Reviewed, UniProtKB/Swiss-Prot O14773 (TPP1_HUMAN)

Names and origin

Protein names

Recommended name:
    Tripeptidyl-peptidase 1
      Short name=TPP-1
    EC=3.4.14.9
Alternative name(s):
    Tripeptidyl-peptidase I
      Short name=TPP-I
    Tripeptidyl aminopeptidase
    Lysosomal pepstatin-insensitive protease
      Short name=LPIC
    Cell growth-inhibiting gene 1 protein

Gene names

Name:	TPP1
Synonyms:	CLN2
ORF Names:	GIG1, UNQ267/PRO304

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	563 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	Lysosomal serine protease with tripeptidyl-peptidase I activity. May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Requires substrates with an unsubstituted N-terminus By similarity.
Catalytic activity	Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity.
Subcellular location	Lysosome. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.9 Ref.12
Tissue specificity	Detected in all tissues examined with highest levels in heart and placenta and relatively similar levels in other tissues.
Post-translational modification	Activated by autocatalytic proteolytical processing upon acidification.
Involvement in disease	Defects in TPP1 are the cause of classical late-infantile neuronal ceroid lipofuscinosis (LINCL) [MIM:204500]; also known as ceroid lipofuscinosis neuronal 2 (CLN2). LINCL is a fatal childhood neurodegenerative disease characterized by progressive visual and mental decline, motor disturbance, epilepsy and behavioral changes. The three main subtypes of childhood NCLs defined by the age of onset, clinical features, and ultrastructural morphology are infantile NCL (INCL), classical late-infantile NCL (LINCL), or juvenile NCL (JNCL), although a number of other distinct variants forms have been described. Ref.1 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22
Sequence similarities	Belongs to the peptidase S53 family.
Caution	Ref.3 sequence is wrongly reported to originate from bovine.
Sequence caution	The sequence AAQ88866.1 differs from that shown. Reason: Frameshift at position 551.

Ontologies

Keywords
Cellular component	Lysosome
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Epilepsy Neuronal ceroid lipofuscinosis
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Glycoprotein Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	bone resorption Inferred from mutant phenotype. Source: UniProtKB lipid metabolic process Ref.1 Traceable author statement. Source: ProtInc lysosome organization Inferred from sequence or structural similarity. Source: UniProtKB nervous system development Ref.1 Inferred from mutant phenotype. Source: UniProtKB neuromuscular process controlling balance Inferred from sequence or structural similarity. Source: UniProtKB peptide catabolic process Inferred from mutant phenotype. Source: UniProtKB proteolysis Ref.1 Inferred from mutant phenotype. Source: UniProtKB
Cellular component	lysosome Ref.1 Inferred from direct assay. Source: UniProtKB melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from sequence or structural similarity. Source: UniProtKB soluble fraction Inferred from direct assay. Source: UniProtKB
Molecular function	peptide binding Inferred from sequence or structural similarity. Source: UniProtKB protein binding Inferred from physical interaction. Source: UniProtKB serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro tripeptidyl-peptidase activity Ref.8 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: O14773-1)

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 2 (identifier: O14773-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-243: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Ref.8

Propeptide

20 – 195

176

Removed in mature form

PRO_0000027374

Chain

196 – 563

368

Tripeptidyl-peptidase 1

PRO_0000027375

Sites

Active site

272

1

Charge relay system By similarity

Active site

276

1

Charge relay system By similarity

Active site

475

1

Charge relay system By similarity

Amino acid modifications

Glycosylation

210

1

N-linked (GlcNAc...)

Glycosylation

222

1

N-linked (GlcNAc...)

Glycosylation

286

1

N-linked (GlcNAc...) Potential

Glycosylation

313

1

N-linked (GlcNAc...)

Glycosylation

443

1

N-linked (GlcNAc...) Ref.10

Natural variations

Alternative sequence

1 – 243

243

Missing in isoform 2.

VSP_013118

Natural variant

62

1

S → L: dbSNP rs2734715.

VAR_037572

Natural variant

77

1

G → R in LINCL. Ref.15

VAR_009603

Natural variant

100

1

Q → R: dbSNP rs1800746. Ref.15 Ref.19

VAR_009604

Natural variant

127

1

R → Q in LINCL. Ref.17 Ref.20

VAR_016790

Natural variant

153

1

S → P in LINCL.

VAR_016791

Natural variant

175

1

R → H Ref.1

VAR_005642

Natural variant

185

1

R → C: dbSNP rs34758634.

