Reviewed, UniProtKB/Swiss-Prot Q15256 (PTPRR_HUMAN)

Names and origin

Protein names

Recommended name:
    Receptor-type tyrosine-protein phosphatase R
    EC=3.1.3.48
Alternative name(s):
    Protein-tyrosine phosphatase PCPTP1
    NC-PTPCOM1
    Ch-1PTPase

Gene names

Name:	PTPRR
Synonyms:	ECPTP, PTPRQ

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	657 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	Sequesters mitogen-activated protein kinases (MAPKs) such as MAPK1, MAPK3 and MAPK14 in the cytoplasm in an inactive form. The MAPKs bind to a dephosphorylated kinase interacting motif, phosphorylation of which by the protein kinase A complex releases the MAPKs for activation and translocation into the nucleus By similarity.
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Subunit structure	Interacts with MAPKs By similarity.
Subcellular location	Isoform Alpha: Cell membrane; Single-pass type I membrane protein. Isoform Delta: Cytoplasm › perinuclear region. Note: Locates to the perinuclear areas within the cytoplasm. Isoform Gamma: Cytoplasm › perinuclear region. Note: Locates to the perinuclear areas within the cytoplasm.
Tissue specificity	Expressed in brain, placenta, small intestine, stomach, uterus and weakly in the prostate. Isoform alpha has been observed only in the brain, isoform gamma in the brain, placenta and uterus and isoform delta in the brain, kidney, placenta, prostate, small intestine and uterus. Ref.2
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Receptor class 7 subfamily. Contains 1 tyrosine-protein phosphatase domain.
Sequence caution	The sequence CAA57957.1 differs from that shown. Reason: Frameshift at position 651. The sequence CAB01957.1 differs from that shown. Reason: Frameshift at position 651.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal Transmembrane
Molecular function	Hydrolase Protein phosphatase Receptor
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	in utero embryonic development Inferred from expression pattern. Source: UniProtKB protein amino acid dephosphorylation Traceable author statement. Source: ProtInc
Cellular component	cell surface Inferred from direct assay. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	protein kinase binding Inferred from sequence or structural similarity. Source: UniProtKB transmembrane receptor protein tyrosine phosphatase activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDH2	P19022	1	EBI-2265659,EBI-2256711
PDGFRB	P09619	1	EBI-2265659,EBI-641237

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform Alpha (identifier: Q15256-1)

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 Gamma (identifier: Q15256-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-245: Missing.

Note: Locates to the perinuclear areas within the cytoplasm.

Isoform Delta (identifier: Q15256-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-206: Missing.
     207-209: SPE → MNQ

Note: Locates to the perinuclear areas within the cytoplasm.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Potential

Chain

22 – 657

636

Receptor-type tyrosine-protein phosphatase R

PRO_0000025459

Regions

Topological domain

22 – 227

206

Extracellular Potential

Transmembrane

228 – 248

21

Potential

Topological domain

249 – 657

409

Cytoplasmic Potential

Domain

393 – 647

255

Tyrosine-protein phosphatase

Sites

Active site

588

1

Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue

339

1

Phosphoserine; by PKA By similarity

Modified residue

370

1

Phosphotyrosine Ref.8

Glycosylation

129

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

1 – 245

245

Missing in isoform Gamma.

VSP_005156

Alternative sequence

1 – 206

206

Missing in isoform Delta.

VSP_005155

Alternative sequence

207 – 209

3

SPE → MNQ in isoform Delta.

VSP_005158

Natural variant

249

1

Y → H: dbSNP rs35987017.

VAR_057140

Natural variant

314

1

K → R: dbSNP rs3803036. Ref.2 Ref.1 Ref.3 Ref.4 Ref.5 Ref.7

VAR_014283

Natural variant

386

1

V → I: dbSNP rs35387004.

VAR_057141

Natural variant

439

1

V → I: dbSNP rs35390084.

VAR_057142

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

657

Helix Strand Turn

Details...

