E3 SUMO-protein ligase PIAS2 - Mus musculus (Mouse)

Preferred order of sections

Names and origin

Protein names

Recommended name:
E3 SUMO-protein ligase PIAS2
EC=6.3.2.-

Alternative name(s):
Androgen receptor-interacting protein 3
Short name=ARIP3
DAB2-interacting protein
Short name=DIP
Msx-interacting zinc finger protein
Protein inhibitor of activated STAT x
Protein inhibitor of activated STAT2

Gene names

Name:	Pias2
Synonyms:	Miz1, Piasx

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	621 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. The effects of this transcriptional coregulation, transactivation or silencing may vary depending upon the biological context and PIAS2 isoform studied. However, it seems to be mostly involved in gene silencing. Binds to sumoylated ELK1 and enhances its transcriptional activity by preventing recruitment of HDAC2 by ELK1, thus reversing SUMO-mediated repression of ELK1 transactivation activity. Isoform PIASx-beta, but not isoform PIASx-alpha, promotes MDM2 sumoylation. Isoform PIASx-alpha promotes PARK7 sumoylation. Isoform PIASx-beta promotes NCOA2 sumoylation more efficiently than isoform PIASx-alpha By similarity.
Pathway	Protein modification; protein sumoylation.
Subunit structure	Binds SUMO1 and UBE2I. Interacts with AXIN1, JUN, MDM2, PARK7, TP53 and TP73 isoform alpha, but not TP73 isoform beta. Interacts with STAT4 following IL12 and IFN-alpha stimulation of T-cells. Interacts also with GTF2I, GTF2IRD1, IKFZ1, DAB2 and MSX2, as well as with several steroid receptors, including ESR1, ESR2, NR3C1, PGR, AR, and with NCOA2. Sumoylation of a target protein seems to enhance the interaction. Binds to sumoylated ELK1. Interacts with PLAG1 By similarity. Binds DNA, such as CDKN1A promoter, in a sequence-specific manner. Interacts with KLF8; the interaction results in SUMO ligation and repression of KLF8 transcriptional activity and of its cell cycle progression into G₁ phase By similarity. Ref.1 Ref.4 Ref.6 Ref.7 Ref.8
Subcellular location	Nucleus speckle. Nucleus › PML body. Note: Colocalizes at least partially with promyelocytic leukemia nuclear bodies (PML NBs). Ref.6 Ref.7
Domain	The LXXLL motif is a transcriptional coregulator signature.
Post-translational modification	Sumoylated. Ref.7
Sequence similarities	Belongs to the PIAS family. Contains 1 PINIT domain. Contains 1 SAP domain. Contains 1 SP-RING-type zinc finger.
Sequence caution	The sequence AAB96678.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB29594.1 differs from that shown. Reason: Frameshift at position 34.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Ligase
PTM	Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.1. Source: MGI positive regulation of transcription, DNA-dependent Inferred from direct assay. Source: MGI protein sumoylation Inferred from direct assay Ref.8. Source: MGI regulation of osteoblast differentiation Inferred from mutant phenotype. Source: MGI regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.4. Source: MGI regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	PML body Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear body Inferred from direct assay. Source: MGI nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW SUMO ligase activity Inferred from direct assay Ref.8. Source: MGI protein binding Inferred from physical interaction Ref.1. Source: MGI ubiquitin protein ligase binding Inferred from physical interaction. Source: BHF-UCL zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8C5D8-1)

Also known as: PIASx-beta; Miz1;

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 2 (identifier: Q8C5D8-2)

Also known as: PIASx-alpha; ARIP3;

The sequence of this isoform differs from the canonical sequence as follows:
551-572: LDFLSLIPVDPQYCPPMFLDSL → EQRRNDINNEVQLGASSDTVQQ
573-621: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sequence conflict

555

1

N → T in AAF12825. Ref.1

Isoform 3 (identifier: Q8C5D8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-9: Missing.
     551-572: LDFLSLIPVDPQYCPPMFLDSL → EQRRNDINNEVQLGASSDTVQQ
     573-621: Missing.

Note: No experimental confirmation available.

Isoform 4 (identifier: Q8C5D8-4)

The sequence of this isoform differs from the canonical sequence as follows:
563-580: YCPPMFLDSLTSPLTASS → SHLTLNSKQYVCHHHQPP
581-621: Missing.

