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P20155

- ISK2_HUMAN

UniProt

P20155 - ISK2_HUMAN

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Protein
Serine protease inhibitor Kazal-type 2
Gene
SPINK2
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. endopeptidase inhibitor activity Source: ProtInc
  2. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW

GO - Biological processi

  1. fertilization Source: Ensembl
  2. male germ cell proliferation Source: Ensembl
  3. negative regulation of serine-type endopeptidase activity Source: Ensembl
  4. seminiferous tubule development Source: Ensembl
  5. spermatid development Source: Ensembl
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: Chromosome 4

Organism-specific databases

HGNCiHGNC:11245. SPINK2.

Subcellular locationi

GO - Cellular componenti

  1. acrosomal vesicle Source: Ensembl
  2. extracellular region Source: UniProtKB-SubCell
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.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241Pyrrolidone carboxylic acid1 Publication
Disulfide bondi36 ↔ 661 Publication
Disulfide bondi44 ↔ 631 Publication
Disulfide bondi52 ↔ 841 Publication

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Proteomic databases

MaxQBiP20155.
PaxDbiP20155.
PRIDEiP20155.

PTM databases

PhosphoSiteiP20155.

Expressioni

Tissue specificityi

Expressed in epididymis (at protein level).1 Publication

Gene expression databases

ArrayExpressiP20155.
BgeeiP20155.
CleanExiHS_SPINK2.
GenevestigatoriP20155.

Organism-specific databases

HPAiCAB020824.
HPA026813.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000248701.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JXDNMR-A23-84[»]
ProteinModelPortaliP20155.
SMRiP20155. Positions 23-84.

Miscellaneous databases

EvolutionaryTraceiP20155.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 8455Kazal-like
Add
BLAST

Sequence similaritiesi

Contains 1 Kazal-like domain.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG255629.
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

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
KEGGihsa:6691.
UCSCiuc003hcg.2. human.

Polymorphism databases

DMDMi123985.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS3508.1.
PIRi JU0152.
RefSeqi NP_001258650.1. NM_001271721.1.
NP_001258651.1. NM_001271722.1.
NP_066937.1. NM_021114.3.
UniGenei Hs.98243.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JXD NMR - A 23-84 [» ]
ProteinModelPortali P20155.
SMRi P20155. Positions 23-84.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000248701.

Protein family/group databases

MEROPSi I01.012.

PTM databases

PhosphoSitei P20155.

Polymorphism databases

DMDMi 123985.

Proteomic databases

MaxQBi P20155.
PaxDbi P20155.
PRIDEi P20155.

Protocols and materials databases

DNASUi 6691.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000248701 ; ENSP00000248701 ; ENSG00000128040 .
GeneIDi 6691.
KEGGi hsa:6691.
UCSCi uc003hcg.2. human.

Organism-specific databases

CTDi 6691.
GeneCardsi GC04M057676.
HGNCi HGNC:11245. SPINK2.
HPAi CAB020824.
HPA026813.
MIMi 605753. gene.
neXtProti NX_P20155.
PharmGKBi PA36075.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG255629.
HOGENOMi HOG000090244.
InParanoidi P20155.
OrthoDBi EOG7BW0M2.
PhylomeDBi P20155.

Miscellaneous databases

EvolutionaryTracei P20155.
GeneWikii SPINK2.
GenomeRNAii 6691.
NextBioi 26077.
PROi P20155.
SOURCEi Search...

Gene expression databases

ArrayExpressi P20155.
Bgeei P20155.
CleanExi HS_SPINK2.
Genevestigatori P20155.

Family and domain databases

InterProi IPR002350. Kazal_dom.
[Graphical view ]
Pfami PF00050. Kazal_1. 1 hit.
[Graphical view ]
SMARTi SM00280. KAZAL. 1 hit.
[Graphical view ]
PROSITEi PS00282. KAZAL_1. 1 hit.
PS51465. KAZAL_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 9, 2014
This is version 125 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

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