Helix

380 – 386

7

Helix

390 – 398

9

Helix

407 – 409

3

Helix

415 – 418

4

Helix

428 – 430

3

Beta strand

431 – 433

3

Helix

442 – 445

4

Beta strand

446 – 452

7

Helix

455 – 457

3

Beta strand

461 – 465

5

Helix

470 – 472

3

Helix

473 – 483

11

Beta strand

487 – 492

6

Beta strand

494 – 499

6

Beta strand

507 – 512

6

Beta strand

515 – 524

10

Beta strand

529 – 537

9

Beta strand

540 – 549

10

Beta strand

554 – 556

3

Helix

562 – 576

15

Beta strand

584 – 587

4

Beta strand

589 – 592

4

Helix

593 – 611

19

Beta strand

612 – 614

3

Helix

616 – 626

11

Helix

634 – 648

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha [UniParc]. Last modified March 6, 2007. Version 2. Checksum: 42CD98F37AC5B638	FASTA	657	73,834
	10 20 30 40 50 60 MRRAVCFPAL CLLLNLHAAG CFSGNNDHFL AINQKKSGKP VFIYKHSQDI EKSLDIAPQK 70 80 90 100 110 120 IYRHSYHSSS EAQVSKRHQI VNSAFPRPAY DPSLNLLAMD GQDLEVENLP IPAANVIVVT 130 140 150 160 170 180 LQMDVNKLNI TLLRIFRQGV AAALGLLPQQ VHINRLIGKK NSIELFVSPI NRKTGISDAL 190 200 210 220 230 240 PSEEVLRSLN INVLHQSLSQ FGITEVSPEK NVLQGQHEAD KIWSKEGFYA VVIFLSIFVI 250 260 270 280 290 300 IVTCLMILYR LKERFQLSLR QDKEKNQEIH LSPITLQPAL SEAKTVHSMV QPEQAPKVLN 310 320 330 340 350 360 VVVDPQGRGA PEIKATTATS VCPSPFKMKP IGLQERRGSN VSLTLDMSSL GNIEPFVSIP 370 380 390 400 410 420 TPREKVAMEY LQSASRILTR SQLRDVVASS HLLQSEFMEI PMNFVDPKEI DIPRHGTKNR 430 440 450 460 470 480 YKTILPNPLS RVCLRPKNVT DSLSTYINAN YIRGYSGKEK AFIATQGPMI NTVDDFWQMV 490 500 510 520 530 540 WQEDSPVIVM ITKLKEKNEK CVLYWPEKRG IYGKVEVLVI SVNECDNYTI RNLVLKQGSH 550 560 570 580 590 600 TQHVKHYWYT SWPDHKTPDS AQPLLQLMLD VEEDRLASQG RGPVVVHCSA GIGRTGCFIA 610 620 630 640 650 TSIGCQQLKE EGVVDALSIV CQLRMDRGGM VQTSEQYEFV HHALCLYESR LSAETVQ
	Isoform Gamma. Checksum: 92D2900B943CBDBB	FASTA	412	46,581
	10 20 30 40 50 60 MILYRLKERF QLSLRQDKEK NQEIHLSPIT LQPALSEAKT VHSMVQPEQA PKVLNVVVDP 70 80 90 100 110 120 QGRGAPEIKA TTATSVCPSP FKMKPIGLQE RRGSNVSLTL DMSSLGNIEP FVSIPTPREK 130 140 150 160 170 180 VAMEYLQSAS RILTRSQLRD VVASSHLLQS EFMEIPMNFV DPKEIDIPRH GTKNRYKTIL 190 200 210 220 230 240 PNPLSRVCLR PKNVTDSLST YINANYIRGY SGKEKAFIAT QGPMINTVDD FWQMVWQEDS 250 260 270 280 290 300 PVIVMITKLK EKNEKCVLYW PEKRGIYGKV EVLVISVNEC DNYTIRNLVL KQGSHTQHVK 310 320 330 340 350 360 HYWYTSWPDH KTPDSAQPLL QLMLDVEEDR LASQGRGPVV VHCSAGIGRT GCFIATSIGC 370 380 390 400 410 QQLKEEGVVD ALSIVCQLRM DRGGMVQTSE QYEFVHHALC LYESRLSAET VQ
	Isoform Delta. Checksum: 7AC02DFE48E42761	FASTA	451	51,046
	10 20 30 40 50 60 MNQKNVLQGQ HEADKIWSKE GFYAVVIFLS IFVIIVTCLM ILYRLKERFQ LSLRQDKEKN 70 80 90 100 110 120 QEIHLSPITL QPALSEAKTV HSMVQPEQAP KVLNVVVDPQ GRGAPEIKAT TATSVCPSPF 130 140 150 160 170 180 KMKPIGLQER RGSNVSLTLD MSSLGNIEPF VSIPTPREKV AMEYLQSASR ILTRSQLRDV 190 200 210 220 230 240 VASSHLLQSE FMEIPMNFVD PKEIDIPRHG TKNRYKTILP NPLSRVCLRP KNVTDSLSTY 250 260 270 280 290 300 INANYIRGYS GKEKAFIATQ GPMINTVDDF WQMVWQEDSP VIVMITKLKE KNEKCVLYWP 310 320 330 340 350 360 EKRGIYGKVE VLVISVNECD NYTIRNLVLK QGSHTQHVKH YWYTSWPDHK TPDSAQPLLQ 370 380 390 400 410 420 LMLDVEEDRL ASQGRGPVVV HCSAGIGRTG CFIATSIGCQ QLKEEGVVDA LSIVCQLRMD 430 440 450 RGGMVQTSEQ YEFVHHALCL YESRLSAETV Q

