P20700 (LMNB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lamin-B1

Gene names

Name:	LMNB1
Synonyms:	LMN2, LMNB

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	586 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	Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin.
Subunit structure	Interacts with lamin-associated polypeptides IA, IB and 2.
Subcellular location	Nucleus inner membrane; Lipid-anchor; Nucleoplasmic side.
Post-translational modification	B-type lamins undergo a series of modifications, such as farnesylation and phosphorylation. Increased phosphorylation of the lamins occurs before envelope disintegration and probably plays a role in regulating lamin associations.
Involvement in disease	Defects in LMNB1 are the cause of leukodystrophy demyelinating autosomal dominant adult-onset (ADLD) [MIM:169500]. ADLD is a slowly progressive and fatal demyelinating leukodystrophy, presenting in the fourth or fifth decade of life. Clinically characterized by early autonomic abnormalities, pyramidal and cerebellar dysfunction, and symmetric demyelination of the CNS. It differs from multiple sclerosis and other demyelinating disorders in that neuropathology shows preservation of oligodendroglia in the presence of subtotal demyelination and lack of astrogliosis. Ref.12
Miscellaneous	The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively.
Sequence similarities	Belongs to the intermediate filament family.

Ontologies

Keywords
Cellular component	Intermediate filament Membrane Nucleus
Coding sequence diversity	Chromosomal rearrangement Polymorphism
Disease	Leukodystrophy
Domain	Coiled coil
PTM	Acetylation Lipoprotein Methylation Phosphoprotein Prenylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cellular component disassembly involved in apoptosis Traceable author statement. Source: Reactome
Cellular component	lamin filament Traceable author statement Ref.2. Source: ProtInc nuclear inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	structural molecule activity Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 583

582

Lamin-B1

PRO_0000063816

Propeptide

584 – 586

3

Removed in mature form Probable

PRO_0000393945

Regions

Region

2 – 34

33

Head

Region

35 – 386

352

Rod

Region

35 – 69

35

Coil 1A

Region

70 – 81

12

Linker 1

Region

82 – 215

134

Coil 1B

Region

216 – 243

28

Linker 2

Region

244 – 386

143

Coil 2

Region

387 – 586

200

Tail

Motif

415 – 420

6

Nuclear localization signal Potential

Compositional bias

552 – 559

8

Glu-rich (highly acidic; could be involved in chromatin binding)

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.6 Ref.20

Modified residue

5

1

Phosphothreonine Ref.20

Modified residue

13

1

Phosphoserine Ref.16

Modified residue

19

1

Phosphothreonine Ref.10

Modified residue

20

1

Phosphothreonine Ref.11 Ref.13 Ref.18 Ref.19 Ref.20 Ref.21

Modified residue

23

1

Phosphoserine Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21

Modified residue

28

1

Phosphoserine Ref.10

Modified residue

157

1

N6-acetyllysine Ref.22

Modified residue

200

1

Phosphoserine Ref.10

Modified residue

271

1

N6-acetyllysine Ref.22

Modified residue

278

1

Phosphoserine Ref.15

Modified residue

279

1

Phosphoserine Ref.15

Modified residue

284

1

Phosphoserine Ref.15

Modified residue

375

1

Phosphoserine Ref.21

Modified residue

391

1

Phosphoserine Ref.9 Ref.13 Ref.15

Modified residue

393

1

Phosphoserine Ref.9

Modified residue

404

1

Phosphoserine Ref.10

Modified residue

483

1

N6-acetyllysine Ref.22

Modified residue

575

1

Phosphothreonine Ref.10 Ref.19 Ref.21

Modified residue

579

1

Phosphoserine Ref.15

Modified residue

583

1

Cysteine methyl ester Probable

Lipidation

583

1

S-farnesyl cysteine Ref.8

Natural variations

Natural variant

501

1

A → V.
Corresponds to variant rs36105360 [ dbSNP | Ensembl ].

