Reviewed, UniProtKB/Swiss-Prot P31016 (DLG4_RAT)

Names and origin

Protein names

Recommended name:
    Disks large homolog 4
Alternative name(s):
    Postsynaptic density protein 95
      Short name=PSD-95
    Synapse-associated protein 90
      Short name=SAP90

Gene names

Name:	Dlg4
Synonyms:	Dlgh4, Psd95

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	724 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Interacts with the cytoplasmic tail of NMDA receptor subunits and shaker-type potassium channels. Required for synaptic plasticity associated with NMDA receptor signaling. Overexpression or depletion of DLG4 changes the ratio of excitatory to inhibitory synapses in hippocampal neurons. May reduce the amplitude of ACCN3 acid-evoked currents by retaining the channel intracellularly. May regulate the intracellular trafficking of ADR1B. Ref.15 Ref.17
Subunit structure	Interacts through its first two PDZ domains with KCNA1, KCNA2, KCNA3, KCNA4 and ERBB4. Interacts through its first PDZ domain with GRIK2, KCNA4 and CRIPT. Interacts through its third PDZ domain with NLGN1, and probably with NLGN2 and NLGN3. May interact with HTR2A. Interacts through its guanylate kinase-like domain with KIF13B. Isoform 2 interacts through an L27 domain with HGS/HRS and the first L27 domain of CASK By similarity. Interacts through its first two PDZ domains with GRIN2A, GRIN2B, GRIN2C, GRIN2D, ACCN3, certain splice forms of GRIN1, KCND2, CXADR and SYNGAP1. Interacts through its second PDZ domain with the PDZ domain of NOS1 or the C-terminus of CAPON. Interacts through its guanylate kinase-like domain with DLGAP1/GKAP, DLGAP2, DLGAP3, DLGAP4, MAP1A and BEGAIN. Interacts through its third PDZ domain with CRIPT. Interacts with ANKS1B, LRFN1 and PRR7.
Subcellular location	Cell membrane; Peripheral membrane protein. Cell junction › synapse › postsynaptic cell membrane › postsynaptic density. Cell junction › synapse. Note: High levels in postsynaptic density of neurons in the forebrain. Also in presynaptic region of inhibitory synapses formed by cerebellar basket cells on axon hillocks of Purkinje cells. Ref.6 Ref.7
Tissue specificity	Brain. Highest levels of isoform 2 in cerebellum, cortex, hippocampus, and corpus striatum. Ref.14
Domain	The PDZ domain 3 mediates interaction with ADR1B By similarity. The L27 domain near the N-terminus of isoform 2 is required for HGS/HRS-dependent targeting to post-synaptic density By similarity.
Post-translational modification	Palmitoylation of isoform 1 is required for targeting to postsynaptic density.
Sequence similarities	Belongs to the MAGUK family. Contains 1 guanylate kinase-like domain. Contains 3 PDZ (DHR) domains. Contains 1 SH3 domain.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Membrane Postsynaptic cell membrane Synapse
Coding sequence diversity	Alternative splicing
Domain	Repeat SH3 domain
PTM	Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	neuronal ion channel clustering Traceable author statement. Source: UniProtKB response to stress Non-traceable author statement. Source: RGD
Cellular component	cell junction Inferred from electronic annotation. Source: UniProtKB-SubCell postsynaptic density Inferred from electronic annotation. Source: UniProtKB-SubCell postsynaptic membrane Inferred from direct assay. Source: MGI synaptosome Inferred from direct assay. Source: MGI
Molecular function	PDZ domain binding Inferred from physical interaction. Source: RGD ionotropic glutamate receptor binding Inferred from physical interaction. Source: RGD protein C-terminus binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ADRB1	P08588	1	EBI-375655,EBI-991009	From a different organism.
Apc	P70478	2	EBI-375655,EBI-631663
ATP2B2	Q01814-1	1	EBI-375655,EBI-1174262	From a different organism.
ATP2B4	P23634-6	1	EBI-375655,EBI-1174437	From a different organism.
Cript	Q792Q4	1	EBI-375655,EBI-632062
Dlgap1	P97836	3	EBI-375655,EBI-80901
Dlgap2	P97837	1	EBI-375655,EBI-81025
Grin2a	Q00959	2	EBI-375655,EBI-630970
Grin2b	Q00960	3	EBI-375655,EBI-396905
Grin2c	Q00961	2	EBI-375655,EBI-631045
Grip1	P97879	1	EBI-375655,EBI-936113
KCNA4	P22459	1	EBI-375655,EBI-631235	From a different organism.
Kcna4	P15385	1	EBI-375655,EBI-631417
Lrfn2	Q460M5	1	EBI-375655,EBI-877185
Map1a	P34926	6	EBI-375655,EBI-631571
Nos1	P29476	1	EBI-375655,EBI-349460
Shank1	Q9WV48	1	EBI-375655,EBI-80909
Sharpin	Q9EQL9	1	EBI-375655,EBI-1394695
Slc6a9	P28572	2	EBI-375655,EBI-848783
Slc6a9	P28572-2	2	EBI-375655,EBI-848796

