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Protein

Testis-specific H1 histone

Gene

H1FNT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Essential for normal spermatogenesis and male fertility. Required for proper cell restructuring and DNA condensation during the elongation phase of spermiogenesis. Involved in the histone-protamine transition of sperm chromatin and the subsequent production of functional sperm. Binds both double-stranded and single-stranded DNA, ATP and protamine-1 (By similarity).By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

  • chromosome condensation Source: UniProtKB-KW
  • multicellular organism development Source: UniProtKB-KW
  • spermatid nucleus elongation Source: UniProtKB
  • sperm chromatin condensation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, DNA condensation, Spermatogenesis

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Testis-specific H1 histone
Alternative name(s):
Haploid germ cell-specific nuclear protein 1
Histone H1t2
Gene namesi
Name:H1FNT
Synonyms:HANP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:24893. H1FNT.

Subcellular locationi

  • Nucleus By similarity
  • Chromosome By similarity

  • Note: In round and elongating spermatids, specifically localizes to a chromatin domain at the apical pole.By similarity

GO - Cellular componenti

  • nuclear chromatin Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA143485486.

Polymorphism and mutation databases

BioMutaiH1FNT.
DMDMi215274115.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 255255Testis-specific H1 histonePRO_0000343414Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei56 – 561PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ75WM6.
PaxDbiQ75WM6.
PeptideAtlasiQ75WM6.
PRIDEiQ75WM6.

PTM databases

PhosphoSiteiQ75WM6.

Expressioni

Tissue specificityi

Testis-specific.1 Publication

Gene expression databases

BgeeiQ75WM6.
CleanExiHS_H1FNT.
GenevisibleiQ75WM6. HS.

Organism-specific databases

HPAiHPA046204.

Interactioni

Protein-protein interaction databases

BioGridi131143. 2 interactions.
STRINGi9606.ENSP00000334805.

Structurei

3D structure databases

ProteinModelPortaliQ75WM6.
SMRiQ75WM6. Positions 59-124.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi129 – 19567Arg-richAdd
BLAST

Sequence similaritiesi

Belongs to the histone H1/H5 family.Curated

Phylogenomic databases

eggNOGiENOG410IX90. Eukaryota.
ENOG4111BIG. LUCA.
GeneTreeiENSGT00730000111596.
HOGENOMiHOG000112840.
InParanoidiQ75WM6.
OMAiKEPPCAR.
OrthoDBiEOG71K64P.
PhylomeDBiQ75WM6.
TreeFamiTF338403.

Sequencei

Sequence statusi: Complete.

Q75WM6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEQALTGEAQ SRWPRRGGSG AMAEAPGPSG ESRGHSATQL PAEKTVGGPS
60 70 80 90 100
RGCSSSVLRV SQLVLQAIST HKGLTLAALK KELRNAGYEV RRKSGRHEAP
110 120 130 140 150
RGQAKATLLR VSGSDAAGYF RVWKVPKPRR KPGRARQEEG TRAPWRTPAA
160 170 180 190 200
PRSSRRRRQP LRKAARKARE VWRRNARAKA KANARARRTR RARPRAKEPP
210 220 230 240 250
CARAKEEAGA TAADEGRGQA VKEDTTPRSG KDKRRSSKPR EEKQEPKKPA

QRTIQ
Length:255
Mass (Da):28,116
Last modified:November 25, 2008 - v3
Checksum:iF5BA8AB6A4D4E912
GO

Sequence cautioni

The sequence BAD13382.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti231 – 2311K → N in AAI18636 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti84 – 841R → G.1 Publication
Corresponds to variant rs2732441 [ dbSNP | Ensembl ].
VAR_044371
Natural varianti108 – 1081L → P.1 Publication
Corresponds to variant rs766280749 [ dbSNP | Ensembl ].
VAR_044372
Natural varianti136 – 1361R → S.1 Publication
Corresponds to variant rs752698412 [ dbSNP | Ensembl ].
VAR_044373
Natural varianti174 – 1741R → Q.2 Publications
Corresponds to variant rs1471997 [ dbSNP | Ensembl ].
VAR_044374
Natural varianti195 – 1951R → Q.
Corresponds to variant rs1471997 [ dbSNP | Ensembl ].
VAR_047359
Natural varianti237 – 2371S → F.1 Publication
Corresponds to variant rs2291483 [ dbSNP | Ensembl ].
VAR_044375