Note: No experimental confirmation available.

Isoform 5 (identifier: Q8C5D8-5)

The sequence of this isoform differs from the canonical sequence as follows:
1-9: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 621

621

E3 SUMO-protein ligase PIAS2

PRO_0000218977

Regions

Domain

11 – 45

35

SAP

Domain

134 – 299

166

PINIT

Zinc finger

331 – 408

78

SP-RING-type

Region

467 – 473

7

SUMO1-binding By similarity

Motif

19 – 23

5

LXXLL motif

Motif

484 – 492

9

Nuclear localization signal Ref.6

Compositional bias

571 – 610

40

Ser-rich

Compositional bias

596 – 602

7

Poly-Ser

Natural variations

Alternative sequence

1 – 9

9

Missing in isoform 3 and isoform 5.

VSP_012198

Alternative sequence

551 – 572

22

LDFLS…FLDSL → EQRRNDINNEVQLGASSDTV QQ in isoform 2 and isoform 3.

VSP_012199

Alternative sequence

563 – 580

18

YCPPM…LTASS → SHLTLNSKQYVCHHHQPP in isoform 4.

VSP_012200

Alternative sequence

573 – 621

49

Missing in isoform 2 and isoform 3.

VSP_012201

Alternative sequence

581 – 621

41

Missing in isoform 4.

