P36952 (SPB5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serpin B5

Alternative name(s):
Maspin
Peptidase inhibitor 5
Short name=PI-5

Gene names

Name:	SERPINB5
Synonyms:	PI5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	375 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Tumor suppressor. It blocks the growth, invasion, and metastatic properties of mammary tumors. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity.
Subunit structure	Interacts with IRF6. Ref.7
Subcellular location	Secreted › extracellular space.
Tissue specificity	Normal mammary epithelial cells.
Sequence similarities	Belongs to the serpin family. Ov-serpin subfamily.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular component movement Traceable author statement Ref.1. Source: ProtInc extracellular matrix organization Inferred from electronic annotation. Source: Compara morphogenesis of an epithelium Inferred from electronic annotation. Source: Compara prostate gland morphogenesis Inferred from electronic annotation. Source: Compara regulation of epithelial cell proliferation Inferred from electronic annotation. Source: Compara regulation of proteolysis Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	cytoplasm Inferred from direct assay Ref.7. Source: UniProtKB extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	serine-type endopeptidase inhibitor activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: P36952-1)

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: P36952-2)

The sequence of this isoform differs from the canonical sequence as follows:
     190-231: TDTKPVQMMN...QNKHLSMFIL → VCGAACSSKR...LRARPAKCLS
     232-375: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 375

375

Serpin B5

PRO_0000032486

Sites

Site

340 – 341

2

Reactive bond homolog By similarity

Amino acid modifications

Glycosylation

99

1

N-linked (GlcNAc...) Potential

Glycosylation

133

1

N-linked (GlcNAc...) Potential

Glycosylation

188

1

N-linked (GlcNAc...) Potential

Glycosylation

361

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

190 – 231

42

TDTKP…SMFIL → VCGAACSSKRSPIIDVKNDR DRVGHKSIPMRNLRARPAKC LS in isoform 2.

VSP_037145

Alternative sequence

232 – 375

144

Missing in isoform 2.

VSP_037146

Natural variant

176

1

S → P. Ref.1 Ref.2 Ref.4 Ref.9
Corresponds to variant rs2289519 [ dbSNP | Ensembl ].

VAR_055223

Natural variant

187

1

V → L. Ref.1
Corresponds to variant rs2289520 [ dbSNP | Ensembl ].

VAR_055224

Natural variant

319

1

I → V. Ref.5
Corresponds to variant rs1455555 [ dbSNP | Ensembl ].

VAR_022115

Experimental info

Sequence conflict

66

1

V → I in AAA18957. Ref.1

Sequence conflict

245

1

K → Q in CAE45703. Ref.5

Secondary structure

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375

Helix Strand Turn

Details...