VAR_031646

Experimental info

Sequence conflict

382

1

E → Q in AAH12295. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

586

Helix Strand Turn

Details...

Beta strand

432 – 438

7

Beta strand

442 – 447

6

Beta strand

453 – 458

6

Beta strand

460 – 462

3

Beta strand

470 – 474

5

Beta strand

479 – 483

5

Beta strand

495 – 500

6

Turn

509 – 511

3

Beta strand

512 – 515

4

Beta strand

527 – 532

6

Beta strand

538 – 546

9

Sequences

	Sequence		Length	Mass (Da)
	P20700 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 73292877745722C4	FASTA	586	66,408
	10 20 30 40 50 60 MATATPVPPR MGSRAGGPTT PLSPTRLSRL QEKEELRELN DRLAVYIDKV RSLETENSAL 70 80 90 100 110 120 QLQVTEREEV RGRELTGLKA LYETELADAR RALDDTARER AKLQIELGKC KAEHDQLLLN 130 140 150 160 170 180 YAKKESDLNG AQIKLREYEA ALNSKDAALA TALGDKKSLE GDLEDLKDQI AQLEASLAAA 190 200 210 220 230 240 KKQLADETLL KVDLENRCQS LTEDLEFRKS MYEEEINETR RKHETRLVEV DSGRQIEYEY 250 260 270 280 290 300 KLAQALHEMR EQHDAQVRLY KEELEQTYHA KLENARLSSE MNTSTVNSAR EELMESRMRI 310 320 330 340 350 360 ESLSSQLSNL QKESRACLER IQELEDLLAK EKDNSRRMLT DKEREMAEIR DQMQQQLNDY 370 380 390 400 410 420 EQLLDVKLAL DMEISAYRKL LEGEEERLKL SPSPSSRVTV SRASSSRSVR TTRGKRKRVD 430 440 450 460 470 480 VEESEASSSV SISHSASATG NVCIEEIDVD GKFIRLKNTS EQDQPMGGWE MIRKIGDTSV 490 500 510 520 530 540 SYKYTSRYVL KAGQTVTIWA ANAGVTASPP TDLIWKNQNS WGTGEDVKVI LKNSQGEEVA 550 560 570 580 QRSTVFKTTI PEEEEEEEEA AGVVVEEELF HQQGTPRASN RSCAIM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"In vitro posttranslational modification of lamin B cloned from a human T-cell line." Pollard K.M., Chan E.K.L., Grant B.J., Sullivan K.F., Tan E.M., Glass C.A. Mol. Cell. Biol. 10:2164-2175(1990) [PubMed: 2325650] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structural organization of the human gene (LMNB1) encoding nuclear lamin B1." Lin F., Worman H.J. Genomics 27:230-236(1995) [PubMed: 7557986] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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]. Tissue: Brain.
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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]. Tissue: Eye and Placenta.
[6]	Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-10; 15-26; 43-49; 80-90; 103-109; 112-123; 125-191; 198-220; 235-250; 259-271; 277-290; 300-312; 321-330; 351-387; 475-483 AND 517-528, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Ovarian carcinoma.
[7]	Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 52-67; 80-90; 112-123; 146-156; 198-208; 210-220; 300-312; 321-330; 351-378 AND 458-473, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[8]	"Human lamin B contains a farnesylated cysteine residue." Farnsworth C.C., Wolda S.L., Gelb M.H., Glomset J.A. J. Biol. Chem. 264:20422-20429(1989) [PubMed: 2684976] [Abstract] Cited for: ISOPRENYLATION AT CYS-583.
[9]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391 AND SER-393, MASS SPECTROMETRY. Tissue: Colon adenocarcinoma.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-23; SER-28; SER-200; SER-404 AND THR-575, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20 AND SER-23, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Lamin B1 duplications cause autosomal dominant leukodystrophy." Padiath Q.S., Saigoh K., Schiffmann R., Asahara H., Yamada T., Koeppen A., Hogan K., Ptacek L.J., Fu Y.-H. Nat. Genet. 38:1114-1123(2006) [PubMed: 16951681] [Abstract] Cited for: INVOLVEMENT IN ADLD.
[13]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-23 AND SER-391, MASS SPECTROMETRY. Tissue: Cervix adenocarcinoma.
[14]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-278; SER-279; SER-284; SER-391 AND SER-579, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20 AND SER-23, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-23 AND THR-575, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5; THR-20 AND SER-23, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[21]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-23; SER-375 AND THR-575, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[22]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-157; LYS-271 AND LYS-483, MASS SPECTROMETRY.
[23]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M34458 mRNA. Translation: AAA36162.1.
L37747 , L37737, L37738, L37739, L37740, L37741, L37742, L37743, L37744, L37745, L37746 Genomic DNA. Translation: AAC37575.1.
AK312603 mRNA. Translation: BAG35493.1.
CH471086 Genomic DNA. Translation: EAW48846.1.
BC012295 mRNA. Translation: AAH12295.1.
BC103723 mRNA. Translation: AAI03724.1.