VAR_037573

Natural variant

206

1

R → C in LINCL. dbSNP rs28940573. Ref.16 Ref.22

VAR_009605

Natural variant

206

1

R → H in LINCL. Ref.16 Ref.22

VAR_016792

Natural variant

277

1

V → M in LINCL. Ref.21

VAR_016793

Natural variant

278

1

Q → P in LINCL. Ref.21

VAR_016794

Natural variant

284

1

G → V in LINCL. Ref.17 Ref.21

VAR_016795

Natural variant

286

1

N → S in LINCL. Ref.20

VAR_016796

Natural variant

287

1

I → N in LINCL. Ref.15

VAR_009606

Natural variant

343

1

E → K in LINCL. Ref.15

VAR_009607

Natural variant

353

1

T → P in LINCL. Ref.20

VAR_016797

Natural variant

365

1

C → R in LINCL. Ref.1 Ref.15

VAR_005643

Natural variant

365

1

C → Y in LINCL. Ref.1 Ref.15

VAR_005644

Natural variant

385

1

V → D in LINCL. Ref.15

VAR_009608

Natural variant

389

1

G → E in LINCL. Ref.15

VAR_009609

Natural variant

422

1

Q → H in LINCL. Ref.15

VAR_009610

Natural variant

428

1

K → N in LINCL. Ref.17

VAR_016798

Natural variant

447

1

R → H in LINCL. Ref.15

VAR_005645

Natural variant

454

1

A → E in LINCL. Ref.15

VAR_009611

Natural variant

473

1

G → R in LINCL. Ref.17 Ref.18

VAR_016799

Natural variant

475

1

S → L in LINCL. Ref.15

VAR_009612

Natural variant

481

1

F → C in LINCL. Ref.21

VAR_016800

Experimental info

Mutagenesis

236

1

H → A: No effect.

Mutagenesis

360

1

D → A: Inactive. Impaired processing.

Mutagenesis

475

1

S → A: Inactive. Impaired processing.

Mutagenesis

517

1

D → A: Inactive. Impaired processing.

Sequence conflict

115

1

I → N in BAD96219. Ref.6

Sequence conflict

373

1

Q → E in AAH14863. Ref.7

Secondary structure

1

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563

Helix Strand Turn

Details...