Helix

2 – 22

21

Beta strand

28 – 30

3

Helix

32 – 45

14

Helix

48 – 57

10

Helix

60 – 62

3

Helix

66 – 80

15

Turn

81 – 83

3

Beta strand

84 – 95

12

Helix

96 – 98

3

Helix

102 – 108

7

Turn

109 – 115

7

Beta strand

116 – 119

4

Turn

121 – 123

3

Helix

125 – 139

15

Turn

140 – 142

3

Turn

147 – 150

4

Beta strand

159 – 168

10

Beta strand

171 – 173

3

Helix

177 – 179

3

Beta strand

181 – 190

10

Beta strand

192 – 209

18

Turn

210 – 213

4

Beta strand

214 – 221

8

Helix

222 – 224

3

Beta strand

225 – 235

11

Helix

239 – 249

11

Helix

252 – 258

7

Helix

261 – 263

3

Beta strand

265 – 274

10

Beta strand

276 – 282

7

Helix

284 – 291

8

Turn

295 – 297

3

Turn

299 – 301

3

Turn

305 – 307

3

Beta strand

315 – 326

12

Turn

337 – 341

5

Beta strand

344 – 349

6

Beta strand

354 – 360

7

Turn

361 – 364

4

Beta strand

365 – 372

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 5, 2009. Version 2. Checksum: 9F24E18505912804	FASTA	375	42,100
	10 20 30 40 50 60 MDALQLANSA FAVDLFKQLC EKEPLGNVLF SPICLSTSLS LAQVGAKGDT ANEIGQVLHF 70 80 90 100 110 120 ENVKDVPFGF QTVTSDVNKL SSFYSLKLIK RLYVDKSLNL STEFISSTKR PYAKELETVD 130 140 150 160 170 180 FKDKLEETKG QINNSIKDLT DGHFENILAD NSVNDQTKIL VVNAAYFVGK WMKKFSESET 190 200 210 220 230 240 KECPFRVNKT DTKPVQMMNM EATFCMGNID SINCKIIELP FQNKHLSMFI LLPKDVEDES 250 260 270 280 290 300 TGLEKIEKQL NSESLSQWTN PSTMANAKVK LSIPKFKVEK MIDPKACLEN LGLKHIFSED 310 320 330 340 350 360 TSDFSGMSET KGVALSNVIH KVCLEITEDG GDSIEVPGAR ILQHKDELNA DHPFIYIIRH 370 NKTRNIIFFG KFCSP
	Isoform 2 [UniParc]. Checksum: 62DF767BBA9B5471	FASTA	231	25,763
	10 20 30 40 50 60 MDALQLANSA FAVDLFKQLC EKEPLGNVLF SPICLSTSLS LAQVGAKGDT ANEIGQVLHF 70 80 90 100 110 120 ENVKDVPFGF QTVTSDVNKL SSFYSLKLIK RLYVDKSLNL STEFISSTKR PYAKELETVD 130 140 150 160 170 180 FKDKLEETKG QINNSIKDLT DGHFENILAD NSVNDQTKIL VVNAAYFVGK WMKKFSESET 190 200 210 220 230 KECPFRVNKV CGAACSSKRS PIIDVKNDRD RVGHKSIPMR NLRARPAKCL S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Maspin, a serpin with tumor-suppressing activity in human mammary epithelial cells." Zou Z., Anisowicz A., Hendrix M.J.C., Thor A., Neveu M., Sheng S., Rafidi K., Seftor E., Sager R. Science 263:526-529(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS PRO-176 AND LEU-187. Tissue: Mammary gland.
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT PRO-176. Tissue: Esophagus.
[3]	"DNA sequence and analysis of human chromosome 18." Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S. Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT PRO-176. Tissue: Prostate.
[5]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 245-375 (ISOFORM 1), VARIANT VAL-319. Tissue: Small intestine.
[6]	"The tumor suppressor maspin does not undergo the stressed to relaxed transition or inhibit trypsin-like serine proteases. Evidence that maspin is not a protease inhibitory serpin." Pemberton P.A., Wong D.T., Gibson H.L., Kiefer M.C., Fitzpatrick P.A., Sager R., Barr P.J. J. Biol. Chem. 270:15832-15837(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 341-360, CHARACTERIZATION.
[7]	"Mammary serine protease inhibitor (Maspin) binds directly to interferon regulatory factor 6: identification of a novel serpin partnership." Bailey C.M., Khalkhali-Ellis Z., Kondo S., Margaryan N.V., Seftor R.E.B., Wheaton W.W., Amir S., Pins M.R., Schutte B.C., Hendrix M.J.C. J. Biol. Chem. 280:34210-34217(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH IRF6.
[8]	"The high resolution crystal structure of the human tumor suppressor maspin reveals a novel conformational switch in the G-helix." Law R.H., Irving J.A., Buckle A.M., Ruzyla K., Buzza M., Bashtannyk-Puhalovich T.A., Beddoe T.C., Nguyen K., Worrall D.M., Bottomley S.P., Bird P.I., Rossjohn J., Whisstock J.C. J. Biol. Chem. 280:22356-22364(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[9]	"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] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] PRO-176, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U04313 mRNA. Translation: AAA18957.1.
AK312765 mRNA. Translation: BAG35631.1.
AC036176 Genomic DNA. No translation available.
BC020713 mRNA. Translation: AAH20713.1.
BX640597 mRNA. Translation: CAE45703.1.

IPI

IPI00644196.
IPI00783625.

PIR

A36898.

RefSeq

NP_002630.2. NM_002639.4.

UniGene

Hs.55279.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WZ9	X-ray	2.10	A/B	1-375	[»]
1XQG	X-ray	3.10	A/B	1-375	[»]
1XQJ	X-ray	3.10	A	1-375	[»]
1XU8	X-ray	2.80	A/B	1-375	[»]

ProteinModelPortal

P36952.

ModBase

Search...

Protein-protein interaction databases

IntAct

P36952. 2 interactions.

STRING

9606.ENSP00000372221.

Protein family/group databases

MEROPS

I04.980.

PTM databases

PhosphoSite

P36952.

Polymorphism databases

DMDM

229462757.

Proteomic databases

PaxDb

P36952.

PRIDE

P36952.

Protocols and materials databases

DNASU

5268.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000382771; ENSP00000372221; ENSG00000206075.
ENST00000489441; ENSP00000467158; ENSG00000206075.

GeneID

5268.

KEGG

hsa:5268.

UCSC

uc002liy.2. human.
uc002liz.4. human.

Organism-specific databases

CTD

5268.

GeneCards

GC18P061117.

H-InvDB

HIX0014501.

HGNC

HGNC:8949. SERPINB5.

HPA

CAB009570.
HPA019025.
HPA019132.
HPA020136.

MIM

154790. gene.

neXtProt

NX_P36952.

PharmGKB

PA35515.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG4826.

HOGENOM

HOG000238519.

HOVERGEN

HBG005957.

InParanoid

P36952.

KO

K10139.

OMA

XEFISST.

OrthoDB

EOG495ZS0.

Gene expression databases

ArrayExpress

P36952.

Bgee

P36952.

CleanEx

HS_SERPINB5.

Genevestigator

P36952.

GermOnline

ENSG00000206075. Homo sapiens.

Family and domain databases

InterPro

IPR023795. Protease_inhib_I4_serpin_CS.
IPR000240. Serpin_B9/Maspin.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]

PANTHER

PTHR11461. PTHR11461. 1 hit.

Pfam

PF00079. Serpin. 1 hit.
[Graphical view]

PRINTS

PR00676. MASPIN.

SMART

SM00093. SERPIN. 1 hit.
[Graphical view]

SUPFAM

SSF56574. Prot_inh_serpin. 1 hit.

PROSITE

PS00284. SERPIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SERPINB5. human.

EvolutionaryTrace

P36952.

GenomeRNAi

5268.

NextBio

20352.

SOURCE

Search...

Entry information

Entry name

SPB5_HUMAN

Accession

Primary (citable) accession number: P36952
Secondary accession number(s): B2R6Y4, Q6N0B4, Q8WW89

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	May 5, 2009
Last modified:	May 1, 2013
This is version 120 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.