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Protein

A-kinase anchor protein 12

Gene

Akap12

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA) and protein kinase C (PKC).By similarity

GO - Molecular functioni

  • adenylate cyclase binding Source: MGI
  • receptor signaling complex scaffold activity Source: MGI

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
A-kinase anchor protein 12
Short name:
AKAP-12
Alternative name(s):
Germ cell lineage protein gercelin
Src-suppressed C kinase substrate
Short name:
SSeCKS
Gene namesi
Name:Akap12
Synonyms:Gag12, Ssecks
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1932576. Akap12.

Subcellular locationi

  • Cytoplasmcytoskeleton By similarity
  • Membrane By similarity; Lipid-anchor By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 16841683A-kinase anchor protein 12PRO_0000304941Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Modified residuei11 – 111PhosphoserineBy similarity
Modified residuei18 – 181PhosphoserineCombined sources
Modified residuei22 – 221PhosphoserineCombined sources
Modified residuei27 – 271PhosphoserineCombined sources
Modified residuei136 – 1361PhosphoserineBy similarity
Modified residuei234 – 2341PhosphoserineCombined sources
Modified residuei244 – 2441PhosphoserineBy similarity
Modified residuei270 – 2701PhosphoserineCombined sources
Modified residuei273 – 2731PhosphoserineCombined sources
Modified residuei330 – 3301PhosphothreonineBy similarity
Modified residuei350 – 3501PhosphoserineCombined sources
Modified residuei353 – 3531PhosphotyrosineCombined sources
Modified residuei371 – 3711PhosphoserineCombined sources
Modified residuei467 – 4671PhosphoserineCombined sources
Modified residuei489 – 4891PhosphoserineCombined sources
Modified residuei505 – 5051PhosphoserineBy similarity
Modified residuei507 – 5071PhosphoserineBy similarity
Modified residuei540 – 5401PhosphoserineBy similarity
Modified residuei543 – 5431PhosphoserineBy similarity
Modified residuei584 – 5841PhosphoserineCombined sources
Modified residuei598 – 5981PhosphoserineBy similarity
Modified residuei613 – 6131PhosphoserineBy similarity
Modified residuei628 – 6281PhosphothreonineBy similarity
Modified residuei630 – 6301PhosphoserineBy similarity
Modified residuei631 – 6311PhosphoserineCombined sources
Modified residuei634 – 6341PhosphoserineCombined sources
Modified residuei637 – 6371PhosphoserineCombined sources
Modified residuei682 – 6821PhosphoserineCombined sources
Modified residuei683 – 6831PhosphoserineCombined sources
Modified residuei684 – 6841PhosphoserineCombined sources
Modified residuei733 – 7331PhosphoserineCombined sources
Modified residuei745 – 7451PhosphoserineBy similarity
Modified residuei767 – 7671PhosphoserineCombined sources
Modified residuei786 – 7861PhosphoserineCombined sources
Modified residuei871 – 8711PhosphothreonineCombined sources
Modified residuei873 – 8731PhosphoserineCombined sources
Modified residuei1059 – 10591PhosphoserineBy similarity
Modified residuei1292 – 12921PhosphoserineBy similarity
Modified residuei1351 – 13511PhosphoserineCombined sources
Modified residuei1355 – 13551PhosphoserineBy similarity
Modified residuei1357 – 13571PhosphoserineBy similarity
Modified residuei1546 – 15461PhosphoserineBy similarity
Modified residuei1645 – 16451PhosphoserineCombined sources

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

EPDiQ9WTQ5.
MaxQBiQ9WTQ5.
PaxDbiQ9WTQ5.
PRIDEiQ9WTQ5.

PTM databases

iPTMnetiQ9WTQ5.
PhosphoSiteiQ9WTQ5.
SwissPalmiQ9WTQ5.

Expressioni

Tissue specificityi

Isoform 1 is predominantly found in the nervous system. Isoform 3 is testis specific.1 Publication

Gene expression databases

BgeeiQ9WTQ5.
CleanExiMM_AKAP12.
ExpressionAtlasiQ9WTQ5. baseline and differential.
GenevisibleiQ9WTQ5. MM.