Helix

202 – 204

3

Helix

206 – 208

3

Turn

209 – 212

4

Helix

234 – 246

13

Helix

271 – 279

9

Helix

282 – 284

3

Beta strand

298 – 300

3

Helix

304 – 310

7

Turn

311 – 314

4

Turn

329 – 335

7

Helix

337 – 348

12

Turn

349 – 351

3

Beta strand

360 – 366

7

Turn

367 – 369

3

Beta strand

370 – 374

5

Turn

379 – 381

3

Beta strand

386 – 390

5

Beta strand

411 – 416

6

Beta strand

425 – 427

3

Beta strand

445 – 449

5

Beta strand

452 – 454

3

Beta strand

458 – 463

6

Beta strand

466 – 470

5

Helix

474 – 476

3

Helix

478 – 484

7

Helix

485 – 487

3

Beta strand

492 – 494

3

Helix

504 – 507

4

Turn

511 – 513

3

Beta strand

514 – 516

3

Beta strand

525 – 528

4

Turn

531 – 533

3

Beta strand

540 – 543

4

Turn

544 – 546

3

Helix

553 – 558

6

Turn

559 – 561

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 30, 2006. Version 2. Checksum: 7299D902F6AE8555	FASTA	563	61,248
	10 20 30 40 50 60 MGLQACLLGL FALILSGKCS YSPEPDQRRT LPPGWVSLGR ADPEEELSLT FALRQQNVER 70 80 90 100 110 120 LSELVQAVSD PSSPQYGKYL TLENVADLVR PSPLTLHTVQ KWLLAAGAQK CHSVITQDFL 130 140 150 160 170 180 TCWLSIRQAE LLLPGAEFHH YVGGPTETHV VRSPHPYQLP QALAPHVDFV GGLHRFPPTS 190 200 210 220 230 240 SLRQRPEPQV TGTVGLHLGV TPSVIRKRYN LTSQDVGSGT SNNSQACAQF LEQYFHDSDL 250 260 270 280 290 300 AQFMRLFGGN FAHQASVARV VGQQGRGRAG IEASLDVQYL MSAGANISTW VYSSPGRHEG 310 320 330 340 350 360 QEPFLQWLML LSNESALPHV HTVSYGDDED SLSSAYIQRV NTELMKAAAR GLTLLFASGD 370 380 390 400 410 420 SGAGCWSVSG RHQFRPTFPA SSPYVTTVGG TSFQEPFLIT NEIVDYISGG GFSNVFPRPS 430 440 450 460 470 480 YQEEAVTKFL SSSPHLPPSS YFNASGRAYP DVAALSDGYW VVSNRVPIPW VSGTSASTPV 490 500 510 520 530 540 FGGILSLINE HRILSGRPPL GFLNPRLYQQ HGAGLFDVTR GCHESCLDEE VEGQGFCSGP 550 560 GWDPVTGWGT PNFPALLKTL LNP
	Isoform 2. Checksum: 707AE6D4A90B0FBC	FASTA	320	34,464
	10 20 30 40 50 60 MRLFGGNFAH QASVARVVGQ QGRGRAGIEA SLDVQYLMSA GANISTWVYS SPGRHEGQEP 70 80 90 100 110 120 FLQWLMLLSN ESALPHVHTV SYGDDEDSLS SAYIQRVNTE LMKAAARGLT LLFASGDSGA 130 140 150 160 170 180 GCWSVSGRHQ FRPTFPASSP YVTTVGGTSF QEPFLITNEI VDYISGGGFS NVFPRPSYQE 190 200 210 220 230 240 EAVTKFLSSS PHLPPSSYFN ASGRAYPDVA ALSDGYWVVS NRVPIPWVSG TSASTPVFGG 250 260 270 280 290 300 ILSLINEHRI LSGRPPLGFL NPRLYQQHGA GLFDVTRGCH ESCLDEEVEG QGFCSGPGWD 310 320 PVTGWGTPNF PALLKTLLNP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Association of mutations in a lysosomal protein with classical late-infantile neuronal ceroid lipofuscinosis." Sleat D.E., Donnelly R.J., Lackland H., Liu C.-G., Sohar I., Pullarkat R.K., Lobel P. Science 277:1802-1805(1997) [PubMed: 9295267] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANTS LINCL ARG-365 AND TYR-365, VARIANT HIS-175. Tissue: Placenta.
[2]	"Structural organization and sequence of CLN2, the defective gene in classical late infantile neuronal ceroid lipofuscinosis." Liu C.-G., Sleat D.E., Donnelly R.J., Lobel P. Genomics 50:206-212(1998) [PubMed: 9653647] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Placenta.
[3]	"Bovine brain homolog of the tripeptidyl peptidase I which is deficient in the human classic late-infantile neuronal ceroid lipofuscinosis." Junaid M.A., Barua M., Pullarkat R.K. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain cortex.
[4]	"Identification of a human growth inhibition gene 1 (GIG1)." Kim J.W. Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[5]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Adipose tissue.
[7]	"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] (ISOFORM 1). Tissue: Lymph.
[8]	"The human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH." Lin L., Sohar I., Lackland H., Lobel P. J. Biol. Chem. 276:2249-2255(2001) [PubMed: 11054422] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-24; 196-200 AND 466-492, MUTAGENESIS, CHARACTERIZATION.
[9]	"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins." Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., Appella E. J. Proteome Res. 2:69-79(2003) [PubMed: 12643545] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[10]	"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry." Zhang H., Li X.-J., Martin D.B., Aebersold R. Nat. Biotechnol. 21:660-666(2003) [PubMed: 12754519] [Abstract] Cited for: GLYCOSYLATION AT ASN-443.
[11]	"Molecular basis of the neuronal ceroid lipofuscinoses: mutations in CLN1, CLN2, CLN3, and CLN5." Mole S.E., Mitchison H.M., Munroe P.B. Hum. Mutat. 14:199-215(1999) [PubMed: 10477428] [Abstract] Cited for: REVIEW ON VARIANTS.
[12]	"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes." Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F. J. Proteome Res. 5:3135-3144(2006) [PubMed: 17081065] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[13]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-210; ASN-222; ASN-313 AND ASN-443, MASS SPECTROMETRY. Tissue: Liver.
[15]	"Mutational analysis of the defective protease in classic late-infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder." Sleat D.E., Gin R.M., Sohar I., Wisniewski K., Sklower-Brooks S., Pullarkat R.K., Palmer D.N., Lerner T.J., Boustany R.-M.N., Uldall P., Siakotos A.N., Donnelly R.J., Lobel P. Am. J. Hum. Genet. 64:1511-1523(1999) [PubMed: 10330339] [Abstract] Cited for: VARIANTS LINCL ARG-77; ASN-287; LYS-343; ARG-365; TYR-365; ASP-385; GLU-389; HIS-422; HIS-447; GLU-454 AND LEU-475, VARIANT ARG-100.
[16]	"Prenatal testing for late infantile neuronal ceroid lipofuscinosis." Berry-Kravis E., Sleat D.E., Sohar I., Meyer P., Donnelly R., Lobel P. Ann. Neurol. 47:254-257(2000) [PubMed: 10665500] [Abstract] Cited for: VARIANT LINCL CYS-206.
[17]	"Heterogeneity of late-infantile neuronal ceroid lipofuscinosis." Zhong N., Moroziewicz D.N., Ju W., Jurkiewicz A., Johnston L., Wisniewski K.E., Brown W.T. Genet. Med. 2:312-318(2000) [PubMed: 11339651] [Abstract] Cited for: VARIANTS LINCL GLN-127; VAL-284; ASN-428 AND ARG-473.
[18]	"Two novel CLN2 gene mutations in a Chinese patient with classical late-infantile neuronal ceroid lipofuscinosis." Lam C.W., Poon P.M., Tong S.F., Ko C.H. Am. J. Med. Genet. 99:161-163(2001) [PubMed: 11241479] [Abstract] Cited for: VARIANT LINCL ARG-473.
[19]	"Expression and analysis of CLN2 variants in CHO cells: Q100R represents a polymorphism, and G389E and R447H represent loss-of-function mutations." Lin L., Lobel P. Hum. Mutat. 18:165-165(2001) [PubMed: 11462245] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS ARG-100; GLU-389 AND HIS-447.
[20]	"Late infantile neuronal ceroid lipofuscinosis: quantitative description of the clinical course in patients with CLN2 mutations." Steinfeld R., Heim P., von Gregory H., Meyer K., Ullrich K., Goebel H.H., Kohlschutter A. Am. J. Med. Genet. 112:347-354(2002) [PubMed: 12376936] [Abstract] Cited for: VARIANTS LINCL GLN-127; SER-286 AND PRO-353.
[21]	"Identification of novel CLN2 mutations shows Canadian specific NCL2 alleles." Ju W., Zhong R., Moore S., Moroziewicz D., Currie J.R., Parfrey P., Brown W.T., Zhong N. J. Med. Genet. 39:822-825(2002) [PubMed: 12414822] [Abstract] Cited for: VARIANTS LINCL MET-277; PRO-278; VAL-284 AND CYS-481.
[22]	"Tripeptidyl peptidase 1 deficiency in neuronal ceroid lipofuscinosis. A novel mutation." Bukina A.M., Tsvetkova I.V., Semiachkina A.N., Il'ina E.S. Vopr. Med. Khim. 48:594-598(2002) [PubMed: 12698559] [Abstract] Cited for: VARIANT LINCL HIS-206.
+	Additional computationally mapped references.

