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Protein

Serpin H1

Gene

Serpinh1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei376 – 3772Reactive bond homologBy similarity

GO - Molecular functioni

  1. poly(A) RNA binding Source: MGI
  2. serine-type endopeptidase inhibitor activity Source: GO_Central
  3. unfolded protein binding Source: MGI

GO - Biological processi

  1. chondrocyte development involved in endochondral bone morphogenesis Source: MGI
  2. collagen biosynthetic process Source: MGI
  3. collagen fibril organization Source: MGI
  4. negative regulation of endopeptidase activity Source: GO_Central
  5. protein maturation Source: MGI
  6. regulation of proteolysis Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Enzyme and pathway databases

ReactomeiREACT_198984. Collagen biosynthesis and modifying enzymes.

Protein family/group databases

MEROPSiI04.036.

Names & Taxonomyi

Protein namesi
Recommended name:
Serpin H1
Alternative name(s):
47 kDa heat shock protein
Collagen-binding protein
Short name:
Colligin
Serine protease inhibitor J6
Gene namesi
Name:Serpinh1
Synonyms:Cbp1, Hsp47
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:88283. Serpinh1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. endoplasmic reticulum Source: MGI
  3. endoplasmic reticulum-Golgi intermediate compartment Source: MGI
  4. endoplasmic reticulum lumen Source: UniProtKB-SubCell
  5. extracellular space Source: InterPro
  6. extracellular vesicular exosome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17171 PublicationAdd
BLAST
Chaini18 – 417400Serpin H1PRO_0000032517Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei93 – 931N6-succinyllysine1 Publication
Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence Analysis
Glycosylationi124 – 1241N-linked (GlcNAc...)Sequence Analysis
Modified residuei206 – 2061N6-acetyllysine1 Publication
Modified residuei295 – 2951N6-succinyllysine1 Publication
Modified residuei318 – 3181N6-acetyllysine1 Publication
Glycosylationi394 – 3941N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

MaxQBiP19324.
PaxDbiP19324.
PRIDEiP19324.

2D gel databases

REPRODUCTION-2DPAGEIPI00114733.

PTM databases

PhosphoSiteiP19324.

Expressioni

Inductioni

By heat shock and retinoic acid.

Gene expression databases

BgeeiP19324.
GenevestigatoriP19324.

Interactioni

Protein-protein interaction databases

BioGridi198530. 4 interactions.
IntActiP19324. 1 interaction.
MINTiMINT-1853582.

Structurei

3D structure databases

ProteinModelPortaliP19324.
SMRiP19324. Positions 35-417.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi414 – 4174Prevents secretion from ERCurated

Sequence similaritiesi

Belongs to the serpin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4826.
GeneTreeiENSGT00770000120524.
HOGENOMiHOG000238519.
HOVERGENiHBG104930.
InParanoidiP19324.
KOiK09501.
OMAiNYEHSKI.
OrthoDBiEOG7GBFX4.
TreeFamiTF343094.

Family and domain databases

InterProiIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00284. SERPIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P19324-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRSLLLGTLC LLAVALAAEV KKPLEAAAPG TAEKLSSKAT TLAERSTGLA
60 70 80 90 100
FSLYQAMAKD QAVENILLSP LVVASSLGLV SLGGKATTAS QAKAVLSAEK
110 120 130 140 150
LRDEEVHTGL GELLRSLSNS TARNVTWKLG SRLYGPSSVS FADDFVRSSK
160 170 180 190 200
QHYNCEHSKI NFRDKRSALQ SINEWASQTT DGKLPEVTKD VERTDGALLV
210 220 230 240 250
NAMFFKPHWD EKFHHKMVDN RGFMVTRSYT VGVTMMHRTG LYNYYDDEKE
260 270 280 290 300
KLQMVEMPLA HKLSSLIILM PHHVEPLERL EKLLTKEQLK AWMGKMQKKA
310 320 330 340 350
VAISLPKGVV EVTHDLQKHL AGLGLTEAID KNKADLSRMS GKKDLYLASV
360 370 380 390 400
FHATAFEWDT EGNPFDQDIY GREELRSPKL FYADHPFIFL VRDNQSGSLL
410
FIGRLVRPKG DKMRDEL
Length:417
Mass (Da):46,534
Last modified:July 27, 2011 - v3
Checksum:i1124A050A6CC4F67
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti176 – 1761A → P in AAA03200. (PubMed:2394749)Curated
Sequence conflicti212 – 2121K → R in CAA43091. (PubMed:1317794)Curated
Sequence conflicti212 – 2121K → R in AAA03200. (PubMed:2394749)Curated
Sequence conflicti216 – 2161K → R in CAA43091. (PubMed:1317794)Curated
Sequence conflicti216 – 2161K → R in AAA03200. (PubMed:2394749)Curated
Sequence conflicti270 – 2712MP → IA in AAA03200. (PubMed:2394749)Curated
Sequence conflicti277 – 2771L → S in AAA03200. (PubMed:2394749)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60676 mRNA. Translation: CAA43091.1.
J05609 mRNA. Translation: AAA03200.1. Sequence problems.
D12907 Genomic DNA. Translation: BAA02298.1.
AK029080 mRNA. Translation: BAC26283.1.
AK031457 mRNA. Translation: BAC27413.1.
AK077660 mRNA. Translation: BAC36935.1.
AK077937 mRNA. Translation: BAC37075.1.
AK086519 mRNA. Translation: BAC39683.1.
AK086523 mRNA. Translation: BAC39684.1.
AK089993 mRNA. Translation: BAC41032.1.
AK090103 mRNA. Translation: BAC41093.1.
AK159998 mRNA. Translation: BAE35546.1.
AK168442 mRNA. Translation: BAE40347.1.
AK168870 mRNA. Translation: BAE40689.1.
AC158748 Genomic DNA. No translation available.
BC085143 mRNA. Translation: AAH85143.1.
CCDSiCCDS21480.1.
PIRiS23453. A42843.
RefSeqiNP_001104513.1. NM_001111043.1.
NP_001104514.1. NM_001111044.1.
NP_001272705.1. NM_001285776.1.
NP_033955.2. NM_009825.2.
XP_006507341.1. XM_006507278.1.
XP_006507342.1. XM_006507279.1.
UniGeneiMm.22708.