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of PCPTP1 encoding protein tyrosine phosphatase." Shiozuka K., Watanabe Y., Ikeda T., Hashimoto S., Kawashima H. Gene 162:279-284(1995) [PubMed: 7557444] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), VARIANT ARG-314. Tissue: Brain.
[2]	"Protein tyrosine phosphatase (PC12, Br7,Sl) family: expression characterization in the adult human and mouse." Augustine K.A., Silbiger S.M., Bucay N., Ulias L., Boynton A., Trebasky L.D., Medlock E.S. Anat. Rec. 258:221-234(2000) [PubMed: 10705342] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; GAMMA AND DELTA), TISSUE SPECIFICITY, VARIANT ARG-314. Tissue: Brain and Colon.
[3]	"Type 2 diabetes locus on 12q15: further mapping and mutation screening of two candidate genes." Bektas A., Hughes J.N., Warram J.H., Krolewski A.S., Doria A. Diabetes 50:204-208(2001) [PubMed: 11147789] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-314.
[4]	"Cloning and characterization of novel PTP (NC-PTPCOM) from neuronal cells." Knyazev P., Cheburkin Y., Knyazev Y., Ullrich A. Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), VARIANT ARG-314. Tissue: Neuroblastoma.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), VARIANT ARG-314. Tissue: Amygdala.
[6]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed: 16541075] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"Molecular cloning and characterization of human epithelial cells specific protein tyrosine phosphatase (EC-PTP)." Knyazev P.G., Ullrich A. Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 289-657 (ISOFORM ALPHA), VARIANT ARG-314. Tissue: Mammary gland.
[8]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-370, MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBLGenBankDDBJ

D64053 mRNA. Translation: BAA10930.1.
U42361 mRNA. Translation: AAD09447.1.
U77917 mRNA. Translation: AAB54007.1.
U77916 mRNA. Translation: AAB54006.1.
AF263029 , AF263016, AF263017, AF263018, AF263019, AF263020, AF263021, AF263022, AF263023, AF263024, AF263025, AF263026, AF263027, AF263028 Genomic DNA. Translation: AAG47642.1.
Z79693 mRNA. Translation: CAB01957.1. Frameshift.
AK312376 mRNA. Translation: BAG35294.1.
AC083809 Genomic DNA. No translation available.
AC084877 Genomic DNA. No translation available.
AC090676 Genomic DNA. No translation available.
AC140066 Genomic DNA. No translation available.
X82635 mRNA. Translation: CAA57957.1. Frameshift.

IPI

IPI00033560.
IPI00107759.
IPI00217021.

RefSeq

NP_002840.1.
NP_570897.1.

UniGene

Hs.506076

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2A8B	X-ray	2.30	A	375-655	[»]

SMR

Q15256. Positions 361-656.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15256. 2 interactions.

PTM databases

PhosphoSite

Q15256.

Genome annotation databases

Ensembl

ENSG00000153233. Homo sapiens. [Contig view]

GeneID

5801.

KEGG

hsa:5801.

Organism-specific databases

GeneCards

GC12M069318.

H-InvDB

HIX0010818.

HGNC

HGNC:9680. PTPRR.

HPA

CAB011461.
HPA011851.

MIM

602853. gene.

PharmGKB

PA34025.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q15256.

Enzyme and pathway databases

BRENDA

3.1.3.48. 247.

Gene expression databases

ArrayExpress

Q15256.

Bgee

Q15256.

CleanEx

HS_PTPRQ.
HS_PTPRR.

GermOnline

ENSG00000153233. Homo sapiens.

Family and domain databases

InterPro

IPR000387. Tyr_Pase.
IPR016130. Tyr_Pase_AS.
IPR008356. Tyr_Pase_KIM-con.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
IPR016334. Tyr_Pase_rcpt_R/non-rcpt_5.
[Graphical view]

Pfam

PF00102. Y_phosphatase. 1 hit.
[Graphical view]

PIRSF

PIRSF001997. PTPRR. 1 hit.

PRINTS

PR01778. KIMPTPASE.
PR00700. PRTYPHPHTASE.

SMART

SM00194. PTPc. 1 hit.
[Graphical view]

PROSITE

PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

22606.

SOURCE

Search...

Entry information

Entry name

PTPRR_HUMAN

Accession

Primary (citable) accession number: Q15256
Secondary accession number(s): B2R5Z7 , O00342, Q92682, Q9UE65

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	March 6, 2007
Last modified:	June 16, 2009
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)