IPI

IPI00217975.

PIR

VEHULB. A34707.

RefSeq

NP_005564.1. NM_005573.3.

UniGene

Hs.89497.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KPW	NMR	-	A	439-549	[»]
3JT0	X-ray	2.39	A/B	426-558	[»]
3TYY	X-ray	2.40	A/B	311-388	[»]
3UMN	X-ray	2.00	A/B/C	428-550	[»]

ProteinModelPortal

P20700.

SMR

P20700. Positions 31-67, 242-309, 311-385, 431-548.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-34897N.

IntAct

P20700. 17 interactions.

MINT

MINT-3009331.

STRING

P20700.

PTM databases

PhosphoSite

P20700.

Polymorphism databases

DMDM

125953.

2D gel databases

Aarhus/Ghent-2DPAGE

7510. IEF.

SWISS-2DPAGE

P20700.

Proteomic databases

PeptideAtlas

P20700.

PRIDE

P20700.

Protocols and materials databases

DNASU

4001.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000261366; ENSP00000261366; ENSG00000113368.

GeneID

4001.

KEGG

hsa:4001.

UCSC

uc003kud.2. human.

Organism-specific databases

CTD

4001.

GeneCards

GC05P126112.

H-InvDB

HIX0005134.

HGNC

HGNC:6637. LMNB1.

HPA

CAB005269.

MIM

150340. gene.
169500. phenotype.

neXtProt

NX_P20700.

Orphanet

99027. Adult-onset autosomal dominant leukodystrophy.

PharmGKB

PA30403.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG325506.

GeneTree

ENSGT00560000076873.

HOGENOM

HOG000007711.

HOVERGEN

HBG013015.

InParanoid

P20700.

KO

K07611.

OMA

HQQGTPR.

OrthoDB

EOG45MN55.

PhylomeDB

P20700.

Enzyme and pathway databases

Pathway_Interaction_DB

caspase_pathway. Caspase cascade in apoptosis.

Reactome

REACT_111183. Meiosis.
REACT_115566. Cell Cycle.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

P20700.

Bgee

P20700.

CleanEx

HS_LMNB1.

Genevestigator

P20700.

GermOnline

ENSG00000113368. Homo sapiens.

Family and domain databases

InterPro

IPR016044. F.
IPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR001322. Lamin_tail_dom.
[Graphical view]

PANTHER

PTHR23239. IF. 1 hit.

Pfam

PF00038. Filament. 1 hit.
PF00932. LTD. 1 hit.
[Graphical view]

PROSITE

PS00226. IF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P20700.

NextBio

15700.

PMAP-CutDB

P20700.

SOURCE

Search...

Entry information

Entry name

LMNB1_HUMAN

Accession

Primary (citable) accession number: P20700
Secondary accession number(s): B2R6J6, Q3SYN7, Q96EI6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	January 23, 2007
Last modified:	May 16, 2012
This is version 131 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.