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Protein

Serine protease inhibitor Kazal-type 2

Gene

SPINK2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Strong inhibitor of acrosin in male and/or female genital tract. Also inhibits trypsin.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei46 – 472Reactive bond

GO - Molecular functioni

  • endopeptidase inhibitor activity Source: ProtInc
  • serine-type endopeptidase inhibitor activity Source: UniProtKB-KW

GO - Biological processi

  • negative regulation of endopeptidase activity Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Protein family/group databases

MEROPSiI01.012.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine protease inhibitor Kazal-type 2
Alternative name(s):
Acrosin-trypsin inhibitor
Epididymis tissue protein Li 172
HUSI-II
Gene namesi
Name:SPINK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:11245. SPINK2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi45 – 451P → A: No effect on inhibitory activity towards trypsin. 1 Publication
Mutagenesisi46 – 461R → A: Loss of inhibitory activity towards trypsin. 1 Publication
Mutagenesisi47 – 471H → A: Reduces inhibitory activity towards trypsin. 1 Publication
Mutagenesisi48 – 481F → A: Reduces inhibitory activity towards trypsin. 1 Publication

Organism-specific databases

PharmGKBiPA36075.

Polymorphism and mutation databases

DMDMi123985.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 PublicationAdd
BLAST
Chaini24 – 8461Serine protease inhibitor Kazal-type 2PRO_0000016561Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241Pyrrolidone carboxylic acid1 Publication
Disulfide bondi36 ↔ 66PROSITE-ProRule annotation1 Publication
Disulfide bondi44 ↔ 63PROSITE-ProRule annotation1 Publication
Disulfide bondi52 ↔ 84PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP20155.
PRIDEiP20155.

PTM databases

PhosphoSiteiP20155.

Expressioni

Tissue specificityi

Expressed in epididymis (at protein level).1 Publication

Gene expression databases

BgeeiP20155.
CleanExiHS_SPINK2.
ExpressionAtlasiP20155. baseline and differential.
GenevisibleiP20155. HS.

Organism-specific databases

HPAiCAB020824.
HPA026813.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ADAMTSL4Q6UY14-33EBI-10200479,EBI-10173507
KRTAP5-9P263713EBI-10200479,EBI-3958099
NOTCH2NLQ7Z3S93EBI-10200479,EBI-945833

Protein-protein interaction databases

BioGridi112569. 4 interactions.
IntActiP20155. 4 interactions.
STRINGi9606.ENSP00000248701.

Structurei

Secondary structure

1
84
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 326Combined sources
Beta strandi51 – 533Combined sources
Turni62 – 643Combined sources
Helixi65 – 706Combined sources
Beta strandi73 – 753Combined sources
Beta strandi78 – 825Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JXDNMR-A23-84[»]
ProteinModelPortaliP20155.
SMRiP20155. Positions 23-84.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20155.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 8455Kazal-likePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 Kazal-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG255629.
GeneTreeiENSGT00530000064285.
HOGENOMiHOG000090244.
InParanoidiP20155.
OrthoDBiEOG7BW0M2.
PhylomeDBiP20155.

Family and domain databases

InterProiIPR002350. Kazal_dom.
[Graphical view]
PfamiPF00050. Kazal_1. 1 hit.
[Graphical view]
SMARTiSM00280. KAZAL. 1 hit.
[Graphical view]
PROSITEiPS00282. KAZAL_1. 1 hit.
PS51465. KAZAL_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P20155-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALSVLRLAL LLLAVTFAAS LIPQFGLFSK YRTPNCSQYR LPGCPRHFNP
60 70 80
VCGSDMSTYA NECTLCMKIR EGGHNIKIIR NGPC
Length:84
Mass (Da):9,291
Last modified:December 1, 1992 - v2
Checksum:iE1DE1792BFB1BB85
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M91438 Genomic DNA. Translation: AAB59431.1.
X57655 mRNA. Translation: CAB37834.1.
M84967 Genomic DNA. No translation available.
GU727622 mRNA. Translation: ADU87624.1.
AK312222 mRNA. Translation: BAG35155.1.
CR542135 mRNA. Translation: CAG46932.1.
CH471057 Genomic DNA. Translation: EAX05513.1.
BC022514 mRNA. Translation: AAH22514.1.
CCDSiCCDS3508.1.
PIRiJU0152.
RefSeqiNP_001258650.1. NM_001271721.1.
NP_001258651.1. NM_001271722.1.
NP_066937.1. NM_021114.3.
UniGeneiHs.98243.

