Q9CQV8 (1433B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
14-3-3 protein beta/alpha

Alternative name(s):
Protein kinase C inhibitor protein 1
Short name=KCIP-1

Cleaved into the following chain:

1. 14-3-3 protein beta/alpha, N-terminally processed

Gene names

Name:

Ywhab

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	246 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negative regulator of osteogenesis. Blocks the nuclear translocation of the phosphorylated form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on cyclin D1 expression resulting in blockage of neuronal apoptosis elicited by SRPK2 By similarity.
Subunit structure	Homodimer, and heterodimer with YWHAG, YWHAE and YWHAQ. Interacts with SSH1 and TORC2/CRTC2. Interacts with GAB2 and YAP1 (phosphorylated form) By similarity. Interacts with SAMSN1. Interacts with PKA-phosphorylated AANAT By similarity. Interacts with the phosphorylated (by AKT1) form of SRPK2 By similarity. Interacts with PRKCE (phosphorylated form). Ref.5 Ref.6
Subcellular location	Cytoplasm By similarity. Melanosome By similarity.
Post-translational modification	Isoform alpha differs from isoform beta in being phosphorylated By similarity. Isoform Short contains a N-acetylmethionine at position 1 By similarity.
Sequence similarities	Belongs to the 14-3-3 family.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative initiation
PTM	Acetylation Nitration Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	protein targeting Inferred from direct assay. Source: MGI
Cellular component	melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein domain specific binding Inferred from direct assay. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]

Isoform Long (identifier: Q9CQV8-1)

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.

Isoform Short (identifier: Q9CQV8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: Missing.

Note: No experimental confirmation available. Contains a N-acetylmethionine at position 1 (By similarity).