VSP_012202

Experimental info

Sequence conflict

73

1

C → S in AAF12825. Ref.1

Sequence conflict

97

1

P → A in AAF12825. Ref.1

Sequence conflict

110

1

T → A in AAF12825. Ref.1

Sequence conflict

119

1

G → E in AAF12825. Ref.1

Sequence conflict

150

1

N → T in AAF12825. Ref.1

Sequence conflict

158

1

D → E in AAF12825. Ref.1

Sequence conflict

173

1

R → G in BAC26579. Ref.2

Sequence conflict

243

1

G → A in AAF12825. Ref.1

Sequence conflict

288

1

N → Q in AAF12825. Ref.1

Sequence conflict

320

1

R → K in AAF12825. Ref.1

Sequence conflict

327

1

L → P in AAF12825. Ref.1

Sequence conflict

375

1

Q → R in AAF12825. Ref.1

Sequence conflict

413

1

V → A in AAF12825. Ref.1

Sequence conflict

438

1

S → I in BAC37407. Ref.2

Sequence conflict

458

1

V → G in AAF12825. Ref.1

Sequence conflict

464 – 466

3

KKK → GTR in AAF12825. Ref.1

Sequences

Sequence		Length	Mass (Da)
Isoform 1 (PIASx-beta) (Miz1) [UniParc]. Last modified December 7, 2004. Version 2. Checksum: E980B834C2A9C58E Show »	FASTA	621	68,426
10 20 30 40 50 60 MADFEELRNM VSSFRVSELQ VLLGFAGRNK SGRKHDLLMR ALHLLKSGCS PAVQIKIREL 70 80 90 100 110 120 YRRRYPRTLE GLCDLSTIKS SVFSLDGSSS PVEPDLPVAG IHSLPSTSIT PHSPSSPVGS 130 140 150 160 170 180 VLLQDTKPTF EMQQPSPPIP PVHPDVQLKN LPFYDVLDVL IKPTSLVQSS IQRFQEKFFI 190 200 210 220 230 240 FALTPQQVRE ICISRDFLPG GRRDYTVQVQ LRLCLAETSC PQEDNYPNSL CIKVNGKLFP 250 260 270 280 290 300 LPGYAPPPKN GIEQKRPGRP LNITSLVRLS SAVPNQISIS WASEIGKNYS MSVYLVRQLT 310 320 330 340 350 360 SAMLLQRLKM KGIRNPDHSR ALIKEKLTAD PDSEIATTSL RVSLMCPLGK MRLTIPCRAV 370 380 390 400 410 420 TCTHLQCFDA ALYLQMNEKK PTWICPVCDK KAAYESLILD GLFMEILNDC SDVDEIKFQE 430 440 450 460 470 480 DGSWCPMRPK KEAMKVTSQP CTKVESSSVF SKPCSVTVAS DASKKKIDVI DLTIESSSDE 490 500 510 520 530 540 EEDPPAKRKC IFMSETQSSP TKGVLMYQPS SVRVPSVTSV DPAAIPPSLT DYSVPFHHTP 550 560 570 580 590 600 VSSMSSDLPG LDFLSLIPVD PQYCPPMFLD SLTSPLTASS TSVTTTSPHE SSTHVSSSSS 610 620 RSETGVITSS GRNIPDIISL D « Hide
Isoform 2 (PIASx-alpha) (ARIP3) [UniParc]. Checksum: 70668C1CEB3702EE Show »	FASTA	572	63,458
10 20 30 40 50 60 MADFEELRNM VSSFRVSELQ VLLGFAGRNK SGRKHDLLMR ALHLLKSGCS PAVQIKIREL 70 80 90 100 110 120 YRRRYPRTLE GLCDLSTIKS SVFSLDGSSS PVEPDLPVAG IHSLPSTSIT PHSPSSPVGS 130 140 150 160 170 180 VLLQDTKPTF EMQQPSPPIP PVHPDVQLKN LPFYDVLDVL IKPTSLVQSS IQRFQEKFFI 190 200 210 220 230 240 FALTPQQVRE ICISRDFLPG GRRDYTVQVQ LRLCLAETSC PQEDNYPNSL CIKVNGKLFP 250 260 270 280 290 300 LPGYAPPPKN GIEQKRPGRP LNITSLVRLS SAVPNQISIS WASEIGKNYS MSVYLVRQLT 310 320 330 340 350 360 SAMLLQRLKM KGIRNPDHSR ALIKEKLTAD PDSEIATTSL RVSLMCPLGK MRLTIPCRAV 370 380 390 400 410 420 TCTHLQCFDA ALYLQMNEKK PTWICPVCDK KAAYESLILD GLFMEILNDC SDVDEIKFQE 430 440 450 460 470 480 DGSWCPMRPK KEAMKVTSQP CTKVESSSVF SKPCSVTVAS DASKKKIDVI DLTIESSSDE 490 500 510 520 530 540 EEDPPAKRKC IFMSETQSSP TKGVLMYQPS SVRVPSVTSV DPAAIPPSLT DYSVPFHHTP 550 560 570 VSSMSSDLPG EQRRNDINNE VQLGASSDTV QQ « Hide
Isoform 3 [UniParc]. Checksum: 25D6D636E852AA07 Show »	FASTA	563	62,352
