 340	1	T → I in AAB53741. (PubMed:9182549)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	486 – 486	1	M → I in AAC27100. 1 Publication Ref.2 Huang L.J.-S., Durick K., Taylor S.S. Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION. Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	486 – 486	1	M → I in AAB53740. (PubMed:9182549)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	486 – 486	1	M → I in AAB53741. (PubMed:9182549)Curated

Alternative sequence

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.</p><p><a href='../manual/var_seq' target='_top'>More...</a></p>Alternative sequencei	1 – 1	1	M → MGCKTGPKPFGGGETIRPIR IRRCSYFTSTDSKM in isoform 2 and isoform 4. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini Ref.1 "Identification of a novel protein kinase A anchoring protein that binds both type I and type II regulatory subunits." Huang L.J.-S., Durick K., Weiner J.A., Chun J., Taylor S.S. J. Biol. Chem. 272:8057-8064(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).		VSP_002847
<p>Describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.</p><p><a href='../manual/var_seq' target='_top'>More...</a></p>Alternative sequencei	526 – 547	22	GSDGN…KPDSP → VAAPPQERGHFGNGGCTGFF EC in isoform 5. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini Ref.3 "Organelle-specific targeting of protein kinase AII (PKAII). Molecular and in situ characterization of murine A kinase anchor proteins that recruit regulatory subunits of PKAII to the cytoplasmic surface of mitochondria." Chen Q., Lin R.-Y., Rubin C.S. J. Biol. Chem. 272:15247-15257(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 5 AND 6).		VSP_002850	Add BLAST
<p>Describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.</p><p><a href='../manual/var_seq' target='_top'>More...</a></p>Alternative sequencei	527 – 544	18	SDGNS…GLTKP → RKVLGCFLGESGRGPIIC in isoform 1 and isoform 2. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini Ref.1 "Identification of a novel protein kinase A anchoring protein that binds both type I and type II regulatory subunits." Huang L.J.-S., Durick K., Weiner J.A., Chun J., Taylor S.S. J. Biol. Chem. 272:8057-8064(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).		VSP_002848	Add BLAST
<p>Describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.</p><p><a href='../manual/var_seq' target='_top'>More...</a></p>Alternative sequencei	545 – 857	313	Missing in isoform 1 and isoform 2. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini Ref.1 "Identification of a novel protein kinase A anchoring protein that binds both type I and type II regulatory subunits." Huang L.J.-S., Durick K., Weiner J.A., Chun J., Taylor S.S. J. Biol. Chem. 272:8057-8064(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).		VSP_002849	Add BLAST
<p>Describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.</p><p><a href='../manual/var_seq' target='_top'>More...</a></p>Alternative sequencei	548 – 857	310	Missing in isoform 5. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini Ref.3 "Organelle-specific targeting of protein kinase AII (PKAII). Molecular and in situ characterization of murine A kinase anchor proteins that recruit regulatory subunits of PKAII to the cytoplasmic surface of mitochondria." Chen Q., Lin R.-Y., Rubin C.S. J. Biol. Chem. 272:15247-15257(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 5 AND 6).		VSP_002851	Add BLAST
<p>Describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.</p><p><a href='../manual/var_seq' target='_top'>More...</a></p>Alternative sequencei	614 – 637	24	SQHHV…NLTNI → CVSVLTRRLSAPCRQSSELD WEEV in isoform 6. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini Ref.3 "Organelle-specific targeting of protein kinase AII (PKAII). Molecular and in situ characterization of murine A kinase anchor proteins that recruit regulatory subunits of PKAII to the cytoplasmic surface of mitochondria." Chen Q., Lin R.-Y., Rubin C.S. J. Biol. Chem. 272:15247-15257(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 5 AND 6).		VSP_002852	Add BLAST
<p>Describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.</p><p><a href='../manual/var_seq' target='_top'>More...</a></p>Alternative sequencei	638 – 857	220	Missing in isoform 6. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini Ref.3 "Organelle-specific targeting of protein kinase AII (PKAII). Molecular and in situ characterization of murine A kinase anchor proteins that recruit regulatory subunits of PKAII to the cytoplasmic surface of mitochondria." Chen Q., Lin R.-Y., Rubin C.S. J. Biol. Chem. 272:15247-15257(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 5 AND 6).		VSP_002853	Add BLAST

Sequence databases

Genome annotation databases

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityⁱ

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/cross_references_section' target='_top'>More...</a></p> Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>Contains the literature citations that are the sources of data used to annotate the entry. Each reference is numbered and contains several subsections allowing a precise description of a given citation.</p><p><a href='../manual/publications_section' target='_top'>More...</a></p>Publicationsⁱ

1. "Identification of a novel protein kinase A anchoring protein that binds both type I and type II regulatory subunits."
   Huang L.J.-S., Durick K., Weiner J.A., Chun J., Taylor S.S.
   J. Biol. Chem. 272:8057-8064(1997) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
   Tissue: Embryo.
   
2. Huang L.J.-S., Durick K., Taylor S.S.
   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
   Cited for: SEQUENCE REVISION.
3. "Organelle-specific targeting of protein kinase AII (PKAII). Molecular and in situ characterization of murine A kinase anchor proteins that recruit regulatory subunits of PKAII to the cytoplasmic surface of mitochondria."
   Chen Q., Lin R.-Y., Rubin C.S.
   J. Biol. Chem. 272:15247-15257(1997) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 5 AND 6).
   Strain: BALB/c.
   Tissue: Testis.
   
4. "Lineage-specific biology revealed by a finished genome assembly of the mouse."
   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.

   , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
   PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
   Strain: C57BL/6J.
   
5. "NH2-Terminal targeting motifs direct dual specificity A-kinase-anchoring protein 1 (D-AKAP1) to either mitochondria or endoplasmic reticulum."
   Huang L.J.-S., Wang L., Ma Y., Durick K., Perkins G., Deerinck T.J., Ellisman M.H., Taylor S.S.
   J. Cell Biol. 145:951-959(1999) [PubMed] [Europe PMC] [Abstract]
   Cited for: SUBCELLULAR LOCATION.
6. "Large-scale phosphorylation analysis of mouse liver."
   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
   Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; SER-101 AND SER-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
   Tissue: Liver.
   
7. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
   J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
   Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
   Tissue: Liver.
   

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Technical termⁱ

Documents

1. MGD cross-references
   Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
2. SIMILARITY comments
   Index of protein domains and families

External Data

<p>Provides links to the UniProt Reference Clusters (<a href="/help/uniref">UniRef</a>). UniRef consists of clusters for UniProtKB sequences (including isoforms) and selected UniParc sequences, in order to obtain complete coverage of the sequence space at resolutions of 100%, 90% and 50% identity.</p><p><a href='../manual/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