Alternative products

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

Isoform 1 (identifier: P31016-1)

Also known as: PSD95-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.

Isoform 2 (identifier: P31016-2)

Also known as: PSD95-beta;

The sequence of this isoform is not available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 724

724

Disks large homolog 4

PRO_0000094562

Regions

Domain

65 – 151

87

PDZ 1

Domain

160 – 246

87

PDZ 2

Domain

313 – 393

81

PDZ 3

Domain

428 – 498

71

SH3

Domain

534 – 709

176

Guanylate kinase-like

Amino acid modifications

Modified residue

142

1

Phosphoserine By similarity

Modified residue

240

1

Phosphotyrosine By similarity

Modified residue

295

1

Phosphoserine By similarity

Modified residue

397

1

Phosphotyrosine By similarity

Modified residue

415

1

Phosphoserine By similarity

Modified residue

418

1

Phosphoserine By similarity

Modified residue

432

1

Phosphotyrosine By similarity

Modified residue

580

1

Phosphotyrosine By similarity

Modified residue

604

1

Phosphotyrosine By similarity

Modified residue

701

1

Phosphotyrosine By similarity

Modified residue

715

1

Phosphotyrosine By similarity

Lipidation

3

1

S-palmitoyl cysteine Ref.12

Lipidation

5

1

S-palmitoyl cysteine Ref.12

Experimental info

Mutagenesis

3

1

C → S: Loss of palmitoylation and targeting to postsynaptic density. Ref.12

Mutagenesis

5

1

C → S: Loss of palmitoylation and targeting to postsynaptic density. Ref.12

Sequence conflict

61

1

M → L in CAA47103. Ref.2

Sequence conflict

78

1

S → T in CAA47103. Ref.2

Sequence conflict

177 – 182

6

GVGNQH → ALGTSI in CAA47103. Ref.2

Sequence conflict

200

1

A → G in CAA47103. Ref.2

Sequence conflict

254

1

S → T in CAA47103. Ref.2

Sequence conflict

540 – 555

16

LGPTK…LLSEF → SLDPPKTVPTMIFSPSS in CAA47103. Ref.2

Sequence conflict

623 – 625

3

GKH → RDQ Ref.4

Secondary structure

1

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724

Helix Strand Turn

Details...