Interactioni

Subunit structurei

Binds to dimeric RII-alpha regulatory subunit of PKC.By similarity

GO - Molecular functioni

  • adenylate cyclase binding Source: MGI
  • receptor signaling complex scaffold activity Source: MGI

Protein-protein interaction databases

BioGridi219914. 8 interactions.
IntActiQ9WTQ5. 11 interactions.
MINTiMINT-1767330.
STRINGi10090.ENSMUSP00000035829.

Structurei

3D structure databases

ProteinModelPortaliQ9WTQ5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini590 – 62031AKAP 1Add
BLAST
Domaini737 – 76731AKAP 2Add
BLAST
Domaini778 – 80831AKAP 3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni253 – 543291Involved in PKC-bindingBy similarityAdd
BLAST
Regioni1501 – 151414RII-bindingBy similarityAdd
BLAST

Sequence similaritiesi

Contains 3 AKAP domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IFC9. Eukaryota.
ENOG4110Y3C. LUCA.
GeneTreeiENSGT00730000111244.
HOGENOMiHOG000293190.
HOVERGENiHBG050472.
InParanoidiQ9WTQ5.
KOiK16528.
OMAiFARTETA.
OrthoDBiEOG7RFTGR.
PhylomeDBiQ9WTQ5.
TreeFamiTF105411.

Family and domain databases

InterProiIPR028540. AKAP12.
IPR001573. Pkinase-A_anch_WSK-motif.
IPR018459. RII_binding_1.
[Graphical view]
PANTHERiPTHR23209. PTHR23209. 1 hit.
PfamiPF10522. RII_binding_1. 1 hit.
PF03832. WSK. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9WTQ5-1) [UniParc]FASTAAdd to basket

Also known as: Alpha

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGAGSSTEQR SPEQPAESDT PSELELSGHG PAAEASGAAG DPADADPATK
60 70 80 90 100
LPQKNGQLSA VNGVAEQEDV HVQEESQDGQ EEEVTVEDVG QRESEDVKEK
110 120 130 140 150
DRAKEMAASS TVVEDITKDE QEETPEIIEQ IPASESNVEE MAQAAESQAN
160 170 180 190 200
DVGFKKVFKF VGFKFTVKKD KNEKSDTVQL LTVKKDEGEG AEASVGAGDH
210 220 230 240 250
QEPGVETVGE SASKESELKQ STEKQEGTLK QAQSSTEIPL QAESGQGTEE
260 270 280 290 300
EAAKDGEENR EKEPTKPLES PTSPVSNETT SSFKKFFTHG WAGWRKKTSF
310 320 330 340 350
KKPKEDDLET SEKRKEQEAE KVDEEEGEKT EPAPAEEQEP AEGTDQARLS
360 370 380 390 400
ADYEKVELPL EDQVGDLEAL SEKCAPLATE VFDEKTEAHQ EVVAEVHVST
410 420 430 440 450
VEKMTKGQGG AEVEGDVVVE GSGESLPPEK LAETQEVPQE AEPVEELMKT
460 470 480 490 500
KEVCVSGGDH TQLTDLSPEE KMLPKHPEGI VSEVEMLSSQ ERIKVQGSPL
510 520 530 540 550
KKLFSSSGLK KLSGKKQKGK RGGGGGDEEP GEYQHIQTES PESADEQKGE
560 570 580 590 600
SSASSPEEPE EIACLEKGPS EAPQEAEAEE GATSDGEKKR EGITPWASFK
610 620 630 640 650
KMVTPKKRVR RPSESDKEEE LDKVKSATLS STESTASGMQ DEVRAVGEEQ
660 670 680 690 700
RSEEPKRRVD TSVSWEALIC VGSSKKRARK ASSSDDEGGP RTLGGDGHRA
710 720 730 740 750
EEASKDKEAD ALPASTQEQD QAHGSSSPEP AGSPSEGEGV STWESFKRLV
760 770 780 790 800
TPRKKSKSKL EERAEDSGAE QLASEIEPSR EESWVSIKKF IPGRRKKRAD
810 820 830 840 850
GKQEQAAVED SGPGEINEDD PDVPAVVPLS EYDAVEREKL EAQRAQENVE
860 870 880 890 900
LPQLKGAVYV SEELSKTLVH TVSVAVIDGT RAVTSAEERS PSWISASMTE
910 920 930 940 950
PLEHAEGVAT PPVGEVTEKD ITAEATPALA QTLPGGKDAH DDIVTSEVDF
960 970 980 990 1000
TSEAVTAAET TEALRAEELT EASGAEETTD MVSAVSQLSD SPDTTEEATP
1010 1020 1030 1040 1050
VQEVEGGMLD TEEQERQTQA VLQAVADKVK EDSQVPATQT LQRAGPKALE
1060 1070 1080 1090 1100
KVEEVEEDSE VLATEKEKDV VPEGPVQEAE TEHLAQGSET VQATPESLEV
1110 1120 1130 1140 1150
PEVTEDVDRA TTCQVIKHQQ LMEQAVAPES SETLTDSETN GSTPLADSDT
1160 1170 1180 1190 1200
PNGTQQDETV DSQDSNAIAA VKQSQVTEEE AAAAQTEGPS TPSSFPAQEE
1210 1220 1230 1240 1250
HREKPGRDVL EPTQALAAGA VPILAKAEVG QEGEAGQFDG EKVKDGQCVK
1260 1270 1280 1290 1300
ELEVPVHTGP NSQKTADLTR DSEVMEVARC QETESNEEQS ISPEKREMGT
1310 1320 1330 1340 1350
DVEKEETETK TEQASEEHEQ ETAAPEHEGT HPKPVLTADM PHSERGKALG
1360 1370 1380 1390 1400
SLEGSPSLPD QDKADCIEVQ VQSSDTPVTQ TTEAVKKVEE TVATSEMDES
1410 1420 1430 1440 1450
LECAGAQSLP AEKLSETGGY GTLQHGEDTV PQGPESQAES IPIIVTPAPE
1460 1470 1480 1490 1500
SILHSDLQRE VSASQKQRSD EDNKPDAGPD AAGKESAARE KILRAEPEIL
1510 1520 1530 1540 1550
ELESKSNKIV QSVIQTAVDQ FARTETAPET HASDLQNQVP VMQADSQGAQ
1560 1570 1580 1590 1600
QMLDKDESDL QVSPQDGTLS AVAQEGLAVS DSSEGMSKAS EMITTLAVES
1610 1620 1630 1640 1650
ASVKESVEKL PLQCKDEKEH AADGPQHQSL AKAEADASGN LTKESPDTNG
1660 1670 1680
PKLTEEGDAL KEEMNKAQTE EDDLQEPKGD LTES
Length:1,684
Mass (Da):180,695
Last modified:November 1, 1999 - v1
Checksum:iE569D55762FCB19E
GO
Isoform 2 (identifier: Q9WTQ5-2) [UniParc]FASTAAdd to basket