10 20 30 40 50 60 MVSSFRVSEL QVLLGFAGRN KSGRKHDLLM RALHLLKSGC SPAVQIKIRE LYRRRYPRTL 70 80 90 100 110 120 EGLCDLSTIK SSVFSLDGSS SPVEPDLPVA GIHSLPSTSI TPHSPSSPVG SVLLQDTKPT 130 140 150 160 170 180 FEMQQPSPPI PPVHPDVQLK NLPFYDVLDV LIKPTSLVQS SIQRFQEKFF IFALTPQQVR 190 200 210 220 230 240 EICISRDFLP GGRRDYTVQV QLRLCLAETS CPQEDNYPNS LCIKVNGKLF PLPGYAPPPK 250 260 270 280 290 300 NGIEQKRPGR PLNITSLVRL SSAVPNQISI SWASEIGKNY SMSVYLVRQL TSAMLLQRLK 310 320 330 340 350 360 MKGIRNPDHS RALIKEKLTA DPDSEIATTS LRVSLMCPLG KMRLTIPCRA VTCTHLQCFD 370 380 390 400 410 420 AALYLQMNEK KPTWICPVCD KKAAYESLIL DGLFMEILND CSDVDEIKFQ EDGSWCPMRP 430 440 450 460 470 480 KKEAMKVTSQ PCTKVESSSV FSKPCSVTVA SDASKKKIDV IDLTIESSSD EEEDPPAKRK 490 500 510 520 530 540 CIFMSETQSS PTKGVLMYQP SSVRVPSVTS VDPAAIPPSL TDYSVPFHHT PVSSMSSDLP 550 560 GEQRRNDINN EVQLGASSDT VQQ « Hide
Isoform 4 [UniParc]. Checksum: 4461E5438EC68633 Show »	FASTA	580	64,421
10 20 30 40 50 60 MADFEELRNM VSSFRVSELQ VLLGFAGRNK SGRKHDLLMR ALHLLKSGCS PAVQIKIREL 70 80 90 100 110 120 YRRRYPRTLE GLCDLSTIKS SVFSLDGSSS PVEPDLPVAG IHSLPSTSIT PHSPSSPVGS 130 140 150 160 170 180 VLLQDTKPTF EMQQPSPPIP PVHPDVQLKN LPFYDVLDVL IKPTSLVQSS IQRFQEKFFI 190 200 210 220 230 240 FALTPQQVRE ICISRDFLPG GRRDYTVQVQ LRLCLAETSC PQEDNYPNSL CIKVNGKLFP 250 260 270 280 290 300 LPGYAPPPKN GIEQKRPGRP LNITSLVRLS SAVPNQISIS WASEIGKNYS MSVYLVRQLT 310 320 330 340 350 360 SAMLLQRLKM KGIRNPDHSR ALIKEKLTAD PDSEIATTSL RVSLMCPLGK MRLTIPCRAV 370 380 390 400 410 420 TCTHLQCFDA ALYLQMNEKK PTWICPVCDK KAAYESLILD GLFMEILNDC SDVDEIKFQE 430 440 450 460 470 480 DGSWCPMRPK KEAMKVTSQP CTKVESSSVF SKPCSVTVAS DASKKKIDVI DLTIESSSDE 490 500 510 520 530 540 EEDPPAKRKC IFMSETQSSP TKGVLMYQPS SVRVPSVTSV DPAAIPPSLT DYSVPFHHTP 550 560 570 580 VSSMSSDLPG LDFLSLIPVD PQSHLTLNSK QYVCHHHQPP « Hide
Isoform 5 [UniParc]. Checksum: 98EA1B83556CDE86 Show »	FASTA	612	67,320
10 20 30 40 50 60 MVSSFRVSEL QVLLGFAGRN KSGRKHDLLM RALHLLKSGC SPAVQIKIRE LYRRRYPRTL 70 80 90 100 110 120 EGLCDLSTIK SSVFSLDGSS SPVEPDLPVA GIHSLPSTSI TPHSPSSPVG SVLLQDTKPT 130 140 150 160 170 180 FEMQQPSPPI PPVHPDVQLK NLPFYDVLDV LIKPTSLVQS SIQRFQEKFF IFALTPQQVR 190 200 210 220 230 240 EICISRDFLP GGRRDYTVQV QLRLCLAETS CPQEDNYPNS LCIKVNGKLF PLPGYAPPPK 250 260 270 280 290 300 NGIEQKRPGR PLNITSLVRL SSAVPNQISI SWASEIGKNY SMSVYLVRQL TSAMLLQRLK 310 320 330 340 350 360 MKGIRNPDHS RALIKEKLTA DPDSEIATTS LRVSLMCPLG KMRLTIPCRA VTCTHLQCFD 370 380 390 400 410 420 AALYLQMNEK KPTWICPVCD KKAAYESLIL DGLFMEILND CSDVDEIKFQ EDGSWCPMRP 430 440 450 460 470 480 KKEAMKVTSQ PCTKVESSSV FSKPCSVTVA SDASKKKIDV IDLTIESSSD EEEDPPAKRK 490 500 510 520 530 540 CIFMSETQSS PTKGVLMYQP SSVRVPSVTS VDPAAIPPSL TDYSVPFHHT PVSSMSSDLP 550 560 570 580 590 600 GLDFLSLIPV DPQYCPPMFL DSLTSPLTAS STSVTTTSPH ESSTHVSSSS SRSETGVITS 610 SGRNIPDIIS LD « Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"p67 isoform of mouse disabled 2 protein acts as a transcriptional activator during the differentiation of F9 cells." Cho S.-Y., Jeon J.W., Lee S.H., Park S.-S. Biochem. J. 352:645-650(2000) [PubMed: 11104669] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH DAB2. Strain: 129. Tissue: Teratocarcinoma.
[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. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4). Strain: C57BL/6J. Tissue: Embryonic lung and Testis.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5). Strain: FVB/N. Tissue: Mammary tumor.
[4]	"Miz1, a novel zinc finger transcription factor that interacts with Msx2 and enhances its affinity for DNA." Wu L., Wu H., Ma L., Sangiorgi F., Wu N., Bell J.R., Lyons G.E., Maxson R. Mech. Dev. 65:3-17(1997) [PubMed: 9256341] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 124-621 (ISOFORM 1), INTERACTION WITH MSX2. Tissue: Embryo.