Beta strand

62 – 69

8

Beta strand

75 – 80

6

Beta strand

82 – 85

4

Beta strand

88 – 91

4

Beta strand

95 – 99

5

Helix

104 – 108

5

Beta strand

119 – 122

4

Helix

130 – 138

9

Beta strand

142 – 150

9

Beta strand

157 – 164

8

Beta strand

171 – 176

6

Beta strand

178 – 180

3

Beta strand

187 – 194

8

Helix

200 – 204

5

Beta strand

211 – 215

5

Beta strand

221 – 224

4

Helix

225 – 233

9

Beta strand

237 – 245

9

Helix

302 – 304

3

Beta strand

312 – 317

6

Beta strand

325 – 329

5

Beta strand

336 – 341

6

Helix

346 – 350

5

Beta strand

357 – 362

6

Helix

372 – 380

9

Beta strand

384 – 392

9

Helix

394 – 398

5

Beta strand

431 – 437

7

Helix

441 – 444

4

Beta strand

459 – 464

6

Beta strand

467 – 475

9

Beta strand

487 – 489

3

Helix

491 – 501

11

Beta strand

523 – 530

8

Beta strand

537 – 541

5

Helix

544 – 554

11

Turn

556 – 558

3

Turn

576 – 578

3

Helix

586 – 594

9

Beta strand

598 – 604

7

Beta strand

607 – 612

6

Helix

613 – 621

9

Beta strand

625 – 628

4

Helix

634 – 640

7

Beta strand

646 – 650

5

Helix

655 – 661

7

Beta strand

663 – 665

3

Helix

667 – 684

18

Helix

685 – 687

3

Beta strand

689 – 692

4

Helix

697 – 711

15

Beta strand

713 – 719

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (PSD95-alpha) [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 7922D4E8E0F9AD85	FASTA	724	80,465
	10 20 30 40 50 60 MDCLCIVTTK KYRYQDEDTP PLEHSPAHLP NQANSPPVIV NTDTLEAPGY ELQVNGTEGE 70 80 90 100 110 120 MEYEEITLER GNSGLGFSIA GGTDNPHIGD DPSIFITKII PGGAAAQDGR LRVNDSILFV 130 140 150 160 170 180 NEVDVREVTH SAAVEALKEA GSIVRLYVMR RKPPAEKVME IKLIKGPKGL GFSIAGGVGN 190 200 210 220 230 240 QHIPGDNSIY VTKIIEGGAA HKDGRLQIGD KILAVNSVGL EDVMHEDAVA ALKNTYDVVY 250 260 270 280 290 300 LKVAKPSNAY LSDSYAPPDI TTSYSQHLDN EISHSSYLGT DYPTAMTPTS PRRYSPVAKD 310 320 330 340 350 360 LLGEEDIPRE PRRIVIHRGS TGLGFNIVGG EDGEGIFISF ILAGGPADLS GELRKGDQIL 370 380 390 400 410 420 SVNGVDLRNA SHEQAAIALK NAGQTVTIIA QYKPEEYSRF EAKIHDLREQ LMNSSLGSGT 430 440 450 460 470 480 ASLRSNPKRG FYIRALFDYD KTKDCGFLSQ ALSFRFGDVL HVIDAGDEEW WQARRVHSDS 490 500 510 520 530 540 ETDDIGFIPS KRRVERREWS RLKAKDWGSS SGSQGREDSV LSYETVTQME VHYARPIIIL 550 560 570 580 590 600 GPTKDRANDD LLSEFPDKFG SCVPHTTRPK REYEIDGRDY HFVSSREKME KDIQAHKFIE 610 620 630 640 650 660 AGQYNSHLYG TSVQSVREVA EQGKHCILDV SANAVRRLQA AHLHPIAIFI RPRSLENVLE 670 680 690 700 710 720 INKRITEEQA RKAFDRATKL EQEFTECFSA IVEGDSFEEI YHKVKRVIED LSGPYIWVPA RERL
	Isoform 2 (PSD95-beta) (Sequence not available).	FASTA	–	–