Also known as: Gamma

The sequence of this isoform differs from the canonical sequence as follows:
     1-105: Missing.

Show »
Length:1,579
Mass (Da):169,743
Checksum:iD448047A8E6CE8F2
GO

Sequence cautioni

The sequence BAC66465.1 differs from that shown. Reason: Frameshift at positions 28 and 43. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 105105Missing in isoform 2. 2 PublicationsVSP_028135Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF326228 mRNA. Translation: AAK16150.1.
AF326230 mRNA. Translation: AAK16152.1.
AB020886 mRNA. Translation: BAA76894.1.
AB025278 mRNA. Translation: BAC66465.1. Frameshift.
AB051563 mRNA. Translation: BAB72161.1.
AB070852 mRNA. Translation: BAB72164.1.
AB070853 mRNA. Translation: BAB72165.1.
AK053844 mRNA. Translation: BAC35553.1.
BC042461 mRNA. Translation: AAH42461.1.
BC043939 mRNA. Translation: AAH43939.1.
CCDSiCCDS56673.1. [Q9WTQ5-1]
RefSeqiNP_112462.1. NM_031185.3. [Q9WTQ5-1]
UniGeneiMm.27481.

Genome annotation databases

EnsembliENSMUST00000045730; ENSMUSP00000035829; ENSMUSG00000038587. [Q9WTQ5-1]
GeneIDi83397.
KEGGimmu:83397.
UCSCiuc007ehh.1. mouse. [Q9WTQ5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF326228 mRNA. Translation: AAK16150.1.
AF326230 mRNA. Translation: AAK16152.1.
AB020886 mRNA. Translation: BAA76894.1.
AB025278 mRNA. Translation: BAC66465.1. Frameshift.
AB051563 mRNA. Translation: BAB72161.1.
AB070852 mRNA. Translation: BAB72164.1.
AB070853 mRNA. Translation: BAB72165.1.
AK053844 mRNA. Translation: BAC35553.1.
BC042461 mRNA. Translation: AAH42461.1.
BC043939 mRNA. Translation: AAH43939.1.
CCDSiCCDS56673.1. [Q9WTQ5-1]
RefSeqiNP_112462.1. NM_031185.3. [Q9WTQ5-1]
UniGeneiMm.27481.