Web resources

NCL CLN2

Neural Ceroid Lipofuscinoses mutation db

GeneReviews

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF017456 mRNA. Translation: AAB80725.1.
AF039704 Genomic DNA. Translation: AAC98480.1.
AF491290 mRNA. Translation: AAM08412.1.
AY268890 mRNA. Translation: AAQ72732.1.
AY358502 mRNA. Translation: AAQ88866.1. Frameshift.
AK222499 mRNA. Translation: BAD96219.1.
BC014863 mRNA. Translation: AAH14863.1.

IPI

IPI00298237.
IPI00554617.

RefSeq

NP_000382.3.

UniGene

Hs.523454

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1R60	model	-	A	196-563	[»]
3EDY	X-ray	1.85	A	20-563	[»]
3EE6	X-ray	2.35	A/B	1-563	[»]

ModBase

Search...

Protein family/group databases

MEROPS

S53.003.

PTM databases

PhosphoSite

O14773.

Proteomic databases

PRIDE

O14773.

Genome annotation databases

Ensembl

ENSG00000166340. Homo sapiens. [Contig view]

GeneID

1200.

KEGG

hsa:1200.

Organism-specific databases

GeneCards

GC11M006591.

H-InvDB

HIX0009410.

HGNC

HGNC:2073. TPP1.

MIM

204500. phenotype.
607998. gene.

Orphanet

216. Ceroid lipofuscinosis, neuronal.
168491. Late infantile neuronal ceroid lipofuscinosis.

PharmGKB

PA26600.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

O14773.

HOVERGEN

O14773.

OMA

O14773. SVIRKRY.

Enzyme and pathway databases

BRENDA

3.4.14.9. 247.

Gene expression databases

ArrayExpress

O14773.

Bgee

O14773.

CleanEx

HS_TPP1.

GermOnline

ENSG00000166340. Homo sapiens.

Family and domain databases

InterPro

IPR000209. Pept_S8_S53.
IPR015366. Peptidase_S53_propep.
[Graphical view]

Gene3D

G3DSA:3.40.50.200. Pept_S8_S53. 1 hit.

Pfam

PF09286. Pro-kuma_activ. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

4955.

PMAP-CutDB

O14773.

SOURCE

Search...

Entry information

Entry name

TPP1_HUMAN

Accession

Primary (citable) accession number: O14773
Secondary accession number(s): Q53HT1 , Q5JAK6, Q6UX56, Q71JP6, Q96C37

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	May 30, 2006
Last modified:	June 16, 2009
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)