Reviewed, UniProtKB/Swiss-Prot Q9ERE9 (JIP2_MOUSE)

Names and origin

Protein names

Recommended name:
    C-jun-amino-terminal kinase-interacting protein 2
      Short name=JNK-interacting protein 2
      Short name=JIP-2
Alternative name(s):
    JNK MAP kinase scaffold protein 2
    Islet-brain-2
      Short name=IB-2
    Mitogen-activated protein kinase 8-interacting protein 2

Gene names

Name:	Mapk8ip2
Synonyms:	Ib2, Jip2

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

Protein attributes

Sequence length	830 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. JIP2 inhibits IL1 beta-induced apoptosis in insulin-secreting cells By similarity.
Subunit structure	Forms homo-or heterooligomeric complexes. Binds specific components of the JNK signaling pathway namely JNK, MAPKK7 and MLK2, MLK3 and DLK By similarity. Also binds the proline-rich domain-containing splice variant of apolipoprotein E receptor 2 (ApoER2). Binds the TPR motif-containing C-terminal of kinesin light chain. Binds the cytoplasmic tails of LRP1 and LRP2 (Megalin).
Subcellular location	Cytoplasm. Note: Accumulates in cell surface projections By similarity.
Tissue specificity	Highly expressed in brain. Expressed in all neurons. Also expressed in testis, primarily in the epididymal epidermis.
Induction	Upon neuron differentiation.
Sequence similarities	Belongs to the JIP scaffold family. Contains 1 PID domain. Contains 1 SH3 domain.
Sequence caution	The sequence AK014339 differs from that shown. Reason: Erroneous termination at position 701. Translated as Cys.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	SH3 domain
Gene Ontology (GO)
Biological process	JNK cascade Ref.1 Inferred from direct assay. Source: MGI regulation of JNK cascade Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cell soma Inferred from direct assay. Source: MGI cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	kinesin binding Inferred from physical interaction. Source: UniProtKB protein kinase binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Appl	P14599	2	EBI-74576,EBI-74135	From a different organism.
Lrp1	Q91ZX7	1	EBI-74576,EBI-300955

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 830	830	C-jun-amino-terminal kinase-interacting protein 2		PRO_0000220632
Regions
	Domain	610 – 671	62	SH3
	Domain	683 – 819	137	PID
	Region	111 – 278	168	JNK-binding domain (JBD)
	Compositional bias	30 – 36	7	Asp/Glu-rich (acidic)
	Compositional bias	85 – 104	20	Asp/Glu-rich (acidic)
	Compositional bias	154 – 157	4	Poly-Asn
	Compositional bias	282 – 293	12	Ser-rich
	Compositional bias	420 – 437	18	Pro-rich
	Compositional bias	472 – 487	16	Asp/Glu-rich (acidic)
Experimental info
	Sequence conflict	216	1	P → Q in AK014339. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9ERE9-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 7EC8EAD19A90163C	FASTA	830	89,900
	10 20 30 40 50 60 MADRAEMFSL STFHSLSPPG CRPPQDISLE EFDDEDLSEI TDDCGLGLSY DSDHCEKDSL 70 80 90 100 110 120 SLGRSEQPHP ICSFQDDFQE FEMIDDNEEE DDEEEEEEEE EEEDGDRQGK AGGGPGSQAL 130 140 150 160 170 180 AGDSLIPSPS LEESHKLRPT TLHLTTLGAQ DSLNNNNGGF TSAPPSSWQE TVLRSPAQEP 190 200 210 220 230 240 LKELPAPLLP AEEERHEVQS LARPGCDCEG NQPPEPPASS GGASPSSDPG IEADLRSHSS 250 260 270 280 290 300 GGHEGRRSSQ ELSSPGSDSE DAGGARLGRM ISSISETELE LSSDGGSSSG RSSHLTNSIE 310 320 330 340 350 360 EASSPASEPE PEPEPLHEPP RRPAFLPVGQ DDTNSEYESG SESEPDLSED ADSPWLLSNL 370 380 390 400 410 420 VSRMISEGSS PIRCPGQCLS PAPRLPEEAA SQANSVPQDC QDPEAGPHVE LVDMDTLCGP 430 440 450 460 470 480 PPPAPAAPRL GPAQPGPCLF LSNPTRDTIT PLWATPGRTA RPGRSCSAAC SEEEEEDEEE 490 500 510 520 530 540 DEEDEEDAED SVVPPGSRTT GSTAPLDASL VYDAVKYTLV VDEHTQLELV SLRRCAGLGN 550 560 570 580 590 600 DSEEDSSCEA SEEEAGATLL GSDQVPEDAS PDSPDLTFSK KFLNVFVNST SRSSSTESFG 610 620 630 640 650 660 LFSCVVNGEE REQTHRAVFR FIPRHPDELE LDVDDPVLVE AEEDDFWFRG FNMRTGERGV 670 680 690 700 710 720 FPAFYAHAVP GPAKDLLGSK RSPCWVDRFD VQFLGSVEVP CHQGNGILCA AMQKIATARK 730 740 750 760 770 780 LTVHLRPPAS CDLEISLRGV KLSLSGGGPE FQRCSHFFQM KNISFCGCHP RNSCYFGFIT 790 800 810 820 830 KHPLLSRFAC HVFVSQESMR PVARSVGRAF LEYYQEHLAF ACPTEDIYLE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The reelin receptor ApoER2 recruits JNK-interacting proteins-1 and -2." Stockinger W., Brandes C., Fasching D., Hermann M., Gotthardt M., Herz J., Schneider W.J., Nimpf J. J. Biol. Chem. 275:25625-25632(2000) [PubMed: 10827199] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH APOER2. Strain: BALB/c. Tissue: Brain.
[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: Embryonic head.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF310135 mRNA. Translation: AAG31800.1. AK014339 mRNA. No translation available.
IPI	IPI00112307.
UniGene	Mm.173337 Mm.391684
3D structure databases
SMR	Q9ERE9. Positions 612-666.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9ERE9. 5 interactions.
PTM databases
PhosphoSite	Q9ERE9.
Proteomic databases
PRIDE	Q9ERE9.
Genome annotation databases
Ensembl	ENSMUSG00000022619. Mus musculus. [Contig view]
Organism-specific databases
MGI	MGI:1926555. Mapk8ip2.
Phylogenomic databases
HOGENOM	Q9ERE9.
HOVERGEN	Q9ERE9.
OMA	Q9ERE9. GARLGRM.
Gene expression databases
ArrayExpress	Q9ERE9.
Bgee	Q9ERE9.
GermOnline	ENSMUSG00000022619. Mus musculus.
Family and domain databases
InterPro	IPR011993. PH_type. IPR006020. PTB_PID. IPR001452. SH3_domain. [Graphical view]
Gene3D	G3DSA:2.30.29.30. PH_type. 1 hit.
Pfam	PF00640. PID. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
SMART	SM00462. PTB. 1 hit. SM00326. SH3. 1 hit. [Graphical view]
PROSITE	PS01179. PID. 1 hit. PS50002. SH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

JIP2_MOUSE

Accession

Primary (citable) accession number: Q9ERE9
Secondary accession number(s): Q9CXI4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 5, 2001
Last sequence update:	March 1, 2001
Last modified:	June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)