Genome annotation databases

EnsembliENST00000248701; ENSP00000248701; ENSG00000128040.
GeneIDi6691.
UCSCiuc003hcg.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M91438 Genomic DNA. Translation: AAB59431.1.
X57655 mRNA. Translation: CAB37834.1.
M84967 Genomic DNA. No translation available.
GU727622 mRNA. Translation: ADU87624.1.
AK312222 mRNA. Translation: BAG35155.1.
CR542135 mRNA. Translation: CAG46932.1.
CH471057 Genomic DNA. Translation: EAX05513.1.
BC022514 mRNA. Translation: AAH22514.1.
CCDSiCCDS3508.1.
PIRiJU0152.
RefSeqiNP_001258650.1. NM_001271721.1.
NP_001258651.1. NM_001271722.1.
NP_066937.1. NM_021114.3.
UniGeneiHs.98243.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JXDNMR-A23-84[»]
ProteinModelPortaliP20155.
SMRiP20155. Positions 23-84.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112569. 4 interactions.
IntActiP20155. 4 interactions.
STRINGi9606.ENSP00000248701.

Protein family/group databases

MEROPSiI01.012.

PTM databases

PhosphoSiteiP20155.

Polymorphism and mutation databases

DMDMi123985.

Proteomic databases

PaxDbiP20155.
PRIDEiP20155.

Protocols and materials databases

DNASUi6691.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000248701; ENSP00000248701; ENSG00000128040.
GeneIDi6691.
UCSCiuc003hcg.2. human.

Organism-specific databases

CTDi6691.
GeneCardsiGC04M057676.
HGNCiHGNC:11245. SPINK2.
HPAiCAB020824.
HPA026813.
MIMi605753. gene.
neXtProtiNX_P20155.
PharmGKBiPA36075.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG255629.
GeneTreeiENSGT00530000064285.
HOGENOMiHOG000090244.
InParanoidiP20155.
OrthoDBiEOG7BW0M2.
PhylomeDBiP20155.

Miscellaneous databases

EvolutionaryTraceiP20155.
GeneWikiiSPINK2.
GenomeRNAii6691.
NextBioi26077.
PROiP20155.
SOURCEiSearch...

Gene expression databases

BgeeiP20155.
CleanExiHS_SPINK2.
ExpressionAtlasiP20155. baseline and differential.
GenevisibleiP20155. HS.

Family and domain databases

InterProiIPR002350. Kazal_dom.
[Graphical view]
PfamiPF00050. Kazal_1. 1 hit.
[Graphical view]
SMARTiSM00280. KAZAL. 1 hit.
[Graphical view]
PROSITEiPS00282. KAZAL_1. 1 hit.
PS51465. KAZAL_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and sequence analysis of the cDNA encoding the human acrosin-trypsin inhibitor (HUSI-II)."
    Moeritz A., Lilja H., Fink E.
    FEBS Lett. 278:127-130(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Organization and sequence of the gene encoding the human acrosin-trypsin inhibitor (HUSI-II)."
    Moeritz A., Grzeschik K.H., Wingender E., Fink E.
    Gene 123:277-281(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Systematic mapping and functional analysis of a family of human epididymal secretory sperm-located proteins."
    Li J., Liu F., Wang H., Liu X., Liu J., Li N., Wan F., Wang W., Zhang C., Jin S., Liu J., Zhu P., Liu Y.
    Mol. Cell. Proteomics 9:2517-2528(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Epididymis.
  4. "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].
    Tissue: Testis.
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  8. "Amino acid sequence elucidation of human acrosin-trypsin inhibitor (HUSI-II) reveals that Kazal-type proteinase inhibitors are structurally related to beta-subunits of glycoprotein hormones."
    Fink E., Hehlein-Fink C., Eulitz M.
    FEBS Lett. 270:222-224(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-84, PYROGLUTAMATE FORMATION AT GLN-24.
    Tissue: Semen.
  9. "Identification of trypsin-inhibitory site and structure determination of human SPINK2 serine proteinase inhibitor."
    Chen T., Lee T.-R., Liang W.-G., Chang W.-S., Lyu P.-C.
    Proteins 77:209-219(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 23-84, FUNCTION, MUTAGENESIS OF PRO-45; ARG-46; HIS-47 AND PHE-48, IDENTIFICATION BY MASS SPECTROMETRY, DISULFIDE BONDS.

Entry informationi

Entry nameiISK2_HUMAN
AccessioniPrimary (citable) accession number: P20155
Secondary accession number(s): Q6FGH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: December 1, 1992
Last modified: July 22, 2015
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.