References

[1]	"The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein." Cho K.-O., Hunt C.A., Kennedy M.B. Neuron 9:929-942(1992) [PubMed: 1419001] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Brain.
[2]	"SAP90, a rat presynaptic protein related to the product of the Drosophila tumor suppressor gene dlg-A." Kistner U., Wenzel B.M., Veh R.W., Cases-Langhoff C., Garner A.M., Appeltauer U., Voss B., Gundelfinger E.D., Garner C.C. J. Biol. Chem. 268:4580-4583(1993) [PubMed: 7680343] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Brain.
[3]	Lubec G., Diao W. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 113-126; 212-233; 300-312; 381-399 AND 598-617, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus.
[4]	Adams L.D., Werny I., Schwartz S.M. Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 566-625. Strain: Wistar Kyoto. Tissue: Vascular smooth muscle.
[5]	"Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95." Kornau H.C., Schenker L.T., Kennedy M.B., Seeburg P.H. Science 269:1737-1740(1995) [PubMed: 7569905] [Abstract] Cited for: INTERACTION WITH GRIN2A; GRIN2B; GRIN2C AND GRIN2D.
[6]	"Cloning and characterization of postsynaptic density 93, a nitric oxide synthase interacting protein." Brenman J.E., Christopherson K.S., Craven S.E., McGee A.W., Bredt D.S. J. Neurosci. 16:7407-7415(1996) [PubMed: 8922396] [Abstract] Cited for: SUBCELLULAR LOCATION.
[7]	"SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density." Takeuchi M., Hata Y., Hirao K., Toyoda A., Irie M., Takai Y. J. Biol. Chem. 272:11943-11951(1997) [PubMed: 9115257] [Abstract] Cited for: INTERACTION WITH DLGAP1; DLGAP2; DLGAP3 AND DLGAP4, SUBCELLULAR LOCATION. Tissue: Brain.
[8]	"BEGAIN (brain-enriched guanylate kinase-associated protein), a novel neuronal PSD-95/SAP90-binding protein." Deguchi M., Hata Y., Takeuchi M., Ide N., Hirao K., Yao I., Irie M., Toyoda A., Takai Y. J. Biol. Chem. 273:26269-26272(1998) [PubMed: 9756850] [Abstract] Cited for: INTERACTION WITH BEGAIN AND DLGAP1.
[9]	"Localization of postsynaptic density-93 to dendritic microtubules and interaction with microtubule-associated protein 1A." Brenman J.E., Topinka J.R., Cooper E.C., McGee A.W., Rosen J., Milroy T., Ralston H.J., Bredt D.S. J. Neurosci. 18:8805-8813(1998) [PubMed: 9786987] [Abstract] Cited for: INTERACTION WITH MAP1A.
[10]	"SynGAP: a synaptic RasGAP that associates with the PSD-95/SAP90 protein family." Kim J.H., Liao D., Lau L.-F., Huganir R.L. Neuron 20:683-691(1998) [PubMed: 9581761] [Abstract] Cited for: INTERACTION WITH SYNGAP1.
[11]	"CRIPT, a novel postsynaptic protein that binds to the third PDZ domain of PSD-95/SAP90." Niethammer M., Valtschanoff J.G., Kapoor T.M., Allison D.W., Weinberg R.J., Craig A.M., Sheng M. Neuron 20:693-707(1998) [PubMed: 9581762] [Abstract] Cited for: INTERACTION WITH CRIPT.
[12]	"Dual palmitoylation of PSD-95 mediates its vesiculotubular sorting, postsynaptic targeting, and ion channel clustering." El-Husseini A.E., Craven S.E., Chetkovich D.M., Firestein B.L., Schnell E., Aoki C., Bredt D.S. J. Cell Biol. 148:159-172(2000) [PubMed: 10629226] [Abstract] Cited for: MUTAGENESIS OF CYS-3 AND CYS-5, PALMITOYLATION AT CYS-3 AND CYS-5.
[13]	"Cell surface targeting and clustering interactions between heterologously expressed PSD-95 and the Shal voltage-gated potassium channel, Kv4.2." Wong W., Newell E.W., Jugloff D.G.M., Jones O.T., Schlichter L.C. J. Biol. Chem. 277:20423-20430(2002) [PubMed: 11923279] [Abstract] Cited for: INTERACTION WITH KCND2.
[14]	"Postsynaptic targeting of alternative postsynaptic density-95 isoforms by distinct mechanisms." Chetkovich D.M., Bunn R.C., Kuo S.-H., Kawasaki Y., Kohwi M., Bredt D.S. J. Neurosci. 22:6415-6425(2002) [PubMed: 12151521] [Abstract] Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[15]	"PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have opposite effects on H+- gated current." Hruska-Hageman A.M., Benson C.J., Leonard A.S., Price M.P., Welsh M.J. J. Biol. Chem. 279:46962-46968(2004) [PubMed: 15317815] [Abstract] Cited for: INTERACTION WITH ACCN3, FUNCTION.
[16]	"A role for the PDZ-binding domain of the coxsackie B virus and adenovirus receptor (CAR) in cell adhesion and growth." Ashbourne-Excoffon K.J.D., Hruska-Hageman A.M., Klotz M., Traver G.L., Zabner J. J. Cell Sci. 117:4401-4409(2004) [PubMed: 15304526] [Abstract] Cited for: INTERACTION WITH CXADR.
[17]	"A balance between excitatory and inhibitory synapses is controlled by PSD-95 and neuroligin." Prange O., Wong T.P., Gerrow K., Wang Y.T., El-Husseini A. Proc. Natl. Acad. Sci. U.S.A. 101:13915-13920(2004) [PubMed: 15358863] [Abstract] Cited for: FUNCTION.
[18]	"Proteomic analysis revealed a novel synaptic proline-rich membrane protein (PRR7) associated with PSD-95 and NMDA receptor." Murata Y., Doi T., Taniguchi H., Fujiyoshi Y. Biochem. Biophys. Res. Commun. 327:183-191(2005) [PubMed: 15629447] [Abstract] Cited for: INTERACTION WITH PRR7.
[19]	"SALM synaptic cell adhesion-like molecules regulate the differentiation of excitatory synapses." Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H., Kaang B.-K., Kim E. Neuron 50:233-245(2006) [PubMed: 16630835] [Abstract] Cited for: INTERACTION WITH LRFN1.
[20]	"Activity-dependent AIDA-1 nuclear signaling regulates nucleolar numbers and protein synthesis in neurons." Jordan B.A., Fernholz B.D., Khatri L., Ziff E.B. Nat. Neurosci. 10:427-435(2007) [PubMed: 17334360] [Abstract] Cited for: INTERACTION WITH ANKS1B.
[21]	"Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ." Doyle D.A., Lee A., Lewis J., Kim E., Sheng M., Mackinnon R. Cell 85:1067-1076(1996) [PubMed: 8674113] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 302-402.
[22]	"Solution structure and backbone dynamics of the second PDZ domain of postsynaptic density-95." Tochio H., Hung F., Li M., Bredt D.S., Zhang M. J. Mol. Biol. 295:225-237(2000) [PubMed: 10623522] [Abstract] Cited for: STRUCTURE BY NMR OF 155-246, INTERACTION WITH NOS1 AND CAPON.
[23]	"Structure of the SH3-guanylate kinase module from PSD-95 suggests a mechanism for regulated assembly of MAGUK scaffolding proteins." McGee A.W., Dakoji S.R., Olsen O., Bredt D.S., Lim W.A., Prehoda K.E. Mol. Cell 8:1291-1301(2001) [PubMed: 11779504] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 430-724.
[24]	"Structural characterization of the intramolecular interaction between the SH3 and guanylate kinase domains of PSD-95." Tavares G.A., Panepucci E.H., Brunger A.T. Mol. Cell 8:1313-1325(2001) [PubMed: 11779506] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 430-724.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M96853 mRNA. Translation: AAA41971.1.
X66474 mRNA. Translation: CAA47103.1.
U77090 mRNA. Translation: AAB38270.1.