3D structure databases

ProteinModelPortaliQ9WTQ5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi219914. 8 interactions.
IntActiQ9WTQ5. 11 interactions.
MINTiMINT-1767330.
STRINGi10090.ENSMUSP00000035829.

PTM databases

iPTMnetiQ9WTQ5.
PhosphoSiteiQ9WTQ5.
SwissPalmiQ9WTQ5.

Proteomic databases

EPDiQ9WTQ5.
MaxQBiQ9WTQ5.
PaxDbiQ9WTQ5.
PRIDEiQ9WTQ5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000045730; ENSMUSP00000035829; ENSMUSG00000038587. [Q9WTQ5-1]
GeneIDi83397.
KEGGimmu:83397.
UCSCiuc007ehh.1. mouse. [Q9WTQ5-1]

Organism-specific databases

CTDi9590.
MGIiMGI:1932576. Akap12.

Phylogenomic databases

eggNOGiENOG410IFC9. Eukaryota.
ENOG4110Y3C. LUCA.
GeneTreeiENSGT00730000111244.
HOGENOMiHOG000293190.
HOVERGENiHBG050472.
InParanoidiQ9WTQ5.
KOiK16528.
OMAiFARTETA.
OrthoDBiEOG7RFTGR.
PhylomeDBiQ9WTQ5.
TreeFamiTF105411.

Miscellaneous databases

NextBioi350523.
PROiQ9WTQ5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WTQ5.
CleanExiMM_AKAP12.
ExpressionAtlasiQ9WTQ5. baseline and differential.
GenevisibleiQ9WTQ5. MM.

Family and domain databases

InterProiIPR028540. AKAP12.
IPR001573. Pkinase-A_anch_WSK-motif.
IPR018459. RII_binding_1.
[Graphical view]
PANTHERiPTHR23209. PTHR23209. 1 hit.
PfamiPF10522. RII_binding_1. 1 hit.
PF03832. WSK. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Gene trap insertion reveals two open reading frames in the mouse SSeCKS gene: the form predominantly detected in the nervous system is suppressed by the insertion while the other, specific of the testis, remains expressed."
    Camus A., Mesbah K., Rallu M., Babinet C., Barra J.
    Mech. Dev. 105:79-91(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
    Tissue: Testis.
  2. "Induction of Src-suppressed C kinase substrate (SSeCKS) in vascular endothelial cells by bacterial lipopolysaccharide."
    Kitamura H., Okita K., Fujikura D., Mori K., Iwanaga T., Saito M.
    J. Histochem. Cytochem. 50:245-255(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: BALB/cJ.
    Tissue: Testis.
  3. "Mouse testicular cell specific gene, GAG12."
    Nishina Y., Motoda Y.
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Testis.
  4. "Molecular cloning and characterization of the mouse germ cell lineage protein cDNA, gercelin, encoding the cytoplasmic AKAP, Gercelin / SSeCKS and the potential germ cell-specific nuclear antigen, GENA."
    Tsuchida J., Tanaka H., Yomogida K., Nozaki M., Maeda N., Matsui Y., Nishimune Y.
    Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Testis.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-605 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Eye.
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 139-1684 (ISOFORMS 1/2).
    Strain: FVB/N.
    Tissue: Mammary tumor.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  8. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  9. "A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
    Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
    J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-682; SER-683 AND SER-684, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Teratocarcinoma.
  10. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-22; SER-27; SER-234; SER-270; SER-273; SER-350; SER-371; SER-467; SER-489; SER-584; SER-631; SER-634; SER-637; SER-682; SER-733; SER-767; SER-786; THR-871; SER-873; SER-1351 AND SER-1645, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiAKA12_MOUSE
AccessioniPrimary (citable) accession number: Q9WTQ5
Secondary accession number(s): Q80SS4
, Q810D4, Q8BPK4, Q99MP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: November 1, 1999
Last modified: March 16, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.