Genome annotation databases

EnsembliENSMUST00000094154; ENSMUSP00000091706; ENSMUSG00000070436.
ENSMUST00000169437; ENSMUSP00000126390; ENSMUSG00000070436.
GeneIDi12406.
KEGGimmu:12406.
UCSCiuc009ilj.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60676 mRNA. Translation: CAA43091.1.
J05609 mRNA. Translation: AAA03200.1. Sequence problems.
D12907 Genomic DNA. Translation: BAA02298.1.
AK029080 mRNA. Translation: BAC26283.1.
AK031457 mRNA. Translation: BAC27413.1.
AK077660 mRNA. Translation: BAC36935.1.
AK077937 mRNA. Translation: BAC37075.1.
AK086519 mRNA. Translation: BAC39683.1.
AK086523 mRNA. Translation: BAC39684.1.
AK089993 mRNA. Translation: BAC41032.1.
AK090103 mRNA. Translation: BAC41093.1.
AK159998 mRNA. Translation: BAE35546.1.
AK168442 mRNA. Translation: BAE40347.1.
AK168870 mRNA. Translation: BAE40689.1.
AC158748 Genomic DNA. No translation available.
BC085143 mRNA. Translation: AAH85143.1.
CCDSiCCDS21480.1.
PIRiS23453. A42843.
RefSeqiNP_001104513.1. NM_001111043.1.
NP_001104514.1. NM_001111044.1.
NP_001272705.1. NM_001285776.1.
NP_033955.2. NM_009825.2.
XP_006507341.1. XM_006507278.1.
XP_006507342.1. XM_006507279.1.
UniGeneiMm.22708.

3D structure databases

ProteinModelPortaliP19324.
SMRiP19324. Positions 35-417.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198530. 4 interactions.
IntActiP19324. 1 interaction.
MINTiMINT-1853582.

Chemistry

ChEMBLiCHEMBL1163113.

Protein family/group databases

MEROPSiI04.036.

PTM databases

PhosphoSiteiP19324.

2D gel databases

REPRODUCTION-2DPAGEIPI00114733.

Proteomic databases

MaxQBiP19324.
PaxDbiP19324.
PRIDEiP19324.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000094154; ENSMUSP00000091706; ENSMUSG00000070436.
ENSMUST00000169437; ENSMUSP00000126390; ENSMUSG00000070436.
GeneIDi12406.
KEGGimmu:12406.
UCSCiuc009ilj.2. mouse.

Organism-specific databases

CTDi871.
MGIiMGI:88283. Serpinh1.

Phylogenomic databases

eggNOGiCOG4826.
GeneTreeiENSGT00770000120524.
HOGENOMiHOG000238519.
HOVERGENiHBG104930.
InParanoidiP19324.
KOiK09501.
OMAiNYEHSKI.
OrthoDBiEOG7GBFX4.
TreeFamiTF343094.

Enzyme and pathway databases

ReactomeiREACT_198984. Collagen biosynthesis and modifying enzymes.

Miscellaneous databases

ChiTaRSiSerpinh1. mouse.
NextBioi281182.
PROiP19324.
SOURCEiSearch...

Gene expression databases

BgeeiP19324.
GenevestigatoriP19324.

Family and domain databases

InterProiIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00284. SERPIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of a mouse 47-kDa heat-shock protein (HSP47), a collagen-binding stress protein, and its expression during the differentiation of F9 teratocarcinoma cells."
    Takechi H., Hirayoshi K., Nakai A., Kudo H., Saga S., Kita T., Nagata K.
    Eur. J. Biochem. 206:323-329(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-43.
    Strain: BALB/c.
  2. "A retinoic acid-inducible mRNA from F9 teratocarcinoma cells encodes a novel protease inhibitor homologue."
    Wang S.-Y., Gudas L.J.
    J. Biol. Chem. 265:15818-15822(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Teratocarcinoma.
  3. Erratum
    Wang S.-Y., Gudas L.J.
    J. Biol. Chem. 266:14135-14135(1991) [PubMed] [Europe PMC] [Abstract]
  4. "Structure of the gene and its retinoic acid-regulatory region for murine J6 serpin. An F9 teratocarcinoma cell retinoic acid-inducible protein."
    Wang S.-Y.
    J. Biol. Chem. 267:15362-15366(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Structure of the gene encoding the mouse 47-kDa heat-shock protein (HSP47)."
    Hosokawa N., Takechi H., Yokota S.I., Hirayoshi K., Nagata K.
    Gene 126:187-193(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head, Heart, Skin, Stomach and Testis.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  8. "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].
    Strain: C57BL/6.
    Tissue: Brain.
  9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-206 AND LYS-318, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-93 AND LYS-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiSERPH_MOUSE
AccessioniPrimary (citable) accession number: P19324
Secondary accession number(s): Q5U4D0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: July 27, 2011
Last modified: February 4, 2015
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.