IPI

IPI00566635.

PIR

A45436.
JH0800.

RefSeq

NP_062567.1.

UniGene

Rn.9765

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BE9	X-ray	1.82	A	302-402	[»]
1BFE	X-ray	2.30	A	302-402	[»]
1IU0	NMR	-	A	61-151	[»]
1IU2	NMR	-	A	61-151	[»]
1JXM	X-ray	2.00	A	430-724	[»]
1JXO	X-ray	2.30	A/B	430-724	[»]
1KJW	X-ray	1.80	A	430-724	[»]
1QLC	NMR	-	A	155-249	[»]
1RGR	NMR	-	A	62-154	[»]
1TP3	X-ray	1.99	A	302-402	[»]
1TP5	X-ray	1.54	A	302-402	[»]
1TQ3	X-ray	1.89	A	302-402	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P31016. 30 interactions.

PTM databases

PhosphoSite

P31016.

Genome annotation databases

Ensembl

ENSRNOG00000018526. Rattus norvegicus. [Contig view]

GeneID

29495.

KEGG

rno:29495.

Organism-specific databases

RGD

68424. Dlgh4.

Phylogenomic databases

HOVERGEN

P31016.

Gene expression databases

ArrayExpress

P31016.

GermOnline

ENSRNOG00000018526. Rattus norvegicus.

Family and domain databases

InterPro

IPR019586. Gua_kin_assoc_C.
IPR008144. Guanylate_kin.
IPR008145. Guanylt/Ca.
IPR016313. M-assoc_guanylate_kinase.
IPR019590. MAGUK_PEST_N.
IPR001478. PDZ/DHR/GLGF.
IPR019583. PDZ_assoc.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]

Pfam

PF10603. Gua_kin_assoc_C. 1 hit.
PF00625. Guanylate_kin. 1 hit.
PF10608. MAGUK_N_PEST. 1 hit.
PF00595. PDZ. 3 hits.
PF10600. PDZ_assoc. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]

PIRSF

PIRSF001741. MAGUK_DLGH. 1 hit.

ProDom

PD000066. SH3. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00072. GuKc. 1 hit.
SM00228. PDZ. 3 hits.
SM00326. SH3. 1 hit.
[Graphical view]

PROSITE

PS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 3 hits.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00536. Guanidine.

NextBio

609380.

Entry information

Entry name

DLG4_RAT

Accession

Primary (citable) accession number: P31016
Secondary accession number(s): P97631

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	June 16, 2009
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)