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY302593 mRNA. Translation: AAP60022.1.
AC024257 Genomic DNA. No translation available.
BC118635 mRNA. Translation: AAI18636.1.
BC119787 mRNA. Translation: AAI19788.1.
AB121028 mRNA. Translation: BAD13382.2. Different initiation.
AY496854 Genomic DNA. Translation: AAS49492.1.
CCDSiCCDS8762.1.
RefSeqiNP_861453.1. NM_181788.1.
UniGeneiHs.155833.

Genome annotation databases

EnsembliENST00000335017; ENSP00000334805; ENSG00000187166.
GeneIDi341567.
KEGGihsa:341567.
UCSCiuc001rrm.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY302593 mRNA. Translation: AAP60022.1.
AC024257 Genomic DNA. No translation available.
BC118635 mRNA. Translation: AAI18636.1.
BC119787 mRNA. Translation: AAI19788.1.
AB121028 mRNA. Translation: BAD13382.2. Different initiation.
AY496854 Genomic DNA. Translation: AAS49492.1.
CCDSiCCDS8762.1.
RefSeqiNP_861453.1. NM_181788.1.
UniGeneiHs.155833.

3D structure databases

ProteinModelPortaliQ75WM6.
SMRiQ75WM6. Positions 59-124.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi131143. 2 interactions.
STRINGi9606.ENSP00000334805.

PTM databases

PhosphoSiteiQ75WM6.

Polymorphism and mutation databases

BioMutaiH1FNT.
DMDMi215274115.

Proteomic databases

EPDiQ75WM6.
PaxDbiQ75WM6.
PeptideAtlasiQ75WM6.
PRIDEiQ75WM6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000335017; ENSP00000334805; ENSG00000187166.
GeneIDi341567.
KEGGihsa:341567.
UCSCiuc001rrm.3. human.

Organism-specific databases

CTDi341567.
GeneCardsiH1FNT.
HGNCiHGNC:24893. H1FNT.
HPAiHPA046204.
neXtProtiNX_Q75WM6.
PharmGKBiPA143485486.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IX90. Eukaryota.
ENOG4111BIG. LUCA.
GeneTreeiENSGT00730000111596.
HOGENOMiHOG000112840.
InParanoidiQ75WM6.
OMAiKEPPCAR.
OrthoDBiEOG71K64P.
PhylomeDBiQ75WM6.
TreeFamiTF338403.

Miscellaneous databases

GenomeRNAii341567.
PROiQ75WM6.

Gene expression databases

BgeeiQ75WM6.
CleanExiHS_H1FNT.
GenevisibleiQ75WM6. HS.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Huang C.Q., Shan Y.X., Wu S.L., Cheng Z.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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], VARIANT GLN-174.
  4. "Expression profiles and single-nucleotide polymorphism analysis of human HANP1/H1T2 encoding a histone H1-like protein."
    Tanaka H., Matsuoka Y., Onishi M., Kitamura K., Miyagawa Y., Nishimura H., Tsujimura A., Okuyama A., Nishimune Y.
    Int. J. Androl. 29:353-359(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-255, FUNCTION, TISSUE SPECIFICITY, VARIANTS GLY-84; PRO-108; SER-136; GLN-174 AND PHE-237.
    Tissue: Testis.
  5. "Polar nuclear localization of H1T2, a histone H1 variant, required for spermatid elongation and DNA condensation during spermiogenesis."
    Martianov I., Brancorsini S., Catena R., Gansmuller A., Kotaja N., Parvinen M., Sassone-Corsi P., Davidson I.
    Proc. Natl. Acad. Sci. U.S.A. 102:2808-2813(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-255.

Entry informationi

Entry nameiH1FNT_HUMAN
AccessioniPrimary (citable) accession number: Q75WM6
Secondary accession number(s): Q147U8, Q5GKZ5, Q7Z694
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: November 25, 2008
Last modified: July 6, 2016
This is version 84 of the entry and version 3 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

Caution

It is uncertain whether Met-1 or Met-22 is the initiator.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.