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 246	246	14-3-3 protein beta/alpha		PRO_0000367902
	Initiator methionine	1	1	Removed; alternate By similarity
	Chain	2 – 246	245	14-3-3 protein beta/alpha, N-terminally processed		PRO_0000000005
Sites
	Site	58	1	Interaction with phosphoserine on interacting protein By similarity
	Site	129	1	Interaction with phosphoserine on interacting protein By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine; in 14-3-3 protein beta/alpha; alternate By similarity
	Modified residue	2	1	N-acetylthreonine; in 14-3-3 protein beta/alpha, N-terminally processed By similarity
	Modified residue	6	1	Phosphoserine By similarity
	Modified residue	70	1	N6-acetyllysine By similarity
	Modified residue	84	1	Nitrated tyrosine Ref.4
	Modified residue	106	1	Nitrated tyrosine Ref.4
	Modified residue	117	1	N6-acetyllysine By similarity
	Modified residue	186	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1 – 2	2	Missing in isoform Short.		VSP_018634
Experimental info
	Sequence conflict	10	1	Q → H in AAC14343. Ref.1
	Sequence conflict	74	1	N → D in AAC14343. Ref.1
	Sequence conflict	126	1	D → Y in BAE29538. Ref.2
	Sequence conflict	126	1	D → Y in BAE30278. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 51C366ED85B38EED	FASTA	246	28,086
	10 20 30 40 50 60 MTMDKSELVQ KAKLAEQAER YDDMAAAMKA VTEQGHELSN EERNLLSVAY KNVVGARRSS 70 80 90 100 110 120 WRVISSIEQK TERNEKKQQM GKEYREKIEA ELQDICNDVL ELLDKYLILN ATQAESKVFY 130 140 150 160 170 180 LKMKGDYFRY LSEVASGENK QTTVSNSQQA YQEAFEISKK EMQPTHPIRL GLALNFSVFY 190 200 210 220 230 240 YEILNSPEKA CSLAKTAFDE AIAELDTLNE ESYKDSTLIM QLLRDNLTLW TSENQGDEGD AGEGEN
	Isoform Short [UniParc]. Checksum: F42896ED9EC6F0D5	FASTA	244	27,854
	10 20 30 40 50 60 MDKSELVQKA KLAEQAERYD DMAAAMKAVT EQGHELSNEE RNLLSVAYKN VVGARRSSWR 70 80 90 100 110 120 VISSIEQKTE RNEKKQQMGK EYREKIEAEL QDICNDVLEL LDKYLILNAT QAESKVFYLK 130 140 150 160 170 180 MKGDYFRYLS EVASGENKQT TVSNSQQAYQ EAFEISKKEM QPTHPIRLGL ALNFSVFYYE 190 200 210 220 230 240 ILNSPEKACS LAKTAFDEAI AELDTLNEES YKDSTLIMQL LRDNLTLWTS ENQGDEGDAG EGEN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Karpitskiy V.V., Shaw A.S. Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6J.
[2]	"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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Bone marrow, Embryo, Kidney, Liver, Thymus and Visual cortex.
[3]	Lubec G., Kang S.U., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-12; 14-57; 61-70; 84-117; 128-169; 196-246 AND 215-224, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[4]	"Endogenously nitrated proteins in mouse brain: links to neurodegenerative disease." Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C., Bigelow D.J. Biochemistry 45:8009-8022(2006) [PubMed: 16800626] [Abstract] Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-84 AND TYR-106, MASS SPECTROMETRY. Tissue: Brain.
[5]	"The regulated assembly of a PKCepsilon complex controls the completion of cytokinesis." Saurin A.T., Durgan J., Cameron A.J., Faisal A., Marber M.S., Parker P.J. Nat. Cell Biol. 10:891-901(2008) [PubMed: 18604201] [Abstract] Cited for: INTERACTION WITH PRKCE.
[6]	"SLy2 targets the nuclear SAP30/HDAC1 complex." Brandt S., Ellwanger K., Beuter-Gunia C., Schuster M., Hausser A., Schmitz I., Beer-Hammer S. Int. J. Biochem. Cell Biol. 42:1472-1481(2010) [PubMed: 20478393] [Abstract] Cited for: INTERACTION WITH SAMSN1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF058797 mRNA. Translation: AAC14343.1. AK002632 mRNA. Translation: BAB22246.1. AK004872 mRNA. Translation: BAB23631.1. AK011389 mRNA. Translation: BAB27587.1. AK083367 mRNA. Translation: BAC38886.1. AK144061 mRNA. Translation: BAE25678.1. AK150414 mRNA. Translation: BAE29538.1. AK151294 mRNA. Translation: BAE30278.1. AK158932 mRNA. Translation: BAE34730.1.
IPI	IPI00230682. IPI00760000.
RefSeq	NP_061223.2. NM_018753.6.
UniGene	Mm.34319.
3D structure databases
ProteinModelPortal	Q9CQV8.
SMR	Q9CQV8. Positions 3-233.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9CQV8. 610 interactions.
STRING	Q9CQV8.
PTM databases
PhosphoSite	Q9CQV8.
2D gel databases
UCD-2DPAGE	Q9CQV8.
Proteomic databases
PRIDE	Q9CQV8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000018470; ENSMUSP00000018470; ENSMUSG00000018326.
GeneID	54401.
KEGG	mmu:54401.
Organism-specific databases
CTD	7529.
MGI	MGI:1891917. Ywhab.
Phylogenomic databases
GeneTree	ENSGT00550000074221.
HOGENOM	HBG611720.
HOVERGEN	HBG050423.
InParanoid	Q9CQV8.
OMA	MGREYRE.
OrthoDB	EOG4N30PR.
PhylomeDB	Q9CQV8.
Gene expression databases
ArrayExpress	Q9CQV8.
Bgee	Q9CQV8.
Genevestigator	Q9CQV8.
GermOnline	ENSMUSG00000018326. Mus musculus.
Family and domain databases
InterPro	IPR000308. 14-3-3. IPR023409. 14-3-3_CS. IPR023410. 14-3-3_domain. [Graphical view]
Gene3D	G3DSA:1.20.190.20. 14-3-3. 1 hit.
KO	K06630.
PANTHER	PTHR18860. 14-3-3. 1 hit.
Pfam	PF00244. 14-3-3. 1 hit. [Graphical view]
PIRSF	PIRSF000868. 14-3-3. 1 hit.
PRINTS	PR00305. 1433ZETA.
SMART	SM00101. 14_3_3. 1 hit. [Graphical view]
SUPFAM	SSF48445. 14-3-3. 1 hit.
PROSITE	PS00796. 1433_1. 1 hit. PS00797. 1433_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	311260.
SOURCE	Search...

Entry information

Entry name

1433B_MOUSE

Accession

Primary (citable) accession number: Q9CQV8
Secondary accession number(s): O70455, Q3TY33, Q3UAN6

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 105 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program