[5]	Erratum Wu L., Wu H., Ma L., Sangiorgi F., Wu N., Bell J.R., Lyons G.E., Maxson R. Mech. Dev. 69:219-219(1997)
[6]	"The SUMO ubiquitin-protein isopeptide ligase family member Miz1/PIASxbeta/Siz2 is a transcriptional cofactor for TFII-I." Tussie-Luna M.I., Michel B., Hakre S., Roy A.L. J. Biol. Chem. 277:43185-43193(2002) [PubMed: 12193603] [Abstract] Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, INTERACTION WITH GTF2I AND GTF2IRD1.
[7]	"PIAS proteins modulate transcription factors by functioning as SUMO-1 ligases." Kotaja N., Karvonen U., Jaenne O.A., Palvimo J.J. Mol. Cell. Biol. 22:5222-5234(2002) [PubMed: 12077349] [Abstract] Cited for: INTERACTION WITH SUMO1 AND UBE2I, SUBCELLULAR LOCATION, SUMOYLATION.
[8]	"Ikaros SUMOylation: switching out of repression." Gomez-del Arco P., Koipally J., Georgopoulos K. Mol. Cell. Biol. 25:2688-2697(2005) [PubMed: 15767674] [Abstract] Cited for: INTERACTION WITH IKFZ1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF201391 mRNA. Translation: AAF12825.1. AK029716 mRNA. Translation: BAC26579.1. AK014871 mRNA. Translation: BAB29594.1. Frameshift. AK078813 mRNA. Translation: BAC37407.1. AK086653 mRNA. Translation: BAC39710.1. BC005596 mRNA. Translation: AAH05596.1. BC034711 mRNA. Translation: AAH34711.1. AF039567 mRNA. Translation: AAB96678.1. Different initiation.
IPI	IPI00169800. IPI00453655. IPI00480308. IPI00480360. IPI00480492.
RefSeq	NP_001157639.1. NM_001164167.1. NP_001157640.1. NM_001164168.1. NP_001157641.1. NM_001164169.1. NP_001157642.1. NM_001164170.1. NP_032628.3. NM_008602.4.
UniGene	Mm.6370.
3D structure databases
ProteinModelPortal	Q8C5D8.
SMR	Q8C5D8. Positions 1-65, 136-427.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1782012.
STRING	Q8C5D8.
PTM databases
PhosphoSite	Q8C5D8.
Proteomic databases
PRIDE	Q8C5D8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000114777; ENSMUSP00000110425; ENSMUSG00000025423.
GeneID	17344.
KEGG	mmu:17344.
UCSC	uc008frb.1. mouse. uc008frc.2. mouse. uc012bfb.1. mouse.
Organism-specific databases
CTD	9063.
MGI	MGI:1096566. Pias2.
Phylogenomic databases
eggNOG	roNOG14857.
GeneTree	ENSGT00550000074410.
HOVERGEN	HBG053598.
InParanoid	Q8C5D8.
OMA	KHDLLMR.
OrthoDB	EOG4RNB85.
PhylomeDB	Q8C5D8.
Gene expression databases
ArrayExpress	Q8C5D8.
Bgee	Q8C5D8.
CleanEx	MM_PIAS2.
Genevestigator	Q8C5D8.
GermOnline	ENSMUSG00000025423. Mus musculus.
Family and domain databases
InterPro	IPR023321. PINIT. IPR003034. SAP_DNA-bd. IPR004181. Znf_MIZ. [Graphical view]
Gene3D	G3DSA:1.10.720.30. G3DSA:1.10.720.30. 1 hit.
KO	K04706.
Pfam	PF02891. zf-MIZ. 1 hit. [Graphical view]
SMART	SM00513. SAP. 1 hit. [Graphical view]
PROSITE	PS51466. PINIT. 1 hit. PS50800. SAP. 1 hit. PS51044. ZF_SP_RING. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	291922.
SOURCE	Search...

Entry information

Entry name

PIAS2_MOUSE

Accession

Primary (citable) accession number: Q8C5D8
Secondary accession number(s): O54987

Q9QZ63

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 7, 2004
Last sequence update:	December 7, 2004
Last modified:	December 14, 2011
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequence annotation (Features)

Molecule processing

Regions

Natural variations

Experimental info

Sequences

References

Cross-references

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

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents